|
Name |
Accession |
Description |
Interval |
E-value |
| SKICH |
pfam17751 |
SKICH domain; The SKICH domains of SKIP and PIPP mediate plasma membrane localization. The ... |
22-125 |
4.18e-47 |
|
SKICH domain; The SKICH domains of SKIP and PIPP mediate plasma membrane localization. The functions of the SKICH domains of NDP52 and CALCOCO1 are not known.
Pssm-ID: 465482 Cd Length: 102 Bit Score: 162.80 E-value: 4.18e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 22 VIFQNVGKSYLPHGALECHYTLTQFIKPHPKDWVGIFKVGWSTARDYYTFLWSplPDNYTEGTAINRSVVFQGYYVPNDD 101
Cdd:pfam17751 1 VVFQNVGEWYPPDEDIECSYTLTPDFTPSSWDWIGLFKVGWKSVNDYVTYVWA--KDDEVEGSNSVRQVLFKASYLPKEP 78
|
90 100
....*....|....*....|....
gi 528503643 102 GEFYQFCYVTHKGEIRGASTPFQF 125
Cdd:pfam17751 79 EGFYQFCYVSNLGSVVGISTPFQF 102
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
133-460 |
5.38e-36 |
|
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: 142.73 E-value: 5.38e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 133 EELLTME-----DEGGSDILVVTTKASYLEQKMEQIQQEKKELLENLDLLQK------------------ERDELIDEKN 189
Cdd:pfam07888 4 DELVTLEeeshgEEGGTDMLLVVPRAELLQNRLEECLQERAELLQAQEAANRqrekekerykrdreqwerQRRELESRVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 190 RLEKEYEQERESSAQLRKDVQELQLSAQSLQEEREEVKRRMEESTARLLQLEEDLIGVTQKGLQKETELDCLKDRVKKLN 269
Cdd:pfam07888 84 ELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 270 lekealeGQLKNEKDEKELYKIHLKNRELENTKLSAELQMLKSVDVNKENTIAQLKDELARVKSCLAEKekqHRQLLans 349
Cdd:pfam07888 164 -------AQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTA---HRKEA--- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 350 spsgESKALREQLRQKEEQLQATQQQANMLKAELRDSSNARDRSMAELYRIRVEAETLKKGQADARAECSRLEQQLEEMK 429
Cdd:pfam07888 231 ----ENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQER 306
|
330 340 350
....*....|....*....|....*....|.
gi 528503643 430 SSTQQEACKESDvlAVAELQREVEDLRLRLQ 460
Cdd:pfam07888 307 ETLQQSAEADKD--RIEKLSAELQRLEERLQ 335
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
156-479 |
4.60e-20 |
|
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: 95.89 E-value: 4.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 156 LEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEEREEVKRRMEESTA 235
Cdd:TIGR02168 682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 236 RLLQLEEDLIGVTQKGLQKETELDCLKDRVKKLNLEKEALEGQLKNEKDEKELYKIHLKNRELENTKLSAELQMLKSVDV 315
Cdd:TIGR02168 762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE 841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 316 NKENTIAQLKDELARVKSCLAEKEKQHRQLLAnsspsgESKALREQLRQKEEQLQATQQQANMLKAELRDSSNARDRSMA 395
Cdd:TIGR02168 842 DLEEQIEELSEDIESLAAEIEELEELIEELES------ELEALLNERASLEEALALLRSELEELSEELRELESKRSELRR 915
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 396 ELYRIRVEAETLKKGQADARAECSRLEQQLEEMKSSTQQEA--CKESDVLAVAELQREVEDLRLRLQ-------MAAEHY 466
Cdd:TIGR02168 916 ELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAeaLENKIEDDEEEARRRLKRLENKIKelgpvnlAAIEEY 995
|
330
....*....|...
gi 528503643 467 KDKYKECQKLQKQ 479
Cdd:TIGR02168 996 EELKERYDFLTAQ 1008
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
152-638 |
2.10e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 93.85 E-value: 2.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 152 KASYLEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEEREEVKRRME 231
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 232 ESTARLLQLEEDLIGVTQKGLQKETELDCLKDRVKKLNLEKEALEGQLKNEKDEKELYKIHLKNRELENTKLSAELQMLK 311
Cdd:COG1196 306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 312 SVDVNKENTIAQLKDELARvkscLAEKEKQHRQLLANSspSGESKALREQLRQKEEQLQATQQQANMLKAELRDSSNARD 391
Cdd:COG1196 386 EELLEALRAAAELAAQLEE----LEEAEEALLERLERL--EEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 392 RSMAELYRIRVEAETLKKGQADARAECSRLEQQ---LEEMKSSTQQEACKESDVLAVAELQREVEDLRLRLQMAAEHYKD 468
Cdd:COG1196 460 ALLELLAELLEEAALLEAALAELLEELAEAAARlllLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAA 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 469 KYKECQKLQKQVVKFNEQQG------VKRSPGSDAAAGPLSASPEASAPGSPSTSDAVLDAII---------HGRLKSSS 533
Cdd:COG1196 540 LEAALAAALQNIVVEDDEVAaaaieyLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDlvasdlreaDARYYVLG 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 534 KEL-DKNDKYRKCKQMLNEERERCSMITDELTKMEVKLREQMKTNESLRMQLAAEEDRYKSQVAEKGRELKELKDSLFVL 612
Cdd:COG1196 620 DTLlGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEAL 699
|
490 500
....*....|....*....|....*.
gi 528503643 613 TKEKEKLEGQLQKSVNREEEQKDSNL 638
Cdd:COG1196 700 LAEEEEERELAEAEEERLEEELEEEA 725
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
157-479 |
1.77e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 84.22 E-value: 1.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 157 EQKMEQIQqekkellENLDLLQKERDELIDEKNRLEKE------Y----EQERESSAQLR-KDVQELQLSAQSLQEEREE 225
Cdd:COG1196 178 ERKLEATE-------ENLERLEDILGELERQLEPLERQaekaerYrelkEELKELEAELLlLKLRELEAELEELEAELEE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 226 VKRRMEESTARLLQLEEDLIGVTQKGLQKETELDCLKDRVKKLNLEKEALEGQLKNEKDEKELYKIHLKNRELENTKLSA 305
Cdd:COG1196 251 LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 306 ELQMLKSVDVNKENTIAQLKDELARVKSCLAEKEKQHRQLLAnsspsgESKALREQLRQKEEQLQATQQQANMLKAELRD 385
Cdd:COG1196 331 ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA------ELAEAEEELEELAEELLEALRAAAELAAQLEE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 386 SSNARDRSMAELYRIRVEAETLKKGQADARAECSRLEQQLEEMKSSTQQEAckesdvLAVAELQREVEDLRLRLQMAAEH 465
Cdd:COG1196 405 LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE------EEEEALLELLAELLEEAALLEAA 478
|
330
....*....|....
gi 528503643 466 YKDKYKECQKLQKQ 479
Cdd:COG1196 479 LAELLEELAEAAAR 492
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
144-628 |
1.86e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 81.14 E-value: 1.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 144 SDILVVTTKASYLEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEER 223
Cdd:COG1196 302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 224 EEVKRRMEESTARLLQLEEDLigvtqkgLQKETELDCLKDRVKKLNLEKEALEGQLKNEKDEKELYKIHLKNRELENTKL 303
Cdd:COG1196 382 EELAEELLEALRAAAELAAQL-------EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 304 SAELQMLKSVDVNKENTIAQLKDELARVKSCLAEKEKQHRQLL-ANSSPSGESKALREqLRQKEEQLQATQQQANMLKAE 382
Cdd:COG1196 455 EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLeAEADYEGFLEGVKA-ALLLAGLRGLAGAVAVLIGVE 533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 383 LRDSSNARDRSMAELYRIRVE--------AETLKKGQADARAECSRLEQQLEEMKSSTQQEACKESDVLAVAELQREVED 454
Cdd:COG1196 534 AAYEAALEAALAAALQNIVVEddevaaaaIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADA 613
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 455 LRLRLQMAAEHYKDKYKECQKLQKQVVKFNEQQGVKRSPGSDAAAGPLSASpeasapGSPSTSDAVLDAIIHGRLKSSSK 534
Cdd:COG1196 614 RYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTG------GSRRELLAALLEAEAELEELAER 687
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 535 ELDKNDKYRKCKQMLNEERERCSMITDELTKMEVKLREQMKTNESLRMQLAAEEDRYKSQVAEKGRELKELKDSLFVLTK 614
Cdd:COG1196 688 LAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELER 767
|
490
....*....|....*.
gi 528503643 615 EKEKLEGQLQK--SVN 628
Cdd:COG1196 768 ELERLEREIEAlgPVN 783
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
156-455 |
6.64e-15 |
|
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: 79.33 E-value: 6.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 156 LEQKMEQIQ--QEKKELLENLDLlqkerDELIDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEEREEVKRRMEES 233
Cdd:TIGR02168 205 LERQAEKAEryKELKAELRELEL-----ALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 234 TARLLQLEEDLIGVTQKGLQKETELDCLKDRVKKLNLEKEALEGQLKNEKDEKELYKihlknreLENTKLSAELQMLKSV 313
Cdd:TIGR02168 280 EEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELA-------EELAELEEKLEELKEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 314 DVNKENTIAQLKDELARVKSCLAEKEKQHRQLLAN-SSPSGESKALREQLRQKEEQLQATQQQANMLKAELRD-----SS 387
Cdd:TIGR02168 353 LESLEAELEELEAELEELESRLEELEEQLETLRSKvAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEEllkklEE 432
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528503643 388 NARDRSMAELYRIRVEAETLKKGQADARAECSRLEQQLEE----MKSSTQQEACKESDVLAVAELQREVEDL 455
Cdd:TIGR02168 433 AELKELQAELEELEEELEELQEELERLEEALEELREELEEaeqaLDAAERELAQLQARLDSLERLQENLEGF 504
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
157-492 |
9.23e-15 |
|
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: 78.96 E-value: 9.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 157 EQKMEQIQQEKKELLENLDLLQKER------DELIDEKNRLE-----KEYEQERESSAQLRKDVQELQLSAQSLQEEREE 225
Cdd:TIGR02169 183 EENIERLDLIIDEKRQQLERLRRERekaeryQALLKEKREYEgyellKEKEALERQKEAIERQLASLEEELEKLTEEISE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 226 VKRRMEESTARLLQLEEDLIGVTqkglqkETELDCLKDRVKKLNLEKEALEGQLKNEKDEKELYKIHLKNRELENTKLSA 305
Cdd:TIGR02169 263 LEKRLEEIEQLLEELNKKIKDLG------EEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 306 ELQMLksvdvnkENTIAQLKDELARVKSCLAEKEKQHRQLLAN-SSPSGESKALREQLRQKEEQLQATQQQANMLKAELR 384
Cdd:TIGR02169 337 EIEEL-------EREIEEERKRRDKLTEEYAELKEELEDLRAElEEVDKEFAETRDELKDYREKLEKLKREINELKRELD 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 385 DSSNARDRSMAELYRIRVEAETLKKGQA-------DARAECSRLEQQLEEMKsstQQEACKESDVLAVAELQREVEDlrl 457
Cdd:TIGR02169 410 RLQEELQRLSEELADLNAAIAGIEAKINeleeekeDKALEIKKQEWKLEQLA---ADLSKYEQELYDLKEEYDRVEK--- 483
|
330 340 350
....*....|....*....|....*....|....*
gi 528503643 458 RLQMAAEHYKDKYKECQKLQKQVVKFNEQQGVKRS 492
Cdd:TIGR02169 484 ELSKLQRELAEAEAQARASEERVRGGRAVEEVLKA 518
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
114-479 |
1.33e-13 |
|
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: 75.10 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 114 GEIRGASTPFQFRANSPTE--EELLTM-EDEGGSDILVvttkaSYLEQKMEQIQQEKKELLENLDLLQKERDELIDEKNR 190
Cdd:TIGR02169 653 GAMTGGSRAPRGGILFSRSepAELQRLrERLEGLKREL-----SSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQ 727
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 191 LEKEYEQERESSAQLRKDVQELQlsaqslqEEREEVKRRMEESTARLLQLEEDLIGVTQKglQKETELDCLKDRVKKLNL 270
Cdd:TIGR02169 728 LEQEEEKLKERLEELEEDLSSLE-------QEIENVKSELKELEARIEELEEDLHKLEEA--LNDLEARLSHSRIPEIQA 798
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 271 EKEALegqlknekdEKELYKIHLKNRELEN--TKLSAELQMLKSVDVNKENTIAQLKDELARVKSCLAEKEKQHRQLLAn 348
Cdd:TIGR02169 799 ELSKL---------EEEVSRIEARLREIEQklNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEE- 868
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 349 sspsgESKALREQLRQKEEQLQATQQQANMLKAELRDSSNARDRSMAELYRIRVEAETLKKGQADARAECSRLEQQLEEM 428
Cdd:TIGR02169 869 -----ELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGED 943
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 528503643 429 KSSTQQEACKESDVLAVAELQREVEDLRLRLQMAAEHYKDKYKECQKLQKQ 479
Cdd:TIGR02169 944 EEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEK 994
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
178-486 |
2.25e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 74.32 E-value: 2.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 178 QKERDELIDEKNRLEKEYEQERESSAQLRKDVQElqlsaqsLQEEREEVKRRMEESTARLLQLEEDLIGVTQKGLQKETE 257
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEE-------LEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 258 LDCLKDRVKKLNLEKEALEGQLKNEKDEKELYKIHLKNRELENTKLSAELQMLKSVDVNKENTIAQLKDELARVKSCLAE 337
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLES 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 338 KEKQ-HRQLLANSSPSGESKALREQLRQKEEQLQATQQQANMLKAELRDSSNARDRSMAELYRIRVEAETLKKGQADARA 416
Cdd:TIGR02168 829 LERRiAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528503643 417 ECSRLEQQLEEmkssTQQEACKESDVLAVAELQRE------VEDLRLRLQMAAEHYKDKYKECQKLQKQVVKFNEQ 486
Cdd:TIGR02168 909 KRSELRRELEE----LREKLAQLELRLEGLEVRIDnlqerlSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENK 980
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
133-415 |
3.78e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 73.55 E-value: 3.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 133 EELLTMEDEGGSDILVVTTKASYLEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQEl 212
Cdd:TIGR02168 242 EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE- 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 213 qlsaqsLQEEREEVKRRMEESTARLLQLEEDLigvtqkgLQKETELDCLKDRVKKLNLEKEALEGQLKNEKDEKELYKIH 292
Cdd:TIGR02168 321 ------LEAQLEELESKLDELAEELAELEEKL-------EELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 293 LKNRELENTKLSAELQMLksvdvnkENTIAQLKDELARVKSCLAEKEKQhRQLLANSSPSGESKALREQLRQKEEQLQAT 372
Cdd:TIGR02168 388 VAQLELQIASLNNEIERL-------EARLERLEDRRERLQQEIEELLKK-LEEAELKELQAELEELEEELEELQEELERL 459
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 528503643 373 QQQANMLKAELRDSSNARDRSMAELYRIRVEAETLKKGQADAR 415
Cdd:TIGR02168 460 EEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLE 502
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
148-609 |
7.55e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 72.38 E-value: 7.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 148 VVTTKASYLEQKMEQIQQ-EKKELLENLDLLQKERDELIDEKNRLEK-----------------EYEQERESSAQLRKDV 209
Cdd:PRK02224 181 VLSDQRGSLDQLKAQIEEkEEKDLHERLNGLESELAELDEEIERYEEqreqaretrdeadevleEHEERREELETLEAEI 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 210 QELQLSAQSLQEEREEVKRRMEESTARLLQLEEDLIGVTQKGLQKETELDCLKDRVKKLNLEKEALEGQLKNE------- 282
Cdd:PRK02224 261 EDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECrvaaqah 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 283 KDEKELYKIHLKNRELENTKLSAELQMLksvdvnkENTIAQLKDELARVKSCLAEKEKQHRQLLA--NSSPS--GESKAL 358
Cdd:PRK02224 341 NEEAESLREDADDLEERAEELREEAAEL-------ESELEEAREAVEDRREEIEELEEEIEELRErfGDAPVdlGNAEDF 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 359 REQLRqkeEQLQATQQQANMLKAELRdssNARDRsMAELYRIRVEAETLKKGQ-----------ADARAECSRLEQQLEE 427
Cdd:PRK02224 414 LEELR---EERDELREREAELEATLR---TARER-VEEAEALLEAGKCPECGQpvegsphvetiEEDRERVEELEAELED 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 428 MKSSTQQEACKESDVLAVAELQREVEDLRLRLQMAAEHYKDKYKE-------CQKLQKQVVKFNEQQGVKRspgSDAAAG 500
Cdd:PRK02224 487 LEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETieekrerAEELRERAAELEAEAEEKR---EAAAEA 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 501 PLSASPEASAPGSPSTSDAVLDAIIHgRLKSSSKELDKNDKYRKCKQMLNEERErcsmitdELTKMEVKLREQMKTNESL 580
Cdd:PRK02224 564 EEEAEEAREEVAELNSKLAELKERIE-SLERIRTLLAAIADAEDEIERLREKRE-------ALAELNDERRERLAEKRER 635
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 528503643 581 RMQLAAE--EDR-------------YKSQVAEKGRELKELKDSL 609
Cdd:PRK02224 636 KRELEAEfdEARieearedkeraeeYLEQVEEKLDELREERDDL 679
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
156-635 |
4.29e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 70.09 E-value: 4.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 156 LEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEY---EQERESSAQLRKDVQELQLSAQSLQEEREEVKRRMEE 232
Cdd:PRK03918 191 IEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVkelEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 233 STARLLQLEE------DLIGVTQKGLQKETELDCLKDRVKKLNLEKEALEGQLKN--------EKDEKELYKIHLKNREL 298
Cdd:PRK03918 271 LKKEIEELEEkvkelkELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGieerikelEEKEERLEELKKKLKEL 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 299 ENTKLSAE-----LQMLKSVDVNKEN--------TIAQLKDELARVKSCLAEKEKQHRQLLANSspsGESKALREQLRQK 365
Cdd:PRK03918 351 EKRLEELEerhelYEEAKAKKEELERlkkrltglTPEKLEKELEELEKAKEEIEEEISKITARI---GELKKEIKELKKA 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 366 EEQLQATQQQANMLKAELRDSSNAR--DRSMAELYRIRVEAETLKKGQADARAECSRLEQQLEemksstqqeacKESDVL 443
Cdd:PRK03918 428 IEELKKAKGKCPVCGRELTEEHRKEllEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLK-----------KESELI 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 444 AVAELQREVEDLRLRLQ-MAAEHYKDKYKECQKLQKQVVKFN-EQQGVKRSPGSDAAAGPLSASPEaSAPGSPSTSDAVL 521
Cdd:PRK03918 497 KLKELAEQLKELEEKLKkYNLEELEKKAEEYEKLKEKLIKLKgEIKSLKKELEKLEELKKKLAELE-KKLDELEEELAEL 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 522 DAIIHGRLKSSSKELDKN--------DKY---RKCKQMLNEERERCSMITDELTKMEVKLREQMKTNESLRMQLAAEEDR 590
Cdd:PRK03918 576 LKELEELGFESVEELEERlkelepfyNEYlelKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKK 655
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 528503643 591 Y-KSQVAEKGRELKELKDSLFVLTKEKEKLEGQLQ---KSVNREEEQKD 635
Cdd:PRK03918 656 YsEEEYEELREEYLELSRELAGLRAELEELEKRREeikKTLEKLKEELE 704
|
|
| Zn-C2H2_TAX1BP1_rpt2 |
cd21970 |
second C2H2-type zinc binding domain found in tax1-binding protein 1 (TAX1BP1) and similar ... |
789-815 |
7.39e-12 |
|
second C2H2-type zinc binding domain found in tax1-binding protein 1 (TAX1BP1) and similar proteins; TAX1BP1, also called TRAF6-binding protein (T6BP), is a novel ubiquitin-binding adaptor protein involved in the negative regulation of the NF-kappaB transcription factor, a key player in inflammatory responses, immunity and tumorigenesis. It inhibits TNF-induced apoptosis by mediating the TNFAIP3 anti-apoptotic activity. It may also play a role in the pro-inflammatory cytokine IL-1 signaling cascade. TAX1BP1 is degraded by caspase-3-like family proteins upon TNF-induced apoptosis. TAX1BP1 contains two C2H2-type zinc binding domains; this model corresponds to the second one.
Pssm-ID: 412016 Cd Length: 27 Bit Score: 60.26 E-value: 7.39e-12
10 20
....*....|....*....|....*..
gi 528503643 789 KICPMCSEQFPLDCDQQLFEKHVLTHF 815
Cdd:cd21970 1 KVCPMCSEQFPPDCDQQVFERHVQTHF 27
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
221-464 |
2.35e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.65 E-value: 2.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 221 EEREEVKRRMEESTARLLQLeEDLIGvtqkglqketELDclkDRVKKLNLEKEALE--GQLKNEKDEKELYKIHLKNREL 298
Cdd:COG1196 172 ERKEEAERKLEATEENLERL-EDILG----------ELE---RQLEPLERQAEKAEryRELKEELKELEAELLLLKLREL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 299 EntklsAELQMLKSVDVNKENTIAQLKDELARVKSCLAEKEKQHRQLlansspSGESKALREQLRQKEEQLQATQQQANM 378
Cdd:COG1196 238 E-----AELEELEAELEELEAELEELEAELAELEAELEELRLELEEL------ELELEEAQAEEYELLAELARLEQDIAR 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 379 LKAELRDSSNARDRSMAELYRIRVEAETLKKGQADARAECSRLEQQLEEMKSSTQQEACKESDVL-AVAELQREVEDLRL 457
Cdd:COG1196 307 LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEaELAEAEEELEELAE 386
|
....*..
gi 528503643 458 RLQMAAE 464
Cdd:COG1196 387 ELLEALR 393
|
|
| Zn-C2H2_12 |
pfam18112 |
Autophagy receptor zinc finger-C2H2 domain; This domain is found in calcium-binding and ... |
762-788 |
3.56e-11 |
|
Autophagy receptor zinc finger-C2H2 domain; This domain is found in calcium-binding and coiled-coil domain 2/NDP25 (CALCOCO2/NDP25) found in Homo sapiens. CALCOCO2/NDP25 is an ubiquitin-binding autophagy receptor involved in the selective autophagic degradation of invading pathogens. This domain is a typical C2H2-type zinc finger which specifically recognizes mono-ubiquitin or poly-ubiquitin chain. The overall ubiquitin-binding mode utilizes the C-terminal alpha-helix to interact with the solvent-exposed surface of the central beta-sheet of ubiquitin, similar to that observed in the RABGEF1/Rabex-5 or POLN/Pol-eta zinc finger.
Pssm-ID: 407946 Cd Length: 27 Bit Score: 58.04 E-value: 3.56e-11
10 20
....*....|....*....|....*..
gi 528503643 762 KRCPLCEVIFPPHYDQSKFEEHVESHW 788
Cdd:pfam18112 1 KECPLCGEMFSPNIDQSEFEEHVESHF 27
|
|
| Zn-C2H2_TAX1BP1_rpt1 |
cd21969 |
first C2H2-type zinc binding domain found in tax1-binding protein 1 (TAX1BP1) and similar ... |
764-787 |
4.33e-11 |
|
first C2H2-type zinc binding domain found in tax1-binding protein 1 (TAX1BP1) and similar proteins; TAX1BP1, also called TRAF6-binding protein (T6BP), is a novel ubiquitin-binding adaptor protein involved in the negative regulation of the NF-kappaB transcription factor, a key player in inflammatory responses, immunity and tumorigenesis. It inhibits TNF-induced apoptosis by mediating the TNFAIP3 anti-apoptotic activity. It may also play a role in the pro-inflammatory cytokine IL-1 signaling cascade. TAX1BP1 is degraded by caspase-3-like family proteins upon TNF-induced apoptosis. TAX1BP1 contains two C2H2-type zinc binding domains; this model corresponds to the first one.
Pssm-ID: 412015 Cd Length: 24 Bit Score: 57.81 E-value: 4.33e-11
10 20
....*....|....*....|....
gi 528503643 764 CPLCEVIFPPHYDQSKFEEHVESH 787
Cdd:cd21969 1 CPLCELVFPPNYDQSKFEQHVESH 24
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
146-401 |
5.13e-11 |
|
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: 65.17 E-value: 5.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 146 ILVVTTKASYLEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEEREE 225
Cdd:COG4942 8 ALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 226 VKRRMEESTARLLQLEEDLIGVTQKgLQKETELDCLkdrvkKLNLEKEALEGQLKNEKDEKELYKiHLKNRELENTKLSA 305
Cdd:COG4942 88 LEKEIAELRAELEAQKEELAELLRA-LYRLGRQPPL-----ALLLSPEDFLDAVRRLQYLKYLAP-ARREQAEELRADLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 306 ELQMLKSVDVNKENTIAQLKDELARVKSCLAEKEKQHRQLLANSspSGESKALREQLRQKEEQLQATQQQANMLKAELRD 385
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARL--EKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
250
....*....|....*.
gi 528503643 386 SSNARDRSMAELYRIR 401
Cdd:COG4942 239 AAERTPAAGFAALKGK 254
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
127-494 |
1.00e-10 |
|
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: 65.76 E-value: 1.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 127 ANSPTEEELLTMEDEGGSDILVVTTKAsyLEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLR 206
Cdd:pfam02463 148 AMMKPERRLEIEEEAAGSRLKRKKKEA--LKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEY 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 207 ---KDVQELQLSAQSLQEEREEVKRRMEESTARLLQLEEDLIGVTQKGLQKETELDCL-KDRVKKLNLEKEALEGQLKNE 282
Cdd:pfam02463 226 llyLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLqEEELKLLAKEEEELKSELLKL 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 283 KDEKELYKIHLKNRELENTKLSAELQMLKSVDVNKENtiaQLKDELARVKSCLAEKEKQHRQLLANSSPSGESKALREQL 362
Cdd:pfam02463 306 ERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEK---ELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 363 RQKEEQLQATQQQANMLKAELRDSsnarDRSMAELYRIRVEAETLKKGQADARAECSRLEQQLEEMKSSTQQEACKESDv 442
Cdd:pfam02463 383 SERLSSAAKLKEEELELKSEEEKE----AQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQE- 457
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 528503643 443 LAVAELQREVEDLRLRLQMAAEHYKDKYKECQKLQKQVVKFNEQQGVKRSPG 494
Cdd:pfam02463 458 LKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGL 509
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
156-490 |
1.28e-10 |
|
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: 65.04 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 156 LEQKMEQIQQEKKEL--LENldllQKERDELIDEKNRLEKEYEQERESSAQLRKDVQelqlSAQSLQEEREEVKRRMEES 233
Cdd:TIGR04523 283 IKELEKQLNQLKSEIsdLNN----QKEQDWNKELKSELKNQEKKLEEIQNQISQNNK----IISQLNEQISQLKKELTNS 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 234 TARLLQLEEDLIGVTQKGLQKETELDCLKDRVKKLNLEKEALEGQLKNEKDEKELYKIHLKNRELENTKLSAELQMLKSV 313
Cdd:TIGR04523 355 ESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKET 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 314 DVNKENTIAQLKDELA----RVKSCLAEKEKQHRQLlanSSPSGESKALREQLRQKEEQLQATQQQANMLKAELRDSSNA 389
Cdd:TIGR04523 435 IIKNNSEIKDLTNQDSvkelIIKNLDNTRESLETQL---KVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEK 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 390 RDRSMAELYRIRVEAETLKKGQADARAECSRLEQQLEEMKSSTQQEACKESdvlaVAELQREVEDLRLRLQMAAEHYKDK 469
Cdd:TIGR04523 512 VKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKE----IDEKNKEIEELKQTQKSLKKKQEEK 587
|
330 340
....*....|....*....|.
gi 528503643 470 YKECQKLQKQVVKFNEQQGVK 490
Cdd:TIGR04523 588 QELIDQKEKEKKDLIKEIEEK 608
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
132-637 |
1.33e-10 |
|
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: 65.38 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 132 EEELLTMEDEGGSDILVVTTKASYLEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQE 211
Cdd:TIGR00618 353 QEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQ 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 212 LQLsaqslQEEREEVKRRMEESTARLLQLEEDLIGVTQKGLQKETELDCLKDRVKKLNLEKEALEGQLKNEKDEKE---- 287
Cdd:TIGR00618 433 QEL-----QQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPcplc 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 288 -------LYKIHLKNRELENTKLSAELQMLKSVDVNKENTIAQLKDELARVKSCLAEKEKQHRQLLANSSPSGESKALRE 360
Cdd:TIGR00618 508 gscihpnPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIP 587
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 361 QLRQKEEQLQATQQQANMLKAELRDSSNARDRSM---AELYRIRVEAETLKKGQADARAECSRLEQQL------EEMKSS 431
Cdd:TIGR00618 588 NLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLqpeQDLQDVRLHLQQCSQELALKLTALHALQLTLtqervrEHALSI 667
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 432 TQQEACK-ESDVLAVAELQREVEDLRLRLQMAAEHYKDKYKECQKLQKQVVKFNEQQGVKRSPGSDAAAGPLSASpeASA 510
Cdd:TIGR00618 668 RVLPKELlASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALN--QSL 745
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 511 PGSPSTSDAVLDAIIHGRLKSSSK---ELDKNDKYRKCKQMLNEERERCSMITDELTKMEVKLREQMKTNESLRM----Q 583
Cdd:TIGR00618 746 KELMHQARTVLKARTEAHFNNNEEvtaALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNlqceT 825
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 528503643 584 LAAEEDRYKSQVAEKGRELKELKDSLFVLTKEKEKLEGQLQKSVNREEEQKDSN 637
Cdd:TIGR00618 826 LVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLN 879
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
186-432 |
2.03e-10 |
|
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: 63.63 E-value: 2.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 186 DEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEEREEVKRRMEESTARLLQLEedligvtqkglqkeTELDCLKDRV 265
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALE--------------QELAALEAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 266 KKLNLEKEALEGQLKNEKDE-KELYKIHLKNRELENTKLsaelqMLKSVDVNKENTIAQLKDELARVKSCLAEKEKQHRQ 344
Cdd:COG4942 86 AELEKEIAELRAELEAQKEElAELLRALYRLGRQPPLAL-----LLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 345 LLANSSpsgesKALREQLRQKEEQLQATQQQANMLKAELRDSSNARDRSMAELYRIRVEAETLKKGQADARAECSRLEQQ 424
Cdd:COG4942 161 ELAALR-----AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
....*...
gi 528503643 425 LEEMKSST 432
Cdd:COG4942 236 AAAAAERT 243
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
133-635 |
2.83e-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: 64.31 E-value: 2.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 133 EELLTMEDEGGSDILVVTTKASYLEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQEL 212
Cdd:TIGR02168 354 ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 213 QLSAqsLQEEREEVKRRMEESTARLLQLEEDLIGVTQKGLQKETELDCLKDRVKKLNLEKEALEGQLKNEKDEKELYKIH 292
Cdd:TIGR02168 434 ELKE--LQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKAL 511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 293 LKNRELEN---------------------TKLSAELQMLKSVDVNKEN-TIAQLKDELARVKSCLAEKEKQHRQLLANSS 350
Cdd:TIGR02168 512 LKNQSGLSgilgvlselisvdegyeaaieAALGGRLQAVVVENLNAAKkAIAFLKQNELGRVTFLPLDSIKGTEIQGNDR 591
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 351 PSGESK----ALREQLRQKEEQLQATQQQ--ANMLKAELRDSSNARDRSMAELYRI-RVEAETLKKG----QADARAECS 419
Cdd:TIGR02168 592 EILKNIegflGVAKDLVKFDPKLRKALSYllGGVLVVDDLDNALELAKKLRPGYRIvTLDGDLVRPGgvitGGSAKTNSS 671
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 420 RLEQQLEEMKSSTQQEACKESdvlaVAELQREVEDLRLRLQMAAEHYKDKYKECQKLQKQVVKFNEQQGVKRSPGSDAAA 499
Cdd:TIGR02168 672 ILERRREIEELEEKIEELEEK----IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEE 747
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 500 GPLSASPEasapgspstsDAVLDAIIHGRLKSSSKELDKNDKYRKCKQMLNEERERCSMITDELTKMEVKLREQMKTNES 579
Cdd:TIGR02168 748 RIAQLSKE----------LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNE 817
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 528503643 580 LRMQLAAEEDRYKSQVAEKGRELKELKDSLFVLTKEKEKLEGQLQKSVNREEEQKD 635
Cdd:TIGR02168 818 EAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELES 873
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
155-435 |
3.41e-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: 63.93 E-value: 3.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 155 YLEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQELQ--LSAQSLQ------EEREEV 226
Cdd:TIGR02169 213 YQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEqlLEELNKKikdlgeEEQLRV 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 227 KRRMEESTARLLQLEEDLIGVTQKGLQKETELDCLKDRVKKLNLEKEALEGQLKNEKDEKELYKIHLKNRELENTKLSAE 306
Cdd:TIGR02169 293 KEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAE 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 307 LQmlksvDVNKENtiAQLKDELARVKSCLAEKEKQHRQLLANSSPSGE-SKALREQLRQKEEQLQATQQQANMLKAELRD 385
Cdd:TIGR02169 373 LE-----EVDKEF--AETRDELKDYREKLEKLKREINELKRELDRLQEeLQRLSEELADLNAAIAGIEAKINELEEEKED 445
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 528503643 386 SSnardrsmAELYRIRVEAETLKKGQADARAECSRLEQ---QLEEMKSSTQQE 435
Cdd:TIGR02169 446 KA-------LEIKKQEWKLEQLAADLSKYEQELYDLKEeydRVEKELSKLQRE 491
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
156-634 |
3.77e-10 |
|
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: 63.91 E-value: 3.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 156 LEQKMEQIQQEKKELLENLDLLQKE--------------RDELIDE------KNRLEKEYEQERESSAQLRKDVQELQLS 215
Cdd:TIGR00606 520 LDQEMEQLNHHTTTRTQMEMLTKDKmdkdeqirkiksrhSDELTSLlgyfpnKKQLEDWLHSKSKEINQTRDRLAKLNKE 599
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 216 AQSLQEEREEVKRRMEESTARLLQLEEDLIGVTQKGlQKETELDCLKDRVKKLNLEKEALEGQlknekdeKELYKIHLKN 295
Cdd:TIGR00606 600 LASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQ-DEESDLERLKEEIEKSSKQRAMLAGA-------TAVYSQFITQ 671
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 296 RELENT----------KLSAELQMLKSvdvNKENTIAQLKDELARVKSCLAEKEKQHRQLLansspsGESKALREQLRQK 365
Cdd:TIGR00606 672 LTDENQsccpvcqrvfQTEAELQEFIS---DLQSKLRLAPDKLKSTESELKKKEKRRDEML------GLAPGRQSIIDLK 742
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 366 EEQLQATQQQANMLKAELRDSSNARDRSMAELYRIRVEAETLKKGQADARAeCSRLEQQLEEMKSSTQQEACKESDV--- 442
Cdd:TIGR00606 743 EKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTI-MERFQMELKDVERKIAQQAAKLQGSdld 821
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 443 LAVAELQREVEDLRLRLQMAAEHYKDKYKECQKLQKQVV----KFNEQQGVKRSPGSDAA-AGPLSASPEASAPGSPSTS 517
Cdd:TIGR00606 822 RTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQhlksKTNELKSEKLQIGTNLQrRQQFEEQLVELSTEVQSLI 901
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 518 DAVLDAiihgRLKSSSKELDKNDKYRKCKQMLNEERERCSMITDELTKMEVKLREQMKTNESLRMQLAAEEDRYKSQvae 597
Cdd:TIGR00606 902 REIKDA----KEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQ--- 974
|
490 500 510
....*....|....*....|....*....|....*..
gi 528503643 598 KGRELKELKDSLFVLTKEKEKLEGQLQKSVNREEEQK 634
Cdd:TIGR00606 975 KETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQK 1011
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
156-645 |
4.58e-10 |
|
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: 63.45 E-value: 4.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 156 LEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDvQELQLSAQSLQEEREEVKRRMEESTA 235
Cdd:TIGR00618 196 AELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQK-REAQEEQLKKQQLLKQLRARIEELRA 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 236 RLLQLEEdligvtqkgLQKETELDClkdRVKKLNLEKEALEgqlKNEKDEKELYKiHLKNRELENTKLSAELQMLksvdV 315
Cdd:TIGR00618 275 QEAVLEE---------TQERINRAR---KAAPLAAHIKAVT---QIEQQAQRIHT-ELQSKMRSRAKLLMKRAAH----V 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 316 NKENTIAQLKDELARVKSCLAEKEKQHRQLLANSSPSGESKALREQLRQKEEQLQATQQQANMLKAELRDSSNARDRSMA 395
Cdd:TIGR00618 335 KQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDT 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 396 ELYRIRVEAETLKKGQADARAECSRLEQQLEEMKSSTQQEackesdVLAVAELQREVEDLRLRLQMAA--EHYKDKYKEC 473
Cdd:TIGR00618 415 RTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCE------KLEKIHLQESAQSLKEREQQLQtkEQIHLQETRK 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 474 QKLQKQVVkfNEQQGVKRspgsDAAAGPLSASPEASAPGSPSTSDAVLDAIIHGRLKssskeldkndkyrkckqmLNEER 553
Cdd:TIGR00618 489 KAVVLARL--LELQEEPC----PLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQ------------------LETSE 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 554 ERCSMITDELTKMEVKLREQMKTNESLRMQLAAEEDRYKSQVAEKGRELKELKDSLFVLTKEKEKLEGQLQksvnREEEQ 633
Cdd:TIGR00618 545 EDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQH----ALLRK 620
|
490
....*....|..
gi 528503643 634 KDSNLDVQSVFL 645
Cdd:TIGR00618 621 LQPEQDLQDVRL 632
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
152-645 |
4.95e-10 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 63.60 E-value: 4.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 152 KASYLEQKMEQIQQEKKELLENLDLLQKERDELID-EKNRLEKEYEQERESSAQLR-------KDVQELQLSAQSL---- 219
Cdd:pfam15921 161 KEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDfEEASGKKIYEHDSMSTMHFRslgsaisKILRELDTEISYLkgri 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 220 ---QEEREEVKRRMEESTARLLQLEEDLIgvTQKGLQKETELDCLKDRVKKLNLEKEALEGQL----KNEKDEKELYKIH 292
Cdd:pfam15921 241 fpvEDQLEALKSESQNKIELLLQQHQDRI--EQLISEHEVEITGLTEKASSARSQANSIQSQLeiiqEQARNQNSMYMRQ 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 293 LKNRELENTKLSAELQMLKSVdvnKENTIAQLKDELARVKSCLAEKEKQHRQLlansspSGESKALREQLRQKEEQLQAT 372
Cdd:pfam15921 319 LSDLESTVSQLRSELREAKRM---YEDKIEELEKQLVLANSELTEARTERDQF------SQESGNLDDQLQKLLADLHKR 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 373 QQQANMLKAElrdssNAR--DRSMAELYRIrveaETLKKGQADARAECSRLEQQLEEMKSSTQQEACKEsdvlaVAELQR 450
Cdd:pfam15921 390 EKELSLEKEQ-----NKRlwDRDTGNSITI----DHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQ-----MAAIQG 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 451 EVEDLRLRLQMAAEHYKDKykecQKLQKQVVKFNEQQGVKRSpgSDAAAGPLSASPEASAPGSPSTSDAVLDaiIHGRLK 530
Cdd:pfam15921 456 KNESLEKVSSLTAQLESTK----EMLRKVVEELTAKKMTLES--SERTVSDLTASLQEKERAIEATNAEITK--LRSRVD 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 531 SSSKELdkndkyrkckQMLNEERERCSMITDELTKMEVKLREQMKTNESLR------MQLAAEEDRYKSQV-AEKGRELK 603
Cdd:pfam15921 528 LKLQEL----------QHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRqqienmTQLVGQHGRTAGAMqVEKAQLEK 597
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 528503643 604 ELKDSLFVLtKEKEKLEGQLQKSVnREEEQKDSNLDVQSVFL 645
Cdd:pfam15921 598 EINDRRLEL-QEFKILKDKKDAKI-RELEARVSDLELEKVKL 637
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
156-363 |
5.92e-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: 63.16 E-value: 5.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 156 LEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEEREEVKRRMEESTA 235
Cdd:TIGR02169 327 LEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKR 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 236 RLLQLEEDLIGVTQKGLQKETELDCLKDRVKKLNLEKEALegQLKNEKDEKELykihlknrelenTKLSAELQMLKSVDV 315
Cdd:TIGR02169 407 ELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDK--ALEIKKQEWKL------------EQLAADLSKYEQELY 472
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 528503643 316 NKENTIAQLKDELARVKSCLAEKEKQHRQLlanSSPSGESKALREQLR 363
Cdd:TIGR02169 473 DLKEEYDRVEKELSKLQRELAEAEAQARAS---EERVRGGRAVEEVLK 517
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
151-377 |
7.66e-10 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 61.77 E-value: 7.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 151 TKASYLEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEEREEVKRRM 230
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 231 EESTARLLQLEEdLIGVTQKG--LQKETELDCLKDRVKKLNLEKEALEGQLKNEKD--EKELYKIHLKNRELENTKLSAE 306
Cdd:COG3883 96 YRSGGSVSYLDV-LLGSESFSdfLDRLSALSKIADADADLLEELKADKAELEAKKAelEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528503643 307 LQMLKsvdvnKENTIAQLKDELARVKSCLAEKEKQHRQLLANSSPSGESKALREQLRQKEEQLQATQQQAN 377
Cdd:COG3883 175 AQQAE-----QEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
156-466 |
8.71e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.09 E-value: 8.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 156 LEQKMEQIQQEKKELLENLDLLQ---KERDELIDEKNRLEKEYEQ--------ERESSAQLRKDVQELQLSAQSLQEERE 224
Cdd:COG4717 130 LYQELEALEAELAELPERLEELEerlEELRELEEELEELEAELAElqeeleelLEQLSLATEEELQDLAEELEELQQRLA 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 225 EVKRRMEESTARLLQLEEDLigvtqKGLQKETELDCLKDRVKKLN----------------------------------- 269
Cdd:COG4717 210 ELEEELEEAQEELEELEEEL-----EQLENELEAAALEERLKEARlllliaaallallglggsllsliltiagvlflvlg 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 270 ---LEKEALEGQLKNEKDEKELYKIHLKNRELENTKLSAELQMLKSVDVNKENTIAQLKDELARVKSCLAEKEKQHRQL- 345
Cdd:COG4717 285 llaLLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELq 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 346 ----------LANSSPSGESKALREQLRQKEEQLQATQQQANmLKAELRDSSNARDRSM---------AELYRIRVEAET 406
Cdd:COG4717 365 leeleqeiaaLLAEAGVEDEEELRAALEQAEEYQELKEELEE-LEEQLEELLGELEELLealdeeeleEELEELEEELEE 443
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 407 LKKGQADARAECSRLEQQLEEMKSSTqqeackesdvlAVAELQREVEDLRLRLQMAAEHY 466
Cdd:COG4717 444 LEEELEELREELAELEAELEQLEEDG-----------ELAELLQELEELKAELRELAEEW 492
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
132-337 |
1.19e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.00 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 132 EEELLTMEDEGGSDILVVTTKASYLEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQE 211
Cdd:TIGR02168 763 IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLED 842
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 212 LQLSAQSLQEEREEVKRRMEESTARLLQLEEDLIGVTQKGLQKETELDCLKDRVKKLNLEKEALEGQLKNEKDE-----K 286
Cdd:TIGR02168 843 LEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRREleelrE 922
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528503643 287 ELYKIHLKNRELENT------KLSAELQMLKSVDVNKENTI----AQLKDELARVKSCLAE 337
Cdd:TIGR02168 923 KLAQLELRLEGLEVRidnlqeRLSEEYSLTLEEAEALENKIeddeEEARRRLKRLENKIKE 983
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
219-480 |
1.75e-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: 61.61 E-value: 1.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 219 LQEEREEVKRRMEESTARLLQLeEDLIGVTQKGLQ-------------------KETELDCLKDRVKKLNLEKEALEGQL 279
Cdd:TIGR02168 170 YKERRKETERKLERTRENLDRL-EDILNELERQLKslerqaekaerykelkaelRELELALLVLRLEELREELEELQEEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 280 K-NEKDEKELykihlkNRELEntKLSAELQMLKSVDVNKENTIAQLKDELARVKSCLAEKEKQhrqllansspsgeskal 358
Cdd:TIGR02168 249 KeAEEELEEL------TAELQ--ELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQ----------------- 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 359 REQLRQKEEQLQATQQQANmlkAELRDSSNARDRSMAELYRIRVEAETLKKGQADARAECSRLEQQLEEMKS-STQQEAC 437
Cdd:TIGR02168 304 KQILRERLANLERQLEELE---AQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESrLEELEEQ 380
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 528503643 438 KESDVLAVAELQREVEDLRLRLQMAAEHYKDKYKECQKLQKQV 480
Cdd:TIGR02168 381 LETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEI 423
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
166-466 |
1.95e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.47 E-value: 1.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 166 EKKELLENLDLLQKERDELidekNRLEKEYEQERESSAQLRkDVQELQLSAQSLQEEREEVKRRMEESTARLLQLEEDLI 245
Cdd:COG4913 219 EEPDTFEAADALVEHFDDL----ERAHEALEDAREQIELLE-PIRELAERYAAARERLAELEYLRAALRLWFAQRRLELL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 246 gvtqkglqkETELDCLKDRVKKLNLEKEALEGQLKNEKDEKelykihlknRELENTKLSAELQmlksvdvnkenTIAQLK 325
Cdd:COG4913 294 ---------EAELEELRAELARLEAELERLEARLDALREEL---------DELEAQIRGNGGD-----------RLEQLE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 326 DELARvksclAEKEKQHRQllansspsGESKALREQLRQ-------KEEQLQATQQQAnmlKAELRDSSNARDRSMAELY 398
Cdd:COG4913 345 REIER-----LERELEERE--------RRRARLEALLAAlglplpaSAEEFAALRAEA---AALLEALEEELEALEEALA 408
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528503643 399 RIRVEAETLKKGQADARAECSRLEQQ-------LEEMKSSTQQEA-CKESDVLAVAELQrEVEDLRLRLQMAAEHY 466
Cdd:COG4913 409 EAEAALRDLRRELRELEAEIASLERRksniparLLALRDALAEALgLDEAELPFVGELI-EVRPEEERWRGAIERV 483
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
168-625 |
2.15e-09 |
|
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: 61.19 E-value: 2.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 168 KELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEEREEVKRRMEESTARLLQLEEDLIgv 247
Cdd:TIGR04523 207 KKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIK-- 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 248 tqkglQKETELDCLKDRVKKLNLEKEA-----LEGQLKNEKDEKELYKIHLKNRELENTKLSAELQMLKSVDVNKENTIA 322
Cdd:TIGR04523 285 -----ELEKQLNQLKSEISDLNNQKEQdwnkeLKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENS 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 323 QLKDElarvkscLAEKEKQHRQLLA-NSSPSGESKALREQLRQKEEQLQATQQQANMLKAELRDSSNARDRSMAELYRIR 401
Cdd:TIGR04523 360 EKQRE-------LEEKQNEIEKLKKeNQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLK 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 402 VEAETLKKGQADARAECSRLEQQLEEMKSSTQQEACKesdvlaVAELQREVEDLRLRLQMAAEHYKDKYKECQKLQKQVV 481
Cdd:TIGR04523 433 ETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQ------LKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKK 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 482 KFNEQQGVKRSPGSDaaagplsaspeasapgSPSTSDAVLDAIIHGRLKSSSKELD--------KNDKYRKCKQMLNEER 553
Cdd:TIGR04523 507 ELEEKVKDLTKKISS----------------LKEKIEKLESEKKEKESKISDLEDElnkddfelKKENLEKEIDEKNKEI 570
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528503643 554 ERCSMITDELTKMEVKLREQMKtneslrmQLAAEEDRYKSQVAEKGRELKELKDSLFVLTKEKEKLEGQLQK 625
Cdd:TIGR04523 571 EELKQTQKSLKKKQEEKQELID-------QKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKN 635
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
156-436 |
4.38e-09 |
|
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: 60.03 E-value: 4.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 156 LEQKMEQIQQEKKELLENLDLLQKerdeLIDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEEREEVKRRMEESTA 235
Cdd:TIGR04523 365 LEEKQNEIEKLKKENQSYKQEIKN----LESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNS 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 236 RLLQLEEdligvtqKGLQKETELDCLKDRVKKLNLEKEALEGQLKNEK------------DEKELYKIHLKNRELENT-- 301
Cdd:TIGR04523 441 EIKDLTN-------QDSVKELIIKNLDNTRESLETQLKVLSRSINKIKqnleqkqkelksKEKELKKLNEEKKELEEKvk 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 302 -------KLSAELQMLKSVDVNKENTIAQLKDEL----ARVKSCLAEKEKQHRQllansspsgesKALrEQLRQKEEQLQ 370
Cdd:TIGR04523 514 dltkkisSLKEKIEKLESEKKEKESKISDLEDELnkddFELKKENLEKEIDEKN-----------KEI-EELKQTQKSLK 581
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528503643 371 ATQQQANMLKAELRDSSNARDRSMAELyriRVEAETLKKGQADARAECSRLEQQ---LEEMKSSTQQEA 436
Cdd:TIGR04523 582 KKQEEKQELIDQKEKEKKDLIKEIEEK---EKKISSLEKELEKAKKENEKLSSIiknIKSKKNKLKQEV 647
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
156-480 |
5.57e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.78 E-value: 5.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 156 LEQKMEQIQQEKKELLENLDLLQK----------------ERDELIDEKNRLEKEYEQEREssaqLRKDVQELQLSAQSL 219
Cdd:COG4717 100 LEEELEELEAELEELREELEKLEKllqllplyqelealeaELAELPERLEELEERLEELRE----LEEELEELEAELAEL 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 220 QEEREEVKRRMEEST-ARLLQLEEDLIGVTQKGLQKETELDCLKDRVKKLNLEKEALEGQLKNEKDEKELYK-------- 290
Cdd:COG4717 176 QEELEELLEQLSLATeEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEarllllia 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 291 ------IHLKNRELENTKLSAELQML--------KSVDVNKENTIAQLKDELARVKSCLA-EKEKQHRQLLANSSPSGES 355
Cdd:COG4717 256 aallalLGLGGSLLSLILTIAGVLFLvlgllallFLLLAREKASLGKEAEELQALPALEElEEEELEELLAALGLPPDLS 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 356 KALREQLRQKEEQLQATQQQANMLKAELRDSSNARDR----------SMAELYRIRVEAETLKkgqaDARAECSRLEQQL 425
Cdd:COG4717 336 PEELLELLDRIEELQELLREAEELEEELQLEELEQEIaallaeagveDEEELRAALEQAEEYQ----ELKEELEELEEQL 411
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 528503643 426 EEMKSSTQQEACKESDvlavAELQREVEDLRLRLQMAAEHYKDKYKECQKLQKQV 480
Cdd:COG4717 412 EELLGELEELLEALDE----EELEEELEELEEELEELEEELEELREELAELEAEL 462
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
126-625 |
5.57e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.15 E-value: 5.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 126 RANSPTEEELLTMEDEGGSDILVVTTKASYLEQKMEQIQQEKKELLENLDLLQKErdeliDEKNRLE--KEYEQERESSA 203
Cdd:PTZ00121 1244 KAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKA-----EEKKKADeaKKKAEEAKKAD 1318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 204 QLRKDVQELQLSAQSLQEEREEVKRRMEESTARLLQLEEDLIGVTQKG----LQKETELDCLKDRVKKLNLEKEALEGQL 279
Cdd:PTZ00121 1319 EAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAeaaeKKKEEAKKKADAAKKKAEEKKKADEAKK 1398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 280 KNEKDEK---ELYKIHLKNRELENTKLSAElQMLKSVDVNKENTIAQLKDEL------------ARVKSCLAEKEKQHRQ 344
Cdd:PTZ00121 1399 KAEEDKKkadELKKAAAAKKKADEAKKKAE-EKKKADEAKKKAEEAKKADEAkkkaeeakkaeeAKKKAEEAKKADEAKK 1477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 345 LLANSSPSGESKALREQLRQKEEQLQaTQQQANMLKAELRDSSNARDRSMAELYRIRVEAETLKKGQADARAECSRLEQQ 424
Cdd:PTZ00121 1478 KAEEAKKADEAKKKAEEAKKKADEAK-KAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEE 1556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 425 L---EEMKSSTQQEACKESDVLAV--AELQREVEDLRLRLQMAAEHYKDKYK-------ECQKLQKQVVKFNEQQGVKRS 492
Cdd:PTZ00121 1557 LkkaEEKKKAEEAKKAEEDKNMALrkAEEAKKAEEARIEEVMKLYEEEKKMKaeeakkaEEAKIKAEELKKAEEEKKKVE 1636
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 493 PGSDAAAGPLSASPEASAPGSPSTSDAVLDAIIHGRLKSSSKELDK--NDKYRKCKQMLNEERERCSMitDELTKM---E 567
Cdd:PTZ00121 1637 QLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKaeEDEKKAAEALKKEAEEAKKA--EELKKKeaeE 1714
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528503643 568 VKLREQMKTNESLRMQLAAEEDRYKSQVAEKGRELK---ELKDSLFVLTKEKEKLEGQLQK 625
Cdd:PTZ00121 1715 KKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKkdeEEKKKIAHLKKEEEKKAEEIRK 1775
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
195-634 |
6.00e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.08 E-value: 6.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 195 YEQERESSAQLRKDVQELQLSAQSLQEEREEVKRRMEESTARLLQLEEDLIgvtqkglQKETELDCLKDRVKKLNLEKEA 274
Cdd:TIGR02169 669 SRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIG-------EIEKEIEQLEQEEEKLKERLEE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 275 LEGQLKNEKDEKElykihlkNRELENTKLSAELQmlksvdvNKENTIAQLKDELARVKSCLAEKEKQHRQllansspsGE 354
Cdd:TIGR02169 742 LEEDLSSLEQEIE-------NVKSELKELEARIE-------ELEEDLHKLEEALNDLEARLSHSRIPEIQ--------AE 799
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 355 SKALREQLRQKEEQLQATQQQanmLKAELRDSSNARDrSMAELYRIRVEAETLKKgqaDARAECSRLEQQLEEMKSStqq 434
Cdd:TIGR02169 800 LSKLEEEVSRIEARLREIEQK---LNRLTLEKEYLEK-EIQELQEQRIDLKEQIK---SIEKEIENLNGKKEELEEE--- 869
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 435 eackesdvlaVAELQREVEDLRLRLQMAAEHYKDKYKECQKLQKQVVKFNEQQGVKRSPGSDAAAGPLSASPEASAPGSP 514
Cdd:TIGR02169 870 ----------LEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDP 939
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 515 STSDavldaiihgrlkssskeldkndkyrkckqmlnEERERCSMITDELTKMEVKLREQMKTNESLRMqLAAEEdryksq 594
Cdd:TIGR02169 940 KGED--------------------------------EEIPEEELSLEDVQAELQRVEEEIRALEPVNM-LAIQE------ 980
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 528503643 595 VAEKGRELKELKDSLFVLTKEKEklegQLQKSVNREEEQK 634
Cdd:TIGR02169 981 YEEVLKRLDELKEKRAKLEEERK----AILERIEEYEKKK 1016
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
156-487 |
6.55e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.93 E-value: 6.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 156 LEQKMEQIQQEKKELLENLDLLQKER--------DELIDEKNRLEKEYEQERESSAQLRKDVQELQL----SAQSLQEER 223
Cdd:COG4913 307 LEAELERLEARLDALREELDELEAQIrgnggdrlEQLEREIERLERELEERERRRARLEALLAALGLplpaSAEEFAALR 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 224 EEVKRRMEESTARLLQLEEDL--IGVTQKGLQKE-----TELDCLKDRVKKLNLE----KEALEGQLKNEKDE----KEL 288
Cdd:COG4913 387 AEAAALLEALEEELEALEEALaeAEAALRDLRRElreleAEIASLERRKSNIPARllalRDALAEALGLDEAElpfvGEL 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 289 YKIHLKNRE-----------------------------LENTKLSAELQMLK--------SVDVNKENTIAQ-------- 323
Cdd:COG4913 467 IEVRPEEERwrgaiervlggfaltllvppehyaaalrwVNRLHLRGRLVYERvrtglpdpERPRLDPDSLAGkldfkphp 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 324 ----LKDELAR---VKSCLAEKE-KQHRQ------LLANSSPSGEsKALREQLRQK-------EEQLQATQQQANMLKAE 382
Cdd:COG4913 547 frawLEAELGRrfdYVCVDSPEElRRHPRaitragQVKGNGTRHE-KDDRRRIRSRyvlgfdnRAKLAALEAELAELEEE 625
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 383 LRDSSNARDRSMAELYRIRVEAETLKKGQ---------ADARAECSRLEQQLEEMKSStqqeackeSDVLAvaELQREVE 453
Cdd:COG4913 626 LAEAEERLEALEAELDALQERREALQRLAeyswdeidvASAEREIAELEAELERLDAS--------SDDLA--ALEEQLE 695
|
410 420 430
....*....|....*....|....*....|....
gi 528503643 454 DLRLRLQMAAEHYKDKYKECQKLQKQVVKFNEQQ 487
Cdd:COG4913 696 ELEAELEELEEELDELKGEIGRLEKELEQAEEEL 729
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
136-384 |
2.02e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 58.10 E-value: 2.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 136 LTMEDEGGSDILVVTTKAS---------------YLEQkmeQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERE 200
Cdd:COG3206 127 LTVEPVKGSNVIEISYTSPdpelaaavanalaeaYLEQ---NLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQ 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 201 SSAQLRKDVQELQLSAQ--SLQEEREEVKRRMEESTARLLQLEEDL--IGVTQKGLQKETELDCLKDRVKKLNLEKEALE 276
Cdd:COG3206 204 KNGLVDLSEEAKLLLQQlsELESQLAEARAELAEAEARLAALRAQLgsGPDALPELLQSPVIQQLRAQLAELEAELAELS 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 277 GQLKNE-------KDEKELYKIHLKNRELEN-TKLSAELQMLKSVDVNKENTIAQLKDELARvkscLAEKEKQHRQLLAn 348
Cdd:COG3206 284 ARYTPNhpdvialRAQIAALRAQLQQEAQRIlASLEAELEALQAREASLQAQLAQLEARLAE----LPELEAELRRLER- 358
|
250 260 270
....*....|....*....|....*....|....*.
gi 528503643 349 sspsgESKALREQLRQKEEQLQATQQQANMLKAELR 384
Cdd:COG3206 359 -----EVEVARELYESLLQRLEEARLAEALTVGNVR 389
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
215-464 |
3.67e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 56.31 E-value: 3.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 215 SAQSLQEEREEVKRRMEESTARLLQLEEDLIGVTQKGLQKETELDCLKDRVKKLNLEKEALEGQLKnekdekelykihlk 294
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA-------------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 295 nrelentKLSAELQMLksvdvnkENTIAQLKDELARVkscLAEKEKQHRQ----LLANSSPSGES-------KALREQLR 363
Cdd:COG4942 87 -------ELEKEIAEL-------RAELEAQKEELAEL---LRALYRLGRQpplaLLLSPEDFLDAvrrlqylKYLAPARR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 364 QKEEQLQATQQQANMLKAELRDSSNARDRSMAELYRIRVEAETLKKGQADARAECSRLEQQLEEMKSSTQQEAckesdvl 443
Cdd:COG4942 150 EQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEA------- 222
|
250 260
....*....|....*....|.
gi 528503643 444 avAELQREVEDLRLRLQMAAE 464
Cdd:COG4942 223 --EELEALIARLEAEAAAAAE 241
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
150-444 |
3.69e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.38 E-value: 3.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 150 TTKASYLEQKMEQIQQEKKELLENLDLLQKERDELiDEKNRLEKEYEQERESSAQLRK-DVQELQLSAqslqEEREEVKR 228
Cdd:PRK03918 458 TAELKRIEKELKEIEEKERKLRKELRELEKVLKKE-SELIKLKELAEQLKELEEKLKKyNLEELEKKA----EEYEKLKE 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 229 RMEESTARLLQLEEDLigvtQKGLQKETELDCLKDRVKKLNLEKEALEGQLKN---------EKDEKELYKIHLKNRELE 299
Cdd:PRK03918 533 KLIKLKGEIKSLKKEL----EKLEELKKKLAELEKKLDELEEELAELLKELEElgfesveelEERLKELEPFYNEYLELK 608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 300 NTK--LSAELQMLKSVdvnkENTIAQLKDELARVKSCLAEKEKQHRQLLANSSP-------------SGESKALREQLRQ 364
Cdd:PRK03918 609 DAEkeLEREEKELKKL----EEELDKAFEELAETEKRLEELRKELEELEKKYSEeeyeelreeylelSRELAGLRAELEE 684
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 365 KEEQLQATQQQANMLKAELrdssnardrsmAELYRIRVEAETLKKgqadARAECSRLEQQLEEMKSSTQQEACKESDVLA 444
Cdd:PRK03918 685 LEKRREEIKKTLEKLKEEL-----------EEREKAKKELEKLEK----ALERVEELREKVKKYKALLKERALSKVGEIA 749
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
158-630 |
3.91e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.08 E-value: 3.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 158 QKMEQIQQEKKELLENLDLLQkerdELIDEKNRLEKEYEQERESSAQLRKDVQEL--QLSAQSLQEEREEVKRRMEESTA 235
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYA----ELQEELEELEEELEELEAELEELREELEKLekLLQLLPLYQELEALEAELAELPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 236 RLLQLEEDLigvtQKGLQKETELDCLKDRVKKLNLEKEALEGQLKNEKDEkelykihlknrELEntKLSAELQMLksvdv 315
Cdd:COG4717 147 RLEELEERL----EELRELEEELEELEAELAELQEELEELLEQLSLATEE-----------ELQ--DLAEELEEL----- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 316 nkENTIAQLKDELARVKSCLAEKEKQHRQLlansspsgESKALREQLRQKEEQLQATQQQANMLKAELRDSSNARDRSMA 395
Cdd:COG4717 205 --QQRLAELEEELEEAQEELEELEEELEQL--------ENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILT 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 396 ELYRIRVEAETLKKGQADARAECSRLEQQLEEMKSSTQQEAckesdvLAVAELQREVEDLRLRLQMAAEHYKDKYKECQK 475
Cdd:COG4717 275 IAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEE------LEEEELEELLAALGLPPDLSPEELLELLDRIEE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 476 LQKQVVKFNEQQgvkrspgSDAAAGPLSASPEASAPGSPSTSDAVLDAIIH---------GRLKSSSKELDK-------- 538
Cdd:COG4717 349 LQELLREAEELE-------EELQLEELEQEIAALLAEAGVEDEEELRAALEqaeeyqelkEELEELEEQLEEllgeleel 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 539 ---------NDKYRKCKQMLNEERERCSMITDELTKMEVKLrEQMKTNESLrMQLAAEEDRYKSQVAEKGRELKELKDSL 609
Cdd:COG4717 422 lealdeeelEEELEELEEELEELEEELEELREELAELEAEL-EQLEEDGEL-AELLQELEELKAELRELAEEWAALKLAL 499
|
490 500
....*....|....*....|.
gi 528503643 610 FVLTKEKEKLEGQLQKSVNRE 630
Cdd:COG4717 500 ELLEEAREEYREERLPPVLER 520
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
151-637 |
4.85e-08 |
|
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: 56.57 E-value: 4.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 151 TKASYLEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEY----EQERESSAQLRKDVQEL---QLSAQSLQEER 223
Cdd:TIGR04523 82 QQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELnkleKQKKENKKNIDKFLTEIkkkEKELEKLNNKY 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 224 EEVKRRMEESTARLLQLEEDLigvtqkgLQKETELDclKDRVKKLNLEKEALEGQLKNEKD---EKELYKIHLKNRELEN 300
Cdd:TIGR04523 162 NDLKKQKEELENELNLLEKEK-------LNIQKNID--KIKNKLLKLELLLSNLKKKIQKNkslESQISELKKQNNQLKD 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 301 T--KLSAELQMLKSVDVNKENTIAQLKDELARVKSCLAEK--------------EKQHRQL------LANSSPSGESKAL 358
Cdd:TIGR04523 233 NieKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKqkeleqnnkkikelEKQLNQLkseisdLNNQKEQDWNKEL 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 359 REQLRQKEEQLQATQQQAnmlkaelrDSSNARDRSMAElyrirvEAETLKKGQADARAECSRLEQQLEEMKSSTQQ-EAC 437
Cdd:TIGR04523 313 KSELKNQEKKLEEIQNQI--------SQNNKIISQLNE------QISQLKKELTNSESENSEKQRELEEKQNEIEKlKKE 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 438 KESDVLAVAELQREVEDLRLRLQMAAEHYKDKYKECQKLQKQVVKFNEQQGVKRSPGSDaaagplsaspEASAPGSPSTS 517
Cdd:TIGR04523 379 NQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIK----------NNSEIKDLTNQ 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 518 DAVLDAIIHgRLKSSSKELDKN-----DKYRKCKQMLN----EERERCSMItDELTKMEVKLREQMKTNESLRMQLAAEE 588
Cdd:TIGR04523 449 DSVKELIIK-NLDNTRESLETQlkvlsRSINKIKQNLEqkqkELKSKEKEL-KKLNEEKKELEEKVKDLTKKISSLKEKI 526
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 528503643 589 DRYKSQVAEKGRELKELKDSL----FVLTkeKEKLEGQLQKSVNREEEQKDSN 637
Cdd:TIGR04523 527 EKLESEKKEKESKISDLEDELnkddFELK--KENLEKEIDEKNKEIEELKQTQ 577
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
179-638 |
6.09e-08 |
|
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: 56.59 E-value: 6.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 179 KERDELIDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEEREEVKRRMEESTARLLQLEEDligvTQKGLQKETEL 258
Cdd:TIGR00606 172 KQKFDEIFSATRYIKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESS----REIVKSYENEL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 259 DCLKDRVKKL--NLEK-EALEGQLKN-EKDEKELYKIHLKNRELENTKLSAELQMLKSVDVNKENTIAQLKDELARVKSC 334
Cdd:TIGR00606 248 DPLKNRLKEIehNLSKiMKLDNEIKAlKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 335 LaEKEKQHRQLLANSSPSGESKALREQLRQKEEQLQATQQQANMLKAELRDSSNARDRSMAELYRIRVEAETLKKGQADA 414
Cdd:TIGR00606 328 L-EKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 415 RAECSRLEQQLEEMKSSTQQEACKESDvlAVAELQREVEDLRLRLQMAAEHYKDKYKECQKLQKQVVKFNEQQGVKRSPG 494
Cdd:TIGR00606 407 AKTAAQLCADLQSKERLKQEQADEIRD--EKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 495 SDAAAGPLSASPEASAPGSPStsdavldaiihgrLKSSSKELDKndkyRKCKqmLNEERERCSMITDELTKMEVKLREQM 574
Cdd:TIGR00606 485 RELSKAEKNSLTETLKKEVKS-------------LQNEKADLDR----KLRK--LDQEMEQLNHHTTTRTQMEMLTKDKM 545
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528503643 575 KTNESLRMQLAAEEDRYKSQVA-------------EKGRELKELKDSLFVLTKEKEKLEgQLQKSVNREEEQKDSNL 638
Cdd:TIGR00606 546 DKDEQIRKIKSRHSDELTSLLGyfpnkkqledwlhSKSKEINQTRDRLAKLNKELASLE-QNKNHINNELESKEEQL 621
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
157-454 |
9.77e-08 |
|
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: 55.95 E-value: 9.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 157 EQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEEREEVKRRMEESTAR 236
Cdd:pfam01576 11 EEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESRLEEEEER 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 237 LLQLEEDLIGVTQKGLQKETELDCLKDRVKKLNLEKEALEGQLK------------NEKDEKElyKIHLKNRELENTKLS 304
Cdd:pfam01576 91 SQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKkleedillledqNSKLSKE--RKLLEERISEFTSNL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 305 AE----LQMLKSVDVNKENTIAQLKDELARVKSCLAEKEKQHRQLLANSSPSGESKA--------LREQLRQKEEQLQAT 372
Cdd:pfam01576 169 AEeeekAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAelqaqiaeLRAQLAKKEEELQAA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 373 QQQANMLKAELRDSSNARDRSMAELYRIRVEAETLKKGQADARAECSRLEQQLEEMKS---------STQQE--ACKESD 441
Cdd:pfam01576 249 LARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTeledtldttAAQQElrSKREQE 328
|
330
....*....|...
gi 528503643 442 vlaVAELQREVED 454
Cdd:pfam01576 329 ---VTELKKALEE 338
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
157-642 |
1.01e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.92 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 157 EQKMEQIQQEKKELLENLDLLQKERDELidEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEEREEVKRRMEESTAR 236
Cdd:PTZ00121 1409 ELKKAAAAKKKADEAKKKAEEKKKADEA--KKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKAD 1486
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 237 LLQLEEDLIGVTQKGLQKETELDCLKDRVKKLNLEKEALEGQLKNEKDEKELYKIHLKNRELENTKLSAELQMLKSVDVN 316
Cdd:PTZ00121 1487 EAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKA 1566
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 317 KENTIAQLKDELARVKSCLAEKEKQHRQLLANSSPSGESKALREQLRQKEEQL----QATQQQANMLKAELRDSSNARDR 392
Cdd:PTZ00121 1567 EEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKikaeELKKAEEEKKKVEQLKKKEAEEK 1646
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 393 SMAELYRIRVEAETLKKGQADARAECSRleQQLEEMKSSTQQEACKESDVLAVAELQREVEDLRLR----------LQMA 462
Cdd:PTZ00121 1647 KKAEELKKAEEENKIKAAEEAKKAEEDK--KKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKeaeekkkaeeLKKA 1724
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 463 AEHYKDKYKECQKLQKQVVKFNEQqgVKRSPGSDAAAGPLSASPEASAPGSPSTSDAVLDAIIHGRLKSSSKELDKNDKY 542
Cdd:PTZ00121 1725 EEENKIKAEEAKKEAEEDKKKAEE--AKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKD 1802
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 543 RKCK-QMLNEERERCSMITDELTKMEV-KLREQMKTNESLRMQLAAEEDRYKSQVAEKGRELKELKDSlfvlTKEKEKLE 620
Cdd:PTZ00121 1803 IFDNfANIIEGGKEGNLVINDSKEMEDsAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADF----NKEKDLKE 1878
|
490 500
....*....|....*....|..
gi 528503643 621 GQLQKSVNREEEQKDSNLDVQS 642
Cdd:PTZ00121 1879 DDEEEIEEADEIEKIDKDDIER 1900
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
156-392 |
1.37e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.31 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 156 LEQKMEQIQqEKKELLENLDLLQKERDELIDEKNRLEK-----EYEQERESSAQLRKDVQELQLSAQSLQEEREEVKRRM 230
Cdd:COG4913 240 AHEALEDAR-EQIELLEPIRELAERYAAARERLAELEYlraalRLWFAQRRLELLEAELEELRAELARLEAELERLEARL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 231 EESTARLLQLEEDLIGvtQKGlqketeldclkDRVKKLNLEKEALEGQLKNEKDEKELYKIHLKNRELENTKLSAELQML 310
Cdd:COG4913 319 DALREELDELEAQIRG--NGG-----------DRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAAL 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 311 KsvdvnkentiAQLKDELARVKSCLAEKEKQHRQLLAnsspsgESKALREQLRQKEEQLQATQQQANMLKAELRDssnAR 390
Cdd:COG4913 386 R----------AEAAALLEALEEELEALEEALAEAEA------ALRDLRRELRELEAEIASLERRKSNIPARLLA---LR 446
|
..
gi 528503643 391 DR 392
Cdd:COG4913 447 DA 448
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
124-487 |
1.52e-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: 55.11 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 124 QFRANSPTEEELLTMED---EGGSDILVVTT-----KASYLEQkMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEY 195
Cdd:pfam05483 353 EFEATTCSLEELLRTEQqrlEKNEDQLKIITmelqkKSSELEE-MTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIA 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 196 EQERESSAQLRKDVQELQLSAQSLQEEREEVKRRMEESTARLLQLEEDLIGVTQKGLQKETELDCLKDRVKKLNLEKEAL 275
Cdd:pfam05483 432 EELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDM 511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 276 EGQLKNEKDekelykihlknrELENTKLSAElQMLKSVDvNKENTIAQLKDELARVKSCLAEKEKQHRQLLANSSPSGES 355
Cdd:pfam05483 512 TLELKKHQE------------DIINCKKQEE-RMLKQIE-NLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARS 577
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 356 kaLREQLRQKEEQLQATQQQANMLKAELRDSSnardRSMAELYRirvEAETL-KKGQADARA-------------ECSRL 421
Cdd:pfam05483 578 --IEYEVLKKEKQMKILENKCNNLKKQIENKN----KNIEELHQ---ENKALkKKGSAENKQlnayeikvnklelELASA 648
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528503643 422 EQQLEEMKSSTQQEAckESDVLAVAELQREVEDLRLRLQMAAEHYKDKYKECQKLQKQVVKFNEQQ 487
Cdd:pfam05483 649 KQKFEEIIDNYQKEI--EDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKH 712
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
179-479 |
1.65e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.07 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 179 KERDELIDE----------KNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEERE------EVKRRMEESTARLL---- 238
Cdd:TIGR02169 153 VERRKIIDEiagvaefdrkKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREkaeryqALLKEKREYEGYELlkek 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 239 -QLEEDLIGVTQKGLQKETELDCLKDRVKKLNLEKEALEGQLKNEKDE-------------KELYKIHLKNRELENTKLS 304
Cdd:TIGR02169 233 eALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKikdlgeeeqlrvkEKIGELEAEIASLERSIAE 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 305 AELQMLKSvdvnkENTIAQLKDELARVKS-------CLAEKEKQHRQLLAN-SSPSGESKALREQLRQKEEQLQATQQQA 376
Cdd:TIGR02169 313 KERELEDA-----EERLAKLEAEIDKLLAeieelerEIEEERKRRDKLTEEyAELKEELEDLRAELEEVDKEFAETRDEL 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 377 NMLKAELRDSSNARDRSMAELYRIRVEAETLKKGQADARAECSRLEQQLEEMKSStqqeacKESDVLAVAELQREVEDLR 456
Cdd:TIGR02169 388 KDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEE------KEDKALEIKKQEWKLEQLA 461
|
330 340
....*....|....*....|...
gi 528503643 457 LRLQMAAEHYKDKYKECQKLQKQ 479
Cdd:TIGR02169 462 ADLSKYEQELYDLKEEYDRVEKE 484
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
127-635 |
1.67e-07 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 55.23 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 127 ANSPTEEELLTMEDEGGSDILVVTTKASYLEQKMEQIQQEKKELLENLDllQKERDELIDEKNRLEKEYEQERESSAQLR 206
Cdd:pfam12128 337 ADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIK--EQNNRDIAGIKDKLAKIREARDRQLAVAE 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 207 KDVQEL------QLSAQ--SLQEEREEVKRRMEESTARL--LQLEEDLigVTQKGlQKETELDCLKDRVKKLNLEKEALE 276
Cdd:pfam12128 415 DDLQALeselreQLEAGklEFNEEEYRLKSRLGELKLRLnqATATPEL--LLQLE-NFDERIERAREEQEAANAEVERLQ 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 277 GQLKNEKDEKELYKIHLKNRELENTKLSAELQMLKSVDVNKENTI--------AQLKDELARVksclAEKEKQHRQLL-- 346
Cdd:pfam12128 492 SELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLlhflrkeaPDWEQSIGKV----ISPELLHRTDLdp 567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 347 --ANSSPSGE----SKALREQLRQKEEQLQATQQ---QANMLKAELRDSSNARDRSMAELYRIRVEAETLKKGQADARA- 416
Cdd:pfam12128 568 evWDGSVGGElnlyGVKLDLKRIDVPEWAASEEElreRLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTa 647
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 417 -ECSRL-------EQQLEEMKSSTQQEACKESDVLAVAELQREVEDLRLRLQMAAEHYKDKYKE--CQKLQKQVVKFNEQ 486
Cdd:pfam12128 648 lKNARLdlrrlfdEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREarTEKQAYWQVVEGAL 727
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 487 qgvkrspgsDAAAGPLSASPEASAPGSPSTSDAvLDAIIHGRLKSSSKELDKNDKYRKCKQMLNEERERCSMITDELTKM 566
Cdd:pfam12128 728 ---------DAQLALLKAAIAARRSGAKAELKA-LETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRY 797
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528503643 567 EVKLREQmktneslrmqLAAEEDRYKSQVAEKGRELKELKDSLFVLTKEKEKLEGQLQKSVNREEEQKD 635
Cdd:pfam12128 798 FDWYQET----------WLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQV 856
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
213-609 |
1.76e-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: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 213 QLSAQSLQEEREEVKRRMEESTARLLQLEEDLIGVtqkglqkETELDCLKDRVKKLNLEKEALEGQLKNEKDEkelykih 292
Cdd:TIGR02168 669 NSSILERRREIEELEEKIEELEEKIAELEKALAEL-------RKELEELEEELEQLRKELEELSRQISALRKD------- 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 293 LKNRELENTKLSAELQMLKSVDVNKENTIAQLKDELARVKSCLAEKEKqhrqllansspsgESKALREQLRQKEEQLQAT 372
Cdd:TIGR02168 735 LARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEA-------------EIEELEAQIEQLKEELKAL 801
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 373 QQQANMLKAELRDSSnardrsmAELYRIRVEAETLKKGQADARAECSRLEQQLEEMKsstqqeackesdvLAVAELQREV 452
Cdd:TIGR02168 802 REALDELRAELTLLN-------EEAANLRERLESLERRIAATERRLEDLEEQIEELS-------------EDIESLAAEI 861
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 453 EDLRLRLQMAAEHYKDKYKECQKLQKQVVKFNEQqgvkrspgsdaaagplsaspeasapgspstsdavLDAIIHGRLKSS 532
Cdd:TIGR02168 862 EELEELIEELESELEALLNERASLEEALALLRSE----------------------------------LEELSEELRELE 907
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528503643 533 SKELDKNDKYRKCKQMLNEERERCSMITDELTKMEVKLREQMKTNESLRMQLAAEEDRYKSQVAEKGRELKELKDSL 609
Cdd:TIGR02168 908 SKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
144-620 |
1.82e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.07 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 144 SDILVVTTKASYLEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEqERESSAQLRKDVQELQLSAQSLQEER 223
Cdd:PRK03918 303 EEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLE-ELEERHELYEEAKAKKEELERLKKRL 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 224 -----EEVKRRMEESTARLLQLEEDLIGVTQKGLQKETELDCLKDRVKKLNLEKEA--LEGQLKNEKDEKEL---YKIHL 293
Cdd:PRK03918 382 tgltpEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpVCGRELTEEHRKELleeYTAEL 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 294 KNRELENTKLSAELQMLKSVDVNKENTIAQLKdELARVKSCLAEKEKQHRQLlansspsgeSKALREQLRQKEEQLQATQ 373
Cdd:PRK03918 462 KRIEKELKEIEEKERKLRKELRELEKVLKKES-ELIKLKELAEQLKELEEKL---------KKYNLEELEKKAEEYEKLK 531
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 374 QQANMLKAELRdssnARDRSMAELYRIRVEAETLKKGQADARAECSRLEQQLEEMKSSTqqeackesdvlaVAELQREVE 453
Cdd:PRK03918 532 EKLIKLKGEIK----SLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFES------------VEELEERLK 595
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 454 DLR------LRLQMAAEHYKDKYKECQKLQKQVVKFNEQQgvkrspgsdaaagplsaspeasapgspstsdavldAIIHG 527
Cdd:PRK03918 596 ELEpfyneyLELKDAEKELEREEKELKKLEEELDKAFEEL-----------------------------------AETEK 640
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 528 RLKSSSKELD-KNDKYRKckqmlnEERERCSMITDELTKMEVKLREQMKTNESLRMQLAAEEDRYKSQVAEKGRELKELK 606
Cdd:PRK03918 641 RLEELRKELEeLEKKYSE------EEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELE 714
|
490
....*....|....
gi 528503643 607 DslfvLTKEKEKLE 620
Cdd:PRK03918 715 K----LEKALERVE 724
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
275-491 |
3.83e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.62 E-value: 3.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 275 LEGQLKNEKDEkeLYKIHLKNRELENTKLSAELQMLKSVDvNKENTIAQLKDELARVKSCLAEKEKQ----------HRQ 344
Cdd:COG4717 47 LLERLEKEADE--LFKPQGRKPELNLKELKELEEELKEAE-EKEEEYAELQEELEELEEELEELEAEleelreelekLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 345 LLANSSPSGESKALREQLRQKEEQLQATQQQanmlkaelrdssnardrsMAELYRIRVEAETLKKGQADARAECSRLEQQ 424
Cdd:COG4717 124 LLQLLPLYQELEALEAELAELPERLEELEER------------------LEELRELEEELEELEAELAELQEELEELLEQ 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528503643 425 LEEMKSSTQQEACKEsdvlaVAELQREVEDLRLRLQMAAEHYKDKYKECQKLQKQVVKFNEQQGVKR 491
Cdd:COG4717 186 LSLATEEELQDLAEE-----LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKE 247
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
133-553 |
4.33e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 53.97 E-value: 4.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 133 EELLTMEDEGgSDILVVTTKASYLEQKMeqiqQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERessAQLRKDVQEL 212
Cdd:pfam15921 531 QELQHLKNEG-DHLRNVQTECEALKLQM----AEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEK---AQLEKEINDR 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 213 QLSAQSLQEEREEVKRRMEESTARLLQLEEDLIGVTQKGLQKETELDCLKDRVKKLNLEKEALEGQLKNEKDEKELYKIH 292
Cdd:pfam15921 603 RLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRN 682
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 293 LKNRELENTKLSAELQM-LKSVDVNKENTIAQLKDELARVKSCLAEKEKQHRQLLANsspSGESKALREQLRQKEEQLQA 371
Cdd:pfam15921 683 FRNKSEEMETTTNKLKMqLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAK---RGQIDALQSKIQFLEEAMTN 759
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 372 TQQQANMLKAELRDSSNARDRSMAELYRIRVEAETLKKGQADARAECSRLEQQLEemKSSTQQEACKesDVLAvaelQRE 451
Cdd:pfam15921 760 ANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALD--KASLQFAECQ--DIIQ----RQE 831
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 452 VEDLRLRLQmaaehykdkykecqklqkQVVKFNEQQGVKRSPGSDAAAGPLSAS----PEASAPGSPSTSDAVLDaiiHG 527
Cdd:pfam15921 832 QESVRLKLQ------------------HTLDVKELQGPGYTSNSSMKPRLLQPAsftrTHSNVPSSQSTASFLSH---HS 890
|
410 420
....*....|....*....|....*.
gi 528503643 528 RLKSSSKEldknDKYRKCKQMLNEER 553
Cdd:pfam15921 891 RKTNALKE----DPTRDLKQLLQELR 912
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
158-429 |
4.43e-07 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 53.30 E-value: 4.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 158 QKMEQIQQEKKELLENLDLLQKERDELI--DEKNRleKEYEQERESSAQLRKDV-----------QELQLSAQSLQEERE 224
Cdd:PRK04778 105 HEINEIESLLDLIEEDIEQILEELQELLesEEKNR--EEVEQLKDLYRELRKSLlanrfsfgpalDELEKQLENLEEEFS 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 225 EVKRRMEE---STAR--LLQLEEDLIGVTQ---------KGLQKE--TELDCLKDRVKKL-----NLEKEALEGQLKNEK 283
Cdd:PRK04778 183 QFVELTESgdyVEAReiLDQLEEELAALEQimeeipellKELQTElpDQLQELKAGYRELveegyHLDHLDIEKEIQDLK 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 284 DE-----KELYKIHLKNRELENTKLSAELQML-----------KSVDVNKENTIA----------QLKDELARVKSC--L 335
Cdd:PRK04778 263 EQidenlALLEELDLDEAEEKNEEIQERIDQLydilerevkarKYVEKNSDTLPDflehakeqnkELKEEIDRVKQSytL 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 336 AEKEKQHRQLLANsspsgESKALREQLRQKEEQLQATQQQANMLKAELRDSSNARDRSMAELYRIRVEAETLKKGQADAR 415
Cdd:PRK04778 343 NESELESVRQLEK-----QLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQEKLSEMLQGLRKDELEAR 417
|
330
....*....|....
gi 528503643 416 AECSRLEQQLEEMK 429
Cdd:PRK04778 418 EKLERYRNKLHEIK 431
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
144-638 |
4.76e-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: 53.82 E-value: 4.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 144 SDILVVTTKASYLEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEER 223
Cdd:pfam02463 293 KEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLE 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 224 EEV------KRRMEESTARLLQLEEDLIGVTQKGLQKETELdcLKDRVKKLNLEKEALEGQLKNEKDEKELYKIHLKNRE 297
Cdd:pfam02463 373 EELlakkklESERLSSAAKLKEEELELKSEEEKEAQLLLEL--ARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEK 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 298 LENTKLSAELQMLKSVDVNKENTIAQLKDELARVKSCLAEKEKQHRQLLANSSPSGESKALREQLRQKEEQLQATQQQAN 377
Cdd:pfam02463 451 EELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGR 530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 378 MLKAELRDSSNARDRSMAelyriRVEAETLKKGQADARAECSRLEQQLEEMKSSTQQE----------ACKESDVLAVAE 447
Cdd:pfam02463 531 LGDLGVAVENYKVAISTA-----VIVEVSATADEVEERQKLVRALTELPLGARKLRLLipklklplksIAVLEIDPILNL 605
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 448 LQREVEDLRLRLQMAAEHYKDKYKECQKLQKQVVKFNEQQGVKRSPGSDAAAGPLSASPEASAPGSPSTSDAVLDAIIHG 527
Cdd:pfam02463 606 AQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKA 685
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 528 RLKSSSKELDKNDKYRKCKQMLNEERERCSMITDELTKMEVKLREQMKTNESLRMQLAAEEDRYKSQVAEKGRELKELKD 607
Cdd:pfam02463 686 ESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEE 765
|
490 500 510
....*....|....*....|....*....|.
gi 528503643 608 SLFVLTKEKEKLEGQLQKSVNREEEQKDSNL 638
Cdd:pfam02463 766 KSELSLKEKELAEEREKTEKLKVEEEKEEKL 796
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
203-372 |
5.58e-07 |
|
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: 51.46 E-value: 5.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 203 AQLRKDVQELQLSAQSLQEEREEVKRRMEESTARLLQLEEDLigvtqkgLQKETELDCLKDRVKKLnlekealEGQLKNE 282
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEI-------KRLELEIEEVEARIKKY-------EEQLGNV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 283 KDEKELYKIhlkNRELENTKL------SAELQMLKSVDvNKENTIAQLKDELARVKSCLAEKEKQHRQLLAnsspsgESK 356
Cdd:COG1579 86 RNNKEYEAL---QKEIESLKRrisdleDEILELMERIE-ELEEELAELEAELAELEAELEEKKAELDEELA------ELE 155
|
170
....*....|....*.
gi 528503643 357 ALREQLRQKEEQLQAT 372
Cdd:COG1579 156 AELEELEAEREELAAK 171
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
131-656 |
6.51e-07 |
|
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: 53.13 E-value: 6.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 131 TEEELLTMEDEGGSDILV---VTTKASYLEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQEREssaQLRK 207
Cdd:TIGR00606 375 TRLELDGFERGPFSERQIknfHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKE---ILEK 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 208 DVQELQLSAQSLQEereevkrrMEESTARLLQLEEDLIGVTQK--GLQKETELDCLKDRVKKLNLEKEALEGQLKNEKDE 285
Cdd:TIGR00606 452 KQEELKFVIKELQQ--------LEGSSDRILELDQELRKAERElsKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQE 523
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 286 KELYKIHLKNRE----LENTKLSAELQM-----------------------LKSVDVNKENTIAQLKDELARVKSCLAEK 338
Cdd:TIGR00606 524 MEQLNHHTTTRTqmemLTKDKMDKDEQIrkiksrhsdeltsllgyfpnkkqLEDWLHSKSKEINQTRDRLAKLNKELASL 603
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 339 EKQHRQLlansspSGESKALREQLRQKEEQL------QATQQQANMLKAELRDSSnaRDRSM----AELYRIRVEAETLK 408
Cdd:TIGR00606 604 EQNKNHI------NNELESKEEQLSSYEDKLfdvcgsQDEESDLERLKEEIEKSS--KQRAMlagaTAVYSQFITQLTDE 675
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 409 KGQA--------DARAECSRLEQQLEEMKSSTQQEacKESDVLAVAELQREVEDLRLRLQMAAEHYKDKYKECQKLQKQV 480
Cdd:TIGR00606 676 NQSCcpvcqrvfQTEAELQEFISDLQSKLRLAPDK--LKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKL 753
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 481 VKFNEQQGVKRSPGSDAAAGPLSASPEASapgspSTSDAVLDAIIHGRLKSSSKELDkndkyRKCKQMLNEERErcsmIT 560
Cdd:TIGR00606 754 QKVNRDIQRLKNDIEEQETLLGTIMPEEE-----SAKVCLTDVTIMERFQMELKDVE-----RKIAQQAAKLQG----SD 819
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 561 DELTKMEVKLREQMKTNESLRMQLAAEEDRYKSQvaEKGRELKELKDSLFVLTKEKEKLEGQLQKSVNREEEQKDSNLDV 640
Cdd:TIGR00606 820 LDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQ--DQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEV 897
|
570
....*....|....*.
gi 528503643 641 QSVFLQYPMPYAQDDP 656
Cdd:TIGR00606 898 QSLIREIKDAKEQDSP 913
|
|
| Zn-C2H2_12 |
pfam18112 |
Autophagy receptor zinc finger-C2H2 domain; This domain is found in calcium-binding and ... |
789-815 |
6.77e-07 |
|
Autophagy receptor zinc finger-C2H2 domain; This domain is found in calcium-binding and coiled-coil domain 2/NDP25 (CALCOCO2/NDP25) found in Homo sapiens. CALCOCO2/NDP25 is an ubiquitin-binding autophagy receptor involved in the selective autophagic degradation of invading pathogens. This domain is a typical C2H2-type zinc finger which specifically recognizes mono-ubiquitin or poly-ubiquitin chain. The overall ubiquitin-binding mode utilizes the C-terminal alpha-helix to interact with the solvent-exposed surface of the central beta-sheet of ubiquitin, similar to that observed in the RABGEF1/Rabex-5 or POLN/Pol-eta zinc finger.
Pssm-ID: 407946 Cd Length: 27 Bit Score: 46.10 E-value: 6.77e-07
10 20
....*....|....*....|....*..
gi 528503643 789 KICPMCSEQFPLDCDQQLFEKHVLTHF 815
Cdd:pfam18112 1 KECPLCGEMFSPNIDQSEFEEHVESHF 27
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
157-454 |
7.79e-07 |
|
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: 52.87 E-value: 7.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 157 EQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLE---KEYEQERESSAQLR----KDVQELQLSAQSLQEEREEVK-- 227
Cdd:pfam01576 741 EEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLEldlKELEAQIDAANKGReeavKQLKKLQAQMKDLQRELEEARas 820
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 228 ------------RRMEESTARLLQLEEDLIGVTQKGLQKETELDCLKDRVKKLNLEKEALE----------GQLKNEKDE 285
Cdd:pfam01576 821 rdeilaqskeseKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQdekrrleariAQLEEELEE 900
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 286 K----ELYKIHLKNRELENTKLSAELQMLKSVDVNKENTIAQLKDELARVKSCLAEKEKQHRQLLANSSPSGESKalreq 361
Cdd:pfam01576 901 EqsntELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVKSKFKSSIAALEAK----- 975
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 362 LRQKEEQLQATQQQANMLKAELRDSSNARDRSMAELYRIRVEAETLKKGQADARAECSRLEQQLEEMKSSTQQEACkesd 441
Cdd:pfam01576 976 IAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASRANA---- 1051
|
330
....*....|...
gi 528503643 442 vlAVAELQREVED 454
Cdd:pfam01576 1052 --ARRKLQRELDD 1062
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
154-486 |
8.09e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.21 E-value: 8.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 154 SYLEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEEREEVKRRMEES 233
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 234 TARLLQLEEDLIGVtqkglqkETELDCLKDRVKKLNLEKEALEGQLKNEKDEKELYKIHLKNRELENTKLSAELQMLKSV 313
Cdd:COG4372 107 QEEAEELQEELEEL-------QKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 314 DVNKEntIAQLKDELARVKSCLAEKEKQHRqlLANSSPSGESKALREQLRQKEEQLQATQQQANMLKAELRDSSNARDRS 393
Cdd:COG4372 180 EAEQA--LDELLKEANRNAEKEEELAEAEK--LIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 394 MAELYRIRVEAETLKKGQADARAECSRLEQQLEEMKSSTQQEACKESDVLAVAELQREVEDLRLRLQMAAEHYKDKYKEC 473
Cdd:COG4372 256 ILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAIL 335
|
330
....*....|...
gi 528503643 474 QKLQKQVVKFNEQ 486
Cdd:COG4372 336 LAELADLLQLLLV 348
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
163-486 |
1.01e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 52.81 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 163 IQQEKKELLENLdlLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEEReevkrrmeestarllqlee 242
Cdd:pfam15921 68 IAYPGKEHIERV--LEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMER------------------- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 243 dligvtqkglqketelDCLKDRVKKLNLEKEALEGQLKNEKDEKELYKIhLKNRELENTklSAELQMLKSVDVNKENTIA 322
Cdd:pfam15921 127 ----------------DAMADIRRRESQSQEDLRNQLQNTVHELEAAKC-LKEDMLEDS--NTQIEQLRKMMLSHEGVLQ 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 323 QLKDELARVKSCLAEKEKQHRQLLA---NSSPSGESKALRE---QLRQKEEQLQATQQQANMLKAELRDS-----SNARD 391
Cdd:pfam15921 188 EIRSILVDFEEASGKKIYEHDSMSTmhfRSLGSAISKILREldtEISYLKGRIFPVEDQLEALKSESQNKielllQQHQD 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 392 RSMAELYRIRVEAETLKKGQADARAECSRLEQQLEEMksstqQEACKESDVL---AVAELQREVEDLRLRLQMAAEHYKD 468
Cdd:pfam15921 268 RIEQLISEHEVEITGLTEKASSARSQANSIQSQLEII-----QEQARNQNSMymrQLSDLESTVSQLRSELREAKRMYED 342
|
330
....*....|....*...
gi 528503643 469 KYKEcqkLQKQVVKFNEQ 486
Cdd:pfam15921 343 KIEE---LEKQLVLANSE 357
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
157-401 |
1.08e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.61 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 157 EQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLekeyeQERESSAQLRKDVQELQLSAQSLQEEREEV---KRRMEES 233
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDAL-----QERREALQRLAEYSWDEIDVASAEREIAELeaeLERLDAS 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 234 TARLLQLEEDLIGVTQKGLQKETELDCLKDRVKKLNLEKEALEGQLKNEKDEKElykihlknrELENTKLSAELQMLksv 313
Cdd:COG4913 684 SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE---------AAEDLARLELRALL--- 751
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 314 dvnkENTIAQLKDElarvksclaEKEKQHRQLLANsspsgESKALREQLRQKEEQLQATQQQAN----MLKAELRDSSNA 389
Cdd:COG4913 752 ----EERFAAALGD---------AVERELRENLEE-----RIDALRARLNRAEEELERAMRAFNrewpAETADLDADLES 813
|
250
....*....|..
gi 528503643 390 RDRSMAELYRIR 401
Cdd:COG4913 814 LPEYLALLDRLE 825
|
|
| Zn-C2H2_CALCOCO1_TAX1BP1_like |
cd21965 |
autophagy receptor zinc finger-C2H2 domain found in calcium-binding and coiled-coil ... |
764-787 |
1.24e-06 |
|
autophagy receptor zinc finger-C2H2 domain found in calcium-binding and coiled-coil domain-containing proteins, TAX1BP1 and similar proteins; The family includes calcium-binding and coiled-coil domain-containing proteins (CALCOCO1 and CALCOCO2), TAX1BP1 and similar proteins. CALCOCO1, also called calphoglin, or coiled-coil coactivator protein, or Sarcoma antigen NY-SAR-3, functions as a coactivator for aryl hydrocarbon and nuclear receptors (NR). CALCOCO2, also called antigen nuclear dot 52 kDa protein, or nuclear domain 10 protein NDP52, or nuclear domain 10 protein 52, or nuclear dot protein 52, is an ubiquitin-binding autophagy receptor involved in the selective autophagic degradation of invading pathogens. TAX1BP1, also called TRAF6-binding protein (T6BP), is a novel ubiquitin-binding adaptor protein involved in the negative regulation of the NF-kappaB transcription factor, a key player in inflammatory responses, immunity and tumorigenesis. The family also includes Drosophila melanogaster Spindle-F (Spn-F) that is the central mediator of IK2 kinase-dependent dendrite pruning in drosophila sensory neurons. This model corresponds to the C2H2-type zinc binding domain found in family members. It is a typical C2H2-type zinc finger which specifically recognizes mono-ubiquitin or poly-ubiquitin chain. The overall ubiquitin-binding mode utilizes the C-terminal alpha-helix to interact with the solvent-exposed surface of the central beta-sheet of ubiquitin, similar to that observed in the RABGEF1/Rabex-5 or POLN/Pol-eta zinc finger.
Pssm-ID: 412012 Cd Length: 24 Bit Score: 45.25 E-value: 1.24e-06
10 20
....*....|....*....|....
gi 528503643 764 CPLCEVIFPPHYDQSKFEEHVESH 787
Cdd:cd21965 1 CPICNKQFPPQVDQEAFEDHVESH 24
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
172-441 |
1.29e-06 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 51.95 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 172 ENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEEreevkrrMEESTARLLQLEEDLIGVT--- 248
Cdd:pfam05701 145 EELESLRKEYASLVSERDIAIKRAEEAVSASKEIEKTVEELTIELIATKES-------LESAHAAHLEAEEHRIGAAlar 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 249 -QKGLQKETELDCLKDRVKKLNlEKEALEGQLKNEKDEKELYKIHLKNrEL----ENT--KLSAELQMLKSVDVNKENTI 321
Cdd:pfam05701 218 eQDKLNWEKELKQAEEELQRLN-QQLLSAKDLKSKLETASALLLDLKA-ELaaymESKlkEEADGEGNEKKTSTSIQAAL 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 322 AQLKDELARVKSCLaEKEKQHRQLLANSSPSgeskaLREQLRQKEEQLQATQQQANMlkaelrdSSNARDRSMAELYRIR 401
Cdd:pfam05701 296 ASAKKELEEVKANI-EKAKDEVNCLRVAAAS-----LRSELEKEKAELASLRQREGM-------ASIAVSSLEAELNRTK 362
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 528503643 402 VEAETLKKGQADARAECSRLEQQLeemksstqQEACKESD 441
Cdd:pfam05701 363 SEIALVQAKEKEAREKMVELPKQL--------QQAAQEAE 394
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
149-465 |
1.39e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.99 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 149 VTTKASYLEQKMEQIQQEKKELLENLDLLQKERDE------LIDEKNRLE--KEYEQERESsaqLRKDVQELQLSAQSLQ 220
Cdd:PRK03918 403 IEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgrELTEEHRKEllEEYTAELKR---IEKELKEIEEKERKLR 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 221 EEREEVK---------RRMEESTARLLQLEEDLIGVTQKGL-QKETELDCLKDRVKKLNLEKEALEGQLKNEKD---EKE 287
Cdd:PRK03918 480 KELRELEkvlkkeselIKLKELAEQLKELEEKLKKYNLEELeKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEElkkKLA 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 288 LYKIHLKNRELENTKLSAELQMLKSVDVNK-ENTIAQLK---DELARVKSCLAEKEKQHRQLlansspsgesKALREQLR 363
Cdd:PRK03918 560 ELEKKLDELEEELAELLKELEELGFESVEElEERLKELEpfyNEYLELKDAEKELEREEKEL----------KKLEEELD 629
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 364 QKEEQLQATQQQANMLKAELRDSSnaRDRSMAELYRIRVEAETLKKGQADARAECSRLEQQLEEMKSS---------TQQ 434
Cdd:PRK03918 630 KAFEELAETEKRLEELRKELEELE--KKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTleklkeeleERE 707
|
330 340 350
....*....|....*....|....*....|...
gi 528503643 435 EACKESDVL--AVAELQREVEDLRLRLQMAAEH 465
Cdd:PRK03918 708 KAKKELEKLekALERVEELREKVKKYKALLKER 740
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
161-487 |
2.02e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 51.66 E-value: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 161 EQIQQEKKELLENlDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDvqelqlSAQSLQEEREEVKRRMEESTARLLQL 240
Cdd:pfam17380 286 ERQQQEKFEKMEQ-ERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQ------AAIYAEQERMAMERERELERIRQEER 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 241 EEDLIGVTQKGLQKETEldclkdrvKKLNLEKEALEGQLKNEKDEKEL-----YKIHLKNRELENTKLSAELQMLKSVDV 315
Cdd:pfam17380 359 KRELERIRQEEIAMEIS--------RMRELERLQMERQQKNERVRQELeaarkVKILEEERQRKIQQQKVEMEQIRAEQE 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 316 N-KENTIAQLKDELARVKSCLAEKEKQHRQLLansspsgeskalrEQLRQKEEQLQatqqqanmlKAELRDSSNARDRSM 394
Cdd:pfam17380 431 EaRQREVRRLEEERAREMERVRLEEQERQQQV-------------ERLRQQEEERK---------RKKLELEKEKRDRKR 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 395 A-ELYRIRVEAETLKKGQADARAECSR--LEQQLEEMKSSTQQEackesdvlavaELQREVEDLRlRLQMAAEhykdkyk 471
Cdd:pfam17380 489 AeEQRRKILEKELEERKQAMIEEERKRklLEKEMEERQKAIYEE-----------ERRREAEEER-RKQQEME------- 549
|
330
....*....|....*.
gi 528503643 472 ECQKLQKQVVKFNEQQ 487
Cdd:pfam17380 550 ERRRIQEQMRKATEER 565
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
254-471 |
2.10e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.45 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 254 KETELDCLKDRVKKLNLEKEALEGQLKNEKDEKELYkihlknrelentklsAELQMLKSVDVNkentIAQLKDELArvks 333
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQERREAL---------------QRLAEYSWDEID----VASAEREIA---- 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 334 claEKEKQHRQLLANSSpsgESKALREQLRQKEEQLQATQQQANMLKAELRDSSNARDRSMAELYRIRVEAETLKKGQAD 413
Cdd:COG4913 672 ---ELEAELERLDASSD---DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL 745
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 528503643 414 ARAEcsRLEQQLEEMKSSTQQEACKESDVLAVAELQREVEDLRLRLQMAAEHYKDKYK 471
Cdd:COG4913 746 ELRA--LLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWP 801
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
131-429 |
2.22e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 51.44 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 131 TEEELLTMEDEGGSDILVVTTKASYLEQKMEQIQQEKKELLENLDLLQKER------DELIDEK-NRLEKEYEQERessA 203
Cdd:PRK01156 403 DPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSvcpvcgTTLGEEKsNHIINHYNEKK---S 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 204 QLRKDVQELQLSAQSLQEEREEVKRRMEESTARLLqleEDLIGVTQKGLQKETELDCLKDRVKKLNlekealEGQLKNEK 283
Cdd:PRK01156 480 RLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEI---NKSINEYNKIESARADLEDIKIKINELK------DKHDKYEE 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 284 DEKELYKIHLKNRELENTKLSAELQMLKSVDVN-----KENTIAQLKDELARVK--------------SCLAEKEKQHRQ 344
Cdd:PRK01156 551 IKNRYKSLKLEDLDSKRTSWLNALAVISLIDIEtnrsrSNEIKKQLNDLESRLQeieigfpddksyidKSIREIENEANN 630
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 345 LLANSSPSGESKALREQLRQK--------------EEQLQATQQQANMLKAELRDSSNARDRSMAELYRIRVEAETLKKG 410
Cdd:PRK01156 631 LNNKYNEIQENKILIEKLRGKidnykkqiaeidsiIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTR 710
|
330
....*....|....*....
gi 528503643 411 QADARAECSRLEQQLEEMK 429
Cdd:PRK01156 711 INELSDRINDINETLESMK 729
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
156-430 |
2.49e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 50.29 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 156 LEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEEREEVKRRMEESTA 235
Cdd:COG1340 13 LEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELRE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 236 RLLQLEEDLigvtQKGLQKETELDCLKDRVKKlnLEKEALEGQLKNEKdEKELY-KIHLKNRELENTKLSAElqmLKSVD 314
Cdd:COG1340 93 ELDELRKEL----AELNKAGGSIDKLRKEIER--LEWRQQTEVLSPEE-EKELVeKIKELEKELEKAKKALE---KNEKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 315 VNKENTIAQLKDELARVK---SCLAEKEKQHRQLLANSspSGESKALREQLRQKEEQLQATQQQANMLKAELRDSSNARD 391
Cdd:COG1340 163 KELRAELKELRKEAEEIHkkiKELAEEAQELHEEMIEL--YKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELR 240
|
250 260 270
....*....|....*....|....*....|....*....
gi 528503643 392 RSMAELYRIRVEAETLKKGQADARAEcSRLEQQLEEMKS 430
Cdd:COG1340 241 ELRKELKKLRKKQRALKREKEKEELE-EKAEEIFEKLKK 278
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
157-460 |
2.83e-06 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 50.89 E-value: 2.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 157 EQKMEQIQQEKKELLENLDLLQKErdelIDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSlQEEREEVKRRMEESTAR 236
Cdd:pfam05557 124 ELELQSTNSELEELQERLDLLKAK----ASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQS-QEQDSEIVKNSKSELAR 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 237 LLQLEEDLigvtQKGLQKETELDCLKDRVKKLNLEKEALEGQLknEKDEKelYKIHLKNRELENTKLSAELQMLKSVDVN 316
Cdd:pfam05557 199 IPELEKEL----ERLREHNKHLNENIENKLLLKEEVEDLKRKL--EREEK--YREEAATLELEKEKLEQELQSWVKLAQD 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 317 KENTIAQLKDELARVKScLAEKEKQHRQllANSSPSGESKALREQLRQKEEQLQATQQQANMLKAELRDSSNARDR---- 392
Cdd:pfam05557 271 TGLNLRSPEDLSRRIEQ-LQQREIVLKE--ENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRlqrr 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 393 ---------------------------SMAELYRIRVEAETLKKGQADARAECSRLEQQLE--------------EMKSS 431
Cdd:pfam05557 348 vllltkerdgyrailesydkeltmsnySPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEelggykqqaqtlerELQAL 427
|
330 340 350
....*....|....*....|....*....|.
gi 528503643 432 TQQEACKESDVLA--VAELQREVEDLRLRLQ 460
Cdd:pfam05557 428 RQQESLADPSYSKeeVDSLRRKLETLELERQ 458
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
318-464 |
5.50e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.02 E-value: 5.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 318 ENTIAQLKDELARVKSCLAEKEKQHRQLLANS---SPSGESKALREQLRQKEEQLQATQQQANMLKAELRDSSNARDRSM 394
Cdd:COG3206 174 RKALEFLEEQLPELRKELEEAEAALEEFRQKNglvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGP 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 395 AELYRIRVEAE--TLKKGQADARAECS--------------RLEQQLEEMKSSTQQEACK-----ESDVLA----VAELQ 449
Cdd:COG3206 254 DALPELLQSPViqQLRAQLAELEAELAelsarytpnhpdviALRAQIAALRAQLQQEAQRilaslEAELEAlqarEASLQ 333
|
170
....*....|....*
gi 528503643 450 REVEDLRLRLQMAAE 464
Cdd:COG3206 334 AQLAQLEARLAELPE 348
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
180-632 |
5.85e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.06 E-value: 5.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 180 ERDELIDEKNRLEKeYEQERESSAQLRKDVQELQLSAQSLQEEREEVKRRMEESTARLLQLEEDLIGVTQKGLQKETELD 259
Cdd:PRK03918 146 SREKVVRQILGLDD-YENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 260 CLKDRVKKLNLEKEALEG-QLKNEKDEKELYKIHLKNRELEntklsaelQMLKSvdvnKENTIAQLKDELARVKScLAEK 338
Cdd:PRK03918 225 KLEKEVKELEELKEEIEElEKELESLEGSKRKLEEKIRELE--------ERIEE----LKKEIEELEEKVKELKE-LKEK 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 339 EKQHRQLlansspSGESKALREQLRQKEEQLQATQQQANMLKAELRDSSNARDR------SMAELYRIRVEAETLKKGQA 412
Cdd:PRK03918 292 AEEYIKL------SEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERleelkkKLKELEKRLEELEERHELYE 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 413 DARAECSRLEQQLEEMKSSTQQEACKESDVLAVA--ELQREVEDLRLRLQMAAEHYKDKYKECQKLQKQVVKFNeqqgVK 490
Cdd:PRK03918 366 EAKAKKEELERLKKRLTGLTPEKLEKELEELEKAkeEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCP----VC 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 491 RSPGSDAAAGPLSASPEASAPGSPSTSDAVLDAI--IHGRLKSSSKELDKNDKYRKCKQMLNEERErcsmITDELTKMEV 568
Cdd:PRK03918 442 GRELTEEHRKELLEEYTAELKRIEKELKEIEEKErkLRKELRELEKVLKKESELIKLKELAEQLKE----LEEKLKKYNL 517
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528503643 569 -KLREQMKTNESLRMQLAAEEDRYKSqVAEKGRELKELKDSLFVLTKEKEKLEGQLQKSVNREEE 632
Cdd:PRK03918 518 eELEKKAEEYEKLKEKLIKLKGEIKS-LKKELEKLEELKKKLAELEKKLDELEEELAELLKELEE 581
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
132-638 |
7.61e-06 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 49.75 E-value: 7.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 132 EEELLTMEDEGGSDILVVTTKASYLEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQE 211
Cdd:pfam07111 150 QEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEAELLRKQLSKTQEELEAQVTLVESLRKYVGE 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 212 LQLS---AQSLQEEREEVKRRMEestarllQLEEDligvtQKGLQKETELdcLKDRVKKLN----LEKEALEGQLK-NEK 283
Cdd:pfam07111 230 QVPPevhSQTWELERQELLDTMQ-------HLQED-----RADLQATVEL--LQVRVQSLThmlaLQEEELTRKIQpSDS 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 284 DEKELYKihlKNRELENT---KLSAELQMLKSVDVNKENTIAQLKDELARVKSCLaekekqhrqllanSSPSGESKALRE 360
Cdd:pfam07111 296 LEPEFPK---KCRSLLNRwreKVFALMVQLKAQDLEHRDSVKQLRGQVAELQEQV-------------TSQSQEQAILQR 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 361 QLRQKEEQLQATQQQANMLKAELRDSSNARDR------SMAELYRIRVEAetLKKGQADARAECSRLEQQLEEMKSSTQQ 434
Cdd:pfam07111 360 ALQDKAAEVEVERMSAKGLQMELSRAQEARRRqqqqtaSAEEQLKFVVNA--MSSTQIWLETTMTRVEQAVARIPSLSNR 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 435 EACKESDV----------LAVAELQRE-----------VEDLRLRLQMAAEHYKDKYKECQK----LQKQVVKFNEQQGV 489
Cdd:pfam07111 438 LSYAVRKVhtikglmarkVALAQLRQEscpppppappvDADLSLELEQLREERNRLDAELQLsahlIQQEVGRAREQGEA 517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 490 KRSPGSDAAAGPLSASPEASApgSPSTSDAVLDAIIHGRLKSSskeldknDKYRKCKQMLNEERE-RCSMITDELTKMEV 568
Cdd:pfam07111 518 ERQQLSEVAQQLEQELQRAQE--SLASVGQQLEVARQGQQEST-------EEAASLRQELTQQQEiYGQALQEKVAEVET 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 569 KLREQM-----KTNESLRMQLAA-----EEDRYKSQVAEKGRELKELKDslfvltkEKEKLEGQ-LQKSVnrEEEQKDSN 637
Cdd:pfam07111 589 RLREQLsdtkrRLNEARREQAKAvvslrQIQHRATQEKERNQELRRLQD-------EARKEEGQrLARRV--QELERDKN 659
|
.
gi 528503643 638 L 638
Cdd:pfam07111 660 L 660
|
|
| Zn-C2H2_CALCOCO1_TAX1BP1_like |
cd21965 |
autophagy receptor zinc finger-C2H2 domain found in calcium-binding and coiled-coil ... |
791-814 |
8.88e-06 |
|
autophagy receptor zinc finger-C2H2 domain found in calcium-binding and coiled-coil domain-containing proteins, TAX1BP1 and similar proteins; The family includes calcium-binding and coiled-coil domain-containing proteins (CALCOCO1 and CALCOCO2), TAX1BP1 and similar proteins. CALCOCO1, also called calphoglin, or coiled-coil coactivator protein, or Sarcoma antigen NY-SAR-3, functions as a coactivator for aryl hydrocarbon and nuclear receptors (NR). CALCOCO2, also called antigen nuclear dot 52 kDa protein, or nuclear domain 10 protein NDP52, or nuclear domain 10 protein 52, or nuclear dot protein 52, is an ubiquitin-binding autophagy receptor involved in the selective autophagic degradation of invading pathogens. TAX1BP1, also called TRAF6-binding protein (T6BP), is a novel ubiquitin-binding adaptor protein involved in the negative regulation of the NF-kappaB transcription factor, a key player in inflammatory responses, immunity and tumorigenesis. The family also includes Drosophila melanogaster Spindle-F (Spn-F) that is the central mediator of IK2 kinase-dependent dendrite pruning in drosophila sensory neurons. This model corresponds to the C2H2-type zinc binding domain found in family members. It is a typical C2H2-type zinc finger which specifically recognizes mono-ubiquitin or poly-ubiquitin chain. The overall ubiquitin-binding mode utilizes the C-terminal alpha-helix to interact with the solvent-exposed surface of the central beta-sheet of ubiquitin, similar to that observed in the RABGEF1/Rabex-5 or POLN/Pol-eta zinc finger.
Pssm-ID: 412012 Cd Length: 24 Bit Score: 42.94 E-value: 8.88e-06
10 20
....*....|....*....|....
gi 528503643 791 CPMCSEQFPLDCDQQLFEKHVLTH 814
Cdd:cd21965 1 CPICNKQFPPQVDQEAFEDHVESH 24
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
187-451 |
1.04e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.75 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 187 EKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEEREEVKRRMEESTARLLQLEEDLIGVTQKGLQKETELDCLKDRVK 266
Cdd:COG4372 11 ARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 267 KLNLEKEALEGQLKNEKDEKELYKIHLKNRELENTKLSAELQMLKSVDVNKENTIAQLKDELARVKSCLAEKEKQ---HR 343
Cdd:COG4372 91 AAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEElaaLE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 344 QLLANSSPSGESKALREQLRQKEEQLQATQQQANMLKAELRDSSNARDRSMAELYRIRVEAETLKKGQADARAECSRLEQ 423
Cdd:COG4372 171 QELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEE 250
|
250 260
....*....|....*....|....*...
gi 528503643 424 QLEEMKSSTQQEACKESDVLAVAELQRE 451
Cdd:COG4372 251 LLEEVILKEIEELELAILVEKDTEEEEL 278
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
161-428 |
1.32e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.88 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 161 EQIQQEKKELLENLDLLQKERDELIDEKNRLE--KEYEQERESSAQLRKDVQELQLSAQSLQEEREEvkrRMEESTARLL 238
Cdd:PRK02224 471 EEDRERVEELEAELEDLEEEVEEVEERLERAEdlVEAEDRIERLEERREDLEELIAERRETIEEKRE---RAEELRERAA 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 239 QLEEDLIGVTQKGLQKETELDCLKDRVKKLNLEKEALEGQLKNekdekeLYKIHLKNRELENtkLSAELQMLKsvdvNKE 318
Cdd:PRK02224 548 ELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIES------LERIRTLLAAIAD--AEDEIERLR----EKR 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 319 NTIAQLKDELarvKSCLAEKEKQHRQLLANSSPSGESKA-------------LREQLRQKEEQLQATQQQANMLKAELRD 385
Cdd:PRK02224 616 EALAELNDER---RERLAEKRERKRELEAEFDEARIEEAredkeraeeyleqVEEKLDELREERDDLQAEIGAVENELEE 692
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 528503643 386 SSNARDRSMA------ELYRIRVEAETLKKGQADARAE-----CSRLEQQLEEM 428
Cdd:PRK02224 693 LEELRERREAlenrveALEALYDEAEELESMYGDLRAElrqrnVETLERMLNET 746
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
133-459 |
1.33e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 48.81 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 133 EELLTMEDEGGSDILVVTTKASYLEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQEL 212
Cdd:pfam02463 685 AESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEE 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 213 QLSAQSLQEEREEVKRRMEESTARLLQLEEDLIGVTQKGLQKETELDCLKDRVKKLNLEKEALEG-----QLKNEKDEKE 287
Cdd:pfam02463 765 EKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKikeeeLEELALELKE 844
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 288 LYK--IHLKNRELENTKLSAELQMLKSVDVNKENTIAQLKDELARVKSCLAEKEKQHRQLLANSSPSGESKALREQLRQK 365
Cdd:pfam02463 845 EQKleKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIK 924
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 366 EEQLQatQQQANMLKAELRDSSNARDRSMA---ELYRIRVEAETLKKgQADARAECSRLEQQLEEMKSSTQQEACKESDV 442
Cdd:pfam02463 925 EEAEI--LLKYEEEPEELLLEEADEKEKEEnnkEEEEERNKRLLLAK-EELGKVNLMAIEEFEEKEERYNKDELEKERLE 1001
|
330
....*....|....*..
gi 528503643 443 LAVAELQREVEDLRLRL 459
Cdd:pfam02463 1002 EEKKKLIRAIIEETCQR 1018
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
190-634 |
1.46e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 48.66 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 190 RLEKEYEQERESSAQLRKDVQELQLSAQSlqeEREEVKRRmEESTARLLQLeedligVTQKGLQKETELDclKDRVKKLN 269
Cdd:pfam10174 120 RLQSEHERQAKELFLLRKTLEEMELRIET---QKQTLGAR-DESIKKLLEM------LQSKGLPKKSGEE--DWERTRRI 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 270 LEKEALEGQLKNEKDEKELYKIHLK---NRELENTKLSAELQMLKSVDVNKENTIAQLK-------DELARVKSCLA--- 336
Cdd:pfam10174 188 AEAEMQLGHLEVLLDQKEKENIHLReelHRRNQLQPDPAKTKALQTVIEMKDTKISSLErnirdleDEVQMLKTNGLlht 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 337 -EKEKQHRQLLANSSPSGESKALREQLRQ----KEEQLQATQQQANMLKAE----------LRDSSNARDRSMAELyRIR 401
Cdd:pfam10174 268 eDREEEIKQMEVYKSHSKFMKNKIDQLKQelskKESELLALQTKLETLTNQnsdckqhievLKESLTAKEQRAAIL-QTE 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 402 VEAETLKKGQADA-RAECSRLEQQLEEMKSSTQQEACKESDVLAVAElqREVEDLRLRLQMAAEHYKDKYKECQKLQKQV 480
Cdd:pfam10174 347 VDALRLRLEEKESfLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKE--RKINVLQKKIENLQEQLRDKDKQLAGLKERV 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 481 VKFNEQqgvkrSPGSDAAAGPLSaspEASapgspSTSDAVLDAIIHGRLKSSSKELDKNDKYRKCKQMLneeRERCSMIT 560
Cdd:pfam10174 425 KSLQTD-----SSNTDTALTTLE---EAL-----SEKERIIERLKEQREREDRERLEELESLKKENKDL---KEKVSALQ 488
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528503643 561 DELTKMEVKLREQMKTNESLRmqlaaeedrykSQVAEKGRELKELKDSLFVLTKEKEKLEGQLQKSVNREEEQK 634
Cdd:pfam10174 489 PELTEKESSLIDLKEHASSLA-----------SSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVR 551
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
132-390 |
1.99e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 48.20 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 132 EEELLTMEDEGGSDILVVTTKASYLEQKMEQ---IQQEKKELLENLDLLQKERDELIDEKNRLEKEYE-QERESSAQLRK 207
Cdd:pfam17380 338 EQERMAMERERELERIRQEERKRELERIRQEeiaMEISRMRELERLQMERQQKNERVRQELEAARKVKiLEEERQRKIQQ 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 208 DVQELQLSAQSLQEEREEVKRRMEESTARLLQLeedligVTQKGLQKETELDCLKD-----RVKKLNLEKEALEGQLKNE 282
Cdd:pfam17380 418 QKVEMEQIRAEQEEARQREVRRLEEERAREMER------VRLEEQERQQQVERLRQqeeerKRKKLELEKEKRDRKRAEE 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 283 KDEKELYKiHLKNRELENTKLSAELQMLKSVDVNKENTIAQlkDELARVksclAEKEKQHRQLLAnsspsgESKALREQL 362
Cdd:pfam17380 492 QRRKILEK-ELEERKQAMIEEERKRKLLEKEMEERQKAIYE--EERRRE----AEEERRKQQEME------ERRRIQEQM 558
|
250 260 270
....*....|....*....|....*....|.
gi 528503643 363 RQKEEQ---LQATQQQANMLKaELRDSSNAR 390
Cdd:pfam17380 559 RKATEErsrLEAMEREREMMR-QIVESEKAR 588
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
156-434 |
2.13e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.41 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 156 LEQKMEQIQQEKKELLENLDL--LQKERDELIDEKNRLEKEYEQER-------------ESSAQLRKDVQELQLSAQSLQ 220
Cdd:PRK04863 289 LELRRELYTSRRQLAAEQYRLveMARELAELNEAESDLEQDYQAASdhlnlvqtalrqqEKIERYQADLEELEERLEEQN 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 221 EEREEVKRRMEESTARLLQLEEDlIGVTQKGLQK-ETELDCLKDRVKKLNLEKEALEG----------QLKNEKDEKELY 289
Cdd:PRK04863 369 EVVEEADEQQEENEARAEAAEEE-VDELKSQLADyQQALDVQQTRAIQYQQAVQALERakqlcglpdlTADNAEDWLEEF 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 290 KIHLKnrELENTKLSAElQMLKSVDVNKE------NTIAQLKDELAR--VKSCLAEKEKQHR--QLLANSSPsgeskALR 359
Cdd:PRK04863 448 QAKEQ--EATEELLSLE-QKLSVAQAAHSqfeqayQLVRKIAGEVSRseAWDVARELLRRLReqRHLAEQLQ-----QLR 519
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528503643 360 EQLRQKEEQLQAtQQQANMLKAEL--RDSSNARDRSMAELYRIRVEA--ETLKKGQADARAECSRLEQQLEEMKSSTQQ 434
Cdd:PRK04863 520 MRLSELEQRLRQ-QQRAERLLAEFckRLGKNLDDEDELEQLQEELEArlESLSESVSEARERRMALRQQLEQLQARIQR 597
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
230-417 |
2.21e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.46 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 230 MEESTARLLQLEEdligvtqkglqKETELDCLKDRVKKLNLEKEALEGQLKNEKDEKELYKIHLKNRELENTKLSAELQM 309
Cdd:COG1579 2 MPEDLRALLDLQE-----------LDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 310 LksvdvnkENTIAQLKDELARVKS------CLAEKEKQHRQLLANSSpsgESKALREQLRQKEEQLQATQQQANMLKAEL 383
Cdd:COG1579 71 V-------EARIKKYEEQLGNVRNnkeyeaLQKEIESLKRRISDLED---EILELMERIEELEEELAELEAELAELEAEL 140
|
170 180 190
....*....|....*....|....*....|....
gi 528503643 384 RDSSNARDRSMAElyrIRVEAETLKKGQADARAE 417
Cdd:COG1579 141 EEKKAELDEELAE---LEAELEELEAEREELAAK 171
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
356-618 |
2.39e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.45 E-value: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 356 KALREQLRQKEEQLQATQQQANMLKAELRDSSNARDRSMAELYRIRVEAETLKKGQADARAECSRLEQQLEEMKsstqqe 435
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK------ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 436 ackesDVLA--VAELQREVEDLRLRLQMAAEHYKDKYKEcQKLQKQVVKFNEQQGVKrspgsdaaagplsaspeasapgs 513
Cdd:COG4942 104 -----EELAelLRALYRLGRQPPLALLLSPEDFLDAVRR-LQYLKYLAPARREQAEE----------------------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 514 pstsdavldaiihgrLKSSSKELDKNdkyrkcKQMLNEERERCSMITDELTKMEVKLREQMKTNESLRMQLAAEEDRYKS 593
Cdd:COG4942 155 ---------------LRADLAELAAL------RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAA 213
|
250 260
....*....|....*....|....*
gi 528503643 594 QVAEKGRELKELKDSLFVLTKEKEK 618
Cdd:COG4942 214 ELAELQQEAEELEALIARLEAEAAA 238
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
131-410 |
2.45e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.21 E-value: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 131 TEEELLTMEDEGGSDILVVTTKASYLEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQ 210
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 211 ELQLSAQSLQEEREEVKRRMEESTA---------RLLQLEEDLIGVTQKGLQKETEldcLKDRVKKLNLEKEALEGQLKN 281
Cdd:COG1340 82 ELNEKLNELREELDELRKELAELNKaggsidklrKEIERLEWRQQTEVLSPEEEKE---LVEKIKELEKELEKAKKALEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 282 EKDEKELYK----IHLKNRELEN--TKLSAELQMLKsvdvnkeNTIAQLKDELARVKsclAEKEKQHRQLLANSSpsgES 355
Cdd:COG1340 159 NEKLKELRAelkeLRKEAEEIHKkiKELAEEAQELH-------EEMIELYKEADELR---KEADELHKEIVEAQE---KA 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 528503643 356 KALREQLRQKEEQLQATQQQANMLKAELRDSsnARDRSMAELYRIRVEA-ETLKKG 410
Cdd:COG1340 226 DELHEEIIELQKELRELRKELKKLRKKQRAL--KREKEKEELEEKAEEIfEKLKKG 279
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
157-387 |
2.50e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 47.79 E-value: 2.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 157 EQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEEREEVKRRMEESTAR 236
Cdd:pfam05483 530 ERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKN 609
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 237 LLQLEEDLIGVTQKGLQKETELDCLKDRVKKLNLE----KEALEGQLKNEKDEKELYKIHLKN--RELENTKLSAE--LQ 308
Cdd:pfam05483 610 IEELHQENKALKKKGSAENKQLNAYEIKVNKLELElasaKQKFEEIIDNYQKEIEDKKISEEKllEEVEKAKAIADeaVK 689
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 309 MLKSVDVNKENTIAQLKDELARVKSCLAE------------KEKQHRQLLANSSPSGESKALREQLRQKEEQLQATQQQA 376
Cdd:pfam05483 690 LQKEIDKRCQHKIAEMVALMEKHKHQYDKiieerdselglyKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEK 769
|
250
....*....|.
gi 528503643 377 NMLKAELRDSS 387
Cdd:pfam05483 770 EKLKMEAKENT 780
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
151-312 |
2.66e-05 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 46.93 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 151 TKASYLEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQEL-QLSAQSLQEEREEVKRR 229
Cdd:smart00787 130 AKKMWYEWRMKLLEGLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLkQLEDELEDCDPTELDRA 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 230 MEESTARLLQLEEDLigvtQKGLQKETELDCLKDRVKKLNLEKEALEGQLKNEKDEKELYKiHLKNRELEntKLSAELQM 309
Cdd:smart00787 210 KEKLKKLLQEIMIKV----KKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCR-GFTFKEIE--KLKEQLKL 282
|
...
gi 528503643 310 LKS 312
Cdd:smart00787 283 LQS 285
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
131-650 |
2.66e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 48.12 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 131 TEEELLTMEDEGGSDILVVTTKASYLEQKMEQIQQEKKELlenldllQKERDELIDEKNRLEKEYEQERESSAQLRKDVQ 210
Cdd:TIGR00606 299 TDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLL-------NQEKTELLVEQGRLQLQADRHQEHIRARDSLIQ 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 211 ELQLSAQSLQEER------------EEVKRRMEESTARLLQLEEDLigvTQKGLQKETELDCLKDRVKKLNlekealegq 278
Cdd:TIGR00606 372 SLATRLELDGFERgpfserqiknfhTLVIERQEDEAKTAAQLCADL---QSKERLKQEQADEIRDEKKGLG--------- 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 279 lknekdekelykihlKNRELENTKLSAELQMLKSVDVNKENTIAQLKDelarvkscLAEKEKQHRQLLANsSPSGESKAL 358
Cdd:TIGR00606 440 ---------------RTIELKKEILEKKQEELKFVIKELQQLEGSSDR--------ILELDQELRKAERE-LSKAEKNSL 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 359 REQLRQKEEQLQATQqqanmlkAELRDSSNARDRSMAELYRirvEAETLKKGQADARAECSRLEQQLEEMKSSTQQEACK 438
Cdd:TIGR00606 496 TETLKKEVKSLQNEK-------ADLDRKLRKLDQEMEQLNH---HTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSL 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 439 ESDVLAVAELQREVEDLRLRLQMAAEHYKDKYKECQKLQKQVVKFNEQQGVKRSpgsdaaagPLSASPEASAPGSPSTSD 518
Cdd:TIGR00606 566 LGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEE--------QLSSYEDKLFDVCGSQDE 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 519 AVLDAIIHGRLKSSSKEL----DKNDKYRKCKQMLNEERERCSMITDELTKMEVKLREQMKTNESLRMQLAAEEDRYKSQ 594
Cdd:TIGR00606 638 ESDLERLKEEIEKSSKQRamlaGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESE 717
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528503643 595 VAEKGRELKEL-------KDSLFVLTKEKEKLEGQLQKsVNREEEQKDSNLDVQSVFLQYPMP 650
Cdd:TIGR00606 718 LKKKEKRRDEMlglapgrQSIIDLKEKEIPELRNKLQK-VNRDIQRLKNDIEEQETLLGTIMP 779
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
156-287 |
2.67e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.46 E-value: 2.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 156 LEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQEL---------QLSAQSLQEEREEV 226
Cdd:COG1579 15 LDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVearikkyeeQLGNVRNNKEYEAL 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528503643 227 KRRMEESTARLLQLEEDLIGVTQKGLQKETELDCLKDRVKKLNLEKEALEGQLKNEKDEKE 287
Cdd:COG1579 95 QKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELE 155
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
158-393 |
3.10e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 47.77 E-value: 3.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 158 QKMEQIQQEKKELLENLDLLQKErdELIDEKNRLEKEYEQER--ESSAQLRKDVQELQLSAQSLQEEREEVKRRmEESTA 235
Cdd:COG5022 823 QKTIKREKKLRETEEVEFSLKAE--VLIQKFGRSLKAKKRFSllKKETIYLQSAQRVELAERQLQELKIDVKSI-SSLKL 899
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 236 RLLQLEEDLIGVTQKG---LQKETELDCLKD-RVKKLNLEKEALEGQLKNEKDEKELYKIHLKNRELENT--KLSAELQM 309
Cdd:COG5022 900 VNLELESEIIELKKSLssdLIENLEFKTELIaRLKKLLNNIDLEEGPSIEYVKLPELNKLHEVESKLKETseEYEDLLKK 979
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 310 LKS--VDVNKENT-IAQLKDELARV---KSCLAEKEKQHRQ-------LLANSSPSGESKALREQLRQKEEQLQATQQQA 376
Cdd:COG5022 980 STIlvREGNKANSeLKNFKKELAELskqYGALQESTKQLKElpvevaeLQSASKIISSESTELSILKPLQKLKGLLLLEN 1059
|
250
....*....|....*..
gi 528503643 377 NMLKAELRDSSNARDRS 393
Cdd:COG5022 1060 NQLQARYKALKLRRENS 1076
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
156-374 |
3.21e-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: 46.73 E-value: 3.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 156 LEQKMEQIQQEKKELLENLDLLQKERDELIDE----KNRLEKEYEQERESS-----AQLRKDVQELQLSAQSLQEERE-- 224
Cdd:pfam15905 106 VEAKLNAAVREKTSLSASVASLEKQLLELTRVnellKAKFSEDGTQKKMSSlsmelMKLRNKLEAKMKEVMAKQEGMEgk 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 225 --EVKRRMEESTARLLQLEEDLIGV----------TQKGLQKETELDCLKDRVKKLNLEKEALEGQLKNekdekelykih 292
Cdd:pfam15905 186 lqVTQKNLEHSKGKVAQLEEKLVSTekekieekseTEKLLEYITELSCVSEQVEKYKLDIAQLEELLKE----------- 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 293 lKNRELENTKLsaelqmlkSVDVNKENTIAQLKDELARVKSCLAEKEKQHRQLLANSSP-SGESKALREQLRQKEEQLQA 371
Cdd:pfam15905 255 -KNDEIESLKQ--------SLEEKEQELSKQIKDLNEKCKLLESEKEELLREYEEKEQTlNAELEELKEKLTLEEQEHQK 325
|
...
gi 528503643 372 TQQ 374
Cdd:pfam15905 326 LQQ 328
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
131-242 |
3.35e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 47.55 E-value: 3.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 131 TEEELLTMEDEGGSDILVVTTKASYLEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQER-ESSAQLRKD- 208
Cdd:COG2433 386 IEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARsEERREIRKDr 465
|
90 100 110
....*....|....*....|....*....|....*
gi 528503643 209 -VQELQLSAQSLQEEREEVKRRMEESTARLLQLEE 242
Cdd:COG2433 466 eISRLDREIERLERELEEERERIEELKRKLERLKE 500
|
|
| Zn-C2H2_TAX1BP1_rpt1 |
cd21969 |
first C2H2-type zinc binding domain found in tax1-binding protein 1 (TAX1BP1) and similar ... |
791-814 |
3.56e-05 |
|
first C2H2-type zinc binding domain found in tax1-binding protein 1 (TAX1BP1) and similar proteins; TAX1BP1, also called TRAF6-binding protein (T6BP), is a novel ubiquitin-binding adaptor protein involved in the negative regulation of the NF-kappaB transcription factor, a key player in inflammatory responses, immunity and tumorigenesis. It inhibits TNF-induced apoptosis by mediating the TNFAIP3 anti-apoptotic activity. It may also play a role in the pro-inflammatory cytokine IL-1 signaling cascade. TAX1BP1 is degraded by caspase-3-like family proteins upon TNF-induced apoptosis. TAX1BP1 contains two C2H2-type zinc binding domains; this model corresponds to the first one.
Pssm-ID: 412015 Cd Length: 24 Bit Score: 41.25 E-value: 3.56e-05
10 20
....*....|....*....|....
gi 528503643 791 CPMCSEQFPLDCDQQLFEKHVLTH 814
Cdd:cd21969 1 CPLCELVFPPNYDQSKFEQHVESH 24
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
159-632 |
3.83e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 47.41 E-value: 3.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 159 KMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDvqeLQLSAQSLQEEREEVKRRMEESTARll 238
Cdd:pfam05483 269 KANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEED---LQIATKTICQLTEEKEAQMEELNKA-- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 239 QLEEDLIgvtqkglqketeldclkdrVKKLNLEKEALEGQLKNEKDEKELYKIHLKNRELENTKLSAELQMLKSVDVNKE 318
Cdd:pfam05483 344 KAAHSFV-------------------VTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 319 NTIAQLKDELARVKSCLAEKEKQHRqllansspsgeskaLREQLRQKEEQ----LQATQQQANMLKAELRDSSNARDRSM 394
Cdd:pfam05483 405 VELEELKKILAEDEKLLDEKKQFEK--------------IAEELKGKEQEliflLQAREKEIHDLEIQLTAIKTSEEHYL 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 395 AELYRIRVEAETLKKGQADARAECSRLeqqleemksstqqeackesdVLAVAELQREVEDLRLRLQMAAEHYKDKYKECQ 474
Cdd:pfam05483 471 KEVEDLKTELEKEKLKNIELTAHCDKL--------------------LLENKELTQEASDMTLELKKHQEDIINCKKQEE 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 475 KLQKQVVKFNEQQGVKRSP----------GSDAAAGPLSASPE-ASAPGSPSTSDAVLDAIIHGRLKSSSKELDKNDKYR 543
Cdd:pfam05483 531 RMLKQIENLEEKEMNLRDElesvreefiqKGDEVKCKLDKSEEnARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNI 610
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 544 KCKQMLNEE-RERCSMITDELTKMEVKLREqmktnesLRMQLAAEEDRYKSQVAEKGRELKELKDSLFVLTKEKEKLEGQ 622
Cdd:pfam05483 611 EELHQENKAlKKKGSAENKQLNAYEIKVNK-------LELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAI 683
|
490
....*....|
gi 528503643 623 LQKSVNREEE 632
Cdd:pfam05483 684 ADEAVKLQKE 693
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
158-632 |
4.03e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 47.35 E-value: 4.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 158 QKMEQIQQEKKELLENLDLLQKERDELIDEKNRLE------KEYEQERESSAQLRKDVQELQLSAQSLQEEREEVKRRME 231
Cdd:TIGR00606 200 QKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLEssreivKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKK 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 232 ESTARLLQLEEDLIGVTQKGLQKETELDCLKDRVKKlNLEKEALEGQLKNEKDEKELYKIHLKNRELEN----TKLSAEL 307
Cdd:TIGR00606 280 QMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVR-EKERELVDCQRELEKLNKERRLLNQEKTELLVeqgrLQLQADR 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 308 QMLKSVDVNKENTIAQLKDELARV-KSCLAEKEKQHRQLLANSSPSGESKA-------LREQLRQKEEQLQATQQQANML 379
Cdd:TIGR00606 359 HQEHIRARDSLIQSLATRLELDGFeRGPFSERQIKNFHTLVIERQEDEAKTaaqlcadLQSKERLKQEQADEIRDEKKGL 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 380 KAELRDSSNARDRSMAELYRIRVEAETLKKGQADARAECSRLEQQLEEMkSSTQQEACKESDVLAVAELQREVEDLRLRL 459
Cdd:TIGR00606 439 GRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAEREL-SKAEKNSLTETLKKEVKSLQNEKADLDRKL 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 460 QMAAE------HYKDKYKECQKLQKQVVKFNEQQGVKRSPGSDAAAGPLSASPEASAPGSPSTSDAVLDAIIHGRLKSSS 533
Cdd:TIGR00606 518 RKLDQemeqlnHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLN 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 534 KELDK---------NDKYRKCKQMLNEER---ERCSMiTDELTKMEvKLREQMKTNESLRMQLAAEEDRYKSQVAEKGRE 601
Cdd:TIGR00606 598 KELASleqnknhinNELESKEEQLSSYEDklfDVCGS-QDEESDLE-RLKEEIEKSSKQRAMLAGATAVYSQFITQLTDE 675
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 528503643 602 ---------------------LKELKDSLFVLTKEKEKLEGQLQKSVNREEE 632
Cdd:TIGR00606 676 nqsccpvcqrvfqteaelqefISDLQSKLRLAPDKLKSTESELKKKEKRRDE 727
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
356-480 |
4.28e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.32 E-value: 4.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 356 KALREQLRQKEEQLQATQQQANMLkaelrDSSNARDRSMAELYRIRVEAETLKKGQADARAECSRLEQQLEemksSTQQE 435
Cdd:COG3206 185 PELRKELEEAEAALEEFRQKNGLV-----DLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLG----SGPDA 255
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 528503643 436 ACKESDVLAVAELQREVEDLRLRLQMAAEHYKDKYKECQKLQKQV 480
Cdd:COG3206 256 LPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQI 300
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
133-460 |
4.63e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 47.36 E-value: 4.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 133 EELLTMEDEGGSDILVVTTKAsyLEQKMEQIQQEkkeLLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQEL 212
Cdd:PRK10929 86 QQLNNERDEPRSVPPNMSTDA--LEQEILQVSSQ---LLEKSRQAQQEQDRAREISDSLSQLPQQQTEARRQLNEIERRL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 213 Q-LSAQSLQEEREEVKRRMEESTARLLQLEE-DLIGVTQKGLQKETEL--DCLKDRVKKLNLEKEALEGQLKNEKDEKel 288
Cdd:PRK10929 161 QtLGTPNTPLAQAQLTALQAESAALKALVDElELAQLSANNRQELARLrsELAKKRSQQLDAYLQALRNQLNSQRQRE-- 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 289 ykihlKNRELENTKLSAE------LQMLKSVDVNKE-----NTIAQLKDELARVKSCLAEKEKQHRQLLA----NSSPSG 353
Cdd:PRK10929 239 -----AERALESTELLAEqsgdlpKSIVAQFKINRElsqalNQQAQRMDLIASQQRQAASQTLQVRQALNtlreQSQWLG 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 354 ESKALREQLRQKEEQLqatqqqANMLKaelrdsSNARDRSMAELyrirveaetlkkgqadaRAECSRLEQQLEEMKSSTQ 433
Cdd:PRK10929 314 VSNALGEALRAQVARL------PEMPK------PQQLDTEMAQL-----------------RVQRLRYEDLLNKQPQLRQ 364
|
330 340
....*....|....*....|....*..
gi 528503643 434 QeacKESDVLAVAELQREVEDLRLRLQ 460
Cdd:PRK10929 365 I---RQADGQPLTAEQNRILDAQLRTQ 388
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
156-279 |
4.96e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 4.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 156 LEQKMEQIQQEKKELLENLDLLQkerdELIDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEEREEVKRRMEE--- 232
Cdd:COG4913 666 AEREIAELEAELERLDASSDDLA----ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAaed 741
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 528503643 233 --STARLLQLEEDLIGVTQKGLQKETELDcLKDRVKKLNLEKEALEGQL 279
Cdd:COG4913 742 laRLELRALLEERFAAALGDAVERELREN-LEERIDALRARLNRAEEEL 789
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
153-434 |
6.11e-05 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 46.07 E-value: 6.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 153 ASYLEqKMEQIQQEKKEL-LENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEEREEVKRRME 231
Cdd:pfam00038 14 ASYID-KVRFLEQQNKLLeTKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 232 ESTARLLQLEEDLigvtqKGLQKEteldclkdrVKKLNLEKEALEGQLKNEKDEKELYKihlKNRELENTKLSAEL---Q 308
Cdd:pfam00038 93 DELNLRTSAENDL-----VGLRKD---------LDEATLARVDLEAKIESLKEELAFLK---KNHEEEVRELQAQVsdtQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 309 MLKSVDVNKENTIAQLKDELARVKSCLAEK-----EKQHRQLLANSSPSGESKAlrEQLRQKEEQLQATQQQANMLKAEL 383
Cdd:pfam00038 156 VNVEMDAARKLDLTSALAEIRAQYEEIAAKnreeaEEWYQSKLEELQQAAARNG--DALRSAKEEITELRRTIQSLEIEL 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 528503643 384 RDSSNARD---RSMAELyrirveAETLKKGQADARAECSRLEQQLEEMKSSTQQ 434
Cdd:pfam00038 234 QSLKKQKAsleRQLAET------EERYELQLADYQELISELEAELQETRQEMAR 281
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
144-348 |
6.19e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.55 E-value: 6.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 144 SDILVVTTKASYLEQKMEQ----IQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSL 219
Cdd:PHA02562 181 QQIQTLDMKIDHIQQQIKTynknIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 220 QEEREEVKRRMEeSTARLLQL----------------EEDLIG-VTQKGLQKETELDCLKDRVKKLNLEKEALEGQLKNE 282
Cdd:PHA02562 261 NTAAAKIKSKIE-QFQKVIKMyekggvcptctqqiseGPDRITkIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKL 339
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528503643 283 KDEKElyKIHLKNREL-----ENTKLSAELQMLKSVDVNKENTIAQLKDELARVKSCLAE--KEKQHRQLLAN 348
Cdd:PHA02562 340 LELKN--KISTNKQSLitlvdKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSElvKEKYHRGIVTD 410
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
151-463 |
7.18e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 46.71 E-value: 7.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 151 TKASYLEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEE---REEVK 227
Cdd:pfam01576 636 TRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDElqaTEDAK 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 228 RRMEESTARL-LQLEEDLIGVTQKGLQK-----------ETEL-DCLKDRV------KKLNLEKEALEGQLKNE---KDE 285
Cdd:pfam01576 716 LRLEVNMQALkAQFERDLQARDEQGEEKrrqlvkqvrelEAELeDERKQRAqavaakKKLELDLKELEAQIDAAnkgREE 795
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 286 --KELYKIHLK----NRELENTKLSAELQMLKSVDVNK-----ENTIAQLKDELA---RVKScLAEKEKQHRQLLANSSP 351
Cdd:pfam01576 796 avKQLKKLQAQmkdlQRELEEARASRDEILAQSKESEKklknlEAELLQLQEDLAaseRARR-QAQQERDELADEIASGA 874
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 352 SGESKALREQLR------QKEEQLQATQQQANMLKAELRDSSNARDRSMAELYRIRVEAETLKKGQadaraecSRLEQQL 425
Cdd:pfam01576 875 SGKSALQDEKRRleariaQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESAR-------QQLERQN 947
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 528503643 426 EEMKSSTQQE--ACKESDVLAVAELQREVEDLRLRLQMAA 463
Cdd:pfam01576 948 KELKAKLQEMegTVKSKFKSSIAALEAKIAQLEEQLEQES 987
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
357-634 |
7.67e-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: 45.91 E-value: 7.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 357 ALREQLRQKEEQLQATQQQANMLKAELRDSSNARDRSMAELYRIRVEAETLKKGQADARAECSRLEQQLeemksstqqea 436
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL----------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 437 ckesdvlavAELQREVEDLRLRLQMAAEHYKDKYKECQKLQKQvvkfneqqgvkrspgsDAAAGPLSASpeasapgspST 516
Cdd:COG4942 86 ---------AELEKEIAELRAELEAQKEELAELLRALYRLGRQ----------------PPLALLLSPE---------DF 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 517 SDAVLDAIIHGRLKSSSKELDKNdkyrkckqmLNEERERCSMITDELTKMEVKLREQMKTNESLRMQLAAEEDRYKSQVA 596
Cdd:COG4942 132 LDAVRRLQYLKYLAPARREQAEE---------LRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLA 202
|
250 260 270
....*....|....*....|....*....|....*...
gi 528503643 597 EKGRELKELKDSLFVLTKEKEKLEGQLQKSVNREEEQK 634
Cdd:COG4942 203 RLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
161-472 |
7.89e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 46.48 E-value: 7.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 161 EQIQQEKKELLENLDLLQKERDELiDEKNRLEKEYEQERES-SAQLRKdVQE---LQLSAQSLQEEREEVKRRMEESTAR 236
Cdd:COG3096 292 RELFGARRQLAEEQYRLVEMAREL-EELSARESDLEQDYQAaSDHLNL-VQTalrQQEKIERYQEDLEELTERLEEQEEV 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 237 LLQLEEDLIGVTQKGLQKETELDCLK----DRVKKLN-LEKEALEGQ-----LKNEKDEKELYKIHLKNRELENTKLSAE 306
Cdd:COG3096 370 VEEAAEQLAEAEARLEAAEEEVDSLKsqlaDYQQALDvQQTRAIQYQqavqaLEKARALCGLPDLTPENAEDYLAAFRAK 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 307 LQMLKSvdvnkenTIAQLKDELARVKSCLAEKEKQHRQLLANSSPSGESKAL---REQLRQKEEQlQATQQQANMLKAEL 383
Cdd:COG3096 450 EQQATE-------EVLELEQKLSVADAARRQFEKAYELVCKIAGEVERSQAWqtaRELLRRYRSQ-QALAQRLQQLRAQL 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 384 RDSSnardRSMAELYRIRVEAETLKKGQADARAECSRLEQQLEEmksstqQEACKESdvlaVAELQREVEDLRLRLQMAA 463
Cdd:COG3096 522 AELE----QRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAE------LEAQLEE----LEEQAAEAVEQRSELRQQL 587
|
....*....
gi 528503643 464 EHYKDKYKE 472
Cdd:COG3096 588 EQLRARIKE 596
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
215-394 |
9.52e-05 |
|
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: 45.79 E-value: 9.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 215 SAQSLQEEREEVKRRMEESTARllQLEEDLIgvtqkgLQKETELDCLKDRVKKLNLEKEALEGQLKNEKDEKELYKIHLK 294
Cdd:pfam05667 302 HTEKLQFTNEAPAATSSPPTKV--ETEEELQ------QQREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 295 NRELENTKLSAELQ-MLKSVDV--NKENTIAQLK-------------------------DELARVKSCLAEKEKQHRQLL 346
Cdd:pfam05667 374 ELKEQNEELEKQYKvKKKTLDLlpDAEENIAKLQalvdasaqrlvelagqwekhrvpliEEYRALKEAKSNKEDESQRKL 453
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 528503643 347 AnsspsgESKALREQLRQKEEQLQATQQQANMLKAELRDSSNARDRSM 394
Cdd:pfam05667 454 E------EIKELREKIKEVAEEAKQKEELYKQLVAEYERLPKDVSRSA 495
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
156-609 |
1.06e-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: 45.94 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 156 LEQKMEQIQQEKKELLENLDllqkerdELIDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEEREEVKRRMEESTA 235
Cdd:pfam01576 487 LSTRLRQLEDERNSLQEQLE-------EEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQ 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 236 RLLQLEE--DLIGVTQKGLQKETE-----LDCLKDRVKKLNLEKEALEGQLKNEK-------DEKELYKIHLKNRELENT 301
Cdd:pfam01576 560 QLEEKAAayDKLEKTKNRLQQELDdllvdLDHQRQLVSNLEKKQKKFDQMLAEEKaisaryaEERDRAEAEAREKETRAL 639
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 302 KLSAELQMLKSVDVNKENTIAQLKDELARVKSC-------LAEKEKQHRQLLAnsspsgESKALREQLRQKEEQLQATQQ 374
Cdd:pfam01576 640 SLARALEEALEAKEELERTNKQLRAEMEDLVSSkddvgknVHELERSKRALEQ------QVEEMKTQLEELEDELQATED 713
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 375 -----QANM--LKAELRDSSNARDRSMAE--------LYRIRVEAETLKKGQADARAECSRLEQQLEEMKSST------Q 433
Cdd:pfam01576 714 aklrlEVNMqaLKAQFERDLQARDEQGEEkrrqlvkqVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIdaankgR 793
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 434 QEACKESDVLA--VAELQREVEDLRLRLQMAAEHYKDKYKECQKLQKQVVKFNEQqgvkrspgsdaaagpLSASpEASAP 511
Cdd:pfam01576 794 EEAVKQLKKLQaqMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQED---------------LAAS-ERARR 857
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 512 GSPSTSDAVLDAIIHGRLKSSSKELDKNDKYRKCKQM---LNEERERCSMITDeltkmevKLREQMKTNESLRMQLAAEe 588
Cdd:pfam01576 858 QAQQERDELADEIASGASGKSALQDEKRRLEARIAQLeeeLEEEQSNTELLND-------RLRKSTLQVEQLTTELAAE- 929
|
490 500
....*....|....*....|....*.
gi 528503643 589 dRYKSQVAEKGREL-----KELKDSL 609
Cdd:pfam01576 930 -RSTSQKSESARQQlerqnKELKAKL 954
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
157-324 |
1.10e-04 |
|
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: 44.13 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 157 EQKMEQIQQEKKELLENLDLLQKERDELideKNRLEkEYEQERESSAQLRKDVQELQLSAQSLQEEREEVKRRMEEstar 236
Cdd:pfam13851 46 EKLMSEIQQENKRLTEPLQKAQEEVEEL---RKQLE-NYEKDKQSLKNLKARLKVLEKELKDLKWEHEVLEQRFEK---- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 237 lLQLEEDLIgvtqkglqKETELDCLKDRVKKLNLEKEALEGQLKN-----EKDEKELYKIhLKNRELENTKLSAELQMLK 311
Cdd:pfam13851 118 -VERERDEL--------YDKFEAAIQDVQQKTGLKNLLLEKKLQAlgetlEKKEAQLNEV-LAAANLDPDALQAVTEKLE 187
|
170
....*....|...
gi 528503643 312 SVDVNKENTIAQL 324
Cdd:pfam13851 188 DVLESKNQLIKDL 200
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
411-629 |
1.68e-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: 44.75 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 411 QADARAECSRLEQQLEEMKSSTQQEACKESDVL-AVAELQREVEDLRLRLQMAAEHYKDKYKECQKLQKQVVKFNEQQGV 489
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLkQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 490 KRSPGSD--AAAGPLSASPEASAPGSPST-SDAVLDAIIHGRLKSSSKELdkNDKYRKCKQMLNEERERCSMITDELTKM 566
Cdd:COG4942 102 QKEELAEllRALYRLGRQPPLALLLSPEDfLDAVRRLQYLKYLAPARREQ--AEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528503643 567 EVKLREQMKTNESLRMQLAAEEDRYKSQVAEKGRELKELKDSLFVLTKEKEKLEGQLQKSVNR 629
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
150-383 |
1.70e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.89 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 150 TTKASYLEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEEREEVKRR 229
Cdd:COG4372 93 QAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQE 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 230 MEESTARLLQLEEDLIGVTQKGLQKETELdclkDRVKKLNLEKEALEGQLKNEKDEKELYKIHLKNRELENTKLSAELQM 309
Cdd:COG4372 173 LQALSEAEAEQALDELLKEANRNAEKEEE----LAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDK 248
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528503643 310 LKSVDVNKENTIAQLKDELARVKSCLAEKEKQHRQLLANSSPSGESKALREQLRQKEEQLQATQQQANMLKAEL 383
Cdd:COG4372 249 EELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALL 322
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
151-302 |
1.82e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.20 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 151 TKASYLEQKMEQIQQEKKELLENLDLLQKERDELideKNRLEKEYEQE----RESSAQLRKDVQELQLSAQSLQEERE-- 224
Cdd:PRK00409 534 QKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKL---LEEAEKEAQQAikeaKKEADEIIKELRQLQKGGYASVKAHEli 610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 225 EVKRRMEEStarllqLEEdligVTQKGLQKETELDCLK--DRVKKLNLEKealEGQLKNEKDEKEL------YKIHLKNR 296
Cdd:PRK00409 611 EARKRLNKA------NEK----KEKKKKKQKEKQEELKvgDEVKYLSLGQ---KGEVLSIPDDKEAivqagiMKMKVPLS 677
|
....*.
gi 528503643 297 ELENTK 302
Cdd:PRK00409 678 DLEKIQ 683
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
132-339 |
1.98e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.92 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 132 EEELLTMEDEGGSDILvvttkaSYLEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEK--------EYEQERESSA 203
Cdd:PRK05771 73 REEKKKVSVKSLEELI------KDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLEPwgnfdldlSLLLGFKYVS 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 204 QLRKDVQELQLSAQSLQEEREEV-----------------KRRMEESTARLLQLEEDLIGVTQKGLQKEtELDCLKDRVK 266
Cdd:PRK05771 147 VFVGTVPEDKLEELKLESDVENVeyistdkgyvyvvvvvlKELSDEVEEELKKLGFERLELEEEGTPSE-LIREIKEELE 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 267 KLNLEKEALEGQLKNEKDEKELYKIHLKNrELENTKLSAE--LQMLKS---------VDVNKENTIAQLKDELARVKSCL 335
Cdd:PRK05771 226 EIEKERESLLEELKELAKKYLEELLALYE-YLEIELERAEalSKFLKTdktfaiegwVPEDRVKKLKELIDKATGGSAYV 304
|
....
gi 528503643 336 AEKE 339
Cdd:PRK05771 305 EFVE 308
|
|
| IpaC_SipC |
pfam09599 |
Salmonella-Shigella invasin protein C (IpaC_SipC); This entry represents a family of proteins ... |
247-441 |
2.01e-04 |
|
Salmonella-Shigella invasin protein C (IpaC_SipC); This entry represents a family of proteins associated with bacterial type III secretion systems, which are injection machines for virulence factors into host cell cytoplasm. Characterized members of this protein family are known to be secreted and are described as invasins, including IpaC from Shigella flexneri and SipC from Salmonella typhimurium. Members may be referred to as invasins, pathogenicity island effectors, and cell invasion proteins.
Pssm-ID: 286655 [Multi-domain] Cd Length: 334 Bit Score: 44.20 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 247 VTQKGLQKETELDCLKDRVKKLNLEKEALEGQLKN-EKDEKELYKIHLKNRELENTKLSAELQMLKSVDVNKENTIAQlK 325
Cdd:pfam09599 134 IAGSALQVGITGVGAKKQMKGLSTERGALKKNLAKqAKLKQEHAEQKLELNGQNKVKLSADEVSHVKIKRNAGTSVLG-K 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 326 DELARVKSCLAEkekQHRQLLANSSPSGESKALREQLRQKEEQLQATQQQanMLKAELRDSSNArdrsmaelyrirveAE 405
Cdd:pfam09599 213 HEIDHSNERLSD---EHAAVLSSEAESLQHKIDMEQMAMEENLLKAQRKQ--MTGDLIMSGSAI--------------AG 273
|
170 180 190
....*....|....*....|....*....|....*.
gi 528503643 406 TLKKGQADARAECSRLEQQLEEMKSSTQQEACKESD 441
Cdd:pfam09599 274 NIAGASGQYAAALERSEQQISQASSRVASTASSERR 309
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
144-287 |
2.05e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.01 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 144 SDILVVTTKASYLEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQ--ERESSAQLRKDVQELQLSAQSLQE 221
Cdd:TIGR04523 496 KELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKddFELKKENLEKEIDEKNKEIEELKQ 575
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528503643 222 EREEVKRRMEESTARLLQLEEDLIGVTQKGLQKETELDCLKDRVKKLNLEKEALEGQLKNEKDEKE 287
Cdd:TIGR04523 576 TQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKN 641
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
156-244 |
2.16e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 45.07 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 156 LEQKMEQIQQEKKELL--------ENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRK----------DVQELQLSAQ 217
Cdd:COG0542 416 LERRLEQLEIEKEALKkeqdeasfERLAELRDELAELEEELEALKARWEAEKELIEEIQElkeeleqrygKIPELEKELA 495
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 528503643 218 SLQEE--------REEVKR----------------RMEES-TARLLQLEEDL 244
Cdd:COG0542 496 ELEEElaelapllREEVTEediaevvsrwtgipvgKLLEGeREKLLNLEEEL 547
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
162-440 |
2.17e-04 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 44.90 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 162 QIQQEKKELLENLDLLQKE----RDELIDEKNRLEKEYEQERESSAQ----LRKDVQELQLSAQSLQEEREEVKRRMEES 233
Cdd:pfam15964 357 QCEQLKSELERQKERLEKElasqQEKRAQEKEALRKEMKKEREELGAtmlaLSQNVAQLEAQVEKVTREKNSLVSQLEEA 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 234 TARLLQLEEDLIGVTQKglqketeldcLKDRVKKLNLEKEALEGQLKnEKDEKELYKIHLKNRELEntKLSAELQMLKSV 313
Cdd:pfam15964 437 QKQLASQEMDVTKVCGE----------MRYQLNQTKMKKDEAEKEHR-EYRTKTGRQLEIKDQEIE--KLGLELSESKQR 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 314 DVNKENTIAQLKDELARVKSCLAEKEKQ-HRQLLANSSP----SGESKALREQLRQKEEQLQATQQQANMlkaelrdssn 388
Cdd:pfam15964 504 LEQAQQDAARAREECLKLTELLGESEHQlHLTRLEKESIqqsfSNEAKAQALQAQQREQELTQKMQQMEA---------- 573
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 528503643 389 ARDRSMAELYRIRVEAETLkkgQADARAECSRLEQQLEEMKSSTQQEACKES 440
Cdd:pfam15964 574 QHDKTVNEQYSLLTSQNTF---IAKLKEECCTLAKKLEEITQKSRSEVEQLS 622
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
143-242 |
2.24e-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: 44.37 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 143 GSDILVVTTKASYLEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEE 222
Cdd:COG4942 128 PEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKE 207
|
90 100
....*....|....*....|
gi 528503643 223 REEVKRRMEESTARLLQLEE 242
Cdd:COG4942 208 LAELAAELAELQQEAEELEA 227
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
152-398 |
2.55e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 2.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 152 KASYLEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEEREEvKRRME 231
Cdd:PTZ00121 1627 KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEE-AKKAE 1705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 232 EstarLLQLEEDLIGVTQKgLQKETEldclKDRVKKLNLEKEALEGQLKNE---KDEKELYKI-HLKNRE---LENTKLS 304
Cdd:PTZ00121 1706 E----LKKKEAEEKKKAEE-LKKAEE----ENKIKAEEAKKEAEEDKKKAEeakKDEEEKKKIaHLKKEEekkAEEIRKE 1776
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 305 AELQMLKSVDVNKENTIAQLKDELARVKSCLAEKEKQHRQ--LLANSSPSGESKALREQLRQKEEQLQ---ATQQQANML 379
Cdd:PTZ00121 1777 KEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEgnLVINDSKEMEDSAIKEVADSKNMQLEeadAFEKHKFNK 1856
|
250
....*....|....*....
gi 528503643 380 KAELRDSSNARDRSMAELY 398
Cdd:PTZ00121 1857 NNENGEDGNKEADFNKEKD 1875
|
|
| YydB |
COG5293 |
Uncharacterized conserved protein YydD, contains DUF2326 domain [Function unknown]; |
154-233 |
2.71e-04 |
|
Uncharacterized conserved protein YydD, contains DUF2326 domain [Function unknown];
Pssm-ID: 444096 [Multi-domain] Cd Length: 572 Bit Score: 44.55 E-value: 2.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 154 SYLEQKMEQIQQEKKELLENLDLLQKERDEL---IDEKNRLEK------EYEQERESSAQLRKD---VQELQLSAQSLQE 221
Cdd:COG5293 326 EYLEEEIAELEAELEELEAELAELGKERAELlslLDSKGALDKykelqeELAELEAELEELESRlekLQELEDEIRELKE 405
|
90
....*....|..
gi 528503643 222 EREEVKRRMEES 233
Cdd:COG5293 406 ERAELKEEIESD 417
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
154-563 |
3.22e-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: 44.65 E-value: 3.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 154 SYLEQKMEQIQQEKKELLENLDLLQKERDELI-------DEKNRLEKEYEQERESSAQLRKDVQELQ--LSAQSLQEE-- 222
Cdd:TIGR00606 698 SDLQSKLRLAPDKLKSTESELKKKEKRRDEMLglapgrqSIIDLKEKEIPELRNKLQKVNRDIQRLKndIEEQETLLGti 777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 223 --REEVKRRMEESTARLLQLEEDLIGVTQKGLQKETELDC--LKDRVKKLNLEKEALEGQLKNEKDEKELYKIHLKNREL 298
Cdd:TIGR00606 778 mpEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGsdLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQE 857
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 299 ENTKLSAELQMLKSVDVNKENTIA-------QLKDELARVKSCLAEKEKQHRQLLANSSPSGESKALREQL-RQKEEQLQ 370
Cdd:TIGR00606 858 QIQHLKSKTNELKSEKLQIGTNLQrrqqfeeQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELiSSKETSNK 937
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 371 ATQQQANMLKAELRDSSNARDRSMAELY----RIRVEAETLKKGQADARAECS----RLEQQLEEMKSSTQQEACKES-- 440
Cdd:TIGR00606 938 KAQDKVNDIKEKVKNIHGYMKDIENKIQdgkdDYLKQKETELNTVNAQLEECEkhqeKINEDMRLMRQDIDTQKIQERwl 1017
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 441 -DVLAVAELQREVEDLRLRL-----QMAAEHYKDKYKECQKLQKQV--VKFNEQQGVKRSPGSDAAAgpLSASPEASAPG 512
Cdd:TIGR00606 1018 qDNLTLRKRENELKEVEEELkqhlkEMGQMQVLQMKQEHQKLEENIdlIKRNHVLALGRQKGYEKEI--KHFKKELREPQ 1095
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 528503643 513 SPSTSDAVLDAIIHGRL-KSSSKELdknDKYRKC-----KQMLNEERERCSMITDEL 563
Cdd:TIGR00606 1096 FRDAEEKYREMMIVMRTtELVNKDL---DIYYKTldqaiMKFHSMKMEEINKIIRDL 1149
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
157-301 |
3.99e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 43.96 E-value: 3.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 157 EQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDV-QELQLSAQSLQEE---REEVKRRMEE 232
Cdd:pfam17380 445 AREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILeKELEERKQAMIEEerkRKLLEKEMEE 524
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 233 STARLLQLEEDLIGVTQKGLQKET-ELDCLKDRVKKLNLEKEALEGQLKNEKDEKELYKIHLKNRELENT 301
Cdd:pfam17380 525 RQKAIYEEERRREAEEERRKQQEMeERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAEYEAT 594
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
158-557 |
4.15e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.18 E-value: 4.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 158 QKMEQIQQEKKELLENLDLLQKERD---ELIDEKN--------RLEKEYEQERESSAQLRKDVQELQLSAQSLQEEREEV 226
Cdd:PRK04863 233 QDMEAALRENRMTLEAIRVTQSDRDlfkHLITESTnyvaadymRHANERRVHLEEALELRRELYTSRRQLAAEQYRLVEM 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 227 KRRMEESTARllqlEEDLigvtqkglqkETELDCLKDRvkkLNLEKEALEGQLKNEKDEKELYKIHLKNRE-LENTKLSA 305
Cdd:PRK04863 313 ARELAELNEA----ESDL----------EQDYQAASDH---LNLVQTALRQQEKIERYQADLEELEERLEEqNEVVEEAD 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 306 ELQMLKSVDVNK-ENTIAQLKDELARVKSCLAEKEK---QHRQ----------LLANSSPSGES-KALREQLRQKEEQLq 370
Cdd:PRK04863 376 EQQEENEARAEAaEEEVDELKSQLADYQQALDVQQTraiQYQQavqalerakqLCGLPDLTADNaEDWLEEFQAKEQEA- 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 371 atQQQANMLKAELRDSSNARDR---SMAELYRI-----RVEA-----ETLKK--------GQADA-RAECSRLEQQLEEM 428
Cdd:PRK04863 455 --TEELLSLEQKLSVAQAAHSQfeqAYQLVRKIagevsRSEAwdvarELLRRlreqrhlaEQLQQlRMRLSELEQRLRQQ 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 429 KSSTQ--QEACKES--DVLAVAELQR-------EVEDLRLRLQMAAEHYKDKYKECQKLQKQVvkfneQQGVKRSPG--- 494
Cdd:PRK04863 533 QRAERllAEFCKRLgkNLDDEDELEQlqeeleaRLESLSESVSEARERRMALRQQLEQLQARI-----QRLAARAPAwla 607
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528503643 495 SDAAAGPLSA-SPEASApgspsTSDAVLDAIIH--GRLKSSSKEldkNDKYRKCKQMLNEERERCS 557
Cdd:PRK04863 608 AQDALARLREqSGEEFE-----DSQDVTEYMQQllERERELTVE---RDELAARKQALDEEIERLS 665
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
156-281 |
4.27e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.17 E-value: 4.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 156 LEQKMEQiQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQELQLsaqSLQEEREEVKRRMEESTA 235
Cdd:COG3096 524 LEQRLRQ-QQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRS---ELRQQLEQLRARIKELAA 599
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528503643 236 R----------LLQLEE-------DLIGVT---QKGLQKETELDCLKDRvkkLNLEKEALEGQLKN 281
Cdd:COG3096 600 RapawlaaqdaLERLREqsgealaDSQEVTaamQQLLEREREATVERDE---LAARKQALESQIER 662
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
156-487 |
5.11e-04 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 43.52 E-value: 5.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 156 LEQKMEQIQQEKKEL-------------LENLD-----------LLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQE 211
Cdd:pfam05622 19 LDQQVSLLQEEKNSLqqenkklqerldqLESGDdsgtpggkkylLLQKQLEQLQEENFRLETARDDYRIKCEELEKEVLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 212 LQLSAQSLQ---EEREEVKRRME---ESTARLLQLEEdLIGVTQKGLQketELDCLKDRVKKlnLEKEALEGQLKNEKDE 285
Cdd:pfam05622 99 LQHRNEELTslaEEAQALKDEMDilrESSDKVKKLEA-TVETYKKKLE---DLGDLRRQVKL--LEERNAEYMQRTLQLE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 286 KELYKIHLKNRELENTKLS-AELQMLKSVDVNK-ENTIAQLKDELARVKSCLAEKEKqhrqLLANsspsgeskalREQLR 363
Cdd:pfam05622 173 EELKKANALRGQLETYKRQvQELHGKLSEESKKaDKLEFEYKKLEEKLEALQKEKER----LIIE----------RDTLR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 364 QKEEQLQATQQQANMLK---AELRDSSNARDRSMAEL----YR---IRVEAET--LKKGQ-ADARAECSRLEQQLEEMKS 430
Cdd:pfam05622 239 ETNEELRCAQLQQAELSqadALLSPSSDPGDNLAAEImpaeIReklIRLQHENkmLRLGQeGSYRERLTELQQLLEDANR 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528503643 431 S-----TQQEACKESdvlaVAELQREVEDLRLRLQMAAEHYKDKYKECQKLQKQVVKFNEQQ 487
Cdd:pfam05622 319 RkneleTQNRLANQR----ILELQQQVEELQKALQEQGSKAEDSSLLKQKLEEHLEKLHEAQ 376
|
|
| ZapB |
COG3074 |
Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome ... |
161-232 |
5.36e-04 |
|
Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442308 [Multi-domain] Cd Length: 79 Bit Score: 39.18 E-value: 5.36e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528503643 161 EQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEEREEVKRRMEE 232
Cdd:COG3074 7 EELEAKVQQAVDTIELLQMEVEELKEKNEELEQENEELQSENEELQSENEQLKTENAEWQERIRSLLGKIDE 78
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
130-492 |
5.47e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 43.41 E-value: 5.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 130 PTEEELLTMEDEGGSDILVVTTKASYLEQKMEQIQQEKKELLENLDLLQKERDELIDEK-NRLEKEYEQERESSA-QLRK 207
Cdd:COG5185 138 IKVEKLDEIADIEASYGEVETGIIKDIFGKLTQELNQNLKKLEIFGLTLGLLKGISELKkAEPSGTVNSIKESETgNLGS 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 208 DVQELQLSAQSLQEEREEVKRRMEESTARLLQLEEDLIgvtQKGLQKETELDCLK-----DRVKKLNLEKEALEGQLKNE 282
Cdd:COG5185 218 ESTLLEKAKEIINIEEALKGFQDPESELEDLAQTSDKL---EKLVEQNTDLRLEKlgenaESSKRLNENANNLIKQFENT 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 283 KDE----KELYKIHLKNRELENTKLSAELqmLKSVDVNKENT---IAQLKDELARVKSCLAEKEKQHRQLLANSSPSGES 355
Cdd:COG5185 295 KEKiaeyTKSIDIKKATESLEEQLAAAEA--EQELEESKRETetgIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVEL 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 356 KALREQLRQKEEQLQAT-----------QQQANMLKAELRDSSNARDRSMAELYR-IRVEAETLKKGQADARAECSRLEQ 423
Cdd:COG5185 373 SKSSEELDSFKDTIESTkesldeipqnqRGYAQEILATLEDTLKAADRQIEELQRqIEQATSSNEEVSKLLNELISELNK 452
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528503643 424 QLEEMKSSTQQEACKESDVLAvAELQREVEDLRLRLQMAAEHyKDKYKEcqKLQKQVVKFNEQQGVKRS 492
Cdd:COG5185 453 VMREADEESQSRLEEAYDEIN-RSVRSKKEDLNEELTQIESR-VSTLKA--TLEKLRAKLERQLEGVRS 517
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
154-369 |
5.90e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.47 E-value: 5.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 154 SYLEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEEREEVKRRMEes 233
Cdd:TIGR04523 464 ESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKIS-- 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 234 tarllqleedligvtqkglQKETELDCLKDRVKKLNLEKEALEGQLKNEKDEKELYKIHLKNRELEN--TKLSAELQMLK 311
Cdd:TIGR04523 542 -------------------DLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQEliDQKEKEKKDLI 602
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 528503643 312 SVDVNKENTIAQLKDELARVKsclaekeKQHRQLLANSSPSGESK-ALREQLRQKEEQL 369
Cdd:TIGR04523 603 KEIEEKEKKISSLEKELEKAK-------KENEKLSSIIKNIKSKKnKLKQEVKQIKETI 654
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
174-472 |
6.25e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.40 E-value: 6.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 174 LDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQELQ--LSAQSLQEErEEVKRRMEESTARLLQLEEDLIGVTQKG 251
Cdd:COG3096 838 LAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNklLPQANLLAD-ETLADRLEELREELDAAQEAQAFIQQHG 916
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 252 lQKETELDCLKDRVKKLNLEKEALEGQLKNEKDEKELykihLKNRELENTKLSAELQML---KSVDVNKENtiAQLKDEL 328
Cdd:COG3096 917 -KALAQLEPLVAVLQSDPEQFEQLQADYLQAKEQQRR----LKQQIFALSEVVQRRPHFsyeDAVGLLGEN--SDLNEKL 989
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 329 arvKSCLAEKEKQHRQLlansspsgeskalREQLRQkeeqLQATQQQANMLKAELRDSSNARDRSMAELYR------IRV 402
Cdd:COG3096 990 ---RARLEQAEEARREA-------------REQLRQ----AQAQYSQYNQVLASLKSSRDAKQQTLQELEQeleelgVQA 1049
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 403 EAETlkkgQADARAECSRLEQQLeemkSSTQQEACKESDVLAVAElqREVEDLRLRLQMAAEHYKDKYKE 472
Cdd:COG3096 1050 DAEA----EERARIRRDELHEEL----SQNRSRRSQLEKQLTRCE--AEMDSLQKRLRKAERDYKQEREQ 1109
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
297-462 |
6.32e-04 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 42.80 E-value: 6.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 297 ELENTKLSAELQMLKsvdvnkentiAQLKDELARVKSCLAEKEKQHRQLLANSSPSGESKALREQLRQKEEQLQATQQQA 376
Cdd:pfam00529 50 QLDPTDYQAALDSAE----------AQLAKAQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 377 NMLKAELrdssnARDRSMAEL-YRIRVEAETLKKGQADARAECSRLEQQLEEM-KSSTQQEACKESDV--------LAVA 446
Cdd:pfam00529 120 AQAQIDL-----ARRRVLAPIgGISRESLVTAGALVAQAQANLLATVAQLDQIyVQITQSAAENQAEVrselsgaqLQIA 194
|
170
....*....|....*.
gi 528503643 447 ELQREVEDLRLRLQMA 462
Cdd:pfam00529 195 EAEAELKLAKLDLERT 210
|
|
| Zn-C2H2_CALCOCO1 |
cd21967 |
C2H2-type zinc binding domain found in calcium-binding and coiled-coil domain-containing ... |
789-815 |
6.36e-04 |
|
C2H2-type zinc binding domain found in calcium-binding and coiled-coil domain-containing protein 1 (CALCOCO1) and similar proteins; CALCOCO1, also called calphoglin, or coiled-coil coactivator protein, or Sarcoma antigen NY-SAR-3, functions as a coactivator for aryl hydrocarbon and nuclear receptors (NR). It is recruited to promoters through its contact with the N-terminal basic helix-loop-helix-Per-Arnt-Sim (PAS) domain of transcription factors or coactivators, such as NCOA2. During ER-activation CALCOCO1 acts synergistically in combination with other NCOA2-binding proteins, such as EP300, CREBBP and CARM1. It is involved in the transcriptional activation of target genes in the Wnt/CTNNB1 pathway. It functions as a secondary coactivator in LEF1-mediated transcriptional activation via its interaction with CTNNB1. In association with CCAR1, CALCOCO1 enhances GATA1- and MED1-mediated transcriptional activation from the gamma-globin promoter during erythroid differentiation of K562 erythroleukemia cells. CALCOCO1 contains a C2H2-type zinc binding domain.
Pssm-ID: 412013 Cd Length: 29 Bit Score: 37.86 E-value: 6.36e-04
10 20
....*....|....*....|....*..
gi 528503643 789 KICPMCSEQFPLDCDQQLFEKHVLTHF 815
Cdd:cd21967 1 KECPICKERFPLECDKDALEDHIDSHF 27
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
157-633 |
6.42e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.57 E-value: 6.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 157 EQKMEQIqqEKKELLENLDLLQ--KERDELIDEKNRL--------------EKEYEQERESSAQL--------------R 206
Cdd:pfam15921 341 EDKIEEL--EKQLVLANSELTEarTERDQFSQESGNLddqlqklladlhkrEKELSLEKEQNKRLwdrdtgnsitidhlR 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 207 KDVQELQLSAQSLQE----EREEVKRRMEESTARLLQLEEDLIGVTQKGLQKETELDCLKDRVKKLNLEKEALEGQLKNE 282
Cdd:pfam15921 419 RELDDRNMEVQRLEAllkaMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTV 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 283 KDEKElyKIHLKNRELENTklSAELQMLKS-VDVnKENTIAQLKDELARVKSCLAEKEKQHRQLlansspSGESKALrEQ 361
Cdd:pfam15921 499 SDLTA--SLQEKERAIEAT--NAEITKLRSrVDL-KLQELQHLKNEGDHLRNVQTECEALKLQM------AEKDKVI-EI 566
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 362 LRQKEEQL-----QATQQQANML--KAELRDSSNARDRSMAELyRIRVEAETLKKGQADARAECSRLEQQLEEMKSSTQQ 434
Cdd:pfam15921 567 LRQQIENMtqlvgQHGRTAGAMQveKAQLEKEINDRRLELQEF-KILKDKKDAKIRELEARVSDLELEKVKLVNAGSERL 645
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 435 EACK----ESDVL--AVAELQREVEDLRLRLQMAAEHYKDKYKECQ------KLQKQVVKFNEQQ---GVKRSPGSDAAA 499
Cdd:pfam15921 646 RAVKdikqERDQLlnEVKTSRNELNSLSEDYEVLKRNFRNKSEEMEtttnklKMQLKSAQSELEQtrnTLKSMEGSDGHA 725
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 500 GPLSASPEASAPGSPSTSDAVLDAI--IHGRLKSSSKEldkndkyrkcKQMLNEERERCSmitDELTKMEVKLREQMKTN 577
Cdd:pfam15921 726 MKVAMGMQKQITAKRGQIDALQSKIqfLEEAMTNANKE----------KHFLKEEKNKLS---QELSTVATEKNKMAGEL 792
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528503643 578 ESLRMQlaaeEDRYKSQVA-------EKGRELKELKDslFVLTKEKEKLEGQLQKSVNREEEQ 633
Cdd:pfam15921 793 EVLRSQ----ERRLKEKVAnmevaldKASLQFAECQD--IIQRQEQESVRLKLQHTLDVKELQ 849
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
156-472 |
6.65e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 42.60 E-value: 6.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 156 LEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLE-KEYEQERESSAQLRKDVQELQLSAQSLQEEREEVKRRMEEST 234
Cdd:pfam13868 28 IAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEeERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 235 ARLlqLEEDLigvtQKGLQKETELDCLKDRVKKLNLEKEALEgQLKNEKDEKELYKIHLKNRELENTKLSAELQMLKsVD 314
Cdd:pfam13868 108 ERI--QEEDQ----AEAEEKLEKQRQLREEIDEFNEEQAEWK-ELEKEEEREEDERILEYLKEKAEREEEREAEREE-IE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 315 VNKENTIAQLKDELARVKSCLAEKEKQHRQLLANSSPSGESKALREQLRQKEEQLQATqQQANMLKAELRDSSNARDRSM 394
Cdd:pfam13868 180 EEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQEL-QQAREEQIELKERRLAEEAER 258
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528503643 395 AELYRIRVEAETLKKGQADARAECSRLEQQLEEMKSSTQQEACKEsdvLAVAELQREVEDLRLRLQMAAEHYKDKYKE 472
Cdd:pfam13868 259 EEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEERE---EQRAAEREEELEEGERLREEEAERRERIEE 333
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
169-409 |
7.47e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 43.50 E-value: 7.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 169 ELLENLDLLQKERDELidEKNRleKEYEQERESSAQLRKDVQEL--QLSAQSLQEEREEVKRRMEESTARLLQLEEDLIG 246
Cdd:TIGR01612 1487 ELKEHIDKSKGCKDEA--DKNA--KAIEKNKELFEQYKKDVTELlnKYSALAIKNKFAKTKKDSEIIIKEIKDAHKKFIL 1562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 247 VTQKGLQKETELdclkdRVKKLNLEKEALegqlKNEKDEKELYKIHLKNRELENtklsaelQMLKSVDVNKentiaqlkd 326
Cdd:TIGR01612 1563 EAEKSEQKIKEI-----KKEKFRIEDDAA----KNDKSNKAAIDIQLSLENFEN-------KFLKISDIKK--------- 1617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 327 elaRVKSCLAEKEKQHRQL--LANSSPSGESKALREQLRQKEEQLQATQQQanmlKAELRDSSNARDRSMAELYRIRVEA 404
Cdd:TIGR01612 1618 ---KINDCLKETESIEKKIssFSIDSQDTELKENGDNLNSLQEFLESLKDQ----KKNIEDKKKELDELDSEIEKIEIDV 1690
|
....*
gi 528503643 405 ETLKK 409
Cdd:TIGR01612 1691 DQHKK 1695
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
146-398 |
8.62e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 42.99 E-value: 8.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 146 ILVVTTKaSYLEQKMEQIQQEkkELLENLDLLQKERDELIdekNRLEKEYEQERESSAQLRKDVQELQLsaqsLQEEREE 225
Cdd:PRK05771 9 VLIVTLK-SYKDEVLEALHEL--GVVHIEDLKEELSNERL---RKLRSLLTKLSEALDKLRSYLPKLNP----LREEKKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 226 VKRRMEESTARllQLEEDLIGVTQKGLQKETELDCLKDRVKKLNLEKEALEgQLKN-EKDEKELYKIHLKNRELENTKLS 304
Cdd:PRK05771 79 VSVKSLEELIK--DVEEELEKIEKEIKELEEEISELENEIKELEQEIERLE-PWGNfDLDLSLLLGFKYVSVFVGTVPED 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 305 AELQMLKSVDVNKENTIAQLKDELARVKSCLAEKEKQHRQLLANSS----PSGESKALREQLRQKEEQLQATQQQANMLK 380
Cdd:PRK05771 156 KLEELKLESDVENVEYISTDKGYVYVVVVVLKELSDEVEEELKKLGferlELEEEGTPSELIREIKEELEEIEKERESLL 235
|
250
....*....|....*...
gi 528503643 381 AELRDSSNARDRSMAELY 398
Cdd:PRK05771 236 EELKELAKKYLEELLALY 253
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
156-237 |
9.93e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 41.35 E-value: 9.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 156 LEQKMEQIQQEKKELLENLDL-LQKERDEL----IDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEEREEVKRRM 230
Cdd:COG1842 56 LERQLEELEAEAEKWEEKARLaLEKGREDLareaLERKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKK 135
|
....*..
gi 528503643 231 EESTARL 237
Cdd:COG1842 136 DTLKARA 142
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
148-381 |
1.13e-03 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 41.20 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 148 VVTTKASYLEQKME----QIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQE-LQLSAQSLQEE 222
Cdd:pfam04012 8 LVRANIHEGLDKAEdpekMLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAaLTKGNEELARE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 223 REEVKRRMEESTARLlqleedligvtqkglqkETELDCLKDRVKKLNLEKEALEGQLKNEKDEKELYKIHLKNRelentk 302
Cdd:pfam04012 88 ALAEKKSLEKQAEAL-----------------ETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKARLKAA------ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528503643 303 lSAELQMLKSVDVNKENTIAqlkDELARVKSCLAEKEKQHRQllanSSPSGESKALREQLRQKEEQLQATQQQANMLKA 381
Cdd:pfam04012 145 -KAQEAVQTSLGSLSTSSAT---DSFERIEEKIEEREARADA----AAELASAVDLDAKLEQAGIQMEVSEDVLARLKA 215
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
132-480 |
1.14e-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: 42.85 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 132 EEELLTMEDEGG----------SDILVVTTKASYLEQKMEQIQQEK-------KELLENLDLLQKERDELIDEKNRLEKE 194
Cdd:pfam01576 137 EEDILLLEDQNSklskerklleERISEFTSNLAEEEEKAKSLSKLKnkheamiSDLEERLKKEEKGRQELEKAKRKLEGE 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 195 YEQERESSAQLRKDVQELQLSAQSLQEEREEVKRRMEESTARLLQLeedligvtQKGLQK-ETELDCLKDRVKKLNLEKE 273
Cdd:pfam01576 217 STDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNA--------LKKIRElEAQISELQEDLESERAARN 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 274 ALEGQLKNEKDEKELYKIHLKNrELENTKLSAELQmlksvdvnkentiAQLKDELARVKSCLAEKEKQHRQLLANsspsg 353
Cdd:pfam01576 289 KAEKQRRDLGEELEALKTELED-TLDTTAAQQELR-------------SKREQEVTELKKALEEETRSHEAQLQE----- 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 354 eskaLREQLRQKEEQLQATQQQANMLKAELRDSSNARDRSMAELyriRVEAETLKKGQADARAECSRLEQQLEEMKS-ST 432
Cdd:pfam01576 350 ----MRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAEL---QAELRTLQQAKQDSEHKRKKLEGQLQELQArLS 422
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 528503643 433 QQEACKESDVLAVAELQREVEDLRLRLQMAAEHYKDKYKECQKLQKQV 480
Cdd:pfam01576 423 ESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQL 470
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
158-232 |
1.26e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 158 QKMEQIQQEKKELLEN-LDLLQKERDELIDEKNRLEKEYEQ--ERESSAQ--LRKDVQELQ-LSAQSLQEEREEVKRRME 231
Cdd:PRK12704 85 QKLEKRLLQKEENLDRkLELLEKREEELEKKEKELEQKQQEleKKEEELEelIEEQLQELErISGLTAEEAKEILLEKVE 164
|
.
gi 528503643 232 E 232
Cdd:PRK12704 165 E 165
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
163-485 |
1.34e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 42.73 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 163 IQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQ--ERESSAQLRKDVQELQLSAQSLQEEREEVKRRMEESTARLLQL 240
Cdd:TIGR01612 498 ILMRMKDFKDIIDFMELYKPDEVPSKNIIGFDIDQniKAKLYKEIEAGLKESYELAKNWKKLIHEIKKELEEENEDSIHL 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 241 EEDLIGVTQKGLQketeldcLKDRVKKLNLEKEALEGQLKNEKDEKELYKihlknrelentklsaelqmlKSVDVNK--E 318
Cdd:TIGR01612 578 EKEIKDLFDKYLE-------IDDEIIYINKLKLELKEKIKNISDKNEYIK--------------------KAIDLKKiiE 630
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 319 NTIAQLkDELARVKSCLAEKEKQHRQLLANSSPSGESKALREQLRQKEEQLQATQQQANM----LKAELRDSSNARDRSM 394
Cdd:TIGR01612 631 NNNAYI-DELAKISPYQVPEHLKNKDKIYSTIKSELSKIYEDDIDALYNELSSIVKENAIdnteDKAKLDDLKSKIDKEY 709
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 395 AELYRIrvEAETLKKGQADARAECSRLEQQLEEMKSSTQQEACKesdvlavaELQREVEDLRLRLQMAAEHYKDKYKECQ 474
Cdd:TIGR01612 710 DKIQNM--ETATVELHLSNIENKKNELLDIIVEIKKHIHGEINK--------DLNKILEDFKNKEKELSNKINDYAKEKD 779
|
330
....*....|.
gi 528503643 475 KLQKQVVKFNE 485
Cdd:TIGR01612 780 ELNKYKSKISE 790
|
|
| Zn-C2H2_CALCOCO2 |
cd21968 |
C2H2-type zinc binding domain found in calcium-binding and coiled-coil domain-containing ... |
789-816 |
1.67e-03 |
|
C2H2-type zinc binding domain found in calcium-binding and coiled-coil domain-containing protein 2 (CALCOCO2) and similar proteins; CALCOCO2, also called antigen nuclear dot 52 kDa protein, or nuclear domain 10 protein NDP52, or nuclear domain 10 protein 52, or nuclear dot protein 52, is an Xenophagy-specific receptor required for autophagy-mediated intracellular bacteria degradation. It acts as an effector protein of galectin-sensed membrane damage that restricts the proliferation of infecting pathogens such as Salmonella typhimurium upon entry into the cytosol by targeting LGALS8-associated bacteria for autophagy. It may play a role in ruffle formation and actin cytoskeleton organization and seems to negatively regulate constitutive secretion. CALCOCO2 contains a C2H2-type zinc binding domain.
Pssm-ID: 412014 Cd Length: 27 Bit Score: 36.66 E-value: 1.67e-03
10 20
....*....|....*....|....*...
gi 528503643 789 KICPMCSEQFPlDCDQQLFEKHVLTHFD 816
Cdd:cd21968 1 FECPICSKIFE-ATSKQEFEDHVFCHSL 27
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
255-515 |
1.68e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 255 ETELDCLKDRVKKLNLEKEALEGQLKNEKDEkelykIHLKNRELEntKLSAELQmlksvdvNKENTIAQLKDELARVKSC 334
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAE-----LEELNEEYN--ELQAELE-------ALQAEIDKLQAEIAEAEAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 335 LAEKEKQHRQLLANSSPSGES-----------------------KALREQLRQKEEQLQATQQQANMLKAELRDSSNARD 391
Cdd:COG3883 81 IEERREELGERARALYRSGGSvsyldvllgsesfsdfldrlsalSKIADADADLLEELKADKAELEAKKAELEAKLAELE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 392 RSMAELYRIRVEAETLKKGQADARAECSRLEQQLEEMKSSTQQEACKESDVLAVAELQREVEDLRLRLQMAAEHYKDKYK 471
Cdd:COG3883 161 ALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 528503643 472 ECQKLQKQVVKFNEQQGVKRSPGSDAAAGPLSASPEASAPGSPS 515
Cdd:COG3883 241 AAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGG 284
|
|
| Zn-C2H2_spn-F |
cd21971 |
C2H2-type zinc binding domain found in Drosophila melanogaster Spindle-F (Spn-F) and similar ... |
789-816 |
1.68e-03 |
|
C2H2-type zinc binding domain found in Drosophila melanogaster Spindle-F (Spn-F) and similar proteins; spn-F is the central mediator of IK2 kinase-dependent dendrite pruning in drosophila sensory neurons. It acts downstream of IKK-related kinase Ik2 in the same pathway for dendrite pruning. Spn-F is a coil-coiled protein containing a C2H2-type zinc binding domain.
Pssm-ID: 412017 Cd Length: 30 Bit Score: 36.74 E-value: 1.68e-03
10 20
....*....|....*....|....*...
gi 528503643 789 KICPMCSEQFPLDCDQQLFEKHVLTHFD 816
Cdd:cd21971 2 RTCPMCGKQFSDQVSFHEFREHVEMHFI 29
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
125-352 |
1.75e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 41.99 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 125 FRANSPTEEELLTMEDE--GGSDILVVTTKASYLEQKMEQIQQEKKELLEnldlLQKERDELIDEKNRLEKEYEQERESS 202
Cdd:COG5022 919 LIENLEFKTELIARLKKllNNIDLEEGPSIEYVKLPELNKLHEVESKLKE----TSEEYEDLLKKSTILVREGNKANSEL 994
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 203 AQLRKDVQELQLSAQSLQEEREEVKRRMEESTArlLQLEEDLIGVTQKGLQKETELDCLKdrvKKLNLEKEALEGQLKNE 282
Cdd:COG5022 995 KNFKKELAELSKQYGALQESTKQLKELPVEVAE--LQSASKIISSESTELSILKPLQKLK---GLLLLENNQLQARYKAL 1069
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528503643 283 KDEKELYKIHLKN-------RELENTKLSAELQMLKSVDVNKENTIAQLKDELARVKSClAEKEKQHRQLLANSSPS 352
Cdd:COG5022 1070 KLRRENSLLDDKQlyqlestENLLKTINVKDLEVTNRNLVKPANVLQFIVAQMIKLNLL-QEISKFLSQLVNTLEPV 1145
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
154-251 |
1.80e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.21 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 154 SYLEQKMEQIQQEkkelLEN----LDLLQKERDELIDEKNRLEKE--------YEQERESSAQLRKDVQELQLSAQSlqE 221
Cdd:PRK11281 202 ALLNAQNDLQRKS----LEGntqlQDLLQKQRDYLTARIQRLEHQlqllqeaiNSKRLTLSEKTVQEAQSQDEAARI--Q 275
|
90 100 110
....*....|....*....|....*....|
gi 528503643 222 EREEVKRRMEEStarlLQLEEDLIGVTQKG 251
Cdd:PRK11281 276 ANPLVAQELEIN----LQLSQRLLKATEKL 301
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
161-291 |
1.92e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.74 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 161 EQIQQEKKELlenldllqkerDELIDEKNRLEKEYEQERESSAQLRKDV----QELQLSAQSLQEEREEVKRRMEESTAR 236
Cdd:PRK00409 509 KLIGEDKEKL-----------NELIASLEELERELEQKAEEAEALLKEAeklkEELEEKKEKLQEEEDKLLEEAEKEAQQ 577
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528503643 237 LL---QLEEDLIGVTQKGLQKETELDC----LKDRVKKLNLEKEALEGQLKNEKDEKELYKI 291
Cdd:PRK00409 578 AIkeaKKEADEIIKELRQLQKGGYASVkaheLIEARKRLNKANEKKEKKKKKQKEKQEELKV 639
|
|
| ZapB |
pfam06005 |
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is ... |
171-237 |
1.92e-03 |
|
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is required for proper Z-ring formation.
Pssm-ID: 428718 [Multi-domain] Cd Length: 71 Bit Score: 37.63 E-value: 1.92e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528503643 171 LENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEEREEVKRRMEESTARL 237
Cdd:pfam06005 3 LELLEQLETKIQAAVDTIALLQMENEELKEENEELKEEANELEEENQQLKQERNQWQERIRGLLGKL 69
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
156-244 |
2.20e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 41.86 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 156 LEQKMEQIQQEKKELLENLDLLQKERDELidekNRLEKEYEQERessAQLRKDVQELQLSAQSL-QEEREEVKRRMEEST 234
Cdd:PRK11448 154 LKQQLELQAREKAQSQALAEAQQQELVAL----EGLAAELEEKQ---QELEAQLEQLQEKAAETsQERKQKRKEITDQAA 226
|
90
....*....|
gi 528503643 235 ARlLQLEEDL 244
Cdd:PRK11448 227 KR-LELSEEE 235
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
156-269 |
2.25e-03 |
|
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: 38.77 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 156 LEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQE-------RESSAQLRKDVQELQLSAQSLQEEREEVKR 228
Cdd:pfam07926 6 LQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQNYERElvlhaedIKALQALREELNELKAEIAELKAEAESAKA 85
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 528503643 229 RMEESTARLLQLEEDLigvtqkglqkETELDCLKDRVKKLN 269
Cdd:pfam07926 86 ELEESEESWEEQKKEL----------EKELSELEKRIEDLN 116
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
155-481 |
2.30e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 41.65 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 155 YLEQKMEQIQQEKKELLENLDllqKERDELIDEKNRLEKEYEQERESSaqlrkdvQELQLSAQSLQEEREEVKRRMEEST 234
Cdd:pfam05557 6 ESKARLSQLQNEKKQMELEHK---RARIELEKKASALKRQLDRESDRN-------QELQKRIRLLEKREAEAEEALREQA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 235 ARLLQLEEDLIGVTQKGLQKETEL-------DCLKDRVKKLNLEKEALEGQLKNEKDEKELYKIHL---KNRELENTKLS 304
Cdd:pfam05557 76 ELNRLKKKYLEALNKKLNEKESQLadareviSCLKNELSELRRQIQRAELELQSTNSELEELQERLdllKAKASEAEQLR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 305 AELQMLKSVDVNKENTIAQLKDELARVKSCLAEKEKQHRQLLANSspsgESKALREQLRQKEEQLQATQQQANMLKAELR 384
Cdd:pfam05557 156 QNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELARIP----ELEKELERLREHNKHLNENIENKLLLKEEVE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 385 DSSNARDR---SMAELYRIRVEAE----TLKKGQADARAEC----------SRLEQQLEEMKSSTQQEACKESDVLAVAE 447
Cdd:pfam05557 232 DLKRKLEReekYREEAATLELEKEkleqELQSWVKLAQDTGlnlrspedlsRRIEQLQQREIVLKEENSSLTSSARQLEK 311
|
330 340 350
....*....|....*....|....*....|....*...
gi 528503643 448 LQREVEDLRLRLQMAAEHYKDKYKE----CQKLQKQVV 481
Cdd:pfam05557 312 ARRELEQELAQYLKKIEDLNKKLKRhkalVRRLQRRVL 349
|
|
| Zn-C2H2_TAX1BP1_rpt2 |
cd21970 |
second C2H2-type zinc binding domain found in tax1-binding protein 1 (TAX1BP1) and similar ... |
762-787 |
2.67e-03 |
|
second C2H2-type zinc binding domain found in tax1-binding protein 1 (TAX1BP1) and similar proteins; TAX1BP1, also called TRAF6-binding protein (T6BP), is a novel ubiquitin-binding adaptor protein involved in the negative regulation of the NF-kappaB transcription factor, a key player in inflammatory responses, immunity and tumorigenesis. It inhibits TNF-induced apoptosis by mediating the TNFAIP3 anti-apoptotic activity. It may also play a role in the pro-inflammatory cytokine IL-1 signaling cascade. TAX1BP1 is degraded by caspase-3-like family proteins upon TNF-induced apoptosis. TAX1BP1 contains two C2H2-type zinc binding domains; this model corresponds to the second one.
Pssm-ID: 412016 Cd Length: 27 Bit Score: 35.99 E-value: 2.67e-03
10 20
....*....|....*....|....*.
gi 528503643 762 KRCPLCEVIFPPHYDQSKFEEHVESH 787
Cdd:cd21970 1 KVCPMCSEQFPPDCDQQVFERHVQTH 26
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
161-638 |
2.97e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 161 EQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEEREEVKRRMEES------- 233
Cdd:PTZ00121 1091 EATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDArkaeear 1170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 234 ---TARLLQLEEDLIGVTQKGLQKETELDCLKDRVKKLNLEKEALEG-QLKNEKDEKELYKIHLKNRELENTKLSAELQM 309
Cdd:PTZ00121 1171 kaeDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEArKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERN 1250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 310 LKSVDVNKENTIAQLKDELARVKSCLAEKEKQHRQL----LANSSPSGESKALREQLRQKEEQlqatQQQANMLKAELRD 385
Cdd:PTZ00121 1251 NEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAeekkKADEAKKAEEKKKADEAKKKAEE----AKKADEAKKKAEE 1326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 386 SSNARDRSMAELYRIRVEAETLKKGQADARAECSRLEQQLEEMKSSTQQEACKESDVLAVAELQREVEDLRLRlqmaAEH 465
Cdd:PTZ00121 1327 AKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKK----AEE 1402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 466 YKDKYKECQKLQKQVVKFNE--QQGVKRSPGSDAAAGPLSASPEASAPGSPSTSDAVLDAIIHGRLKSSSKELDKNDKYR 543
Cdd:PTZ00121 1403 DKKKADELKKAAAAKKKADEakKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEA 1482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 544 KCKQMLNEERERCSMITDELTKMEvklrEQMKTNESLRmqlAAEEDRYKSQV--AEKGRELKELKDSLFVLTKEKEKLEG 621
Cdd:PTZ00121 1483 KKADEAKKKAEEAKKKADEAKKAA----EAKKKADEAK---KAEEAKKADEAkkAEEAKKADEAKKAEEKKKADELKKAE 1555
|
490 500
....*....|....*....|....*
gi 528503643 622 QLQKS--------VNREEEQKDSNL 638
Cdd:PTZ00121 1556 ELKKAeekkkaeeAKKAEEDKNMAL 1580
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
158-399 |
3.07e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 40.51 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 158 QKMEQIQQEKKELLENL------------DLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQELQlsAQSLQEeree 225
Cdd:pfam09787 14 QKAARILQSKEKLIASLkegsgvegldssTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELE--AQQQEE---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 226 vkrrMEESTARLLQLEEDLIGVTQKGLQKETELDCLKDrvkklnlEKEALEGQLKNEKDEkelYKIHLKNRELENTKLSA 305
Cdd:pfam09787 88 ----AESSREQLQELEEQLATERSARREAEAELERLQE-------ELRYLEEELRRSKAT---LQSRIKDREAEIEKLRN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 306 ELqMLKSvdvNKENTIAQLKDELARVKSCLAEKEKQHRQLlansspSGESKALREQLRQKEEQLQATQQQA----NMLKA 381
Cdd:pfam09787 154 QL-TSKS---QSSSSQSELENRLHQLTETLIQKQTMLEAL------STEKNSLVLQLERMEQQIKELQGEGsngtSINME 223
|
250
....*....|....*...
gi 528503643 382 ELRDSSNARDRSMAELYR 399
Cdd:pfam09787 224 GISDGEGTRLRNVPGLFS 241
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
301-435 |
3.07e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 40.51 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 301 TKLSAELQMLKSVDVNKENTIAQLKDELARVKSCLAEKEKQHRQllansspsgESKALREQLRQKEEQLQATQQQANMLK 380
Cdd:pfam09787 43 TALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQE---------EAESSREQLQELEEQLATERSARREAE 113
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 528503643 381 AELRDSSNARDRSMAELYRIRVeaeTLKKGQADARAECSRLEQQL--EEMKSSTQQE 435
Cdd:pfam09787 114 AELERLQEELRYLEEELRRSKA---TLQSRIKDREAEIEKLRNQLtsKSQSSSSQSE 167
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
157-244 |
3.08e-03 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 38.36 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 157 EQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEEREEVKRRMEESTAR 236
Cdd:pfam20492 33 EETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEEKEQLEAELAEAQEEIARLEEEVERKEEEARRLQEE 112
|
....*...
gi 528503643 237 LLQLEEDL 244
Cdd:pfam20492 113 LEEAREEE 120
|
|
| EzrA |
COG4477 |
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome ... |
156-233 |
3.26e-03 |
|
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443574 [Multi-domain] Cd Length: 567 Bit Score: 40.98 E-value: 3.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 156 LEQKMEQIQQEKKELLENLD-------LLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEEREEVKR 228
Cdd:COG4477 352 LEKQIEELEKRYDEIDERIEeekvaysELQEELEEIEEQLEEIEEEQEEFSEKLKSLRKDELEAREKLDELKKKLREIKR 431
|
....*
gi 528503643 229 RMEES 233
Cdd:COG4477 432 RLEKS 436
|
|
| Zn-C2H2_CALCOCO1 |
cd21967 |
C2H2-type zinc binding domain found in calcium-binding and coiled-coil domain-containing ... |
762-788 |
3.77e-03 |
|
C2H2-type zinc binding domain found in calcium-binding and coiled-coil domain-containing protein 1 (CALCOCO1) and similar proteins; CALCOCO1, also called calphoglin, or coiled-coil coactivator protein, or Sarcoma antigen NY-SAR-3, functions as a coactivator for aryl hydrocarbon and nuclear receptors (NR). It is recruited to promoters through its contact with the N-terminal basic helix-loop-helix-Per-Arnt-Sim (PAS) domain of transcription factors or coactivators, such as NCOA2. During ER-activation CALCOCO1 acts synergistically in combination with other NCOA2-binding proteins, such as EP300, CREBBP and CARM1. It is involved in the transcriptional activation of target genes in the Wnt/CTNNB1 pathway. It functions as a secondary coactivator in LEF1-mediated transcriptional activation via its interaction with CTNNB1. In association with CCAR1, CALCOCO1 enhances GATA1- and MED1-mediated transcriptional activation from the gamma-globin promoter during erythroid differentiation of K562 erythroleukemia cells. CALCOCO1 contains a C2H2-type zinc binding domain.
Pssm-ID: 412013 Cd Length: 29 Bit Score: 35.55 E-value: 3.77e-03
10 20
....*....|....*....|....*..
gi 528503643 762 KRCPLCEVIFPPHYDQSKFEEHVESHW 788
Cdd:cd21967 1 KECPICKERFPLECDKDALEDHIDSHF 27
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
166-625 |
3.92e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.77 E-value: 3.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 166 EKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEEREEVKRRMEESTARLLQLEEDLI 245
Cdd:TIGR04523 34 EEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 246 GVTQKGLQKETELDCLKDRVKKLNLEKEALEGQLKNEkdEKELYKIHLKNRELENTKLSAELQMLKsvdvnkentiaqLK 325
Cdd:TIGR04523 114 NDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKK--EKELEKLNNKYNDLKKQKEELENELNL------------LE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 326 DELARVK-----------------SCLAEKEKQHRQLLA--------NSSPSGESKALREQLRQKEEQLQATQQQANMLK 380
Cdd:TIGR04523 180 KEKLNIQknidkiknkllklelllSNLKKKIQKNKSLESqiselkkqNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLK 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 381 AELRDSSNARDRSMAELYRIRVEAETLKKGQADARAECSRLEQQLE-----EMKSSTQQEACKESDV--------LAVAE 447
Cdd:TIGR04523 260 DEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEqdwnkELKSELKNQEKKLEEIqnqisqnnKIISQ 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 448 LQREVEDLRLRLQMAAEHYKDKYKECQKLQKQVVKF-NEQQGVKRSpgsdaaagPLSASPEASAPGSPSTSDAVLDAIIH 526
Cdd:TIGR04523 340 LNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLkKENQSYKQE--------IKNLESQINDLESKIQNQEKLNQQKD 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 527 GRLKSSSKELDKNDK-YRKCKQMLNEERERCSMITDELTKMEVKLREQMKTNESLRMQLAAEEDRY---KSQVAEKGREL 602
Cdd:TIGR04523 412 EQIKKLQQEKELLEKeIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSInkiKQNLEQKQKEL 491
|
490 500
....*....|....*....|...
gi 528503643 603 KELKDSLFVLTKEKEKLEGQLQK 625
Cdd:TIGR04523 492 KSKEKELKKLNEEKKELEEKVKD 514
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
155-240 |
4.22e-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: 4.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 155 YLEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERessAQLRKDVQELQLSAQSLQEEREEVKRRMEEst 234
Cdd:COG1579 100 SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKK---AELDEELAELEAELEELEAEREELAAKIPP-- 174
|
....*.
gi 528503643 235 aRLLQL 240
Cdd:COG1579 175 -ELLAL 179
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
181-464 |
4.50e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.71 E-value: 4.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 181 RDELIDEknrLEKEYEQERESSAQLRKDVQELQLSAQSL----------------QEEREEVKRRMEESTARLLQLEEDL 244
Cdd:PRK04863 784 REKRIEQ---LRAEREELAERYATLSFDVQKLQRLHQAFsrfigshlavafeadpEAELRQLNRRRVELERALADHESQE 860
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 245 IGVTQKglqketeLDCLKDRVKKLNlekeALEGQLKNEKDEkelykiHLKNR--ELENtKLSAELQMLKSVDVNkENTIA 322
Cdd:PRK04863 861 QQQRSQ-------LEQAKEGLSALN----RLLPRLNLLADE------TLADRveEIRE-QLDEAEEAKRFVQQH-GNALA 921
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 323 QLKDELarvkSCLAEKEKQHRQllansspsgeskaLREQLRQKEEQLQATQQQANMLKaELRdsSNARDRSMAELYRIRV 402
Cdd:PRK04863 922 QLEPIV----SVLQSDPEQFEQ-------------LKQDYQQAQQTQRDAKQQAFALT-EVV--QRRAHFSYEDAAEMLA 981
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528503643 403 EA----ETLKKGQADARAECSRLEQQLEEmkssTQQEACKESDVLA------------VAELQREVEDLRLRLQMAAE 464
Cdd:PRK04863 982 KNsdlnEKLRQRLEQAEQERTRAREQLRQ----AQAQLAQYNQVLAslkssydakrqmLQELKQELQDLGVPADSGAE 1055
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
193-362 |
5.12e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 40.71 E-value: 5.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 193 KEYEQERESSAQLRKDVQELQLSAQSLQEEREEVKRRMEESTARLLQLEEDLIGVTQKGLQKETELDCLKDRVKKLNLE- 271
Cdd:COG3096 522 AELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARa 601
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 272 ------KEALEgQLKNEKDEkelykihlknrELENTK-LSAELQMLksvdVNKENTIAQLKDELARVKSCLaekEKQHRQ 344
Cdd:COG3096 602 pawlaaQDALE-RLREQSGE-----------ALADSQeVTAAMQQL----LEREREATVERDELAARKQAL---ESQIER 662
|
170
....*....|....*....
gi 528503643 345 LLANSSP-SGESKALREQL 362
Cdd:COG3096 663 LSQPGGAeDPRLLALAERL 681
|
|
| DUF3450 |
pfam11932 |
Protein of unknown function (DUF3450); This family of proteins are functionally ... |
146-232 |
5.40e-03 |
|
Protein of unknown function (DUF3450); This family of proteins are functionally uncharacterized. This protein is found in bacteria and eukaryotes. Proteins in this family are about 260 amino acids in length.
Pssm-ID: 432198 [Multi-domain] Cd Length: 238 Bit Score: 39.52 E-value: 5.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 146 ILVVTTKASYLEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEEREE 225
Cdd:pfam11932 1 LLALLLASGALAATLDQALDLAEKAVAAAAQSQKKIDKWDDEKQELLAEYRALKAELESLEVYNRQLERLVASQEQEIAS 80
|
....*..
gi 528503643 226 VKRRMEE 232
Cdd:pfam11932 81 LERQIEE 87
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
161-290 |
5.74e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 40.34 E-value: 5.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 161 EQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESsaqlrkDVQELQLSAQSLQEEREEVKRRMEESTARLLQL 240
Cdd:TIGR00618 774 LQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPS------DEDILNLQCETLVQEEEQFLSRLEEKSATLGEI 847
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 528503643 241 EEDLIGVTQKGLQKETeldcLKDRVKKLNLEKEALEG--QLKNEKDEKELYK 290
Cdd:TIGR00618 848 THQLLKYEECSKQLAQ----LTQEQAKIIQLSDKLNGinQIKIQFDGDALIK 895
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
144-235 |
5.75e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.81 E-value: 5.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 144 SDILVVTTKASYLEQKMEQIQQ-------EKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQELQLSA 216
Cdd:COG3883 119 DRLSALSKIADADADLLEELKAdkaeleaKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQL 198
|
90
....*....|....*....
gi 528503643 217 QSLQEEREEVKRRMEESTA 235
Cdd:COG3883 199 AELEAELAAAEAAAAAAAA 217
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
151-383 |
5.86e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 40.28 E-value: 5.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 151 TKASYLEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRK------DVQELQLSAQSLqeerE 224
Cdd:PRK11281 49 NKQKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEAlkddndEETRETLSTLSL----R 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 225 EVKRRMEESTARLLQLEEDLIGVTQK--GLQKETEldclkdRVKKL---NLEK-EALEGQLKNEKDEKELYKIHLKNrel 298
Cdd:PRK11281 125 QLESRLAQTLDQLQNAQNDLAEYNSQlvSLQTQPE------RAQAAlyaNSQRlQQIRNLLKGGKVGGKALRPSQRV--- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 299 entKLSAELQML--------KSVDVNKE-NTIAQLKDELARVKSCLAEKEKQHRQLLANSSPSGESKalrEQLRQKEEQL 369
Cdd:PRK11281 196 ---LLQAEQALLnaqndlqrKSLEGNTQlQDLLQKQRDYLTARIQRLEHQLQLLQEAINSKRLTLSE---KTVQEAQSQD 269
|
250
....*....|....*
gi 528503643 370 QATQQQAN-MLKAEL 383
Cdd:PRK11281 270 EAARIQANpLVAQEL 284
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
156-389 |
6.07e-03 |
|
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular sites as centrioles, basal bodies, and along ciliary and flagellar doublet microtubules. Tektins form unique protofilaments, organized as longitudinal polymers of tektin heterodimers with axial periodicity matching tubulin. Tektin polypeptides consist of several alpha-helical regions that are predicted to form coiled coils. Indeed, tektins share considerable structural similarities with intermediate filament proteins. Possible functional roles for tektins are: stabilization of tubulin protofilaments; attachment of A and B-tubules in ciliary/flagellar microtubule doublets and C-tubules in centrioles; binding of axonemal components.
Pssm-ID: 460827 [Multi-domain] Cd Length: 383 Bit Score: 39.84 E-value: 6.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 156 LEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYE-------------QERESsaqlRKDV--------QELQL 214
Cdd:pfam03148 48 LGERIQDITFWKSELEKELEELDEEIELLLEEKRRLEKALEaleeplhiaqeclTLREK----RQGIdlvhdeveKELLK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 215 SAQSLQEEREEVKRRMEESTARLLQLEEdligvtqkgLQKETELDcLKDRVKKLNLEKEALegQLKNEKDEKELY----K 290
Cdd:pfam03148 124 EVELIEGIQELLQRTLEQAWEQLRLLRA---------ARHKLEKD-LSDKKEALEIDEKCL--SLNNTSPNISYKpgptR 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 291 IHLKNRELE-------NTKLSAELQMLKS------VDVNKENTIAQLKDELARVKSCLAEKEKQHRQLLANsspsgeska 357
Cdd:pfam03148 192 IPPNSSTPEewekftqDNIERAEKERAASaqlrelIDSILEQTANDLRAQADAVNFALRKRIEETEDAKNK--------- 262
|
250 260 270
....*....|....*....|....*....|..
gi 528503643 358 LREQLRQKEEQLQATQQQANMLKAELRDSSNA 389
Cdd:pfam03148 263 LEWQLKKTLQEIAELEKNIEALEKAIRDKEAP 294
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
152-352 |
6.73e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 40.11 E-value: 6.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 152 KASYLEQKMEQIQQEKKELLENLDLLQKERDEliDEKNRLEKEYEQEREssaQLRKDVQELQLSAQSLQEEREEVKRR-- 229
Cdd:pfam17380 403 KVKILEEERQRKIQQQKVEMEQIRAEQEEARQ--REVRRLEEERAREME---RVRLEEQERQQQVERLRQQEEERKRKkl 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 230 -MEESTARLLQLEEDLIGVTQKGLQKETELDCLKDRVKKLnLEKEALEGQ--LKNEKDEKELYKIHLKNRELENTKLSAE 306
Cdd:pfam17380 478 eLEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKL-LEKEMEERQkaIYEEERRREAEEERRKQQEMEERRRIQE 556
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 528503643 307 lQMLKSVDVNKENTIAQLKDELARVkscLAEKEKQHRQLLANSSPS 352
Cdd:pfam17380 557 -QMRKATEERSRLEAMEREREMMRQ---IVESEKARAEYEATTPIT 598
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
159-242 |
6.79e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 40.06 E-value: 6.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 159 KMEQIQ--QEKKELLENLDLLQKERDELIDEKN--------RLEKEYEQERESSAQLRKDVQELQLSAQSLQEEREEVKR 228
Cdd:COG0542 403 RMEIDSkpEELDELERRLEQLEIEKEALKKEQDeasferlaELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQ 482
|
90
....*....|....
gi 528503643 229 RMEESTARLLQLEE 242
Cdd:COG0542 483 RYGKIPELEKELAE 496
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
366-434 |
7.49e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 39.93 E-value: 7.49e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528503643 366 EEQLQATQQQANMLKAELRDSSNARDRSMAELYRIRVEAETLKKGQADARAECSRLEQQLEEMKSSTQQ 434
Cdd:PRK11448 141 ENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAE 209
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
156-248 |
8.51e-03 |
|
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];
Pssm-ID: 443204 [Multi-domain] Cd Length: 287 Bit Score: 38.94 E-value: 8.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528503643 156 LEQKMEQIQQEKKELLenldllqKERDELIDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEEREEVKRRMEESTA 235
Cdd:COG4026 140 LKEKIDEIAKEKEKLT-------KENEELESELEELREEYKKLREENSILEEEFDNIKSEYSDLKSRFEELLKKRLLEVF 212
|
90
....*....|...
gi 528503643 236 RLLQLEEDLIGVT 248
Cdd:COG4026 213 SLEELWKELFPEE 225
|
|
| |
