|
Name |
Accession |
Description |
Interval |
E-value |
| SKICH |
pfam17751 |
SKICH domain; The SKICH domains of SKIP and PIPP mediate plasma membrane localization. The ... |
22-125 |
4.20e-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: 4.20e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 22 VIFQNVGKSYLPHGALECHYTLTQFIKPHPKDWVGIFKVGWSTARDYYTFLWSplPDNYTEGTAINRSVVFQGYYVPNDD 101
Cdd:pfam17751 1 VVFQNVGEWYPPDEDIECSYTLTPDFTPSSWDWIGLFKVGWKSVNDYVTYVWA--KDDEVEGSNSVRQVLFKASYLPKEP 78
|
90 100
....*....|....*....|....
gi 1207119093 102 GEFYQFCYVTHKGEIRGASTPFQF 125
Cdd:pfam17751 79 EGFYQFCYVSNLGSVVGISTPFQF 102
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
133-461 |
7.77e-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: 142.34 E-value: 7.77e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 133 EELLTME-----DEGGSDILVVTTKASYLEQKMEQIQQEKKELLENLDLLQK------------------ERDELIDEKN 189
Cdd:pfam07888 4 DELVTLEeeshgEEGGTDMLLVVPRAELLQNRLEECLQERAELLQAQEAANRqrekekerykrdreqwerQRRELESRVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 190 RLEKEYEQERESSAQLRKDVQELQLSAQSLQEEREEVKRRMEESTARLLQLEEDLIGVTQKGLQKETELDCLKDRVKKLN 269
Cdd:pfam07888 84 ELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 270 lekealeGQLKNEKDEKELYKIHLKNRELENTKLSAELQMLKSVDVNKENTIAQLKDELARVKSCLAEkekQHRQLLans 349
Cdd:pfam07888 164 -------AQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTT---AHRKEA--- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 350 spsgESKALREQLRQKEEQLQATQQQANMLKAELRDSSNARDRSMAELYRIRVEAETLKKGQADARAecsrleqQLEEMK 429
Cdd:pfam07888 231 ----ENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASL-------ALREGR 299
|
330 340 350
....*....|....*....|....*....|....*.
gi 1207119093 430 SSTQQE----AQCKESDVLAVAELQREVEDLRLRLQ 461
Cdd:pfam07888 300 ARWAQEretlQQSAEADKDRIEKLSAELQRLEERLQ 335
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
149-639 |
1.40e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 97.70 E-value: 1.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 149 VTTKASYLEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEEREEVKR 228
Cdd:COG1196 237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 229 RMEESTARLLQLEEDLIGVTQKGLQKETELDCLKDRVKKLNLEKEALEGQLKNEKDEKELYKIHLKNRELENTKLSAELQ 308
Cdd:COG1196 317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 309 MLKSVDVNKENTIAQLKDELARVKSCLAEKEKQHRQLLANSSpsgESKALREQLRQKEEQLQATQQQANMLKAELRDSSN 388
Cdd:COG1196 397 ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEE---EEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 389 ARDRSMAELYRIRVEAETLKKGQADARAEcsrLEQQLEEMKSSTQQEAQCKESDVLAVAELQREVEDLRLRLQMAAEHYK 468
Cdd:COG1196 474 LLEAALAELLEELAEAAARLLLLLEAEAD---YEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQN 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 469 DKYKECQKLQKQVvkfneqQGVKRSPGSDAAAGPLSASPEASAPGSPSTSDAVLDAII---------HGRLKSSSKEL-D 538
Cdd:COG1196 551 IVVEDDEVAAAAI------EYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDlvasdlreaDARYYVLGDTLlG 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 539 KNDKYRKCKQMLNEERERCSMITDELTKMEVKLREQMKTNESLRMQLAAEEDRYKSQVAEKGRELKELKDSLFVLTKEKE 618
Cdd:COG1196 625 RTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEE 704
|
490 500
....*....|....*....|.
gi 1207119093 619 KLEGQLQKSVNREEEQKDSNL 639
Cdd:COG1196 705 EERELAEAEEERLEEELEEEA 725
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
156-480 |
2.41e-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: 97.05 E-value: 2.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 156 LEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEEREEVKRRMEESTA 235
Cdd:TIGR02168 682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 236 RLLQLEEDLIGVTQKGLQKETELDCLKDRVKKLNLEKEALEGQLKNEKDEKELYKIHLKNRELENTKLSAELQMLKSVDV 315
Cdd:TIGR02168 762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE 841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 316 NKENTIAQLKDELARVKSCLAEKEKQHRQLLAnsspsgESKALREQLRQKEEQLQATQQQANMLKAELRDSSNARDRSMA 395
Cdd:TIGR02168 842 DLEEQIEELSEDIESLAAEIEELEELIEELES------ELEALLNERASLEEALALLRSELEELSEELRELESKRSELRR 915
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 396 ELYRIRVEAETLKKGQADARAECSRLEQQLEEMKSSTQQEA-QCKESDVLAVAELQREVEDLRLRLQ-------MAAEHY 467
Cdd:TIGR02168 916 ELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAeALENKIEDDEEEARRRLKRLENKIKelgpvnlAAIEEY 995
|
330
....*....|...
gi 1207119093 468 KDKYKECQKLQKQ 480
Cdd:TIGR02168 996 EELKERYDFLTAQ 1008
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
157-461 |
2.56e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 86.91 E-value: 2.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 157 EQKMEQIQqekkellENLDLLQKERDELIDEKNRLEKE------Y----EQERESSAQLR-KDVQELQLSAQSLQEEREE 225
Cdd:COG1196 178 ERKLEATE-------ENLERLEDILGELERQLEPLERQaekaerYrelkEELKELEAELLlLKLRELEAELEELEAELEE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 226 VKRRMEESTARLLQLEEDLIGVTQKGLQKETELDCLKDRVKKLNLEKEALEGQLKNEKDEKELYKIHLKNRELENTKLSA 305
Cdd:COG1196 251 LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 306 ELQMLKSVDVNKENTIAQLKDELARVKSCLAEKEKQHRQLLAnsspsgESKALREQLRQKEEQLQATQQQANMLKAELRD 385
Cdd:COG1196 331 ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA------ELAEAEEELEELAEELLEALRAAAELAAQLEE 404
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207119093 386 SSNARDRSMAELYRIRVEAETLKKGQADARAECSRLEQQLEEMKSSTQQEAQCKESDVLAVAELQREVEDLRLRLQ 461
Cdd:COG1196 405 LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALA 480
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
144-629 |
5.49e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 82.68 E-value: 5.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 144 SDILVVTTKASYLEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEER 223
Cdd:COG1196 302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 224 EEVKRRMEESTARLLQLEEDLigvtqkgLQKETELDCLKDRVKKLNLEKEALEGQLKNEKDEKELYKIHLKNRELENTKL 303
Cdd:COG1196 382 EELAEELLEALRAAAELAAQL-------EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 304 SAELQMLKSVDVNKENTIAQLKDELARVKSCLAEKEKQHRQLL-ANSSPSGESKALREqLRQKEEQLQATQQQANMLKAE 382
Cdd:COG1196 455 EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLeAEADYEGFLEGVKA-ALLLAGLRGLAGAVAVLIGVE 533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 383 LRDSSNARDRSMAELYRIRVE--------AETLKKgQADARAECSRLEQQLEEMKSSTQQEAQCKESDVLAVAELQREVE 454
Cdd:COG1196 534 AAYEAALEAALAAALQNIVVEddevaaaaIEYLKA-AKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREAD 612
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 455 DLRLRLQMAAEHYKDKYKECQKLQKQVVKFNEQQGVKRSPGSDAAAGPLSASpeasapGSPSTSDAVLDAIIHGRLKSSS 534
Cdd:COG1196 613 ARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTG------GSRRELLAALLEAEAELEELAE 686
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 535 KELDKNDKYRKCKQMLNEERERCSMITDELTKMEVKLREQMKTNESLRMQLAAEEDRYKSQVAEKGRELKELKDSLFVLT 614
Cdd:COG1196 687 RLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELE 766
|
490
....*....|....*..
gi 1207119093 615 KEKEKLEGQLQK--SVN 629
Cdd:COG1196 767 RELERLEREIEAlgPVN 783
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
157-460 |
2.44e-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: 80.50 E-value: 2.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 157 EQKMEQIQQEKKELLENLDLLQKER------DELIDEKNRLE-----KEYEQERESSAQLRKDVQELQLSAQSLQEEREE 225
Cdd:TIGR02169 183 EENIERLDLIIDEKRQQLERLRRERekaeryQALLKEKREYEgyellKEKEALERQKEAIERQLASLEEELEKLTEEISE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 226 VKRRMEESTARLLQLEEDLIGVTqkglqkETELDCLKDRVKKLNLEKEALEGQLKNEKDEKELYKIHLKNRELENTKLSA 305
Cdd:TIGR02169 263 LEKRLEEIEQLLEELNKKIKDLG------EEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 306 ELQMLksvdvnkENTIAQLKDELARVKSCLAEKEKQHRQLLAN-SSPSGESKALREQLRQKEEQLQATQQQANMLKAELR 384
Cdd:TIGR02169 337 EIEEL-------EREIEEERKRRDKLTEEYAELKEELEDLRAElEEVDKEFAETRDELKDYREKLEKLKREINELKRELD 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 385 DSSNARDRSMAELYRIRVEAETLKKGQA-------DARAECSRLEQQLEEMKSSTQQEAQCKESDVLAVAELQREVEDLR 457
Cdd:TIGR02169 410 RLQEELQRLSEELADLNAAIAGIEAKINeleeekeDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQ 489
|
...
gi 1207119093 458 LRL 460
Cdd:TIGR02169 490 REL 492
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
156-456 |
3.48e-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: 80.10 E-value: 3.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 156 LEQKMEQIQ--QEKKELLENLDLlqkerDELIDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEEREEVKRRMEES 233
Cdd:TIGR02168 205 LERQAEKAEryKELKAELRELEL-----ALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 234 TARLLQLEEDLIGVTQKGLQKETELDCLKDRVKKLNLEKEALEGQLKNEKDEKELYKihlknreLENTKLSAELQMLKSV 313
Cdd:TIGR02168 280 EEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELA-------EELAELEEKLEELKEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 314 DVNKENTIAQLKDELARVKSCLAEKEKQHRQLLAN-SSPSGESKALREQLRQKEEQLQATQQQANMLKAELRD-----SS 387
Cdd:TIGR02168 353 LESLEAELEELEAELEELESRLEELEEQLETLRSKvAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEEllkklEE 432
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207119093 388 NARDRSMAELYRIRVEAETLKKGQADARAECSRLEQQLEEMKS---STQQEAQCKESDVLAVAELQREVEDL 456
Cdd:TIGR02168 433 AELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQaldAAERELAQLQARLDSLERLQENLEGF 504
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
178-487 |
6.06e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 76.25 E-value: 6.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 178 QKERDELIDEKNRLEKEYEQERESSAQLRKDVQElqlsaqsLQEEREEVKRRMEESTARLLQLEEDLIGVTQKGLQKETE 257
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEE-------LEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 258 LDCLKDRVKKLNLEKEALEGQLKNEKDEKELYKIHLKNRELENTKLSAELQMLKSVDVNKENTIAQLKDELARVKSCLAE 337
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLES 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 338 KEKQ-HRQLLANSSPSGESKALREQLRQKEEQLQATQQQANMLKAELRDSSNARDRSMAELYRIRVEAETLKKGQADARA 416
Cdd:TIGR02168 829 LERRiAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207119093 417 ECSRLEQQLEEMKSSTQQEAQCKESDVLAVAELQREV-EDLRLRLQMAAEHYKDKYKECQKLQKQVVKFNEQ 487
Cdd:TIGR02168 909 KRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLsEEYSLTLEEAEALENKIEDDEEEARRRLKRLENK 980
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
133-415 |
4.06e-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: 4.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 133 EELLTMEDEGGSDILVVTTKASYLEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQEl 212
Cdd:TIGR02168 242 EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE- 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 213 qlsaqsLQEEREEVKRRMEESTARLLQLEEDLigvtqkgLQKETELDCLKDRVKKLNLEKEALEGQLKNEKDEKELYKIH 292
Cdd:TIGR02168 321 ------LEAQLEELESKLDELAEELAELEEKL-------EELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 293 LKNRELENTKLSAELQMLksvdvnkENTIAQLKDELARVKSCLAEKEKQhRQLLANSSPSGESKALREQLRQKEEQLQAT 372
Cdd:TIGR02168 388 VAQLELQIASLNNEIERL-------EARLERLEDRRERLQQEIEELLKK-LEEAELKELQAELEELEEELEELQEELERL 459
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1207119093 373 QQQANMLKAELRDSSNARDRSMAELYRIRVEAETLKKGQADAR 415
Cdd:TIGR02168 460 EEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLE 502
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
114-481 |
6.35e-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: 72.79 E-value: 6.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 114 GEIRGASTPFQFRANSPTE--EELLTM-EDEGGSDILVvttkaSYLEQKMEQIQQEKKELLENLDLLQKERDELIDEKNR 190
Cdd:TIGR02169 653 GAMTGGSRAPRGGILFSRSepAELQRLrERLEGLKREL-----SSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQ 727
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 191 LEKEYEQERESSAQLRKDVQELQlsaqslqEEREEVKRRMEESTARLLQLEEDL------------------IGVTQKGL 252
Cdd:TIGR02169 728 LEQEEEKLKERLEELEEDLSSLE-------QEIENVKSELKELEARIEELEEDLhkleealndlearlshsrIPEIQAEL 800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 253 QK--------ETELDCLKDRVKKLNLEKEALEGQLKNEKDEKELYKIHLKNRELENTKLSAELQMLKSVDVNKENTIAQL 324
Cdd:TIGR02169 801 SKleeevsriEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDL 880
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 325 KDELARVKSCLAEKEKQHRQLlanSSPSGESKALREQLRQKEEQLQATQQQANMLKAELRDSSNARDRSMAELYRIRVEA 404
Cdd:TIGR02169 881 ESRLGDLKKERDELEAQLREL---ERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQ 957
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207119093 405 ETLKKGQADARAecsrleqqLEEMKSSTQQEAQckesdvlAVAELQREVEDLRLRLQMAAEHYKDKYKECQKLQKQV 481
Cdd:TIGR02169 958 AELQRVEEEIRA--------LEPVNMLAIQEYE-------EVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
148-610 |
1.17e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 71.99 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 148 VVTTKASYLEQKMEQIQQ-EKKELLENLDLLQKERDELIDEKNRLEK-----------------EYEQERESSAQLRKDV 209
Cdd:PRK02224 181 VLSDQRGSLDQLKAQIEEkEEKDLHERLNGLESELAELDEEIERYEEqreqaretrdeadevleEHEERREELETLEAEI 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 210 QELQLSAQSLQEEREEVKRRMEESTARLLQLEEDLIGVTQKGLQKETELDCLKDRVKKLNLEKEALEGQLKNE------- 282
Cdd:PRK02224 261 EDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECrvaaqah 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 283 KDEKELYKIHLKNRELENTKLSAELQMLksvdvnkENTIAQLKDELARVKSCLAEKEKQHRQLLA--NSSPS--GESKAL 358
Cdd:PRK02224 341 NEEAESLREDADDLEERAEELREEAAEL-------ESELEEAREAVEDRREEIEELEEEIEELRErfGDAPVdlGNAEDF 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 359 REQLRqkeEQLQATQQQANMLKAELRDSSNARDRSMA---------------------ELYRIRVEAETLKKGQADARAE 417
Cdd:PRK02224 414 LEELR---EERDELREREAELEATLRTARERVEEAEAlleagkcpecgqpvegsphveTIEEDRERVEELEAELEDLEEE 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 418 CSRLEQQLEEMKSSTQQEAQckesdvlaVAELQREVEDLRLRLQMAAEHYKDKYKECQKLQKQVVKFNEQQGVKRspgSD 497
Cdd:PRK02224 491 VEEVEERLERAEDLVEAEDR--------IERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKR---EA 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 498 AAAGPLSASPEASAPGSPSTSDAVLDAIIHgRLKSSSKELDKNDKYRKCKQMLNEERErcsmitdELTKMEVKLREQMKT 577
Cdd:PRK02224 560 AAEAEEEAEEAREEVAELNSKLAELKERIE-SLERIRTLLAAIADAEDEIERLREKRE-------ALAELNDERRERLAE 631
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1207119093 578 NESLRMQLAAE--EDR-------------YKSQVAEKGRELKELKDSL 610
Cdd:PRK02224 632 KRERKRELEAEfdEARieearedkeraeeYLEQVEEKLDELREERDDL 679
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
221-465 |
3.95e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.35 E-value: 3.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 221 EEREEVKRRMEESTARLLQLEeDLIGvtqkglqketELDclkDRVKKLNLEKEALE--GQLKNEKDEKELYKIHLKNREL 298
Cdd:COG1196 172 ERKEEAERKLEATEENLERLE-DILG----------ELE---RQLEPLERQAEKAEryRELKEELKELEAELLLLKLREL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 299 EntklsAELQMLKSVDVNKENTIAQLKDELARVKSCLAEKEKQHRQLlansspSGESKALREQLRQKEEQLQATQQQANM 378
Cdd:COG1196 238 E-----AELEELEAELEELEAELEELEAELAELEAELEELRLELEEL------ELELEEAQAEEYELLAELARLEQDIAR 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 379 LKAELRDSSNARDRSMAELYRIRVEAETLKKGQADARAECSRLEQQLEEMKSSTQQEAQCKESDVLAVAELQREVEDLRL 458
Cdd:COG1196 307 LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386
|
....*..
gi 1207119093 459 RLQMAAE 465
Cdd:COG1196 387 ELLEALR 393
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
156-636 |
5.41e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 69.71 E-value: 5.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 156 LEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEY---EQERESSAQLRKDVQELQLSAQSLQEEREEVKRRMEE 232
Cdd:PRK03918 191 IEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVkelEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 233 STARLLQLEE------DLIGVTQKGLQKETELDCLKDRVKKLNLEKEALEGQLKN--------EKDEKELYKIHLKNREL 298
Cdd:PRK03918 271 LKKEIEELEEkvkelkELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGieerikelEEKEERLEELKKKLKEL 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 299 ENTKLSAE-----LQMLKSVDVNKEN--------TIAQLKDELARVKSCLAEKEKQHRQLLANSspsGESKALREQLRQK 365
Cdd:PRK03918 351 EKRLEELEerhelYEEAKAKKEELERlkkrltglTPEKLEKELEELEKAKEEIEEEISKITARI---GELKKEIKELKKA 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 366 EEQLQATQQQANMLKAELRDSSNAR--DRSMAELYRIRVEAETLKKGQADARAECSRLEQQLEemksstqqeaqcKESDV 443
Cdd:PRK03918 428 IEELKKAKGKCPVCGRELTEEHRKEllEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLK------------KESEL 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 444 LAVAELQREVEDLRLRLQ-MAAEHYKDKYKECQKLQKQVVKFN-EQQGVKRSPGSDAAAGPLSASPEaSAPGSPSTSDAV 521
Cdd:PRK03918 496 IKLKELAEQLKELEEKLKkYNLEELEKKAEEYEKLKEKLIKLKgEIKSLKKELEKLEELKKKLAELE-KKLDELEEELAE 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 522 LDAIIHGRLKSSSKELDKN--------DKY---RKCKQMLNEERERCSMITDELTKMEVKLREQMKTNESLRMQLAAEED 590
Cdd:PRK03918 575 LLKELEELGFESVEELEERlkelepfyNEYlelKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEK 654
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1207119093 591 RY-KSQVAEKGRELKELKDSLFVLTKEKEKLEGQLQ---KSVNREEEQKD 636
Cdd:PRK03918 655 KYsEEEYEELREEYLELSRELAGLRAELEELEKRREeikKTLEKLKEELE 704
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
132-638 |
6.92e-12 |
|
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: 69.23 E-value: 6.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 132 EEELLTMEDEGGSDILVVTTKASYLEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQE 211
Cdd:TIGR00618 353 QEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQ 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 212 LQLsaqslQEEREEVKRRMEESTARLLQLEEDLIGVTQKGLQKETELDCLKDRVKKLNLEKEALEGQLKNEKDEKEL--- 288
Cdd:TIGR00618 433 QEL-----QQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCplc 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 289 -----YKIHLK---NRELENTKLSAELQMLKSVDVNKENTIAQLKDELARVKSCLAEKEKQHRQLLANSSPSGESKALRE 360
Cdd:TIGR00618 508 gscihPNPARQdidNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIP 587
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 361 QLRQKEEQLQATQQQANMLKAELRDSSNARDRSM---AELYRIRVEAETLKKGQADARAECSRLEQQL------EEMKSS 431
Cdd:TIGR00618 588 NLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLqpeQDLQDVRLHLQQCSQELALKLTALHALQLTLtqervrEHALSI 667
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 432 TQQEAQCKESDVLAVAELQREVEDLRLRLQMAAEHYKDKYKECQKLQKQVVKFNEQQGVKRSPGSDAAAGPLSASpeASA 511
Cdd:TIGR00618 668 RVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALN--QSL 745
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 512 PGSPSTSDAVLDAIIHGRLKSSSK---ELDKNDKYRKCKQMLNEERERCSMITDELTKMEVKLREQMKTNESLRM----Q 584
Cdd:TIGR00618 746 KELMHQARTVLKARTEAHFNNNEEvtaALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNlqceT 825
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1207119093 585 LAAEEDRYKSQVAEKGRELKELKDSLFVLTKEKEKLEGQLQKSVNREEEQKDSN 638
Cdd:TIGR00618 826 LVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLN 879
|
|
| Zn-C2H2_TAX1BP1_rpt2 |
cd21970 |
second C2H2-type zinc binding domain found in tax1-binding protein 1 (TAX1BP1) and similar ... |
790-816 |
7.55e-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: 7.55e-12
10 20
....*....|....*....|....*..
gi 1207119093 790 KICPMCSEQFPLDCDQQLFEKHVLTHF 816
Cdd:cd21970 1 KVCPMCSEQFPPDCDQQVFERHVQTHF 27
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
166-467 |
8.10e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 69.17 E-value: 8.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 166 EKKELLENLDLLQKERDELidekNRLEKEYEQERESSAQLRkDVQELQLSAQSLQEEREEVKRRMEESTARLLQLEEDLI 245
Cdd:COG4913 219 EEPDTFEAADALVEHFDDL----ERAHEALEDAREQIELLE-PIRELAERYAAARERLAELEYLRAALRLWFAQRRLELL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 246 gvtqkglqkETELDCLKDRVKKLNLEKEALEGQLKNEKDEKelykihlknRELENTKLSAELQMLKSVdvnkENTIAQLK 325
Cdd:COG4913 294 ---------EAELEELRAELARLEAELERLEARLDALREEL---------DELEAQIRGNGGDRLEQL----EREIERLE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 326 DELARVKsclaEKEKQHRQLLAnsspsgeskALREQLRQKEEQLQATQQQAnmlKAELRDSSNARDRSMAELYRIRVEAE 405
Cdd:COG4913 352 RELEERE----RRRARLEALLA---------ALGLPLPASAEEFAALRAEA---AALLEALEEELEALEEALAEAEAALR 415
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207119093 406 TLKKGQADARAECSRLEQQ-------LEEMKSSTQQEAQCKESDVLAVAELQrEVEDLRLRLQMAAEHY 467
Cdd:COG4913 416 DLRRELRELEAEIASLERRksniparLLALRDALAEALGLDEAELPFVGELI-EVRPEEERWRGAIERV 483
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
172-487 |
9.58e-12 |
|
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: 68.93 E-value: 9.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 172 ENLDLLQKERDELIDEKNRLEKEYEQE---RESSAQLRKdvQELQLSAQSLQEEREEvKRRMEESTARLLQLEEDLigvt 248
Cdd:TIGR02168 186 ENLDRLEDILNELERQLKSLERQAEKAeryKELKAELRE--LELALLVLRLEELREE-LEELQEELKEAEEELEEL---- 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 249 QKGLQ-KETELDCLKDRVKKLNLEKEALEG---QLKNEKDEKELYKIHLKNRE--LENTKLSAELQMLKSvdvnkENTIA 322
Cdd:TIGR02168 259 TAELQeLEEKLEELRLEVSELEEEIEELQKelyALANEISRLEQQKQILRERLanLERQLEELEAQLEEL-----ESKLD 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 323 QLKDELARVKSCLAEKEKQHRQLLAnsspsgESKALREQLRQKEEQLQATQQQANMLKAELRDssnardrsmaelyrirv 402
Cdd:TIGR02168 334 ELAEELAELEEKLEELKEELESLEA------ELEELEAELEELESRLEELEEQLETLRSKVAQ----------------- 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 403 eaetLKKGQADARAECSRLEQQLEEMKSS-----TQQEAQCKESDVLAVAELQREVEDLRLRLQMAAEHYKDKYKECQKL 477
Cdd:TIGR02168 391 ----LELQIASLNNEIERLEARLERLEDRrerlqQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEEL 466
|
330
....*....|
gi 1207119093 478 QKQVVKFNEQ 487
Cdd:TIGR02168 467 REELEEAEQA 476
|
|
| Zn-C2H2_12 |
pfam18112 |
Autophagy receptor zinc finger-C2H2 domain; This domain is found in calcium-binding and ... |
763-789 |
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 1207119093 763 KRCPLCEVIFPPHYDQSKFEEHVESHW 789
Cdd:pfam18112 1 KECPLCGEMFSPNIDQSEFEEHVESHF 27
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
156-646 |
3.87e-11 |
|
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: 66.92 E-value: 3.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 156 LEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDvQELQLSAQSLQEEREEVKRRMEESTA 235
Cdd:TIGR00618 196 AELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQK-REAQEEQLKKQQLLKQLRARIEELRA 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 236 RLLQLEEdligvtqkgLQKETELDClkdRVKKLNLEKEALEgqlKNEKDEKELYKiHLKNRELENTKLSAELQMLksvdV 315
Cdd:TIGR00618 275 QEAVLEE---------TQERINRAR---KAAPLAAHIKAVT---QIEQQAQRIHT-ELQSKMRSRAKLLMKRAAH----V 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 316 NKENTIAQLKDELARVKSCLAEKEKQHRQLLANSSPSGESKALREQLRQKEEQLQATQQQANMLKAELRDSSNARDRSMA 395
Cdd:TIGR00618 335 KQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDT 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 396 ELYRIRVeaetLKKGQADARAECSRLEQQLEEMKSSTQQEAQCKESDVLAVAELQREVEDLRLRLQmAAEHYKDKYKECQ 475
Cdd:TIGR00618 415 RTSAFRD----LQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQ-TKEQIHLQETRKK 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 476 KLQKQVVkfNEQQGVKRspgsDAAAGPLSASPEASAPGSPSTSDAVLDAIIHGRLKssskeldkndkyrkckqmLNEERE 555
Cdd:TIGR00618 490 AVVLARL--LELQEEPC----PLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQ------------------LETSEE 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 556 RCSMITDELTKMEVKLREQMKTNESLRMQLAAEEDRYKSQVAEKGRELKELKDSLFVLTKEKEKLEGQLQksvnREEEQK 635
Cdd:TIGR00618 546 DVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQH----ALLRKL 621
|
490
....*....|.
gi 1207119093 636 DSNLDVQSVFL 646
Cdd:TIGR00618 622 QPEQDLQDVRL 632
|
|
| Zn-C2H2_TAX1BP1_rpt1 |
cd21969 |
first C2H2-type zinc binding domain found in tax1-binding protein 1 (TAX1BP1) and similar ... |
765-788 |
4.38e-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: 4.38e-11
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
146-401 |
5.51e-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: 5.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 146 ILVVTTKASYLEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEEREE 225
Cdd:COG4942 8 ALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 226 VKRRMEESTARLLQLEEDLIGVTQKgLQKETELDCLkdrvkKLNLEKEALEGQLKNEKDEKELYKiHLKNRELENTKLSA 305
Cdd:COG4942 88 LEKEIAELRAELEAQKEELAELLRA-LYRLGRQPPL-----ALLLSPEDFLDAVRRLQYLKYLAP-ARREQAEELRADLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 306 ELQMLKSVDVNKENTIAQLKDELARVKSCLAEKEKQHRQLLANSspSGESKALREQLRQKEEQLQATQQQANMLKAELRD 385
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARL--EKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
250
....*....|....*.
gi 1207119093 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 ... |
127-470 |
8.92e-11 |
|
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: 8.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 127 ANSPTEEELLTMEDEGGSDILVVTTKAsyLEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLR 206
Cdd:pfam02463 148 AMMKPERRLEIEEEAAGSRLKRKKKEA--LKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEY 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 207 ---KDVQELQLSAQSLQEEREEVKRRMEESTARLLQLEEDLIGVTQKGLQKETELDCL-KDRVKKLNLEKEALEGQLKNE 282
Cdd:pfam02463 226 llyLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLqEEELKLLAKEEEELKSELLKL 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 283 KDEKELYKIHLKNRELENTKLSAELQMLKSVDVNKENtiaQLKDELARVKSCLAEKEKQHRQLLANSSPSGESKALREQL 362
Cdd:pfam02463 306 ERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEK---ELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 363 RQKEEQLQATQQQANMLKAELRDSsnarDRSMAELYRIRVEAETLKKGQADARAECSRLEQQLEEMKSSTQQEAQCKESD 442
Cdd:pfam02463 383 SERLSSAAKLKEEELELKSEEEKE----AQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQEL 458
|
330 340
....*....|....*....|....*....
gi 1207119093 443 VLAVAELQRE-VEDLRLRLQMAAEHYKDK 470
Cdd:pfam02463 459 KLLKDELELKkSEDLLKETQLVKLQEQLE 487
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
155-452 |
9.52e-11 |
|
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: 65.86 E-value: 9.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 155 YLEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQELQ--LSAQSLQ------EEREEV 226
Cdd:TIGR02169 213 YQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEqlLEELNKKikdlgeEEQLRV 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 227 KRRMEESTARLLQLEEDLIGVTQKGLQKETELDCLKDRVKKLNLEKEALEGQLKNEKDEKELYKIHLKNRELENTKLSAE 306
Cdd:TIGR02169 293 KEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAE 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 307 LQmlksvDVNKENtiAQLKDELARVKSCLAEKEKQHRQLLANSSPSGE-SKALREQLRQKEEQLQATQQQANMLKAELRD 385
Cdd:TIGR02169 373 LE-----EVDKEF--AETRDELKDYREKLEKLKREINELKRELDRLQEeLQRLSEELADLNAAIAGIEAKINELEEEKED 445
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 386 SSnardrsmAELYRIRVEAETLKKGQADARAECSRLEQ---QLEEMKSSTQQEAQCKESDVLAVAELQRE 452
Cdd:TIGR02169 446 KA-------LEIKKQEWKLEQLAADLSKYEQELYDLKEeydRVEKELSKLQRELAEAEAQARASEERVRG 508
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
152-646 |
1.91e-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: 64.75 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 152 KASYLEQKMEQIQQEKKELLENLDLLQKERDELID-EKNRLEKEYEQERESSAQLR-------KDVQELQLSAQSL---- 219
Cdd:pfam15921 161 KEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDfEEASGKKIYEHDSMSTMHFRslgsaisKILRELDTEISYLkgri 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 220 ---QEEREEVKRRMEESTARLLQLEEDLIgvTQKGLQKETELDCLKDRVKKLNLEKEALEGQL----KNEKDEKELYKIH 292
Cdd:pfam15921 241 fpvEDQLEALKSESQNKIELLLQQHQDRI--EQLISEHEVEITGLTEKASSARSQANSIQSQLeiiqEQARNQNSMYMRQ 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 293 LKNRELENTKLSAELQMLKSVdvnKENTIAQLKDELARVKSCLAEKEKQHRQLlansspSGESKALREQLRQKEEQLQAT 372
Cdd:pfam15921 319 LSDLESTVSQLRSELREAKRM---YEDKIEELEKQLVLANSELTEARTERDQF------SQESGNLDDQLQKLLADLHKR 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 373 QQQANMLKAElrdssNAR--DRSMAELYRIrveaETLKKGQADARAECSRLEQQLEEMKSSTQQEAQCKESDVLAVAELQ 450
Cdd:pfam15921 390 EKELSLEKEQ-----NKRlwDRDTGNSITI----DHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESL 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 451 REVEDLRLRLQMAAEhykdkykecqKLQKQVVKFNEQQGVKRSpgSDAAAGPLSASPEASAPGSPSTSDAVLDaiIHGRL 530
Cdd:pfam15921 461 EKVSSLTAQLESTKE----------MLRKVVEELTAKKMTLES--SERTVSDLTASLQEKERAIEATNAEITK--LRSRV 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 531 KSSSKELdkndkyrkckQMLNEERERCSMITDELTKMEVKLREQMKTNESLR------MQLAAEEDRYKSQV-AEKGREL 603
Cdd:pfam15921 527 DLKLQEL----------QHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRqqienmTQLVGQHGRTAGAMqVEKAQLE 596
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1207119093 604 KELKDSLFVLtKEKEKLEGQLQKSVnREEEQKDSNLDVQSVFL 646
Cdd:pfam15921 597 KEINDRRLEL-QEFKILKDKKDAKI-RELEARVSDLELEKVKL 637
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
133-625 |
1.95e-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: 64.69 E-value: 1.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 133 EELLTMEDEGGSDILVVTTKASYLEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQEL 212
Cdd:TIGR02168 354 ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 213 QLSAqsLQEEREEVKRRMEESTARLLQLEEDLIGVTQKGLQKETELDCLKDRVKKLNLEKEALEGQLKNEKDEKELYKIH 292
Cdd:TIGR02168 434 ELKE--LQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKAL 511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 293 LKNRELEN---------------------TKLSAELQMLKSVDVNKEN-TIAQLKDELARVKSCLAEKEKQHRQLLANSS 350
Cdd:TIGR02168 512 LKNQSGLSgilgvlselisvdegyeaaieAALGGRLQAVVVENLNAAKkAIAFLKQNELGRVTFLPLDSIKGTEIQGNDR 591
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 351 PSGESK--------------------------------------ALREQLR----------------------------- 363
Cdd:TIGR02168 592 EILKNIegflgvakdlvkfdpklrkalsyllggvlvvddldnalELAKKLRpgyrivtldgdlvrpggvitggsaktnss 671
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 364 ---QKEEQLQATQQQAnMLKAELRDSSNARDRSMAELYRIRVEAETLKKGQADARAECSRLEQQLEEMKSSTQQEAQCKE 440
Cdd:TIGR02168 672 ileRRREIEELEEKIE-ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIA 750
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 441 SDVLAVAELQREVEDLRLRLQMAAEHYKDKYKECQKLQKQVVKFNEQQGVKRSPGSD--AAAGPLSASPEASAPGSPSTS 518
Cdd:TIGR02168 751 QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDElrAELTLLNEEAANLRERLESLE 830
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 519 DAVLDAIIHGRLKSSSKElDKNDKYRKCKQMLNEERERCSMITDELTKMEV---KLREQMKTNESLRMQLAAEEDRYKSQ 595
Cdd:TIGR02168 831 RRIAATERRLEDLEEQIE-ELSEDIESLAAEIEELEELIEELESELEALLNeraSLEEALALLRSELEELSEELRELESK 909
|
570 580 590
....*....|....*....|....*....|
gi 1207119093 596 VAEKGRELKELKDSLFVLTKEKEKLEGQLQ 625
Cdd:TIGR02168 910 RSELRRELEELREKLAQLELRLEGLEVRID 939
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
186-432 |
2.22e-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: 63.24 E-value: 2.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 186 DEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEEREEVKRRMEESTARLLQLEedligvtqkglqkeTELDCLKDRV 265
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALE--------------QELAALEAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 266 KKLNLEKEALEGQLKNEKDE-KELYKIHLKNRELENTKLsaelqMLKSVDVNKENTIAQLKDELARVKSCLAEKEKQHRQ 344
Cdd:COG4942 86 AELEKEIAELRAELEAQKEElAELLRALYRLGRQPPLAL-----LLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 345 LLANSSpsgesKALREQLRQKEEQLQATQQQANMLKAELRDSSNARDRSMAELYRIRVEAETLKKGQADARAECSRLEQQ 424
Cdd:COG4942 161 ELAALR-----AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
....*...
gi 1207119093 425 LEEMKSST 432
Cdd:COG4942 236 AAAAAERT 243
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
156-491 |
2.88e-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: 63.89 E-value: 2.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 156 LEQKMEQIQQEKKEL--LENldllQKERDELIDEKNRLEKEYEQERESSAQLRKDVQelqlSAQSLQEEREEVKRRMEES 233
Cdd:TIGR04523 283 IKELEKQLNQLKSEIsdLNN----QKEQDWNKELKSELKNQEKKLEEIQNQISQNNK----IISQLNEQISQLKKELTNS 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 234 TARLLQLEEDLIGVTQKGLQKETELDCLKDRVKKLNLEKEALEGQLKNEKDEKELYKIHLKNRELENTKLSAELQMLKSV 313
Cdd:TIGR04523 355 ESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKET 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 314 DVNKENTIAQLKDELA----RVKSCLAEKEKQHRQLlanSSPSGESKALREQLRQKEEQLQATQQQANMLKAELRDSSNA 389
Cdd:TIGR04523 435 IIKNNSEIKDLTNQDSvkelIIKNLDNTRESLETQL---KVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEK 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 390 RDRSMAELYRIRVEAETLKKGQADARAECSRLEQQLEEMKSSTQQEAQCKESDvlavaELQREVEDLRLRLQMAAEHYKD 469
Cdd:TIGR04523 512 VKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEID-----EKNKEIEELKQTQKSLKKKQEE 586
|
330 340
....*....|....*....|..
gi 1207119093 470 KYKECQKLQKQVVKFNEQQGVK 491
Cdd:TIGR04523 587 KQELIDQKEKEKKDLIKEIEEK 608
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
156-635 |
5.83e-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: 63.14 E-value: 5.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 156 LEQKMEQIQQEKKELLENLDLLQKE--------------RDELIDE------KNRLEKEYEQERESSAQLRKDVQELQLS 215
Cdd:TIGR00606 520 LDQEMEQLNHHTTTRTQMEMLTKDKmdkdeqirkiksrhSDELTSLlgyfpnKKQLEDWLHSKSKEINQTRDRLAKLNKE 599
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 216 AQSLQEEREEVKRRMEESTARLLQLEEDLIGVTQKGlQKETELDCLKDRVKKLNLEKEALEGQlknekdeKELYKIHLKN 295
Cdd:TIGR00606 600 LASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQ-DEESDLERLKEEIEKSSKQRAMLAGA-------TAVYSQFITQ 671
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 296 RELENT----------KLSAELQMLKSvdvNKENTIAQLKDELARVKSCLAEKEKQHRQLLansspsGESKALREQLRQK 365
Cdd:TIGR00606 672 LTDENQsccpvcqrvfQTEAELQEFIS---DLQSKLRLAPDKLKSTESELKKKEKRRDEML------GLAPGRQSIIDLK 742
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 366 EEQLQATQQQANMLKAELRDSSNARDRSMAELYRIRVEAETLKKGQADARAeCSRLEQQLEEM-KSSTQQEAQCKESDV- 443
Cdd:TIGR00606 743 EKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTI-MERFQMELKDVeRKIAQQAAKLQGSDLd 821
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 444 LAVAELQREVEDLRLRLQMAAEHYKDKYKECQKLQKQVV----KFNEQQGVKRSPGSDAA-AGPLSASPEASAPGSPSTS 518
Cdd:TIGR00606 822 RTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQhlksKTNELKSEKLQIGTNLQrRQQFEEQLVELSTEVQSLI 901
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 519 DAVLDAiihgRLKSSSKELDKNDKYRKCKQMLNEERERCSMITDELTKMEVKLREQMKTNESLRMQLAAEEDRYKSQvae 598
Cdd:TIGR00606 902 REIKDA----KEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQ--- 974
|
490 500 510
....*....|....*....|....*....|....*..
gi 1207119093 599 KGRELKELKDSLFVLTKEKEKLEGQLQKSVNREEEQK 635
Cdd:TIGR00606 975 KETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQK 1011
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
156-363 |
6.04e-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: 6.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 156 LEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEEREEVKRRMEESTA 235
Cdd:TIGR02169 327 LEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKR 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 236 RLLQLEEDLIGVTQKGLQKETELDCLKDRVKKLNLEKEALegQLKNEKDEKELykihlknrelenTKLSAELQMLKSVDV 315
Cdd:TIGR02169 407 ELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDK--ALEIKKQEWKL------------EQLAADLSKYEQELY 472
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1207119093 316 NKENTIAQLKDELARVKSCLAEKEKQHRQLlanSSPSGESKALREQLR 363
Cdd:TIGR02169 473 DLKEEYDRVEKELSKLQRELAEAEAQARAS---EERVRGGRAVEEVLK 517
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
151-377 |
9.00e-10 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 61.38 E-value: 9.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 151 TKASYLEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEEREEVKRRM 230
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 231 EESTARLLQLEEdLIGVTQKG--LQKETELDCLKDRVKKLNLEKEALEGQLKNEKD--EKELYKIHLKNRELENTKLSAE 306
Cdd:COG3883 96 YRSGGSVSYLDV-LLGSESFSdfLDRLSALSKIADADADLLEELKADKAELEAKKAelEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207119093 307 LQMLKsvdvnKENTIAQLKDELARVKSCLAEKEKQHRQLLANSSPSGESKALREQLRQKEEQLQATQQQAN 377
Cdd:COG3883 175 AQQAE-----QEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
156-467 |
1.28e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.71 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 156 LEQKMEQIQQEKKELLENLDLLQ---KERDELIDEKNRLEKEYEQ--------ERESSAQLRKDVQELQLSAQSLQEERE 224
Cdd:COG4717 130 LYQELEALEAELAELPERLEELEerlEELRELEEELEELEAELAElqeeleelLEQLSLATEEELQDLAEELEELQQRLA 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 225 EVKRRMEESTARLLQLEEDLigvtqKGLQKETELDCLKDRVKKLN----------------------------------- 269
Cdd:COG4717 210 ELEEELEEAQEELEELEEEL-----EQLENELEAAALEERLKEARlllliaaallallglggsllsliltiagvlflvlg 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 270 ---LEKEALEGQLKNEKDEKELYKIHLKNRELENTKLSAELQMLKSVDVNKENTIAQLKDELARVKSCLAEKEKQHRQL- 345
Cdd:COG4717 285 llaLLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELq 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 346 ----------LANSSPSGESKALREQLRQKEEQLQATQQQANmLKAELRDSSNARDRSM---------AELYRIRVEAET 406
Cdd:COG4717 365 leeleqeiaaLLAEAGVEDEEELRAALEQAEEYQELKEELEE-LEEQLEELLGELEELLealdeeeleEELEELEEELEE 443
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207119093 407 LKKGQADARAECSRLEQQLEEMKSSTqqeaqckesdvlAVAELQREVEDLRLRLQMAAEHY 467
Cdd:COG4717 444 LEEELEELREELAELEAELEQLEEDG------------ELAELLQELEELKAELRELAEEW 492
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
132-337 |
1.31e-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: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 132 EEELLTMEDEGGSDILVVTTKASYLEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQE 211
Cdd:TIGR02168 763 IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLED 842
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 212 LQLSAQSLQEEREEVKRRMEESTARLLQLEEDLIGVTQKGLQKETELDCLKDRVKKLNLEKEALEGQLKNEKDE-----K 286
Cdd:TIGR02168 843 LEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRREleelrE 922
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207119093 287 ELYKIHLKNRELENT------KLSAELQMLKSVDVNKENTI----AQLKDELARVKSCLAE 337
Cdd:TIGR02168 923 KLAQLELRLEGLEVRidnlqeRLSEEYSLTLEEAEALENKIeddeEEARRRLKRLENKIKE 983
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
168-626 |
2.21e-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: 2.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 168 KELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEEREEVKRRMEESTARLLQLEEDLIgv 247
Cdd:TIGR04523 207 KKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIK-- 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 248 tqkglQKETELDCLKDRVKKLNLEKEA-----LEGQLKNEKDEKELYKIHLKNRELENTKLSAELQMLKSVDVNKENTIA 322
Cdd:TIGR04523 285 -----ELEKQLNQLKSEISDLNNQKEQdwnkeLKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENS 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 323 QLKDElarvkscLAEKEKQHRQLLA-NSSPSGESKALREQLRQKEEQLQATQQQANMLKAELRDSSNARDRSMAELYRIR 401
Cdd:TIGR04523 360 EKQRE-------LEEKQNEIEKLKKeNQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLK 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 402 VEAETLKKGQADARAECSRLEQQLEEMKSSTQQEAQckesdvlAVAELQREVEDLRLRLQMAAEHYKDKYKECQKLQKQV 481
Cdd:TIGR04523 433 ETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLET-------QLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEK 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 482 VKFNEQQGVKRSPGSDaaagplsaspeasapgSPSTSDAVLDAIIHGRLKSSSKELD--------KNDKYRKCKQMLNEE 553
Cdd:TIGR04523 506 KELEEKVKDLTKKISS----------------LKEKIEKLESEKKEKESKISDLEDElnkddfelKKENLEKEIDEKNKE 569
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207119093 554 RERCSMITDELTKMEVKLREQMKtneslrmQLAAEEDRYKSQVAEKGRELKELKDSLFVLTKEKEKLEGQLQK 626
Cdd:TIGR04523 570 IEELKQTQKSLKKKQEEKQELID-------QKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKN 635
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
157-634 |
2.39e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 61.31 E-value: 2.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 157 EQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQELQlSAQSLQEEREEVKRRMEESTAR 236
Cdd:PTZ00121 1174 DAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVK-KAEEAKKDAEEAKKAEEERNNE 1252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 237 LLQLEEDLIGVTQKGLQKETELDCLK--DRVKKLNLEKEALEGQLKNEKDE-KELYKIHLKNRELENTKLSAELQMLKSV 313
Cdd:PTZ00121 1253 EIRKFEEARMAHFARRQAAIKAEEARkaDELKKAEEKKKADEAKKAEEKKKaDEAKKKAEEAKKADEAKKKAEEAKKKAD 1332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 314 DVNKENTIAQLKDELARVKSCLAEKE--KQHRQLLANSSPSGESKALREQLRQKEEQLQATQQ-----QANMLKAELRDS 386
Cdd:PTZ00121 1333 AAKKKAEEAKKAAEAAKAEAEAAADEaeAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEakkkaEEDKKKADELKK 1412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 387 SNARDRSMAELYRIRVE---AETLKKgQADARAECSRLEQQLEEMKSStqQEAQCKESDVLAVAELQREVEDLRL--RLQ 461
Cdd:PTZ00121 1413 AAAAKKKADEAKKKAEEkkkADEAKK-KAEEAKKADEAKKKAEEAKKA--EEAKKKAEEAKKADEAKKKAEEAKKadEAK 1489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 462 MAAEHYKDKYKECQKLQKQVVKFNEQQGVKRSPGSDAA--AGPLSASPEASAPGSPSTSDAVLDAiihgrlksssKELDK 539
Cdd:PTZ00121 1490 KKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAkkAEEAKKADEAKKAEEKKKADELKKA----------EELKK 1559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 540 NDKYRKCKQMLNEERERCSMI--TDELTKMEVKLREQMKTNESLRMQLAAEEDRYKSQVAEKGRELKELKDSLFVLTKEK 617
Cdd:PTZ00121 1560 AEEKKKAEEAKKAEEDKNMALrkAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLK 1639
|
490
....*....|....*....
gi 1207119093 618 EKLEGQLQKS--VNREEEQ 634
Cdd:PTZ00121 1640 KKEAEEKKKAeeLKKAEEE 1658
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
156-437 |
2.54e-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: 60.80 E-value: 2.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 156 LEQKMEQIQQEKKELLENLDLLQKerdeLIDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEEREEVKRRMEESTA 235
Cdd:TIGR04523 365 LEEKQNEIEKLKKENQSYKQEIKN----LESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNS 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 236 RLLQLEEdligvtqKGLQKETELDCLKDRVKKLNLEKEALEGQLKNEK------------DEKELYKIHLKNRELENT-- 301
Cdd:TIGR04523 441 EIKDLTN-------QDSVKELIIKNLDNTRESLETQLKVLSRSINKIKqnleqkqkelksKEKELKKLNEEKKELEEKvk 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 302 -------KLSAELQMLKSVDVNKENTIAQLKDEL----ARVKSCLAEKEKQHRQllansspsgesKALrEQLRQKEEQLQ 370
Cdd:TIGR04523 514 dltkkisSLKEKIEKLESEKKEKESKISDLEDELnkddFELKKENLEKEIDEKN-----------KEI-EELKQTQKSLK 581
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 371 ATQQQANMLKAELRDSSNARDRSMAELyriRVEAETLKKGQADARAECSRLEQQ---LEEMKSSTQQEAQ 437
Cdd:TIGR04523 582 KKQEEKQELIDQKEKEKKDLIKEIEEK---EKKISSLEKELEKAKKENEKLSSIiknIKSKKNKLKQEVK 648
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
158-638 |
4.32e-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: 4.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 158 QKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEEREEVKRRMEESTARL 237
Cdd:TIGR04523 96 DKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENEL 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 238 LQLEEDLigvtqkgLQKETELDCLKDRVKKLNLEKEALEGQL-KNEKDEKELYKIHLKNRELENT--KLSAELQMLKSVD 314
Cdd:TIGR04523 176 NLLEKEK-------LNIQKNIDKIKNKLLKLELLLSNLKKKIqKNKSLESQISELKKQNNQLKDNieKKQQEINEKTTEI 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 315 VNKENTIAQLKDELARVKSCLAEK--------------EKQHRQL------LANSSPSGESKALREQLRQKEEQLQATQQ 374
Cdd:TIGR04523 249 SNTQTQLNQLKDEQNKIKKQLSEKqkeleqnnkkikelEKQLNQLkseisdLNNQKEQDWNKELKSELKNQEKKLEEIQN 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 375 QAnmlkaelrDSSNARDRSMAElyrirvEAETLKKGQADARAECSRLEQQLEEMKSSTQQEAQCKESDVLAVAELQREVE 454
Cdd:TIGR04523 329 QI--------SQNNKIISQLNE------QISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQIN 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 455 DLRLRLQMAAEHYKDKYKECQKLQKQVVKFNEQQGVKRSPGSDaaagplsaspEASAPGSPSTSDAVLDAIIHgRLKSSS 534
Cdd:TIGR04523 395 DLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIK----------NNSEIKDLTNQDSVKELIIK-NLDNTR 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 535 KELDKN-----DKYRKCKQMLN----EERERCSMItDELTKMEVKLREQMKTNESLRMQLAAEEDRYKSQVAEKGRELKE 605
Cdd:TIGR04523 464 ESLETQlkvlsRSINKIKQNLEqkqkELKSKEKEL-KKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISD 542
|
490 500 510
....*....|....*....|....*....|....*..
gi 1207119093 606 LKDSL----FVLTkeKEKLEGQLQKSVNREEEQKDSN 638
Cdd:TIGR04523 543 LEDELnkddFELK--KENLEKEIDEKNKEIEELKQTQ 577
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
242-636 |
5.33e-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: 5.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 242 EDLIGVTQKGLQKET---ELDCLKDRVKKLNL---EKEALEGQLKNEKDEKELYK-IHLKNRELENTKLSAELQMLKSVD 314
Cdd:TIGR02169 160 DEIAGVAEFDRKKEKaleELEEVEENIERLDLiidEKRQQLERLRREREKAERYQaLLKEKREYEGYELLKEKEALERQK 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 315 VNKENTIAQLKDELARVKSCLAEKEKqhrqllansspsgESKALREQLRQKEEQLQA-TQQQANMLKAELRDSSNAR--- 390
Cdd:TIGR02169 240 EAIERQLASLEEELEKLTEEISELEK-------------RLEEIEQLLEELNKKIKDlGEEEQLRVKEKIGELEAEIasl 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 391 DRSMAELYRirvEAETLKKGQADARAECSRLEQQLEEMKSSTQQEAQCKESDVLAVAELQREVEDLRLRLQMAAEHYKDK 470
Cdd:TIGR02169 307 ERSIAEKER---ELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAET 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 471 YKECQKLQKQVVKFNEQQGvkrspgsdaaagplsaspeasapgspsTSDAVLDAIIHGRLKSSSKELDKNDKYRKCKQML 550
Cdd:TIGR02169 384 RDELKDYREKLEKLKREIN---------------------------ELKRELDRLQEELQRLSEELADLNAAIAGIEAKI 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 551 NEERERCSMITDELTKMEVKLreqmktneslrMQLAAEEDRYKSQVAEKGRELKELKDSLFVLTKEKEKLEGQLQKSVNR 630
Cdd:TIGR02169 437 NELEEEKEDKALEIKKQEWKL-----------EQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEER 505
|
....*.
gi 1207119093 631 EEEQKD 636
Cdd:TIGR02169 506 VRGGRA 511
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
195-635 |
8.02e-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: 59.31 E-value: 8.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 195 YEQERESSAQLRKDVQELQLSAQSLQEEREEVKRRMEESTARLLQLEEDLIgvtqkglQKETELDCLKDRVKKLNLEKEA 274
Cdd:TIGR02169 669 SRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIG-------EIEKEIEQLEQEEEKLKERLEE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 275 LEGQLKNEKDEKElykihlkNRELENTKLSAELQmlksvdvNKENTIAQLKDELARVKSCLAEKEKQHRQllansspsGE 354
Cdd:TIGR02169 742 LEEDLSSLEQEIE-------NVKSELKELEARIE-------ELEEDLHKLEEALNDLEARLSHSRIPEIQ--------AE 799
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 355 SKALREQLRQKEEQLQATQQQanmLKAELRDSSNARDrSMAELYRIRVEAETLKKgqaDARAECSRLEQQLEEMKSStqq 434
Cdd:TIGR02169 800 LSKLEEEVSRIEARLREIEQK---LNRLTLEKEYLEK-EIQELQEQRIDLKEQIK---SIEKEIENLNGKKEELEEE--- 869
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 435 eaqckesdvlaVAELQREVEDLRLRLQMAAEHYKDKYKECQKLQKQVVKFNEQQGVKRSPGSDAAAGPLSASPEASAPGS 514
Cdd:TIGR02169 870 -----------LEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIED 938
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 515 PSTSDavldaiihgrlkssskeldkndkyrkckqmlnEERERCSMITDELTKMEVKLREQMKTNESLRMqLAAEEdryks 594
Cdd:TIGR02169 939 PKGED--------------------------------EEIPEEELSLEDVQAELQRVEEEIRALEPVNM-LAIQE----- 980
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1207119093 595 qVAEKGRELKELKDSLFVLTKEKEklegQLQKSVNREEEQK 635
Cdd:TIGR02169 981 -YEEVLKRLDELKEKRAKLEEERK----AILERIEEYEKKK 1016
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
156-488 |
9.30e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.16 E-value: 9.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 156 LEQKMEQIQQEKKELLENLDLLQKER--------DELIDEKNRLEKEYEQERESSAQLRKDVQELQL----SAQSLQEER 223
Cdd:COG4913 307 LEAELERLEARLDALREELDELEAQIrgnggdrlEQLEREIERLERELEERERRRARLEALLAALGLplpaSAEEFAALR 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 224 EEVKRRMEESTARLLQLEEDL--IGVTQKGLQKE-----TELDCLKDRVKKLNLE----KEALEGQLKNEKDE----KEL 288
Cdd:COG4913 387 AEAAALLEALEEELEALEEALaeAEAALRDLRRElreleAEIASLERRKSNIPARllalRDALAEALGLDEAElpfvGEL 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 289 YKIHLKNRE-----------------------------LENTKLSAELQMLK--------SVDVNKENTIAQ-------- 323
Cdd:COG4913 467 IEVRPEEERwrgaiervlggfaltllvppehyaaalrwVNRLHLRGRLVYERvrtglpdpERPRLDPDSLAGkldfkphp 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 324 ----LKDELAR---VKSCLAEKE-KQHRQ------LLANSSPSGEsKALREQLRQK-------EEQLQATQQQANMLKAE 382
Cdd:COG4913 547 frawLEAELGRrfdYVCVDSPEElRRHPRaitragQVKGNGTRHE-KDDRRRIRSRyvlgfdnRAKLAALEAELAELEEE 625
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 383 LRDSSNARDRSMAELYRIRVEAETLKKGQ---------ADARAECSRLEQQLEEMKSStqqeaqckeSDVLAvaELQREV 453
Cdd:COG4913 626 LAEAEERLEALEAELDALQERREALQRLAeyswdeidvASAEREIAELEAELERLDAS---------SDDLA--ALEEQL 694
|
410 420 430
....*....|....*....|....*....|....*
gi 1207119093 454 EDLRLRLQMAAEHYKDKYKECQKLQKQVVKFNEQQ 488
Cdd:COG4913 695 EELEAELEELEEELDELKGEIGRLEKELEQAEEEL 729
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
156-481 |
1.02e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.01 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 156 LEQKMEQIQQEKKELLENLDLLQK----------------ERDELIDEKNRLEKEYEQEREssaqLRKDVQELQLSAQSL 219
Cdd:COG4717 100 LEEELEELEAELEELREELEKLEKllqllplyqelealeaELAELPERLEELEERLEELRE----LEEELEELEAELAEL 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 220 QEEREEVKRRMEEST-ARLLQLEEDLIGVTQKGLQKETELDCLKDRVKKLNLEKEALEGQLKNEKDEKELYK-------- 290
Cdd:COG4717 176 QEELEELLEQLSLATeEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEarllllia 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 291 ------IHLKNRELENTKLSAELQML--------KSVDVNKENTIAQLKDELARVKSCLA-EKEKQHRQLLANSSPSGES 355
Cdd:COG4717 256 aallalLGLGGSLLSLILTIAGVLFLvlgllallFLLLAREKASLGKEAEELQALPALEElEEEELEELLAALGLPPDLS 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 356 KALREQLRQKEEQLQATQQQANMLKAELRDSSNARDR----------SMAELYRIRVEAETLKkgqaDARAECSRLEQQL 425
Cdd:COG4717 336 PEELLELLDRIEELQELLREAEELEEELQLEELEQEIaallaeagveDEEELRAALEQAEEYQ----ELKEELEELEEQL 411
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1207119093 426 EEMKSSTQQEAqckesDVLAVAELQREVEDLRLRLQMAAEHYKDKYKECQKLQKQV 481
Cdd:COG4717 412 EELLGELEELL-----EALDEEELEEELEELEEELEELEEELEELREELAELEAEL 462
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
215-465 |
1.50e-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: 57.47 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 215 SAQSLQEEREEVKRRMEESTARLLQLEEDLIGVTQKGLQKETELDCLKDRVKKLNLEKEALEGQLKnekdekelykihlk 294
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA-------------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 295 nrelentKLSAELQMLksvdvnkENTIAQLKDELARVkscLAEKEKQHRQ----LLANSSPSGES-------KALREQLR 363
Cdd:COG4942 87 -------ELEKEIAEL-------RAELEAQKEELAEL---LRALYRLGRQpplaLLLSPEDFLDAvrrlqylKYLAPARR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 364 QKEEQLQATQQQANMLKAELRdssnardRSMAELYRIRVEAETLKKGQADARAECSRLEQQLEEMKSSTQQEAQCKESDv 443
Cdd:COG4942 150 EQAEELRADLAELAALRAELE-------AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQE- 221
|
250 260
....*....|....*....|..
gi 1207119093 444 laVAELQREVEDLRLRLQMAAE 465
Cdd:COG4942 222 --AEELEALIARLEAEAAAAAE 241
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
157-626 |
1.75e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.61 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 157 EQKMEQIQQEKKELLENLDLLQ--KERDELIDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEEREEVKRRMEESt 234
Cdd:PTZ00121 1339 EEAKKAAEAAKAEAEAAADEAEaaEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAK- 1417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 235 arllqleedligvtqkglQKETELDCLKDRVKKLNLEKEALEGQLKNEkdekELYKIHLKNRELENTKLSAElQMLKSVD 314
Cdd:PTZ00121 1418 ------------------KKADEAKKKAEEKKKADEAKKKAEEAKKAD----EAKKKAEEAKKAEEAKKKAE-EAKKADE 1474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 315 VNKENTIAQLKDELARVKSCLAEKEKQHRQllansspSGESKALREQLRQKEEQLQATQQQANMLKAELRDSSNARDRSM 394
Cdd:PTZ00121 1475 AKKKAEEAKKADEAKKKAEEAKKKADEAKK-------AAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKK 1547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 395 AELYRirvEAETLKKGQADARAECSRLEQQLEEMKSSTQQEA-QCKESDVLAVAELQREVEDLRLRLQMAAEHYKDKYKE 473
Cdd:PTZ00121 1548 ADELK---KAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAkKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEE 1624
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 474 CQKlQKQVVKFNEQQGVKRSPGSDAAAGPLSASPEASAPGSPSTSDAVLDaiihgrlKSSSKELDK--NDKYRKCKQMLN 551
Cdd:PTZ00121 1625 LKK-AEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEED-------KKKAEEAKKaeEDEKKAAEALKK 1696
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 552 EERERCSMitDELTKM---EVKLREQMKTNESLRMQLAAEEDRYKSQVAEKGRELK---ELKDSLFVLTKEKEKLEGQLQ 625
Cdd:PTZ00121 1697 EAEEAKKA--EELKKKeaeEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKkdeEEKKKIAHLKKEEEKKAEEIR 1774
|
.
gi 1207119093 626 K 626
Cdd:PTZ00121 1775 K 1775
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
318-641 |
2.03e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.14 E-value: 2.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 318 ENTIAQLKDELARVKSCLAEKEKQHRQLLANSSPSGESKALREQLRQKE------------EQLQATQQQANMLKAELRD 385
Cdd:TIGR02168 178 ERKLERTRENLDRLEDILNELERQLKSLERQAEKAERYKELKAELRELElallvlrleelrEELEELQEELKEAEEELEE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 386 SSNARDRSMAELYRIRVE-------AETLKKGQADARAECSRLEQQLEEMKSSTQQEAQCKESDVLAVAELQREVEDLRL 458
Cdd:TIGR02168 258 LTAELQELEEKLEELRLEvseleeeIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 459 RLQMAAEHYKDKYKECQKLQKQVVKFNEQQGVkrspgsdaaagplsaspeasapgspstsdavldaiihgrLKSSSKELD 538
Cdd:TIGR02168 338 ELAELEEKLEELKEELESLEAELEELEAELEE---------------------------------------LESRLEELE 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 539 K-----NDKYRKCKQMLNEERERCSMITDELTKMEVKLREQMKTNESLRMQLA-AEEDRYKSQVAEKGRELKELKDSLFV 612
Cdd:TIGR02168 379 EqletlRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEeAELKELQAELEELEEELEELQEELER 458
|
330 340 350
....*....|....*....|....*....|....*
gi 1207119093 613 LTKEKEKLEGQLQK------SVNREEEQKDSNLDV 641
Cdd:TIGR02168 459 LEEALEELREELEEaeqaldAAERELAQLQARLDS 493
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
136-384 |
2.11e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 57.72 E-value: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 136 LTMEDEGGSDILVVTTKAS---------------YLEQkmeQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERE 200
Cdd:COG3206 127 LTVEPVKGSNVIEISYTSPdpelaaavanalaeaYLEQ---NLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQ 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 201 SSAQLRKDVQELQLSAQ--SLQEEREEVKRRMEESTARLLQLEEDL--IGVTQKGLQKETELDCLKDRVKKLNLEKEALE 276
Cdd:COG3206 204 KNGLVDLSEEAKLLLQQlsELESQLAEARAELAEAEARLAALRAQLgsGPDALPELLQSPVIQQLRAQLAELEAELAELS 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 277 GQLKNE-------KDEKELYKIHLKNRELEN-TKLSAELQMLKSVDVNKENTIAQLKDELARvkscLAEKEKQHRQLLAn 348
Cdd:COG3206 284 ARYTPNhpdvialRAQIAALRAQLQQEAQRIlASLEAELEALQAREASLQAQLAQLEARLAE----LPELEAELRRLER- 358
|
250 260 270
....*....|....*....|....*....|....*.
gi 1207119093 349 sspsgESKALREQLRQKEEQLQATQQQANMLKAELR 384
Cdd:COG3206 359 -----EVEVARELYESLLQRLEEARLAEALTVGNVR 389
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
157-455 |
2.40e-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: 57.88 E-value: 2.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 157 EQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEEREEVKRRMEESTAR 236
Cdd:pfam01576 11 EEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESRLEEEEER 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 237 LLQLEEDLIGVTQKGLQKETELDCLKDRVKKLNLEKEALEGQLK------------NEKDEKElyKIHLKNRELENTKLS 304
Cdd:pfam01576 91 SQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKkleedillledqNSKLSKE--RKLLEERISEFTSNL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 305 AE----LQMLKSVDVNKENTIAQLKDELARVKSCLAEKEKQHRQLLANSSPSGESKA--------LREQLRQKEEQLQAT 372
Cdd:pfam01576 169 AEeeekAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAelqaqiaeLRAQLAKKEEELQAA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 373 QQQANMLKAELRDSSNARDRSMAELYRIRVEAETLKKGQADARAECSRLEQQLEEMKS---------STQQEAQCKESDv 443
Cdd:pfam01576 249 LARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTeledtldttAAQQELRSKREQ- 327
|
330
....*....|..
gi 1207119093 444 lAVAELQREVED 455
Cdd:pfam01576 328 -EVTELKKALEE 338
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
158-631 |
2.92e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.47 E-value: 2.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 158 QKMEQIQQEKKELLENLDLLQkerdELIDEKNRLEKEYEQERESSAQLRKDVQEL--QLSAQSLQEEREEVKRRMEESTA 235
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYA----ELQEELEELEEELEELEAELEELREELEKLekLLQLLPLYQELEALEAELAELPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 236 RLLQLEEDLigvtQKGLQKETELDCLKDRVKKLNLEKEALEGQLKNEKDEkelykiHLKNRELENTKLSAELQMLKSVDV 315
Cdd:COG4717 147 RLEELEERL----EELRELEEELEELEAELAELQEELEELLEQLSLATEE------ELQDLAEELEELQQRLAELEEELE 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 316 NKENTIAQLKDELARVKSCLAEKEKQHR----------------------------------------------QLLANS 349
Cdd:COG4717 217 EAQEELEELEEELEQLENELEAAALEERlkearlllliaaallallglggsllsliltiagvlflvlgllallfLLLARE 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 350 SPSGESKALREQLRQKEEQLQATQQQAnmLKAELRDSSNARDRSMAELYRirvEAETLKkgqaDARAECSRLEQQLEEMK 429
Cdd:COG4717 297 KASLGKEAEELQALPALEELEEEELEE--LLAALGLPPDLSPEELLELLD---RIEELQ----ELLREAEELEEELQLEE 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 430 SSTQQEAQCKESDVlavaelqREVEDLRLRLQmaaehykdKYKECQKLQKQVVKFNEQqgvkrspgsdaaagpLSASPEA 509
Cdd:COG4717 368 LEQEIAALLAEAGV-------EDEEELRAALE--------QAEEYQELKEELEELEEQ---------------LEELLGE 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 510 SAPGSPSTSDAVLdaiihgrlkssskeldkNDKYRKCKQMLNEERERCSMITDELTKMEVKLrEQMKTNESLrMQLAAEE 589
Cdd:COG4717 418 LEELLEALDEEEL-----------------EEELEELEEELEELEEELEELREELAELEAEL-EQLEEDGEL-AELLQEL 478
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1207119093 590 DRYKSQVAEKGRELKELKDSLFVLTKEKEKLEGQLQKSVNRE 631
Cdd:COG4717 479 EELKAELRELAEEWAALKLALELLEEAREEYREERLPPVLER 520
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
337-666 |
4.92e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.87 E-value: 4.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 337 EKEKQHRQLLAnsspsgESKALREQLRQKEEQLQATQQQANMLKAELRDSSNARDRSMAELYRIRVEAETLKKGQADARA 416
Cdd:COG1196 222 LKELEAELLLL------KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 417 ECSRLEQQLEEMKSSTQQEAQCKESDVLAVAELQREVEDLRLRLQMAAEHYKDKYKECQKLQKQVVKFNEQQgvkrspgs 496
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL-------- 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 497 daaagplsaspeasapgspSTSDAVLDAIIHGRLKSSSKELDKNDKYRKCKQMLNEERERCSMITDELTKMEVKLREQMK 576
Cdd:COG1196 368 -------------------LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 577 TNESLRMQLAAEEDRYKSQVAEKGRELKELKDSLFVLTKEKEKLEGQLQK--SVNREEEQKDSNLDVQSVFLQYPMPYAQ 654
Cdd:COG1196 429 ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAAlaELLEELAEAAARLLLLLEAEADYEGFLE 508
|
330
....*....|..
gi 1207119093 655 DDPSPLLVPQRP 666
Cdd:COG1196 509 GVKAALLLAGLR 520
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
124-488 |
7.04e-08 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 56.27 E-value: 7.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 124 QFRANSPTEEELLTMED---EGGSDILVVTT-----KASYLEQkMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEY 195
Cdd:pfam05483 353 EFEATTCSLEELLRTEQqrlEKNEDQLKIITmelqkKSSELEE-MTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIA 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 196 EQERESSAQLRKDVQELQLSAQSLQEEREEVKRRMEESTARLLQLEEDLIGVTQKGLQKETELDCLKDRVKKLNLEKEAL 275
Cdd:pfam05483 432 EELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDM 511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 276 EGQLKNEKDekelykihlknrELENTKLSAElQMLKSVDvNKENTIAQLKDELARVKSCLAEKEKQHRQLLANSSPSGES 355
Cdd:pfam05483 512 TLELKKHQE------------DIINCKKQEE-RMLKQIE-NLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARS 577
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 356 kaLREQLRQKEEQLQATQQQANMLKAELRDSSnardRSMAELYRirvEAETL-KKGQADARA-------------ECSRL 421
Cdd:pfam05483 578 --IEYEVLKKEKQMKILENKCNNLKKQIENKN----KNIEELHQ---ENKALkKKGSAENKQlnayeikvnklelELASA 648
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207119093 422 EQQLEEMKSSTQQEAQCKEsdvLAVAELQREVEDLRLRLQMAAEHYKDKYKECQKLQKQVVKFNEQQ 488
Cdd:pfam05483 649 KQKFEEIIDNYQKEIEDKK---ISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKH 712
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
131-657 |
7.29e-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: 7.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 131 TEEELLTMEDEGGSDILV---VTTKASYLEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQEREssaQLRK 207
Cdd:TIGR00606 375 TRLELDGFERGPFSERQIknfHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKE---ILEK 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 208 DVQELQLSAQSLQEereevkrrMEESTARLLQLEEDLIGVTQK--GLQKETELDCLKDRVKKLNLEKEALEGQLKNEKDE 285
Cdd:TIGR00606 452 KQEELKFVIKELQQ--------LEGSSDRILELDQELRKAERElsKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQE 523
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 286 KELykihlKNRELENTKlsaELQMLKSVDVNKENTIAQLKDELARVKSCLAEKEKQHRQLLAN-SSPSGESKALREQLRQ 364
Cdd:TIGR00606 524 MEQ-----LNHHTTTRT---QMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWlHSKSKEINQTRDRLAK 595
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 365 KEEQLQATQQQANMLKAELRdSSNARDRSMAE--------------LYRIRVEAETLKKGQADARAECSRLEQQLEEMKS 430
Cdd:TIGR00606 596 LNKELASLEQNKNHINNELE-SKEEQLSSYEDklfdvcgsqdeesdLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTD 674
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 431 STQQEAQCKESDVLAVAELQREVEDLRLRLQMAAEHYKDKYKECQKLQKQ------------------VVKFNEQQGVKR 492
Cdd:TIGR00606 675 ENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRrdemlglapgrqsiidlkEKEIPELRNKLQ 754
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 493 SPGSDAAAGPLSASP-----EASAPGSPSTSDAVLDAIIHGRLKSSSKELDkndkyRKCKQMLNEERErcsmITDELTKM 567
Cdd:TIGR00606 755 KVNRDIQRLKNDIEEqetllGTIMPEEESAKVCLTDVTIMERFQMELKDVE-----RKIAQQAAKLQG----SDLDRTVQ 825
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 568 EVKLREQMKTNESLRMQLAAEEDRYKSQvaEKGRELKELKDSLFVLTKEKEKLEGQLQKSVNREEEQKDSNLDVQSVFLQ 647
Cdd:TIGR00606 826 QVNQEKQEKQHELDTVVSKIELNRKLIQ--DQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIRE 903
|
570
....*....|
gi 1207119093 648 YPMPYAQDDP 657
Cdd:TIGR00606 904 IKDAKEQDSP 913
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
179-639 |
7.41e-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: 56.21 E-value: 7.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 179 KERDELIDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEEREEVKRRMEESTARLLQLEEDligvTQKGLQKETEL 258
Cdd:TIGR00606 172 KQKFDEIFSATRYIKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESS----REIVKSYENEL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 259 DCLKDRVKKL--NLEK-EALEGQLKN-EKDEKELYKIHLKNRELENTKLSAELQMLKSVDVNKENTIAQLKDELARVKSC 334
Cdd:TIGR00606 248 DPLKNRLKEIehNLSKiMKLDNEIKAlKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 335 LaEKEKQHRQLLANSSPSGEskalreqLRQKEEQLQATQQQANMLKAELRDSSNArdrsmaelyrIRVEAETLKKGQADA 414
Cdd:TIGR00606 328 L-EKLNKERRLLNQEKTELL-------VEQGRLQLQADRHQEHIRARDSLIQSLA----------TRLELDGFERGPFSE 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 415 R----AECSRLEQQLEEMKSSTQQEAQCKESDVLAvaelQREVEDLRLRLQMAAEHYKDKYKECQKLQKQvVKFNEQQGV 490
Cdd:TIGR00606 390 RqiknFHTLVIERQEDEAKTAAQLCADLQSKERLK----QEQADEIRDEKKGLGRTIELKKEILEKKQEE-LKFVIKELQ 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 491 KRSPGSDAAAGPLSASPEASAPGSPSTSDAVLDAIIHGRLKSSSKELDKNDKYRKckqmLNEERERCSMITDELTKMEVK 570
Cdd:TIGR00606 465 QLEGSSDRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRK----LDQEMEQLNHHTTTRTQMEML 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 571 LREQMKTNESLRMQLAAEEDRYKSQVA-------------EKGRELKELKDSLFVLTKEKEKLEgQLQKSVNREEEQKDS 637
Cdd:TIGR00606 541 TKDKMDKDEQIRKIKSRHSDELTSLLGyfpnkkqledwlhSKSKEINQTRDRLAKLNKELASLE-QNKNHINNELESKEE 619
|
..
gi 1207119093 638 NL 639
Cdd:TIGR00606 620 QL 621
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
150-436 |
9.87e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.84 E-value: 9.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 150 TTKASYLEQKMEQIQQEKKELLENLDLLQKERDELiDEKNRLEKEYEQERESSAQLRK-DVQELQLSAqslqEEREEVKR 228
Cdd:PRK03918 458 TAELKRIEKELKEIEEKERKLRKELRELEKVLKKE-SELIKLKELAEQLKELEEKLKKyNLEELEKKA----EEYEKLKE 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 229 RMEESTARLLQLEEDLigvtQKGLQKETELDCLKDRVKKLNLEKEALEGQLKN---------EKDEKELYKIHLKNRELE 299
Cdd:PRK03918 533 KLIKLKGEIKSLKKEL----EKLEELKKKLAELEKKLDELEEELAELLKELEElgfesveelEERLKELEPFYNEYLELK 608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 300 NTK--LSAELQMLKSVdvnkENTIAQLKDELARVKSCLAEKEKQHRQLLANSSP-------------SGESKALREQLRQ 364
Cdd:PRK03918 609 DAEkeLEREEKELKKL----EEELDKAFEELAETEKRLEELRKELEELEKKYSEeeyeelreeylelSRELAGLRAELEE 684
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207119093 365 KEEQLQATQQQANMLKAELrdssnardrsmAELYRIRVEAETLKKgqadARAECSRLEQQLEEMKSSTQQEA 436
Cdd:PRK03918 685 LEKRREEIKKTLEKLKEEL-----------EEREKAKKELEKLEK----ALERVEELREKVKKYKALLKERA 741
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
164-330 |
9.91e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.08 E-value: 9.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 164 QQEKKELLEN-LDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQELQLSA-QSLQEEREEVKRRMEESTARLLQLE 241
Cdd:COG4913 286 AQRRLELLEAeLEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRlEQLEREIERLERELEERERRRARLE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 242 EDLIGVtqkGLQKETELDCLKDRVKKLNLEKEALEGQLknEKDEKELYKIHLKNRELEN--TKLSAELQMLKSVDVNKEN 319
Cdd:COG4913 366 ALLAAL---GLPLPASAEEFAALRAEAAALLEALEEEL--EALEEALAEAEAALRDLRRelRELEAEIASLERRKSNIPA 440
|
170
....*....|.
gi 1207119093 320 TIAQLKDELAR 330
Cdd:COG4913 441 RLLALRDALAE 451
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
144-639 |
9.98e-08 |
|
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: 55.75 E-value: 9.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 144 SDILVVTTKASYLEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEER 223
Cdd:pfam02463 293 KEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLE 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 224 EEV------KRRMEESTARLLQLEEDLIGVTQKGLQKETELdcLKDRVKKLNLEKEALEGQLKNEKDEKELYKIHLKNRE 297
Cdd:pfam02463 373 EELlakkklESERLSSAAKLKEEELELKSEEEKEAQLLLEL--ARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEK 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 298 LENTKLSAELQMLKSVDVNKENTIAQLKDELARVKSCLAEKEKQHRQLLANSSPSGESKALREQLRQKEEQLQATQQQAN 377
Cdd:pfam02463 451 EELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGR 530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 378 MLKAELRDSSNARDRSMAelyriRVEAETLKKGQADARAECSRLEQQLEEMKSSTQQEAQCKESDVLAVAELQREVEDLR 457
Cdd:pfam02463 531 LGDLGVAVENYKVAISTA-----VIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNL 605
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 458 LRLQMAAEHY---------KDKYKECQKLQKQVVKFNEQQGVKRSPGSDAAAGPLSASPEASAPGSPSTSDAVLDAIIHG 528
Cdd:pfam02463 606 AQLDKATLEAdeddkrakvVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKA 685
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 529 RLKSSSKELDKNDKYRKCKQMLNEERERCSMITDELTKMEVKLREQMKTNESLRMQLAAEEDRYKSQVAEKGRELKELKD 608
Cdd:pfam02463 686 ESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEE 765
|
490 500 510
....*....|....*....|....*....|.
gi 1207119093 609 SLFVLTKEKEKLEGQLQKSVNREEEQKDSNL 639
Cdd:pfam02463 766 KSELSLKEKELAEEREKTEKLKVEEEKEEKL 796
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
213-626 |
1.69e-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: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 213 QLSAQSLQEEREEVKRRMEESTARLLQLEEDLIGVtqkglqkETELDCLKDRVKKLNLEKEALEGQLKNEKDEkelykih 292
Cdd:TIGR02168 669 NSSILERRREIEELEEKIEELEEKIAELEKALAEL-------RKELEELEEELEQLRKELEELSRQISALRKD------- 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 293 LKNRELENTKLSAELQMLKSVDVNKENTIAQLKDELARVKSCLAEKEKqhrqllansspsgESKALREQLRQKEEQLQAT 372
Cdd:TIGR02168 735 LARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEA-------------EIEELEAQIEQLKEELKAL 801
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 373 QQQANMLKAELRDssnardrsmaelyrirveaetLKKGQADARAECSRLEQQLEEMKSSTQQEAQCKESDVLAVAELQRE 452
Cdd:TIGR02168 802 REALDELRAELTL---------------------LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAE 860
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 453 VEDLRLRLQMAAEHYKDKYKECQKLQKQVVKFNEQqgvkrspgsdaaagplsaspeasapgspstsdavLDAIIHGRLKS 532
Cdd:TIGR02168 861 IEELEELIEELESELEALLNERASLEEALALLRSE----------------------------------LEELSEELREL 906
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 533 SSKELDKNDKYRKCKQMLNEERERCSMITDELTKMEVKLREQMKTN-----------ESLRMQLAAEEDRYKSQVAEKGR 601
Cdd:TIGR02168 907 ESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTleeaealenkiEDDEEEARRRLKRLENKIKELGP 986
|
410 420 430
....*....|....*....|....*....|..
gi 1207119093 602 -------ELKELKDSLFVLTKEKEKLEGQLQK 626
Cdd:TIGR02168 987 vnlaaieEYEELKERYDFLTAQKEDLTEAKET 1018
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
144-621 |
2.42e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.68 E-value: 2.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 144 SDILVVTTKASYLEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEqERESSAQLRKDVQELQLSAQSLQEER 223
Cdd:PRK03918 303 EEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLE-ELEERHELYEEAKAKKEELERLKKRL 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 224 -----EEVKRRMEESTARLLQLEEDLIGVTQKGLQKETELDCLKDRVKKLNLEKEA--LEGQLKNEKDEKEL---YKIHL 293
Cdd:PRK03918 382 tgltpEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpVCGRELTEEHRKELleeYTAEL 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 294 KNRELENTKLSAELQMLKSVDVNKENTIAQLKdELARVKSCLAEKEKQHRQLlansspsgeSKALREQLRQKEEQLQATQ 373
Cdd:PRK03918 462 KRIEKELKEIEEKERKLRKELRELEKVLKKES-ELIKLKELAEQLKELEEKL---------KKYNLEELEKKAEEYEKLK 531
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 374 QQANMLKAELRdssnARDRSMAELYRIRVEAETLKKGQADARAECSRLEQQLEEMKSSTqqeaqckesdvlaVAELQREV 453
Cdd:PRK03918 532 EKLIKLKGEIK----SLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFES-------------VEELEERL 594
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 454 EDLR------LRLQMAAEHYKDKYKECQKLQKQVVKFNEQQgvkrspgsdaaagplsaspeasapgspstsdavldAIIH 527
Cdd:PRK03918 595 KELEpfyneyLELKDAEKELEREEKELKKLEEELDKAFEEL-----------------------------------AETE 639
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 528 GRLKSSSKELD-KNDKYRKckqmlnEERERCSMITDELTKMEVKLREQMKTNESLRMQLAAEEDRYKSQVAEKGRELKEL 606
Cdd:PRK03918 640 KRLEELRKELEeLEKKYSE------EEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKEL 713
|
490
....*....|....*
gi 1207119093 607 KDslfvLTKEKEKLE 621
Cdd:PRK03918 714 EK----LEKALERVE 724
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
163-487 |
3.99e-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: 3.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 163 IQQEKKELLENLdlLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEEReevkrrmeestarllqlee 242
Cdd:pfam15921 68 IAYPGKEHIERV--LEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMER------------------- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 243 dligvtqkglqketelDCLKDRVKKLNLEKEALEGQLKNEKDEKELYKIhLKNRELENTklSAELQMLKSVDVNKENTIA 322
Cdd:pfam15921 127 ----------------DAMADIRRRESQSQEDLRNQLQNTVHELEAAKC-LKEDMLEDS--NTQIEQLRKMMLSHEGVLQ 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 323 QLKDELARVKSCLAEKEKQHRQLLA---NSSPSGESKALRE---QLRQKEEQLQATQQQANMLKAELRDS-----SNARD 391
Cdd:pfam15921 188 EIRSILVDFEEASGKKIYEHDSMSTmhfRSLGSAISKILREldtEISYLKGRIFPVEDQLEALKSESQNKielllQQHQD 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 392 RSMAELYRIRVEAETLKKGQADARAECSRLEQQLEEMksstQQEAQCKESDVLA-VAELQREVEDLRLRLQMAAEHYKDK 470
Cdd:pfam15921 268 RIEQLISEHEVEITGLTEKASSARSQANSIQSQLEII----QEQARNQNSMYMRqLSDLESTVSQLRSELREAKRMYEDK 343
|
330
....*....|....*..
gi 1207119093 471 YKEcqkLQKQVVKFNEQ 487
Cdd:pfam15921 344 IEE---LEKQLVLANSE 357
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
158-429 |
5.05e-07 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 53.30 E-value: 5.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 158 QKMEQIQQEKKELLENLDLLQKERDELI--DEKNRleKEYEQERESSAQLRKDV-----------QELQLSAQSLQEERE 224
Cdd:PRK04778 105 HEINEIESLLDLIEEDIEQILEELQELLesEEKNR--EEVEQLKDLYRELRKSLlanrfsfgpalDELEKQLENLEEEFS 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 225 EVKRRMEE---STAR--LLQLEEDLIGVTQ---------KGLQKE--TELDCLKDRVKKL-----NLEKEALEGQLKNEK 283
Cdd:PRK04778 183 QFVELTESgdyVEAReiLDQLEEELAALEQimeeipellKELQTElpDQLQELKAGYRELveegyHLDHLDIEKEIQDLK 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 284 DE-----KELYKIHLKNRELENTKLSAELQML-----------KSVDVNKENTIA----------QLKDELARVKSC--L 335
Cdd:PRK04778 263 EQidenlALLEELDLDEAEEKNEEIQERIDQLydilerevkarKYVEKNSDTLPDflehakeqnkELKEEIDRVKQSytL 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 336 AEKEKQHRQLLANsspsgESKALREQLRQKEEQLQATQQQANMLKAELRDSSNARDRSMAELYRIRVEAETLKKGQADAR 415
Cdd:PRK04778 343 NESELESVRQLEK-----QLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQEKLSEMLQGLRKDELEAR 417
|
330
....*....|....
gi 1207119093 416 AECSRLEQQLEEMK 429
Cdd:PRK04778 418 EKLERYRNKLHEIK 431
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
133-554 |
5.46e-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: 53.58 E-value: 5.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 133 EELLTMEDEGgSDILVVTTKASYLEQKMeqiqQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERessAQLRKDVQEL 212
Cdd:pfam15921 531 QELQHLKNEG-DHLRNVQTECEALKLQM----AEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEK---AQLEKEINDR 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 213 QLSAQSLQEEREEVKRRMEESTARLLQLEEDLIGVTQKGLQKETELDCLKDRVKKLNLEKEALEGQLKNEKDEKELYKIH 292
Cdd:pfam15921 603 RLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRN 682
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 293 LKNRELENTKLSAELQM-LKSVDVNKENTIAQLKDELARVKSCLAEKEKQHRQLLANsspSGESKALREQLRQKEEQLQA 371
Cdd:pfam15921 683 FRNKSEEMETTTNKLKMqLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAK---RGQIDALQSKIQFLEEAMTN 759
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 372 TQQQANMLKAELRDSSNARDRSMAELYRIRVEAETLKKGQADARAECSRLEQQLEEmksSTQQEAQCKesDVLAvaelQR 451
Cdd:pfam15921 760 ANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDK---ASLQFAECQ--DIIQ----RQ 830
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 452 EVEDLRLRLQmaaehykdkykecqklqkQVVKFNEQQGVKRSPGSDAAAGPLSAS----PEASAPGSPSTSDAVLDaiiH 527
Cdd:pfam15921 831 EQESVRLKLQ------------------HTLDVKELQGPGYTSNSSMKPRLLQPAsftrTHSNVPSSQSTASFLSH---H 889
|
410 420
....*....|....*....|....*..
gi 1207119093 528 GRLKSSSKEldknDKYRKCKQMLNEER 554
Cdd:pfam15921 890 SRKTNALKE----DPTRDLKQLLQELR 912
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
203-372 |
5.91e-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: 5.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 203 AQLRKDVQELQLSAQSLQEEREEVKRRMEESTARLLQLEEDLigvtqkgLQKETELDCLKDRVKKLnlekealEGQLKNE 282
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEI-------KRLELEIEEVEARIKKY-------EEQLGNV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 283 KDEKELYKIhlkNRELENTKL------SAELQMLKSVDvNKENTIAQLKDELARVKSCLAEKEKQHRQLLAnsspsgESK 356
Cdd:COG1579 86 RNNKEYEAL---QKEIESLKRrisdleDEILELMERIE-ELEEELAELEAELAELEAELEEKKAELDEELA------ELE 155
|
170
....*....|....*.
gi 1207119093 357 ALREQLRQKEEQLQAT 372
Cdd:COG1579 156 AELEELEAEREELAAK 171
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
157-455 |
6.53e-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: 53.26 E-value: 6.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 157 EQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLE---KEYEQERESSAQLR----KDVQELQLSAQSLQEEREEVK-- 227
Cdd:pfam01576 741 EEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLEldlKELEAQIDAANKGReeavKQLKKLQAQMKDLQRELEEARas 820
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 228 ------------RRMEESTARLLQLEEDLIGVTQKGLQKETELDCLKDRVKKLNLEKEALE----------GQLKNEKDE 285
Cdd:pfam01576 821 rdeilaqskeseKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQdekrrleariAQLEEELEE 900
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 286 K----ELYKIHLKNRELENTKLSAELQMLKSVDVNKENTIAQLKDELARVKSCLAEKEKQHRQLLANSSPSGESKalreq 361
Cdd:pfam01576 901 EqsntELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVKSKFKSSIAALEAK----- 975
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 362 LRQKEEQLQATQQQANMLKAELRDSSNARDRSMAELYRIRVEAETLKKGQADARAECSRLEQQLEEMKSSTQQEAQCKEs 441
Cdd:pfam01576 976 IAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASRANAARR- 1054
|
330
....*....|....
gi 1207119093 442 dvlavaELQREVED 455
Cdd:pfam01576 1055 ------KLQRELDD 1062
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
172-455 |
6.69e-07 |
|
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: 52.72 E-value: 6.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 172 ENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEEreevkrrMEESTARLLQLEEDLIGVT--- 248
Cdd:pfam05701 145 EELESLRKEYASLVSERDIAIKRAEEAVSASKEIEKTVEELTIELIATKES-------LESAHAAHLEAEEHRIGAAlar 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 249 -QKGLQKETELDCLKDRVKKLNlEKEALEGQLKNEKDEKELYKIHLKNrEL----ENT--KLSAELQMLKSVDVNKENTI 321
Cdd:pfam05701 218 eQDKLNWEKELKQAEEELQRLN-QQLLSAKDLKSKLETASALLLDLKA-ELaaymESKlkEEADGEGNEKKTSTSIQAAL 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 322 AQLKDELARVKSCLaEKEKQHRQLLANSSPSgeskaLREQLRQKEEQLQATQQQANMlkaelrdSSNARDRSMAELYRIR 401
Cdd:pfam05701 296 ASAKKELEEVKANI-EKAKDEVNCLRVAAAS-----LRSELEKEKAELASLRQREGM-------ASIAVSSLEAELNRTK 362
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1207119093 402 VEAETLKKGQADARAECSRLEQQLEEmkssTQQEA-QCKESDVLAVAELQREVED 455
Cdd:pfam05701 363 SEIALVQAKEKEAREKMVELPKQLQQ----AAQEAeEAKSLAQAAREELRKAKEE 413
|
|
| Zn-C2H2_12 |
pfam18112 |
Autophagy receptor zinc finger-C2H2 domain; This domain is found in calcium-binding and ... |
790-816 |
6.78e-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: 6.78e-07
10 20
....*....|....*....|....*..
gi 1207119093 790 KICPMCSEQFPLDCDQQLFEKHVLTHF 816
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 ... |
161-480 |
1.02e-06 |
|
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: 52.48 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 161 EQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQEressAQLRKDVQELQLSAQSLQE--EREEVKRRMEESTARLL 238
Cdd:pfam01576 222 EQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQK----NNALKKIRELEAQISELQEdlESERAARNKAEKQRRDL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 239 QLE--------EDLIGVT--QKGL--QKETELDCLK---------------DRVKKLNLEKEALEGQLKNEKDEKELYKI 291
Cdd:pfam01576 298 GEElealktelEDTLDTTaaQQELrsKREQEVTELKkaleeetrsheaqlqEMRQKHTQALEELTEQLEQAKRNKANLEK 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 292 HLKNRELENTKLSAELQMLKSVDVNKENTIAQLKDELARVKSCLAEKEKQHRQL-------------LANSSPSGESKAL 358
Cdd:pfam01576 378 AKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELaeklsklqselesVSSLLNEAEGKNI 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 359 R--EQLRQKEEQLQATQQQanmLKAELRDSSN--ARDRSM-AELYRIRVEAETLKKGQADARAECSRLEQQLEEMKSSTQ 433
Cdd:pfam01576 458 KlsKDVSSLESQLQDTQEL---LQEETRQKLNlsTRLRQLeDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLE 534
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1207119093 434 QEAQCKESDVLAVAELQREVEDLRLRLQMAAEHYKDKYKECQKLQKQ 480
Cdd:pfam01576 535 EDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQE 581
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
127-636 |
1.07e-06 |
|
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: 52.53 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 127 ANSPTEEELLTMEDEGGSDILVVTTKASYLEQKMEQIQQEKKELLENLDllQKERDELIDEKNRLEKEYEQERESSAQLR 206
Cdd:pfam12128 337 ADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIK--EQNNRDIAGIKDKLAKIREARDRQLAVAE 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 207 KDVQEL------QLSAQ--SLQEEREEVKRRMEESTARL--LQLEEDLigVTQKGlQKETELDCLKDRVKKLNLEKEALE 276
Cdd:pfam12128 415 DDLQALeselreQLEAGklEFNEEEYRLKSRLGELKLRLnqATATPEL--LLQLE-NFDERIERAREEQEAANAEVERLQ 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 277 GQLKNEKDEKELYKIHLKNRELENTKLSAELQMLKSVDVNKENTI--------AQLKDELARVksclAEKEKQHRQLL-- 346
Cdd:pfam12128 492 SELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLlhflrkeaPDWEQSIGKV----ISPELLHRTDLdp 567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 347 --ANSSPSGE----SKALREQLRQKEEQLQATQQ---QANMLKAELRDSSNARDRSMAELYRIRVEAETLKKGQADARA- 416
Cdd:pfam12128 568 evWDGSVGGElnlyGVKLDLKRIDVPEWAASEEElreRLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTa 647
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 417 -ECSRLEQQ--LEEMKSS----TQQEAQCKESDVLAVAELQREVEDLRLRLQMAAEHYKDKYKE--CQKLQKQVVKFNEQ 487
Cdd:pfam12128 648 lKNARLDLRrlFDEKQSEkdkkNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREarTEKQAYWQVVEGAL 727
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 488 qgvkrspgsDAAAGPLSASPEASAPGSPSTSDAvLDAIIHGRLKSSSKELDKNDKYRKCKQMLNEERERCSMITDELTKM 567
Cdd:pfam12128 728 ---------DAQLALLKAAIAARRSGAKAELKA-LETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRY 797
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207119093 568 EVKLREQmktneslrmqLAAEEDRYKSQVAEKGRELKELKDSLFVLTKEKEKLEGQLQKSVNREEEQKD 636
Cdd:pfam12128 798 FDWYQET----------WLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQV 856
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
157-401 |
1.15e-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: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 157 EQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLekeyeQERESSAQLRKDVQELQLSAQSLQEEREEV---KRRMEES 233
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDAL-----QERREALQRLAEYSWDEIDVASAEREIAELeaeLERLDAS 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 234 TARLLQLEEDLIGVTQKGLQKETELDCLKDRVKKLNLEKEALEGQLKNEKDEKElykihlknrELENTKLSAELQMLksv 313
Cdd:COG4913 684 SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE---------AAEDLARLELRALL--- 751
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 314 dvnkENTIAQLKDElarvksclaEKEKQHRQLLANsspsgESKALREQLRQKEEQLQATQQQAN----MLKAELRDSSNA 389
Cdd:COG4913 752 ----EERFAAALGD---------AVERELRENLEE-----RIDALRARLNRAEEELERAMRAFNrewpAETADLDADLES 813
|
250
....*....|..
gi 1207119093 390 RDRSMAELYRIR 401
Cdd:COG4913 814 LPEYLALLDRLE 825
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
161-462 |
1.29e-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: 52.05 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 161 EQIQQEKKELLENlDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDvqelqlSAQSLQEEREEVKRRMEESTARLLQL 240
Cdd:pfam17380 286 ERQQQEKFEKMEQ-ERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQ------AAIYAEQERMAMERERELERIRQEER 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 241 EEDLIGVTQKGLQKETEldclkdrvKKLNLEKEALEGQLKNEKDEKEL-----YKIHLKNRELENTKLSAELQMLKSVDV 315
Cdd:pfam17380 359 KRELERIRQEEIAMEIS--------RMRELERLQMERQQKNERVRQELeaarkVKILEEERQRKIQQQKVEMEQIRAEQE 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 316 N-KENTIAQLKDELARVKSCLAEKEKQHRQLLansspsgeskalrEQLRQKEEQLQatqqqanmlKAELRDSSNARDRSM 394
Cdd:pfam17380 431 EaRQREVRRLEEERAREMERVRLEEQERQQQV-------------ERLRQQEEERK---------RKKLELEKEKRDRKR 488
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207119093 395 A-ELYRIRVEAETLKKGQADARAECSR--LEQQLEEMKSSTQQEAQCKESDVLAVAELQREvEDLRLRLQM 462
Cdd:pfam17380 489 AeEQRRKILEKELEERKQAMIEEERKRklLEKEMEERQKAIYEEERRREAEEERRKQQEME-ERRRIQEQM 558
|
|
| Zn-C2H2_CALCOCO1_TAX1BP1_like |
cd21965 |
autophagy receptor zinc finger-C2H2 domain found in calcium-binding and coiled-coil ... |
765-788 |
1.30e-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: 1.30e-06
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
154-417 |
1.47e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.44 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 154 SYLEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEEREEVKRRMEES 233
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 234 TARLLQLEEDLIGVTQKGLQKETELDCLKDRVKKLNLEKEALEGQLKN-----EKDEKELYKIHLKNRELENTKLSAELQ 308
Cdd:COG4372 107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKEleeqlESLQEELAALEQELQALSEAEAEQALD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 309 MLKSVDVNKENTIAQLKDELARVKScLAEKEKQHRQLLANSSPSGESKALREQLRQKEEQLQATQQQANMLKAELRDSSN 388
Cdd:COG4372 187 ELLKEANRNAEKEEELAEAEKLIES-LPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELEL 265
|
250 260
....*....|....*....|....*....
gi 1207119093 389 ARDRSMAELYRIRVEAETLKKGQADARAE 417
Cdd:COG4372 266 AILVEKDTEEEELEIAALELEALEEAALE 294
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
156-427 |
1.86e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.06 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 156 LEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEEREEVKRRMEESTA 235
Cdd:COG4372 50 LREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQ 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 236 RLLQLEEDLIGVTQKGLQKETELDCLKDRVKKLNLEKEALEGQLKNEKDEKELYKIHLKNRELENTKLSAElqmlksVDV 315
Cdd:COG4372 130 QRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEE------ELA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 316 NKENTIAQLKDELARVKSCLAEKEKQHRQLLANSSPSGESKALREQLRQKEEQLQATQQQANMLKAELRDSSNARDRSMA 395
Cdd:COG4372 204 EAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAAL 283
|
250 260 270
....*....|....*....|....*....|..
gi 1207119093 396 ELYRIRVEAETLKKGQADARAECSRLEQQLEE 427
Cdd:COG4372 284 ELEALEEAALELKLLALLLNLAALSLIGALED 315
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
131-429 |
2.19e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 51.44 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 131 TEEELLTMEDEGGSDILVVTTKASYLEQKMEQIQQEKKELLENLDLLQKER------DELIDEK-NRLEKEYEQERessA 203
Cdd:PRK01156 403 DPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSvcpvcgTTLGEEKsNHIINHYNEKK---S 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 204 QLRKDVQELQLSAQSLQEEREEVKRRMEESTARLLqleEDLIGVTQKGLQKETELDCLKDRVKKLNlekealEGQLKNEK 283
Cdd:PRK01156 480 RLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEI---NKSINEYNKIESARADLEDIKIKINELK------DKHDKYEE 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 284 DEKELYKIHLKNRELENTKLSAELQMLKSVDVN-----KENTIAQLKDELARVK--------------SCLAEKEKQHRQ 344
Cdd:PRK01156 551 IKNRYKSLKLEDLDSKRTSWLNALAVISLIDIEtnrsrSNEIKKQLNDLESRLQeieigfpddksyidKSIREIENEANN 630
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 345 LLANSSPSGESKALREQLRQK--------------EEQLQATQQQANMLKAELRDSSNARDRSMAELYRIRVEAETLKKG 410
Cdd:PRK01156 631 LNNKYNEIQENKILIEKLRGKidnykkqiaeidsiIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTR 710
|
330
....*....|....*....
gi 1207119093 411 QADARAECSRLEQQLEEMK 429
Cdd:PRK01156 711 INELSDRINDINETLESMK 729
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
275-492 |
2.26e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.31 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 275 LEGQLKNEKDEkeLYKIHLKNRELENTKLSAELQMLKSVDvNKENTIAQLKDELARVKSCLAEKEKQ----------HRQ 344
Cdd:COG4717 47 LLERLEKEADE--LFKPQGRKPELNLKELKELEEELKEAE-EKEEEYAELQEELEELEEELEELEAEleelreelekLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 345 LLANSSPSGESKALREQLRQKEEQLQATQQQanmlkaelrdssnardrsMAELYRIRVEAETLKKGQADARAECSRLEQQ 424
Cdd:COG4717 124 LLQLLPLYQELEALEAELAELPERLEELEER------------------LEELRELEEELEELEAELAELQEELEELLEQ 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207119093 425 LEEMKSSTQQEAQckesdvLAVAELQREVEDLRLRLQMAAEHYKDKYKECQKLQKQVVKFNEQQGVKR 492
Cdd:COG4717 186 LSLATEEELQDLA------EELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKE 247
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
133-461 |
2.45e-06 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 51.21 E-value: 2.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 133 EELLTMEDEGGSDILVVTTKAsyLEQKMEQIQQEkkeLLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQEL 212
Cdd:PRK10929 86 QQLNNERDEPRSVPPNMSTDA--LEQEILQVSSQ---LLEKSRQAQQEQDRAREISDSLSQLPQQQTEARRQLNEIERRL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 213 Q-LSAQSLQEEREEVKRRMEESTARLLQLEE-DLIGVTQKGLQKETEL--DCLKDRVKKLNLEKEALEGQLKNEKDEKel 288
Cdd:PRK10929 161 QtLGTPNTPLAQAQLTALQAESAALKALVDElELAQLSANNRQELARLrsELAKKRSQQLDAYLQALRNQLNSQRQRE-- 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 289 ykihlKNRELENTKLSAE------LQMLKSVDVNKE-----NTIAQLKDELARVKSCLAEKEKQHRQLLA----NSSPSG 353
Cdd:PRK10929 239 -----AERALESTELLAEqsgdlpKSIVAQFKINRElsqalNQQAQRMDLIASQQRQAASQTLQVRQALNtlreQSQWLG 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 354 ESKALREQLRQKEEQLqatqqqANMLKaelrdsSNARDRSMAELyriRVEaetlkkgqadaraecsRLeqQLEEMKSSTQ 433
Cdd:PRK10929 314 VSNALGEALRAQVARL------PEMPK------PQQLDTEMAQL---RVQ----------------RL--RYEDLLNKQP 360
|
330 340
....*....|....*....|....*...
gi 1207119093 434 QEAQCKESDVLAVAELQREVEDLRLRLQ 461
Cdd:PRK10929 361 QLRQIRQADGQPLTAEQNRILDAQLRTQ 388
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
156-430 |
2.61e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 49.91 E-value: 2.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 156 LEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEEREEVKRRMEESTA 235
Cdd:COG1340 13 LEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELRE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 236 RLLQLEEDLigvtQKGLQKETELDCLKDRVKKlnLEKEALEGQLKNEKdEKELY-KIHLKNRELENTKLSAElqmLKSVD 314
Cdd:COG1340 93 ELDELRKEL----AELNKAGGSIDKLRKEIER--LEWRQQTEVLSPEE-EKELVeKIKELEKELEKAKKALE---KNEKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 315 VNKENTIAQLKDELARVK---SCLAEKEKQHRQLLANSspSGESKALREQLRQKEEQLQATQQQANMLKAELRDSSNARD 391
Cdd:COG1340 163 KELRAELKELRKEAEEIHkkiKELAEEAQELHEEMIEL--YKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELR 240
|
250 260 270
....*....|....*....|....*....|....*....
gi 1207119093 392 RSMAELYRIRVEAETLKKGQADARAEcSRLEQQLEEMKS 430
Cdd:COG1340 241 ELRKELKKLRKKQRALKREKEKEELE-EKAEEIFEKLKK 278
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
254-472 |
3.47e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 3.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 254 KETELDCLKDRVKKLNLEKEALEGQLKNEKDEKELYkihlknrelentklsAELQMLKSVDVNkentIAQLKDELArvks 333
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQERREAL---------------QRLAEYSWDEID----VASAEREIA---- 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 334 claEKEKQHRQLLANSSpsgESKALREQLRQKEEQLQATQQQANMLKAELRDSSNARDRSMAELYRIRVEAEtlkkgqAD 413
Cdd:COG4913 672 ---ELEAELERLDASSD---DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE------AA 739
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207119093 414 ARAECSRLEQQLEEMKSSTQQEAQckESDVLA-----VAELQREVEDLRLRLQMAAEHYKDKYK 472
Cdd:COG4913 740 EDLARLELRALLEERFAAALGDAV--ERELREnleerIDALRARLNRAEEELERAMRAFNREWP 801
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
261-500 |
3.49e-06 |
|
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: 50.15 E-value: 3.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 261 LKDRVKKLNLEKEALEGQLKNEKDEKELYKIHLKNRELENTKLSAELQMLKSVDVNKENTIAQLKDELARVKSCLAEKEK 340
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 341 QHRQLLANSSPSGESKALREQLRQKEeqlqatQQQANMLKAELRDSSNARDRSMAELYRIRVEAETLKKGQADARAEcsr 420
Cdd:COG4942 105 ELAELLRALYRLGRQPPLALLLSPED------FLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE--- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 421 LEQQLEEMKSSTQQEAQCKESDVLAVAELQREVEDLRLRLQMAAEHYKDKYKECQKLQKQvvkfnEQQGVKRSPGSDAAA 500
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE-----AAAAAERTPAAGFAA 250
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
131-651 |
3.78e-06 |
|
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: 50.82 E-value: 3.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 131 TEEELLTMEDEGGSDILVVTTKASYLEQKMEQIQQEKKELlenldllQKERDELIDEKNRLEKEYEQERESSAQLRKDVQ 210
Cdd:TIGR00606 299 TDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLL-------NQEKTELLVEQGRLQLQADRHQEHIRARDSLIQ 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 211 ELQLSAQSLQEER------------EEVKRRMEESTARLLQLEEDLigvTQKGLQKETELDCLKDRVKKLNlekealegq 278
Cdd:TIGR00606 372 SLATRLELDGFERgpfserqiknfhTLVIERQEDEAKTAAQLCADL---QSKERLKQEQADEIRDEKKGLG--------- 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 279 lknekdekelykihlKNRELENTKLSAELQMLKSVDVNKENTIAQLKDelarvkscLAEKEKQHRQLLANsSPSGESKAL 358
Cdd:TIGR00606 440 ---------------RTIELKKEILEKKQEELKFVIKELQQLEGSSDR--------ILELDQELRKAERE-LSKAEKNSL 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 359 REQLRQKEEQLQATQqqanmlkAELRDSSNARDRSMAELYRirvEAETLKKGQADARAECSRlEQQLEEMKSSTQQEAQC 438
Cdd:TIGR00606 496 TETLKKEVKSLQNEK-------ADLDRKLRKLDQEMEQLNH---HTTTRTQMEMLTKDKMDK-DEQIRKIKSRHSDELTS 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 439 KESDVLAVAELQREVEDLRLRLQMAAEHYKDKYKECQKLQKQVVKFNEQQGVKRSpgsdaaagPLSASPEASAPGSPSTS 518
Cdd:TIGR00606 565 LLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEE--------QLSSYEDKLFDVCGSQD 636
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 519 DAVLDAIIHGRLKSSSKEL----DKNDKYRKCKQMLNEERERCSMITDELTKMEVKLREQMKTNESLRMQLAAEEDRYKS 594
Cdd:TIGR00606 637 EESDLERLKEEIEKSSKQRamlaGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTES 716
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207119093 595 QVAEKGRELKEL-------KDSLFVLTKEKEKLEGQLQKsVNREEEQKDSNLDVQSVFLQYPMP 651
Cdd:TIGR00606 717 ELKKKEKRRDEMlglapgrQSIIDLKEKEIPELRNKLQK-VNRDIQRLKNDIEEQETLLGTIMP 779
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
318-493 |
4.41e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.40 E-value: 4.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 318 ENTIAQLKDELARVKSCLAEKEKQHRQLLANS---SPSGESKALREQLRQKEEQLQATQQQANMLKAELRDSSNARDRSM 394
Cdd:COG3206 174 RKALEFLEEQLPELRKELEEAEAALEEFRQKNglvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGP 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 395 AELYRIRVEAE--TLKKGQADARAECS--------------RLEQQLEEMKSSTQQEAQCKESDVLA-VAELQREVEDLR 457
Cdd:COG3206 254 DALPELLQSPViqQLRAQLAELEAELAelsarytpnhpdviALRAQIAALRAQLQQEAQRILASLEAeLEALQAREASLQ 333
|
170 180 190
....*....|....*....|....*....|....*.
gi 1207119093 458 LRLqmaaEHYKDKYKECQKLQKQVVKFNEQQGVKRS 493
Cdd:COG3206 334 AQL----AQLEARLAELPELEAELRRLEREVEVARE 365
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
157-422 |
7.12e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.14 E-value: 7.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 157 EQKMEQIQQEKKELLENLDLLQK-ERDELIDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEEREEVKRRMEESTA 235
Cdd:PTZ00121 1531 EEAKKADEAKKAEEKKKADELKKaEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE 1610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 236 RLLQLEEDLIGVTQkgLQKETELDCLKDRVKKLNLEKEALEGQLKNEKDEKELYKIHLKNRELENTKLSAELQMLKSVDV 315
Cdd:PTZ00121 1611 EAKKAEEAKIKAEE--LKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEK 1688
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 316 NKENTIAQLKDELARVKSCLAEKEKQHRQLLANSSPSGESKALREQLRQKEEQLQATQQQANMLKAELRDSSNARDRSMA 395
Cdd:PTZ00121 1689 KAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEK 1768
|
250 260
....*....|....*....|....*..
gi 1207119093 396 ELYRIRVEAETLKKGQADARAECSRLE 422
Cdd:PTZ00121 1769 KAEEIRKEKEAVIEEELDEEDEKRRME 1795
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
157-461 |
8.71e-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: 49.35 E-value: 8.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 157 EQKMEQIQQEKKELLENLDLLQKErdelIDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSlQEEREEVKRRMEESTAR 236
Cdd:pfam05557 124 ELELQSTNSELEELQERLDLLKAK----ASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQS-QEQDSEIVKNSKSELAR 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 237 LLQLEEDLigvtQKGLQKETELDCLKDRVKKLNLEKEALEGQLknEKDEKelYKIHLKNRELENTKLSAELQMLKSVDVN 316
Cdd:pfam05557 199 IPELEKEL----ERLREHNKHLNENIENKLLLKEEVEDLKRKL--EREEK--YREEAATLELEKEKLEQELQSWVKLAQD 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 317 KENTIAQLKDELARVKScLAEKEKQHRQllANSSPSGESKALREQLRQKEEQLQATQQQANMLKAELRDSSNARDR---- 392
Cdd:pfam05557 271 TGLNLRSPEDLSRRIEQ-LQQREIVLKE--ENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRlqrr 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 393 ---------------------------SMAELYRIRVEAETLKKGQADA-----------------RAECSRLEQQLEEM 428
Cdd:pfam05557 348 vllltkerdgyrailesydkeltmsnySPQLLERIEEAEDMTQKMQAHNeemeaqlsvaeeelggyKQQAQTLERELQAL 427
|
330 340 350
....*....|....*....|....*....|...
gi 1207119093 429 KSSTQQEAQCKESDvlAVAELQREVEDLRLRLQ 461
Cdd:pfam05557 428 RQQESLADPSYSKE--EVDSLRRKLETLELERQ 458
|
|
| Zn-C2H2_CALCOCO1_TAX1BP1_like |
cd21965 |
autophagy receptor zinc finger-C2H2 domain found in calcium-binding and coiled-coil ... |
792-815 |
9.06e-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: 9.06e-06
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
156-642 |
1.04e-05 |
|
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: 49.35 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 156 LEQKMEQIQQEKKELLenlDLLQKERDELIDEKNRLEKEYeQERESSAQLRKD-----------VQELQLSAQSLQEERE 224
Cdd:pfam15921 115 LQTKLQEMQMERDAMA---DIRRRESQSQEDLRNQLQNTV-HELEAAKCLKEDmledsntqieqLRKMMLSHEGVLQEIR 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 225 EVKRRMEESTARLLQLEEDLIGVTQKGL---------QKETELDCLKDRVKKLNLEKEALEGQLKNE-----KDEKELYK 290
Cdd:pfam15921 191 SILVDFEEASGKKIYEHDSMSTMHFRSLgsaiskilrELDTEISYLKGRIFPVEDQLEALKSESQNKielllQQHQDRIE 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 291 IHLKNRELENTKLSAELQMLKSvDVNKENTIAQLKDELARVKSCLAEKEKQHRQllanSSPSGESKALREQLRQKEEQLQ 370
Cdd:pfam15921 271 QLISEHEVEITGLTEKASSARS-QANSIQSQLEIIQEQARNQNSMYMRQLSDLE----STVSQLRSELREAKRMYEDKIE 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 371 ATQQQANMLKAELRDSSNARDRSMAELYRIRveaETLKKGQADaraecsrLEQQLEEMKSSTQQEAQCKESDV---LAVA 447
Cdd:pfam15921 346 ELEKQLVLANSELTEARTERDQFSQESGNLD---DQLQKLLAD-------LHKREKELSLEKEQNKRLWDRDTgnsITID 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 448 ELQREVEDLRLRLQMAAEHYKDKYKECQ-KLQKQVVKFneqQGVKRSPgsdAAAGPLSASPEASApgspSTSDAVLDAII 526
Cdd:pfam15921 416 HLRRELDDRNMEVQRLEALLKAMKSECQgQMERQMAAI---QGKNESL---EKVSSLTAQLESTK----EMLRKVVEELT 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 527 HGRLKSSSKELDKNDKYRKCKQMLNEERERCSMITDELTKMEVKLRE--QMKTNESLRMQLAAEEDRYKSQVAEKGRELK 604
Cdd:pfam15921 486 AKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQElqHLKNEGDHLRNVQTECEALKLQMAEKDKVIE 565
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1207119093 605 ELK---DSLFVLTKEKEKLEGQLQ-KSVNREEEQKDSNLDVQ 642
Cdd:pfam15921 566 ILRqqiENMTQLVGQHGRTAGAMQvEKAQLEKEINDRRLELQ 607
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
161-428 |
1.33e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.88 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 161 EQIQQEKKELLENLDLLQKERDELIDEKNRLE--KEYEQERESSAQLRKDVQELQLSAQSLQEEREEvkrRMEESTARLL 238
Cdd:PRK02224 471 EEDRERVEELEAELEDLEEEVEEVEERLERAEdlVEAEDRIERLEERREDLEELIAERRETIEEKRE---RAEELRERAA 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 239 QLEEDLIGVTQKGLQKETELDCLKDRVKKLNLEKEALEGQLKNekdekeLYKIHLKNRELENtkLSAELQMLKsvdvNKE 318
Cdd:PRK02224 548 ELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIES------LERIRTLLAAIAD--AEDEIERLR----EKR 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 319 NTIAQLKDELarvKSCLAEKEKQHRQLLANSSPSGESKA-------------LREQLRQKEEQLQATQQQANMLKAELRD 385
Cdd:PRK02224 616 EALAELNDER---RERLAEKRERKRELEAEFDEARIEEAredkeraeeyleqVEEKLDELREERDDLQAEIGAVENELEE 692
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1207119093 386 SSNARDRSMA------ELYRIRVEAETLKKGQADARAE-----CSRLEQQLEEM 428
Cdd:PRK02224 693 LEELRERREAlenrveALEALYDEAEELESMYGDLRAElrqrnVETLERMLNET 746
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
180-636 |
1.50e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 180 ERDELIDEKNRLEKeYEQERESSAQLRKDVQELQLSAQSLQEEREEVKRRMEESTARLLQLEEDLIGVTQKGLQKETELD 259
Cdd:PRK03918 146 SREKVVRQILGLDD-YENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 260 CLKDRVKKLNLEKEALEG-QLKNEKDEKELYKIHLKNRELEntklsaelQMLKSvdvnKENTIAQLKDELARVKScLAEK 338
Cdd:PRK03918 225 KLEKEVKELEELKEEIEElEKELESLEGSKRKLEEKIRELE--------ERIEE----LKKEIEELEEKVKELKE-LKEK 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 339 EKQHRQLlansspSGESKALREQLRQKEEQLQATQQQANMLKAELRDSSNARDRsmaelyrirveAETLKKGQADARAEC 418
Cdd:PRK03918 292 AEEYIKL------SEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEER-----------LEELKKKLKELEKRL 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 419 SRLEQQLEEMKSSTQQEAQC----KESDVLAVAELQREVEDLRlrlqmaaehykdkyKECQKLQKQVVKFNEQQGVKRSP 494
Cdd:PRK03918 355 EELEERHELYEEAKAKKEELerlkKRLTGLTPEKLEKELEELE--------------KAKEEIEEEISKITARIGELKKE 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 495 GSD--AAAGPL-SASPEASAPGSPSTSDAVLDAI--IHGRLKSSSKELDKNDKyrKCKQMLNEERERCSMITDE--LTKM 567
Cdd:PRK03918 421 IKElkKAIEELkKAKGKCPVCGRELTEEHRKELLeeYTAELKRIEKELKEIEE--KERKLRKELRELEKVLKKEseLIKL 498
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 568 EvKLREQMKTNESLRMQLAAEEDRYKSQVAEKGRE-LKELKDSLFVLTKEKEKLEGQLQKSVNREEEQKD 636
Cdd:PRK03918 499 K-ELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEkLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDE 567
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
156-437 |
1.50e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.80 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 156 LEQKMEQIQQEKKELLENLDL--LQKERDELIDEKNRLEKEYEQER-------------ESSAQLRKDVQELQLSAQSLQ 220
Cdd:PRK04863 289 LELRRELYTSRRQLAAEQYRLveMARELAELNEAESDLEQDYQAASdhlnlvqtalrqqEKIERYQADLEELEERLEEQN 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 221 EEREEVKRRMEESTARLLQLEEDlIGVTQKGLQK-ETELDCLKDRVKKLNLEKEALEG----------QLKNEKDEKELY 289
Cdd:PRK04863 369 EVVEEADEQQEENEARAEAAEEE-VDELKSQLADyQQALDVQQTRAIQYQQAVQALERakqlcglpdlTADNAEDWLEEF 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 290 KIHLKnrELENTKLSAElQMLKSVDVNKE------NTIAQLKDELAR--VKSCLAEKEKQHR--QLLANSSPsgeskALR 359
Cdd:PRK04863 448 QAKEQ--EATEELLSLE-QKLSVAQAAHSqfeqayQLVRKIAGEVSRseAWDVARELLRRLReqRHLAEQLQ-----QLR 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 360 EQLRQKEEQLQAtQQQANMLKAEL--RDSSNARDRSMAELYRIRVEA--ETLKKGQADARAECSRLEQQLEEMKSSTQQE 435
Cdd:PRK04863 520 MRLSELEQRLRQ-QQRAERLLAEFckRLGKNLDDEDELEQLQEELEArlESLSESVSEARERRMALRQQLEQLQARIQRL 598
|
..
gi 1207119093 436 AQ 437
Cdd:PRK04863 599 AA 600
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
151-464 |
1.54e-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: 48.63 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 151 TKASYLEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEE---REEVK 227
Cdd:pfam01576 636 TRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDElqaTEDAK 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 228 RRMEESTARL-LQLEEDLIGVTQKGLQK-----------ETEL-DCLKDRV------KKLNLEKEALEGQLKNE---KDE 285
Cdd:pfam01576 716 LRLEVNMQALkAQFERDLQARDEQGEEKrrqlvkqvrelEAELeDERKQRAqavaakKKLELDLKELEAQIDAAnkgREE 795
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 286 --KELYKIHLK----NRELENTKLSAELQMLKSVDVNK-----ENTIAQLKDELA---RVKScLAEKEKQHRQLLANSSP 351
Cdd:pfam01576 796 avKQLKKLQAQmkdlQRELEEARASRDEILAQSKESEKklknlEAELLQLQEDLAaseRARR-QAQQERDELADEIASGA 874
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 352 SGESKALREQLR------QKEEQLQATQQQANMLKAELRDSSNARDRSMAELYRIRVEAETLKKGQadaraecSRLEQQL 425
Cdd:pfam01576 875 SGKSALQDEKRRleariaQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESAR-------QQLERQN 947
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1207119093 426 EEMKSSTQQ-EAQCKESDVLAVAELQREVEDLRLRLQMAA 464
Cdd:pfam01576 948 KELKAKLQEmEGTVKSKFKSSIAALEAKIAQLEEQLEQES 987
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
132-639 |
1.95e-05 |
|
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: 48.21 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 132 EEELLTMEDEGGSDILVVTTKASYLEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQE 211
Cdd:pfam07111 150 QEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEAELLRKQLSKTQEELEAQVTLVESLRKYVGE 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 212 LQLS---AQSLQEEREEVKRRMEestarllQLEEDligvtQKGLQKETELdcLKDRVKKLN----LEKEALEGQLK-NEK 283
Cdd:pfam07111 230 QVPPevhSQTWELERQELLDTMQ-------HLQED-----RADLQATVEL--LQVRVQSLThmlaLQEEELTRKIQpSDS 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 284 DEKELYKihlKNRELENT---KLSAELQMLKSVDVNKENTIAQLKDELARVKSCLaekekqhrqllanSSPSGESKALRE 360
Cdd:pfam07111 296 LEPEFPK---KCRSLLNRwreKVFALMVQLKAQDLEHRDSVKQLRGQVAELQEQV-------------TSQSQEQAILQR 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 361 QLRQKEEQLQATQQQANMLKAELRDSSNARDR------SMAELYRIRVEAetLKKGQADARAECSRLEQQLEEMKSSTQQ 434
Cdd:pfam07111 360 ALQDKAAEVEVERMSAKGLQMELSRAQEARRRqqqqtaSAEEQLKFVVNA--MSSTQIWLETTMTRVEQAVARIPSLSNR 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 435 EAQCKE---------SDVLAVAELQRE-----------VEDLRLRLQMAAEHYKDKYKECQK----LQKQVVKFNEQQGV 490
Cdd:pfam07111 438 LSYAVRkvhtikglmARKVALAQLRQEscpppppappvDADLSLELEQLREERNRLDAELQLsahlIQQEVGRAREQGEA 517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 491 KRSPGSDAAAGPLSASPEASApgSPSTSDAVLDAIIHGRLKSSskeldknDKYRKCKQMLNEERE-RCSMITDELTKMEV 569
Cdd:pfam07111 518 ERQQLSEVAQQLEQELQRAQE--SLASVGQQLEVARQGQQEST-------EEAASLRQELTQQQEiYGQALQEKVAEVET 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 570 KLREQM-----KTNESLRMQLAA-----EEDRYKSQVAEKGRELKELKDslfvltkEKEKLEGQ-LQKSVnrEEEQKDSN 638
Cdd:pfam07111 589 RLREQLsdtkrRLNEARREQAKAvvslrQIQHRATQEKERNQELRRLQD-------EARKEEGQrLARRV--QELERDKN 659
|
.
gi 1207119093 639 L 639
Cdd:pfam07111 660 L 660
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
132-390 |
1.98e-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: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 132 EEELLTMEDEGGSDILVVTTKASYLEQKMEQ---IQQEKKELLENLDLLQKERDELIDEKNRLEKEYE-QERESSAQLRK 207
Cdd:pfam17380 338 EQERMAMERERELERIRQEERKRELERIRQEeiaMEISRMRELERLQMERQQKNERVRQELEAARKVKiLEEERQRKIQQ 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 208 DVQELQLSAQSLQEEREEVKRRMEESTARLLQLeedligVTQKGLQKETELDCLKD-----RVKKLNLEKEALEGQLKNE 282
Cdd:pfam17380 418 QKVEMEQIRAEQEEARQREVRRLEEERAREMER------VRLEEQERQQQVERLRQqeeerKRKKLELEKEKRDRKRAEE 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 283 KDEKELYKiHLKNRELENTKLSAELQMLKSVDVNKENTIAQlkDELARVksclAEKEKQHRQLLAnsspsgESKALREQL 362
Cdd:pfam17380 492 QRRKILEK-ELEERKQAMIEEERKRKLLEKEMEERQKAIYE--EERRRE----AEEERRKQQEME------ERRRIQEQM 558
|
250 260 270
....*....|....*....|....*....|.
gi 1207119093 363 RQKEEQ---LQATQQQANMLKaELRDSSNAR 390
Cdd:pfam17380 559 RKATEErsrLEAMEREREMMR-QIVESEKAR 588
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
230-417 |
2.38e-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: 2.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 230 MEESTARLLQLEEdligvtqkglqKETELDCLKDRVKKLNLEKEALEGQLKNEKDEKELYKIHLKNRELENTKLSAELQM 309
Cdd:COG1579 2 MPEDLRALLDLQE-----------LDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 310 LksvdvnkENTIAQLKDELARVKS------CLAEKEKQHRQLLANSSpsgESKALREQLRQKEEQLQATQQQANMLKAEL 383
Cdd:COG1579 71 V-------EARIKKYEEQLGNVRNnkeyeaLQKEIESLKRRISDLED---EILELMERIEELEEELAELEAELAELEAEL 140
|
170 180 190
....*....|....*....|....*....|....
gi 1207119093 384 RDSSNARDRSMAElyrIRVEAETLKKGQADARAE 417
Cdd:COG1579 141 EEKKAELDEELAE---LEAELEELEAEREELAAK 171
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
131-410 |
2.52e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.83 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 131 TEEELLTMEDEGGSDILVVTTKASYLEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQ 210
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 211 ELQLSAQSLQEEREEVKRRMEESTA---------RLLQLEEDLIGVTQKGLQKETEldcLKDRVKKLNLEKEALEGQLKN 281
Cdd:COG1340 82 ELNEKLNELREELDELRKELAELNKaggsidklrKEIERLEWRQQTEVLSPEEEKE---LVEKIKELEKELEKAKKALEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 282 EKDEKELYK----IHLKNRELEN--TKLSAELQMLKsvdvnkeNTIAQLKDELARVKsclAEKEKQHRQLLANSSpsgES 355
Cdd:COG1340 159 NEKLKELRAelkeLRKEAEEIHKkiKELAEEAQELH-------EEMIELYKEADELR---KEADELHKEIVEAQE---KA 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1207119093 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 |
2.52e-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: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 157 EQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEEREEVKRRMEESTAR 236
Cdd:pfam05483 530 ERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKN 609
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 237 LLQLEEDLIGVTQKGLQKETELDCLKDRVKKLNLE----KEALEGQLKNEKDEKELYKIHLKN--RELENTKLSAE--LQ 308
Cdd:pfam05483 610 IEELHQENKALKKKGSAENKQLNAYEIKVNKLELElasaKQKFEEIIDNYQKEIEDKKISEEKllEEVEKAKAIADeaVK 689
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 309 MLKSVDVNKENTIAQLKDELARVKSCLAE------------KEKQHRQLLANSSPSGESKALREQLRQKEEQLQATQQQA 376
Cdd:pfam05483 690 LQKEIDKRCQHKIAEMVALMEKHKHQYDKiieerdselglyKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEK 769
|
250
....*....|.
gi 1207119093 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 |
2.69e-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: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 151 TKASYLEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQEL-QLSAQSLQEEREEVKRR 229
Cdd:smart00787 130 AKKMWYEWRMKLLEGLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLkQLEDELEDCDPTELDRA 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 230 MEESTARLLQLEEDLigvtQKGLQKETELDCLKDRVKKLNLEKEALEGQLKNEKDEKELYKiHLKNRELEntKLSAELQM 309
Cdd:smart00787 210 KEKLKKLLQEIMIKV----KKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCR-GFTFKEIE--KLKEQLKL 282
|
...
gi 1207119093 310 LKS 312
Cdd:smart00787 283 LQS 285
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
156-287 |
2.83e-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: 2.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 156 LEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQEL---------QLSAQSLQEEREEV 226
Cdd:COG1579 15 LDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVearikkyeeQLGNVRNNKEYEAL 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207119093 227 KRRMEESTARLLQLEEDLIGVTQKGLQKETELDCLKDRVKKLNLEKEALEGQLKNEKDEKE 287
Cdd:COG1579 95 QKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELE 155
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
187-405 |
2.91e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.20 E-value: 2.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 187 EKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEEREEVKRRMEESTARLLQLEEDLIGVTQKGLQKETELDCLKDRVK 266
Cdd:COG4372 11 ARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 267 KLNLEKEALEGQLKNEKDEKELYKIHLKNRELENTKLSAELQMLKSVDVNKENTIAQLKDELARVKSCLAEKEKQ---HR 343
Cdd:COG4372 91 AAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEElaaLE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207119093 344 QLLANSSPSGESKALREQLRQKEEQLQATQQQANMLKAELRDSSNARDRSMAELYRIRVEAE 405
Cdd:COG4372 171 QELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLG 232
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
189-473 |
3.10e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.70 E-value: 3.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 189 NRLEKEYEQEressaQLRKDVQELQLSAQSLQEEREEVKRRMEESTARL--LQLEEDLIGVTQKGLQKETELDCLKDRVK 266
Cdd:COG3206 155 NALAEAYLEQ-----NLELRREEARKALEFLEEQLPELRKELEEAEAALeeFRQKNGLVDLSEEAKLLLQQLSELESQLA 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 267 KLNLEKEALEGQLKNekdekelykihlknrelentkLSAELQMLKSV--DVNKENTIAQLKDELARVKSCLAEkekqhrq 344
Cdd:COG3206 230 EARAELAEAEARLAA---------------------LRAQLGSGPDAlpELLQSPVIQQLRAQLAELEAELAE------- 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 345 llansspsgeskaLREQLRQKEEQLQATQQQANMLKAELRdssnardrsmAELYRIRVEAETLKKGqadARAECSRLEQQ 424
Cdd:COG3206 282 -------------LSARYTPNHPDVIALRAQIAALRAQLQ----------QEAQRILASLEAELEA---LQAREASLQAQ 335
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1207119093 425 LEEMKSstqqeaqckesDVLAVAELQREVEDLRLRLQMAAEHYKD---KYKE 473
Cdd:COG3206 336 LAQLEA-----------RLAELPELEAELRRLEREVEVARELYESllqRLEE 376
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
158-393 |
3.13e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 47.77 E-value: 3.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 158 QKMEQIQQEKKELLENLDLLQKErdELIDEKNRLEKEYEQER--ESSAQLRKDVQELQLSAQSLQEEREEVKRRmEESTA 235
Cdd:COG5022 823 QKTIKREKKLRETEEVEFSLKAE--VLIQKFGRSLKAKKRFSllKKETIYLQSAQRVELAERQLQELKIDVKSI-SSLKL 899
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 236 RLLQLEEDLIGVTQKG---LQKETELDCLKD-RVKKLNLEKEALEGQLKNEKDEKELYKIHLKNRELENT--KLSAELQM 309
Cdd:COG5022 900 VNLELESEIIELKKSLssdLIENLEFKTELIaRLKKLLNNIDLEEGPSIEYVKLPELNKLHEVESKLKETseEYEDLLKK 979
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 310 LKS--VDVNKENT-IAQLKDELARV---KSCLAEKEKQHRQ-------LLANSSPSGESKALREQLRQKEEQLQATQQQA 376
Cdd:COG5022 980 STIlvREGNKANSeLKNFKKELAELskqYGALQESTKQLKElpvevaeLQSASKIISSESTELSILKPLQKLKGLLLLEN 1059
|
250
....*....|....*..
gi 1207119093 377 NMLKAELRDSSNARDRS 393
Cdd:COG5022 1060 NQLQARYKALKLRRENS 1076
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
131-242 |
3.30e-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: 3.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 131 TEEELLTMEDEGGSDILVVTTKASYLEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQER-ESSAQLRKD- 208
Cdd:COG2433 386 IEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARsEERREIRKDr 465
|
90 100 110
....*....|....*....|....*....|....*
gi 1207119093 209 -VQELQLSAQSLQEEREEVKRRMEESTARLLQLEE 242
Cdd:COG2433 466 eISRLDREIERLERELEEERERIEELKRKLERLKE 500
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
156-374 |
3.33e-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: 3.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 156 LEQKMEQIQQEKKELLENLDLLQKERDELIDE----KNRLEKEYEQERESS-----AQLRKDVQELQLSAQSLQEERE-- 224
Cdd:pfam15905 106 VEAKLNAAVREKTSLSASVASLEKQLLELTRVnellKAKFSEDGTQKKMSSlsmelMKLRNKLEAKMKEVMAKQEGMEgk 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 225 --EVKRRMEESTARLLQLEEDLIGV----------TQKGLQKETELDCLKDRVKKLNLEKEALEGQLKNekdekelykih 292
Cdd:pfam15905 186 lqVTQKNLEHSKGKVAQLEEKLVSTekekieekseTEKLLEYITELSCVSEQVEKYKLDIAQLEELLKE----------- 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 293 lKNRELENTKLsaelqmlkSVDVNKENTIAQLKDELARVKSCLAEKEKQHRQLLANSSP-SGESKALREQLRQKEEQLQA 371
Cdd:pfam15905 255 -KNDEIESLKQ--------SLEEKEQELSKQIKDLNEKCKLLESEKEELLREYEEKEQTlNAELEELKEKLTLEEQEHQK 325
|
...
gi 1207119093 372 TQQ 374
Cdd:pfam15905 326 LQQ 328
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
356-619 |
3.48e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.07 E-value: 3.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 356 KALREQLRQKEEQLQATQQQANMLKAELRDSSNARDRSMAELYRIRVEAETLKKGQADARAECSRLEQQLEEMKsstqqe 435
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK------ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 436 aqckesDVLA--VAELQREVEDLRLRLQMAAEHYKDKYKEcQKLQKQVVKFNEQQGVKrspgsdaaagplsaspeasapg 513
Cdd:COG4942 104 ------EELAelLRALYRLGRQPPLALLLSPEDFLDAVRR-LQYLKYLAPARREQAEE---------------------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 514 spstsdavldaiihgrLKSSSKELDKNdkyrkcKQMLNEERERCSMITDELTKMEVKLREQMKTNESLRMQLAAEEDRYK 593
Cdd:COG4942 155 ----------------LRADLAELAAL------RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELA 212
|
250 260
....*....|....*....|....*.
gi 1207119093 594 SQVAEKGRELKELKDSLFVLTKEKEK 619
Cdd:COG4942 213 AELAELQQEAEELEALIARLEAEAAA 238
|
|
| Zn-C2H2_TAX1BP1_rpt1 |
cd21969 |
first C2H2-type zinc binding domain found in tax1-binding protein 1 (TAX1BP1) and similar ... |
792-815 |
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
|
| Filament |
pfam00038 |
Intermediate filament protein; |
153-437 |
3.80e-05 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 46.45 E-value: 3.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 153 ASYLEqKMEQIQQEKKEL-LENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEEREEVKRRME 231
Cdd:pfam00038 14 ASYID-KVRFLEQQNKLLeTKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 232 ESTARLLQLEEDLigvtqKGLQKEteldclkdrVKKLNLEKEALEGQLKNEKDEKELYKihlKNRELENTKLSAEL---Q 308
Cdd:pfam00038 93 DELNLRTSAENDL-----VGLRKD---------LDEATLARVDLEAKIESLKEELAFLK---KNHEEEVRELQAQVsdtQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 309 MLKSVDVNKENTIAQLKDELARVKSCLAEK-----EKQHRQLLANSSPSGESKAlrEQLRQKEEQLQATQQQANMLKAEL 383
Cdd:pfam00038 156 VNVEMDAARKLDLTSALAEIRAQYEEIAAKnreeaEEWYQSKLEELQQAAARNG--DALRSAKEEITELRRTIQSLEIEL 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1207119093 384 RDSSNARD---RSMAELyrirveAETLKKGQADARAECSRLEQQLEEMKSSTQQEAQ 437
Cdd:pfam00038 234 QSLKKQKAsleRQLAET------EERYELQLADYQELISELEAELQETRQEMARQLR 284
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
190-635 |
4.88e-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: 47.12 E-value: 4.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 190 RLEKEYEQERESSAQLRKDVQELQLSAQSlqeEREEVKRRmEESTARLLQLeedligVTQKGLQKETELDclKDRVKKLN 269
Cdd:pfam10174 120 RLQSEHERQAKELFLLRKTLEEMELRIET---QKQTLGAR-DESIKKLLEM------LQSKGLPKKSGEE--DWERTRRI 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 270 LEKEALEGQLKNEKDEKELYKIHLK---NRELENTKLSAELQMLKSVDVNKENTIAQLK-------DELARVKSCLA--- 336
Cdd:pfam10174 188 AEAEMQLGHLEVLLDQKEKENIHLReelHRRNQLQPDPAKTKALQTVIEMKDTKISSLErnirdleDEVQMLKTNGLlht 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 337 -EKEKQHRQLLANSSPSGESKALREQLRQ----KEEQLQATQQQANMLKAE----------LRDSSNARDRSMAEL---- 397
Cdd:pfam10174 268 eDREEEIKQMEVYKSHSKFMKNKIDQLKQelskKESELLALQTKLETLTNQnsdckqhievLKESLTAKEQRAAILqtev 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 398 --YRIRVE--AETLKKGQ---ADARAECSRLEQQLEEMKsstqqeaqckesDVLAVAElqREVEDLRLRLQMAAEHYKDK 470
Cdd:pfam10174 348 daLRLRLEekESFLNKKTkqlQDLTEEKSTLAGEIRDLK------------DMLDVKE--RKINVLQKKIENLQEQLRDK 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 471 YKECQKLQKQVVKFNEQqgvkrSPGSDAAAGPLSaspEASapgspSTSDAVLDAIIHGRLKSSSKELDKNDKYRKCKQML 550
Cdd:pfam10174 414 DKQLAGLKERVKSLQTD-----SSNTDTALTTLE---EAL-----SEKERIIERLKEQREREDRERLEELESLKKENKDL 480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 551 neeRERCSMITDELTKMEVKLREQMKTNESLRmqlaaeedrykSQVAEKGRELKELKDSLFVLTKEKEKLEGQLQKSVNR 630
Cdd:pfam10174 481 ---KEKVSALQPELTEKESSLIDLKEHASSLA-----------SSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNA 546
|
....*
gi 1207119093 631 EEEQK 635
Cdd:pfam10174 547 EEAVR 551
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
159-633 |
4.91e-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: 47.02 E-value: 4.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 159 KMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDvqeLQLSAQSLQEEREEVKRRMEESTARll 238
Cdd:pfam05483 269 KANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEED---LQIATKTICQLTEEKEAQMEELNKA-- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 239 QLEEDLIgvtqkglqketeldclkdrVKKLNLEKEALEGQLKNEKDEKELYKIHLKNRELENTKLSAELQMLKSVDVNKE 318
Cdd:pfam05483 344 KAAHSFV-------------------VTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 319 NTIAQLKDELARVKSCLAEKEKQHRqllansspsgeskaLREQLRQKEEQ----LQATQQQANMLKAELRDSSNARDRSM 394
Cdd:pfam05483 405 VELEELKKILAEDEKLLDEKKQFEK--------------IAEELKGKEQEliflLQAREKEIHDLEIQLTAIKTSEEHYL 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 395 AELYRIRVEAETLKKGQADARAECSRLeqqleemksstqqeaqckesdVLAVAELQREVEDLRLRLQMAAEHYKDKYKEC 474
Cdd:pfam05483 471 KEVEDLKTELEKEKLKNIELTAHCDKL---------------------LLENKELTQEASDMTLELKKHQEDIINCKKQE 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 475 QKLQKQVVKFNEQQGVKRSP----------GSDAAAGPLSASPE-ASAPGSPSTSDAVLDAIIHGRLKSSSKELDKNDKY 543
Cdd:pfam05483 530 ERMLKQIENLEEKEMNLRDElesvreefiqKGDEVKCKLDKSEEnARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKN 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 544 RKCKQMLNEE-RERCSMITDELTKMEVKLREqmktnesLRMQLAAEEDRYKSQVAEKGRELKELKDSLFVLTKEKEKLEG 622
Cdd:pfam05483 610 IEELHQENKAlKKKGSAENKQLNAYEIKVNK-------LELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKA 682
|
490
....*....|.
gi 1207119093 623 QLQKSVNREEE 633
Cdd:pfam05483 683 IADEAVKLQKE 693
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
157-634 |
4.94e-05 |
|
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: 47.04 E-value: 4.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 157 EQKMEQIqqEKKELLENLDLLQ--KERDELIDEKNRL--------------EKEYEQERESSAQL--------------R 206
Cdd:pfam15921 341 EDKIEEL--EKQLVLANSELTEarTERDQFSQESGNLddqlqklladlhkrEKELSLEKEQNKRLwdrdtgnsitidhlR 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 207 KDVQELQLSAQSLQE----EREEVKRRMEESTARLLQLEEDLIGVTQKGLQKETELDCLKDRVKKLNLEKEALEGQLKNE 282
Cdd:pfam15921 419 RELDDRNMEVQRLEAllkaMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTV 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 283 KD------EKElYKIHLKNRELenTKLSA-------ELQMLKsvdvNKENTIAQLKDELARVKSCLAEKEKQ---HRQLL 346
Cdd:pfam15921 499 SDltaslqEKE-RAIEATNAEI--TKLRSrvdlklqELQHLK----NEGDHLRNVQTECEALKLQMAEKDKVieiLRQQI 571
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 347 ANSSP-SGESKALREQLRQKEEQLQATQQQANMLKAELRDSSNARDRSMAELYRIRVEAETLKKGQADARAECSRLEQQL 425
Cdd:pfam15921 572 ENMTQlVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDI 651
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 426 EEMKSSTQQEAQCKESDVLAVAE----LQREVEDLRLRLQMAAEHYKDKYKECQKLQKQVvkfneQQGVKRSPGSDAAAG 501
Cdd:pfam15921 652 KQERDQLLNEVKTSRNELNSLSEdyevLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQT-----RNTLKSMEGSDGHAM 726
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 502 PLSASPEASAPGSPSTSDAVLDAI--IHGRLKSSSKEldkndkyrkcKQMLNEERERCSmitDELTKMEVKLREQMKTNE 579
Cdd:pfam15921 727 KVAMGMQKQITAKRGQIDALQSKIqfLEEAMTNANKE----------KHFLKEEKNKLS---QELSTVATEKNKMAGELE 793
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207119093 580 SLRMQlaaeEDRYKSQVA-------EKGRELKELKDslFVLTKEKEKLEGQLQKSVNREEEQ 634
Cdd:pfam15921 794 VLRSQ----ERRLKEKVAnmevaldKASLQFAECQD--IIQRQEQESVRLKLQHTLDVKELQ 849
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
156-279 |
5.09e-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: 5.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 156 LEQKMEQIQQEKKELLENLDLLQkerdELIDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEEREEVKRRMEE--- 232
Cdd:COG4913 666 AEREIAELEAELERLDASSDDLA----ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAaed 741
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1207119093 233 --STARLLQLEEDLIGVTQKGLQKETELDcLKDRVKKLNLEKEALEGQL 279
Cdd:COG4913 742 laRLELRALLEERFAAALGDAVERELREN-LEERIDALRARLNRAEEEL 789
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
133-486 |
6.00e-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: 46.89 E-value: 6.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 133 EELLTMEDEGGSDILVVTTKASYLEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQEL 212
Cdd:pfam02463 685 AESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEE 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 213 QLSAQSLQEEREEVKRRMEESTARLLQLEEDLIGVTQKGLQKETELDCLKDRVKKLNLEKEALEG-----QLKNEKDEKE 287
Cdd:pfam02463 765 EKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKikeeeLEELALELKE 844
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 288 LYKIHLKNRELENTKLsaelqmlksvdvnkentiaqlkdELARVKSCLAEKEKQHRQLLANSSPSGESKALREQLRQKEE 367
Cdd:pfam02463 845 EQKLEKLAEEELERLE-----------------------EEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKE 901
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 368 QLQATQQQANMLKAELRDSSNARDRSMAELYRIRVEAETLKKGQADARAECSRLEQQLEEMKSSTQQEAQCKESDVLAVA 447
Cdd:pfam02463 902 LEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIE 981
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1207119093 448 ELQREVE----DLRLRLQMAAEHYKDKYKECQKLQKQVVKFNE 486
Cdd:pfam02463 982 EFEEKEErynkDELEKERLEEEKKKLIRAIIEETCQRLKEFLE 1024
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
144-348 |
6.36e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.55 E-value: 6.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 144 SDILVVTTKASYLEQKMEQ----IQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSL 219
Cdd:PHA02562 181 QQIQTLDMKIDHIQQQIKTynknIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 220 QEEREEVKRRMEeSTARLLQL----------------EEDLIG-VTQKGLQKETELDCLKDRVKKLNLEKEALEGQLKNE 282
Cdd:PHA02562 261 NTAAAKIKSKIE-QFQKVIKMyekggvcptctqqiseGPDRITkIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKL 339
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207119093 283 KDEKElyKIHLKNREL-----ENTKLSAELQMLKSVDVNKENTIAQLKDELARVKSCLAE--KEKQHRQLLAN 348
Cdd:PHA02562 340 LELKN--KISTNKQSLitlvdKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSElvKEKYHRGIVTD 410
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
323-622 |
6.47e-05 |
|
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: 46.59 E-value: 6.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 323 QLKDELARVKSCLA--EKEKQHRQLLANSSpsgESKALREQLRQKEEQLQATQQQANMLKAELRDSSNARDRSMAELYRI 400
Cdd:TIGR02168 217 ELKAELRELELALLvlRLEELREELEELQE---ELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYAL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 401 RVEAETLKKGQADARAECSRLEQQLEEMKSSTQQEAQCKESDVLAVAELQREVEDLRLRLQMAAEHYKDKYKECQKLQKQ 480
Cdd:TIGR02168 294 ANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESR 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 481 VVKFNEQQGVKRSPGSDAAAGPLSASPEASAPGSpstsdavldaiihgRLKSSSKELDKNDKYRK--CKQMLNEERERCS 558
Cdd:TIGR02168 374 LEELEEQLETLRSKVAQLELQIASLNNEIERLEA--------------RLERLEDRRERLQQEIEelLKKLEEAELKELQ 439
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207119093 559 MITDELTKMEVKLREQMKTNESLRMQLAAEEDRYKSQVAEKGRELKELKDSLFVLTKEKEKLEG 622
Cdd:TIGR02168 440 AELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
161-437 |
7.45e-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: 7.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 161 EQIQQEKKELLENLDLLQKERDELiDEKNRLEKEYEQERES-SAQLRKdVQE---LQLSAQSLQEEREEVKRRMEESTAR 236
Cdd:COG3096 292 RELFGARRQLAEEQYRLVEMAREL-EELSARESDLEQDYQAaSDHLNL-VQTalrQQEKIERYQEDLEELTERLEEQEEV 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 237 LLQLEEDLIGVTQKGLQKETELDCLK----DRVKKLN-LEKEALEGQ-----LKNEKDEKELYKIHLKNRELENTKLSAE 306
Cdd:COG3096 370 VEEAAEQLAEAEARLEAAEEEVDSLKsqlaDYQQALDvQQTRAIQYQqavqaLEKARALCGLPDLTPENAEDYLAAFRAK 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 307 LQMLKS--------VDVNKEnTIAQLKDELARVKSCLAEKE-----KQHRQLLANSsPSGESKALR-EQLRQK---EEQL 369
Cdd:COG3096 450 EQQATEevleleqkLSVADA-ARRQFEKAYELVCKIAGEVErsqawQTARELLRRY-RSQQALAQRlQQLRAQlaeLEQR 527
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207119093 370 QATQQQANMLKAELRDSSNAR--DRSMAELYRIRVEA--ETLKKGQADARAECSRLEQQLEEMKSSTQQEAQ 437
Cdd:COG3096 528 LRQQQNAERLLEEFCQRIGQQldAAEELEELLAELEAqlEELEEQAAEAVEQRSELRQQLEQLRARIKELAA 599
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
411-630 |
8.03e-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: 8.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 411 QADARAECSRLEQQLEEMKSSTQQEAQCKESDVLAVAELQREVEDLRLRLQMAAEHYKDKYKECQKLQKQVVKFNEQQGV 490
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 491 KRSPGSD--AAAGPLSASPEASAPGSPST-SDAVLDAIIHGRLKSSSKELdkNDKYRKCKQMLNEERERCSMITDELTKM 567
Cdd:COG4942 102 QKEELAEllRALYRLGRQPPLALLLSPEDfLDAVRRLQYLKYLAPARREQ--AEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207119093 568 EVKLREQMKTNESLRMQLAAEEDRYKSQVAEKGRELKELKDSLFVLTKEKEKLEGQLQKSVNR 630
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
132-630 |
8.42e-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: 46.35 E-value: 8.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 132 EEELLTMEdeggsdilVVTTKASYLEQKMEQIQQE--KKEllENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDV 209
Cdd:pfam10174 271 EEEIKQME--------VYKSHSKFMKNKIDQLKQElsKKE--SELLALQTKLETLTNQNSDCKQHIEVLKESLTAKEQRA 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 210 QELQLSAQSLQEEREEVKRRMEESTARLLQLEEDLIGVTQKGLQKETELDCLKDRVKKLNLEKEALEGQLKNEKDEKELY 289
Cdd:pfam10174 341 AILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGL 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 290 KIHLKNRELENTKLSAELQMLKSVDVNKENTIAQLKDELARVKSCLAEKEKQHRQllansspsgESKALREQLRQKEEQL 369
Cdd:pfam10174 421 KERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERLEELESLKK---------ENKDLKEKVSALQPEL 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 370 QATQQQANMLK--AELRDSSNARDRSMAELYRIRVEAEtlkkgqadaRAECSRLEQQLEEMKSSTQQEAQCKE-SDVLAV 446
Cdd:pfam10174 492 TEKESSLIDLKehASSLASSGLKKDSKLKSLEIAVEQK---------KEECSKLENQLKKAHNAEEAVRTNPEiNDRIRL 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 447 AEL------------QREVEDLR--LRLQMAAEHYKDK---------YKECQKLQKQVVKFNEQQGVKRSPGSDAAAGPL 503
Cdd:pfam10174 563 LEQevarykeesgkaQAEVERLLgiLREVENEKNDKDKkiaelesltLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEAR 642
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 504 SASPEASAPGSPSTSDAVLDAiihgrLKSSSKELDKNDKYRKCKQMLNEERERcsmitdELTKMEVKLREQMKtnESLRM 583
Cdd:pfam10174 643 RREDNLADNSQQLQLEELMGA-----LEKTRQELDATKARLSSTQQSLAEKDG------HLTNLRAERRKQLE--EILEM 709
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1207119093 584 Q----LAA--EEDRYKSQVAEKGRELKELKDSLFVLTKEKEKLEGQL-QKSVNR 630
Cdd:pfam10174 710 KqealLAAisEKDANIALLELSSSKKKKTQEEVMALKREKDRLVHQLkQQTQNR 763
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
215-394 |
9.96e-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: 9.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 215 SAQSLQEEREEVKRRMEESTARllQLEEDLIgvtqkgLQKETELDCLKDRVKKLNLEKEALEGQLKNEKDEKELYKIHLK 294
Cdd:pfam05667 302 HTEKLQFTNEAPAATSSPPTKV--ETEEELQ------QQREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 295 NRELENTKLSAELQ-MLKSVDV--NKENTIAQLK-------------------------DELARVKSCLAEKEKQHRQLL 346
Cdd:pfam05667 374 ELKEQNEELEKQYKvKKKTLDLlpDAEENIAKLQalvdasaqrlvelagqwekhrvpliEEYRALKEAKSNKEDESQRKL 453
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1207119093 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 ... |
149-481 |
1.07e-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: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 149 VTTKASYLEQKMEQIQQEKKELLENLDLLQkerdELIDEKNRLEKEYEQERESSAQLRKDVQelqlsaqSLQEEREEVKR 228
Cdd:pfam01576 463 VSSLESQLQDTQELLQEETRQKLNLSTRLR----QLEDERNSLQEQLEEEEEAKRNVERQLS-------TLQAQLSDMKK 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 229 RMEESTARLLQLEE-------DLIGVTQKGLQKETELDCLKDRVKKLNLEKEALEGQLKNEKD-----EKELYKIH--LK 294
Cdd:pfam01576 532 KLEEDAGTLEALEEgkkrlqrELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQlvsnlEKKQKKFDqmLA 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 295 NRELENTKLSAELQMLKSVDVNKENTIAQLKDELARVKSCLAEKEKQHRQLLAN-----SSPSGESKALREQLRQK---E 366
Cdd:pfam01576 612 EEKAISARYAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEmedlvSSKDDVGKNVHELERSKralE 691
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 367 EQLQATQQQANMLKAELRDSSNARDRSMAELYRIRVEAETLKKGQADARAECSR-LEQQLEEMKSSTQQEAQCKESDVLA 445
Cdd:pfam01576 692 QQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFERDLQARDEQGEEKRRqLVKQVRELEAELEDERKQRAQAVAA 771
|
330 340 350
....*....|....*....|....*....|....*.
gi 1207119093 446 VAELQREVEDLRLRLQMAAEHYKDKYKECQKLQKQV 481
Cdd:pfam01576 772 KKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQM 807
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
357-635 |
1.13e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.14 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 357 ALREQLRQKEEQLQATQQQANMLKAELRDSSNARDRSMAELYRIRVEAETLKKGQADARAECSRLEQQLeemksstqqea 436
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL----------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 437 qckesdvlavAELQREVEDLRLRLQMAAEHYKDKYKECQKLQKQvvkfneqqgvkrspgsDAAAGPLSASpeasapgspS 516
Cdd:COG4942 86 ----------AELEKEIAELRAELEAQKEELAELLRALYRLGRQ----------------PPLALLLSPE---------D 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 517 TSDAVLDAIIHGRLKSSSKELDKNdkyrkckqmLNEERERCSMITDELTKMEVKLREQMKTNESLRMQLAAEEDRYKSQV 596
Cdd:COG4942 131 FLDAVRRLQYLKYLAPARREQAEE---------LRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLL 201
|
250 260 270
....*....|....*....|....*....|....*....
gi 1207119093 597 AEKGRELKELKDSLFVLTKEKEKLEGQLQKSVNREEEQK 635
Cdd:COG4942 202 ARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
174-473 |
1.13e-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: 46.10 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 174 LDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQELQ--LSAQSLQEErEEVKRRMEESTARLLQLEEDLIGVTQKG 251
Cdd:COG3096 838 LAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNklLPQANLLAD-ETLADRLEELREELDAAQEAQAFIQQHG 916
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 252 lQKETELDCLKDRVKKLNLEKEALEGQLKNEKDEKELykihLKNRELENTKLSAELQML---KSVDVNKENtiAQLKDEL 328
Cdd:COG3096 917 -KALAQLEPLVAVLQSDPEQFEQLQADYLQAKEQQRR----LKQQIFALSEVVQRRPHFsyeDAVGLLGEN--SDLNEKL 989
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 329 arvKSCLAEKEKQHRQLlansspsgeskalREQLRQkeeqLQATQQQANMLKAELRDSSNARDRSMAELYR------IRV 402
Cdd:COG3096 990 ---RARLEQAEEARREA-------------REQLRQ----AQAQYSQYNQVLASLKSSRDAKQQTLQELEQeleelgVQA 1049
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207119093 403 EAETlkkgQADARAECSRLEQQLEEMKSS-TQQEAQckesdvLAVAElqREVEDLRLRLQMAAEHYKDKYKE 473
Cdd:COG3096 1050 DAEA----EERARIRRDELHEELSQNRSRrSQLEKQ------LTRCE--AEMDSLQKRLRKAERDYKQEREQ 1109
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
157-324 |
1.16e-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: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 157 EQKMEQIQQEKKELLENLDLLQKERDELideKNRLEkEYEQERESSAQLRKDVQELQLSAQSLQEEREEVKRRMEEstar 236
Cdd:pfam13851 46 EKLMSEIQQENKRLTEPLQKAQEEVEEL---RKQLE-NYEKDKQSLKNLKARLKVLEKELKDLKWEHEVLEQRFEK---- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 237 lLQLEEDLIgvtqkglqKETELDCLKDRVKKLNLEKEALEGQLKN-----EKDEKELYKIhLKNRELENTKLSAELQMLK 311
Cdd:pfam13851 118 -VERERDEL--------YDKFEAAIQDVQQKTGLKNLLLEKKLQAlgetlEKKEAQLNEV-LAAANLDPDALQAVTEKLE 187
|
170
....*....|...
gi 1207119093 312 SVDVNKENTIAQL 324
Cdd:pfam13851 188 DVLESKNQLIKDL 200
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
158-633 |
1.31e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 45.81 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 158 QKMEQIQQEKKELLENLDLLQKERDELIDEKNRLE------KEYEQERESSAQLRKDVQELQLSAQSLQEEREEVKRRME 231
Cdd:TIGR00606 200 QKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLEssreivKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKK 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 232 ESTARLLQLEEDLIGVTQKGLQKETELDCLKDRVKKlNLEKEALEGQLKNEKDEKELYKIHLKNRELEN----TKLSAEL 307
Cdd:TIGR00606 280 QMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVR-EKERELVDCQRELEKLNKERRLLNQEKTELLVeqgrLQLQADR 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 308 QMLKSVDVNKENTIAQLKDELARV-KSCLAEKEKQHRQLLANSSPSGESKA-------LREQLRQKEEQLQATQQQANML 379
Cdd:TIGR00606 359 HQEHIRARDSLIQSLATRLELDGFeRGPFSERQIKNFHTLVIERQEDEAKTaaqlcadLQSKERLKQEQADEIRDEKKGL 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 380 KAELRDSSNARDRSMAELYRIRVEAETLKKGQADARAECSRLEQQLEEMksSTQQEAQCKESDVLAVAELQREVEDLRLR 459
Cdd:TIGR00606 439 GRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAEREL--SKAEKNSLTETLKKEVKSLQNEKADLDRK 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 460 LQMAAE------HYKDKYKECQKLQKQVVKFNEQQGVKRSPGSDAAAGPLSASPEASAPGSPSTSDAVLDAIIHGRLKSS 533
Cdd:TIGR00606 517 LRKLDQemeqlnHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKL 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 534 SKELDK---------NDKYRKCKQMLNEER---ERCSMiTDELTKMEvKLREQMKTNESLRMQLAAEEDRYKSQVAEKGR 601
Cdd:TIGR00606 597 NKELASleqnknhinNELESKEEQLSSYEDklfDVCGS-QDEESDLE-RLKEEIEKSSKQRAMLAGATAVYSQFITQLTD 674
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1207119093 602 E---------------------LKELKDSLFVLTKEKEKLEGQLQKSVNREEE 633
Cdd:TIGR00606 675 EnqsccpvcqrvfqteaelqefISDLQSKLRLAPDKLKSTESELKKKEKRRDE 727
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
297-463 |
1.32e-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: 44.72 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 297 ELENTKLSAELQMLKsvdvnkentiAQLKDELARVKSCLAEKEKQHRQLLANSSPSGESKALREQLRQKEEQLQATQQQA 376
Cdd:pfam00529 50 QLDPTDYQAALDSAE----------AQLAKAQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 377 NMLKAELrdssnARDRSMAEL-YRIR---VEAETL-KKGQADARAECSRLEQQLEEMKSSTQQEAQCKESDV----LAVA 447
Cdd:pfam00529 120 AQAQIDL-----ARRRVLAPIgGISReslVTAGALvAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELsgaqLQIA 194
|
170
....*....|....*.
gi 1207119093 448 ELQREVEDLRLRLQMA 463
Cdd:pfam00529 195 EAEAELKLAKLDLERT 210
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
150-383 |
1.86e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 150 TTKASYLEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEEREEVKRR 229
Cdd:COG4372 93 QAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQE 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 230 MEESTARLLQLEEDLIGVTQKGLQKETELdclkDRVKKLNLEKEALEGQLKNEKDEKELYKIHLKNRELENTKLSAELQM 309
Cdd:COG4372 173 LQALSEAEAEQALDELLKEANRNAEKEEE----LAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDK 248
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207119093 310 LKSVDVNKENTIAQLKDELARVKSCLAEKEKQHRQLLANSSPSGESKALREQLRQKEEQLQATQQQANMLKAEL 383
Cdd:COG4372 249 EELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALL 322
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
151-302 |
1.87e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.20 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 151 TKASYLEQKMEQIQQEKKELLENLDLLQKERDELideKNRLEKEYEQE----RESSAQLRKDVQELQLSAQSLQEERE-- 224
Cdd:PRK00409 534 QKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKL---LEEAEKEAQQAikeaKKEADEIIKELRQLQKGGYASVKAHEli 610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 225 EVKRRMEEStarllqLEEdligVTQKGLQKETELDCLK--DRVKKLNLEKealEGQLKNEKDEKEL------YKIHLKNR 296
Cdd:PRK00409 611 EARKRLNKA------NEK----KEKKKKKQKEKQEELKvgDEVKYLSLGQ---KGEVLSIPDDKEAivqagiMKMKVPLS 677
|
....*.
gi 1207119093 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 1207119093 132 EEELLTMEDEGGSDILvvttkaSYLEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEK--------EYEQERESSA 203
Cdd:PRK05771 73 REEKKKVSVKSLEELI------KDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLEPwgnfdldlSLLLGFKYVS 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 204 QLRKDVQELQLSAQSLQEEREEV-----------------KRRMEESTARLLQLEEDLIGVTQKGLQKEtELDCLKDRVK 266
Cdd:PRK05771 147 VFVGTVPEDKLEELKLESDVENVeyistdkgyvyvvvvvlKELSDEVEEELKKLGFERLELEEEGTPSE-LIREIKEELE 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 267 KLNLEKEALEGQLKNEKDEKELYKIHLKNrELENTKLSAE--LQMLKS---------VDVNKENTIAQLKDELARVKSCL 335
Cdd:PRK05771 226 EIEKERESLLEELKELAKKYLEELLALYE-YLEIELERAEalSKFLKTdktfaiegwVPEDRVKKLKELIDKATGGSAYV 304
|
....
gi 1207119093 336 AEKE 339
Cdd:PRK05771 305 EFVE 308
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
144-287 |
2.12e-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: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 144 SDILVVTTKASYLEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQ--ERESSAQLRKDVQELQLSAQSLQE 221
Cdd:TIGR04523 496 KELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKddFELKKENLEKEIDEKNKEIEELKQ 575
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207119093 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 1207119093 156 LEQKMEQIQQEKKELL--------ENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRK----------DVQELQLSAQ 217
Cdd:COG0542 416 LERRLEQLEIEKEALKkeqdeasfERLAELRDELAELEEELEALKARWEAEKELIEEIQElkeeleqrygKIPELEKELA 495
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1207119093 218 SLQEE--------REEVKR----------------RMEES-TARLLQLEEDL 244
Cdd:COG0542 496 ELEEElaelapllREEVTEediaevvsrwtgipvgKLLEGeREKLLNLEEEL 547
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
143-242 |
2.41e-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: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 143 GSDILVVTTKASYLEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEE 222
Cdd:COG4942 128 PEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKE 207
|
90 100
....*....|....*....|
gi 1207119093 223 REEVKRRMEESTARLLQLEE 242
Cdd:COG4942 208 LAELAAELAELQQEAEELEA 227
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
152-398 |
2.56e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 152 KASYLEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEEREEvKRRME 231
Cdd:PTZ00121 1627 KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEE-AKKAE 1705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 232 EstarLLQLEEDLIGVTQKgLQKETEldclKDRVKKLNLEKEALEGQLKNE---KDEKELYKI-HLKNRE---LENTKLS 304
Cdd:PTZ00121 1706 E----LKKKEAEEKKKAEE-LKKAEE----ENKIKAEEAKKEAEEDKKKAEeakKDEEEKKKIaHLKKEEekkAEEIRKE 1776
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 305 AELQMLKSVDVNKENTIAQLKDELARVKSCLAEKEKQHRQ--LLANSSPSGESKALREQLRQKEEQLQ---ATQQQANML 379
Cdd:PTZ00121 1777 KEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEgnLVINDSKEMEDSAIKEVADSKNMQLEeadAFEKHKFNK 1856
|
250
....*....|....*....
gi 1207119093 380 KAELRDSSNARDRSMAELY 398
Cdd:PTZ00121 1857 NNENGEDGNKEADFNKEKD 1875
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
162-435 |
2.58e-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: 44.51 E-value: 2.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 162 QIQQEKKELLENLDLLQKE----RDELIDEKNRLEKEYEQERESSAQ----LRKDVQELQLSAQSLQEEREEVKRRMEES 233
Cdd:pfam15964 357 QCEQLKSELERQKERLEKElasqQEKRAQEKEALRKEMKKEREELGAtmlaLSQNVAQLEAQVEKVTREKNSLVSQLEEA 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 234 TARLLQLEEDLIGVTQKglqketeldcLKDRVKKLNLEKEALEGQLKnEKDEKELYKIHLKNRELEntKLSAELQMLKSV 313
Cdd:pfam15964 437 QKQLASQEMDVTKVCGE----------MRYQLNQTKMKKDEAEKEHR-EYRTKTGRQLEIKDQEIE--KLGLELSESKQR 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 314 DVNKENTIAQLKDELARVKSCLAEKEKQ-HRQLLANSSP----SGESKALREQLRQKEEQLQATQQQANMlkaelrdssn 388
Cdd:pfam15964 504 LEQAQQDAARAREECLKLTELLGESEHQlHLTRLEKESIqqsfSNEAKAQALQAQQREQELTQKMQQMEA---------- 573
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1207119093 389 ARDRSMAELYRIRVEAETLkkgQADARAECSRLEQQLEEMKSSTQQE 435
Cdd:pfam15964 574 QHDKTVNEQYSLLTSQNTF---IAKLKEECCTLAKKLEEITQKSRSE 617
|
|
| YydB |
COG5293 |
Uncharacterized conserved protein YydD, contains DUF2326 domain [Function unknown]; |
154-233 |
2.72e-04 |
|
Uncharacterized conserved protein YydD, contains DUF2326 domain [Function unknown];
Pssm-ID: 444096 [Multi-domain] Cd Length: 572 Bit Score: 44.55 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 154 SYLEQKMEQIQQEKKELLENLDLLQKERDEL---IDEKNRLEK------EYEQERESSAQLRKD---VQELQLSAQSLQE 221
Cdd:COG5293 326 EYLEEEIAELEAELEELEAELAELGKERAELlslLDSKGALDKykelqeELAELEAELEELESRlekLQELEDEIRELKE 405
|
90
....*....|..
gi 1207119093 222 EREEVKRRMEES 233
Cdd:COG5293 406 ERAELKEEIESD 417
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
154-564 |
2.73e-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: 2.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 154 SYLEQKMEQIQQEKKELLENLDLLQKERDELI-------DEKNRLEKEYEQERESSAQLRKDVQELQ--LSAQSLQEE-- 222
Cdd:TIGR00606 698 SDLQSKLRLAPDKLKSTESELKKKEKRRDEMLglapgrqSIIDLKEKEIPELRNKLQKVNRDIQRLKndIEEQETLLGti 777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 223 --REEVKRRMEESTARLLQLEEDLIGVTQKGLQKETELDC--LKDRVKKLNLEKEALEGQLKNEKDEKELYKIHLKNREL 298
Cdd:TIGR00606 778 mpEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGsdLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQE 857
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 299 ENTKLSAELQMLKSVDVNKENTIA-------QLKDELARVKSCLAEKEKQHRQLLANSSPSGESKALREQL-RQKEEQLQ 370
Cdd:TIGR00606 858 QIQHLKSKTNELKSEKLQIGTNLQrrqqfeeQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELiSSKETSNK 937
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 371 ATQQQANMLKAELRDSSNARDRSMAELY----RIRVEAETLKKGQADARAECSRLEQQLEE--------MKSSTQQEAQC 438
Cdd:TIGR00606 938 KAQDKVNDIKEKVKNIHGYMKDIENKIQdgkdDYLKQKETELNTVNAQLEECEKHQEKINEdmrlmrqdIDTQKIQERWL 1017
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 439 KESDVLAVAELQ-REVEDLRLRL--QMAAEHYKDKYKECQKLQKQV--VKFNEQQGVKRSPGSDAAAgpLSASPEASAPG 513
Cdd:TIGR00606 1018 QDNLTLRKRENElKEVEEELKQHlkEMGQMQVLQMKQEHQKLEENIdlIKRNHVLALGRQKGYEKEI--KHFKKELREPQ 1095
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1207119093 514 SPSTSDAVLDAIIHGRL-KSSSKELdknDKYRKC-----KQMLNEERERCSMITDEL 564
Cdd:TIGR00606 1096 FRDAEEKYREMMIVMRTtELVNKDL---DIYYKTldqaiMKFHSMKMEEINKIIRDL 1149
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
132-481 |
3.87e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.01 E-value: 3.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 132 EEELLTMEDEGG----------SDILVVTTKASYLEQKMEQIQQEK-------KELLENLDLLQKERDELIDEKNRLEKE 194
Cdd:pfam01576 137 EEDILLLEDQNSklskerklleERISEFTSNLAEEEEKAKSLSKLKnkheamiSDLEERLKKEEKGRQELEKAKRKLEGE 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 195 YEQERESSAQLRKDVQELQLSAQSLQEEREEVKRRMEESTARLLQLeedligvtQKGLQK-ETELDCLKDRVKKLNLEKE 273
Cdd:pfam01576 217 STDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNA--------LKKIRElEAQISELQEDLESERAARN 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 274 ALEGQLKNEKDEKELYKIHLKNrELENTKLSAELQmlksvdvnkentiAQLKDELARVKSCLAEKEKQHRQLLANsspsg 353
Cdd:pfam01576 289 KAEKQRRDLGEELEALKTELED-TLDTTAAQQELR-------------SKREQEVTELKKALEEETRSHEAQLQE----- 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 354 eskaLREQLRQKEEQLQATQQQANMLKAELRDSSNARDRSMAELyriRVEAETLKKGQADARAECSRLEQQLEEMKSSTQ 433
Cdd:pfam01576 350 ----MRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAEL---QAELRTLQQAKQDSEHKRKKLEGQLQELQARLS 422
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1207119093 434 QEAQCKESDVLAVAELQREVEDLRLRLQMAAEHYKDKYKECQKLQKQV 481
Cdd:pfam01576 423 ESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQL 470
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
318-635 |
3.91e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.16 E-value: 3.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 318 ENTIAQLKDELARVKSCLAEKEKQHRQLlansspsgeskalREQlRQKEEQLQATQQQANMLKAELRdsSNARDRSMAEL 397
Cdd:COG1196 178 ERKLEATEENLERLEDILGELERQLEPL-------------ERQ-AEKAERYRELKEELKELEAELL--LLKLRELEAEL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 398 YRIRVEAETLKKGQADARAECSRLEQQLEEMKSSTQQEAQCKESDVLAVAELQREVEDLRLRLQMAAEHYKDKYKECQKL 477
Cdd:COG1196 242 EELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 478 QKQVVKFNEQQGVKRSPGSDAAAGPLSASPEASApgspstSDAVLDAIIHGRLKSSSKELDKNDKYRKCKQMLNEERERC 557
Cdd:COG1196 322 EEELAELEEELEELEEELEELEEELEEAEEELEE------AEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207119093 558 SMITDELTKMEVKLREQMKTNESLRMQLAAEEDRYKSQVAEKGRELKELKDSLFVLTKEKEKLEGQLQKSVNREEEQK 635
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
157-301 |
3.96e-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: 3.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 157 EQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDV-QELQLSAQSLQEE---REEVKRRMEE 232
Cdd:pfam17380 445 AREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILeKELEERKQAMIEEerkRKLLEKEMEE 524
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 233 STARLLQLEEDLIGVTQKGLQKET-ELDCLKDRVKKLNLEKEALEGQLKNEKDEKELYKIHLKNRELENT 301
Cdd:pfam17380 525 RQKAIYEEERRREAEEERRKQQEMeERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAEYEAT 594
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
156-281 |
4.42e-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: 4.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 156 LEQKMEQiQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQELQLsaqSLQEEREEVKRRMEESTA 235
Cdd:COG3096 524 LEQRLRQ-QQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRS---ELRQQLEQLRARIKELAA 599
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207119093 236 R----------LLQLEE-------DLIGVT---QKGLQKETELDCLKDRvkkLNLEKEALEGQLKN 281
Cdd:COG3096 600 RapawlaaqdaLERLREqsgealaDSQEVTaamQQLLEREREATVERDE---LAARKQALESQIER 662
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
156-465 |
5.35e-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: 42.98 E-value: 5.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 156 LEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLE-KEYEQERESSAQLRKDVQELQLSAQSLQEEREEVKRRMEEST 234
Cdd:pfam13868 28 IAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEeERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 235 ARLlqLEEDLigvtQKGLQKETELDCLKDRVKKLNLEKEALEgQLKNEKDEKELYKIHLKNRELENTKLSAELQMLKsVD 314
Cdd:pfam13868 108 ERI--QEEDQ----AEAEEKLEKQRQLREEIDEFNEEQAEWK-ELEKEEEREEDERILEYLKEKAEREEEREAEREE-IE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 315 VNKENTIAQLKDELARVKSCLAEKEKQHRQLLANSSPSGESKALREQLRQKEEQLQATqQQANMLKAELRDSSNARDRSM 394
Cdd:pfam13868 180 EEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQEL-QQAREEQIELKERRLAEEAER 258
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207119093 395 AELYRIRVEAETLKKGQADARAECSRLEQQLEEMKsstQQEAQCKESDVLAVAELQREVEDLRLRLQMAAE 465
Cdd:pfam13868 259 EEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRR---ELEKQIEEREEQRAAEREEELEEGERLREEEAE 326
|
|
| ZapB |
COG3074 |
Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome ... |
161-232 |
5.58e-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: 5.58e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207119093 161 EQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEEREEVKRRMEE 232
Cdd:COG3074 7 EELEAKVQQAVDTIELLQMEVEELKEKNEELEQENEELQSENEELQSENEQLKTENAEWQERIRSLLGKIDE 78
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
156-488 |
5.97e-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: 43.14 E-value: 5.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 156 LEQKMEQIQQEKKEL-------------LENLD-----------LLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQE 211
Cdd:pfam05622 19 LDQQVSLLQEEKNSLqqenkklqerldqLESGDdsgtpggkkylLLQKQLEQLQEENFRLETARDDYRIKCEELEKEVLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 212 LQLSAQSLQ---EEREEVKRRME---ESTARLLQLEEdLIGVTQKGLQketELDCLKDRVKKlnLEKEALEGQLKNEKDE 285
Cdd:pfam05622 99 LQHRNEELTslaEEAQALKDEMDilrESSDKVKKLEA-TVETYKKKLE---DLGDLRRQVKL--LEERNAEYMQRTLQLE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 286 KELYKIHLKNRELENTKLS-AELQMLKSVDVNK-ENTIAQLKDELARVKSCLAEKEKqhrqLLANsspsgeskalREQLR 363
Cdd:pfam05622 173 EELKKANALRGQLETYKRQvQELHGKLSEESKKaDKLEFEYKKLEEKLEALQKEKER----LIIE----------RDTLR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 364 QKEEQLQATQQQANMLK---AELRDSSNARDRSMAEL----YR---IRVEAET--LKKGQ-ADARAECSRLEQQLEEMKS 430
Cdd:pfam05622 239 ETNEELRCAQLQQAELSqadALLSPSSDPGDNLAAEImpaeIReklIRLQHENkmLRLGQeGSYRERLTELQQLLEDANR 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207119093 431 STQQ-EAQCKESDVlAVAELQREVEDLRLRLQMAAEHYKDKYKECQKLQKQVVKFNEQQ 488
Cdd:pfam05622 319 RKNElETQNRLANQ-RILELQQQVEELQKALQEQGSKAEDSSLLKQKLEEHLEKLHEAQ 376
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
154-369 |
6.21e-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: 6.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 154 SYLEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEEREEVKRRMEes 233
Cdd:TIGR04523 464 ESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKIS-- 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 234 tarllqleedligvtqkglQKETELDCLKDRVKKLNLEKEALEGQLKNEKDEKELYKIHLKNRELEN--TKLSAELQMLK 311
Cdd:TIGR04523 542 -------------------DLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQEliDQKEKEKKDLI 602
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207119093 312 SVDVNKENTIAQLKDELARVKsclaekeKQHRQLLANSSPSGESK-ALREQLRQKEEQL 369
Cdd:TIGR04523 603 KEIEEKEKKISSLEKELEKAK-------KENEKLSSIIKNIKSKKnKLKQEVKQIKETI 654
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
133-355 |
6.28e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 6.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 133 EELLTMEDEGGSDILVVTTKASYLEQKMEQIQQEKKELLENLDLLQKERDElIDEKNRLEKEYEQERESSAQLRKDVQEL 212
Cdd:PTZ00121 1650 EELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEE-AKKAEELKKKEAEEKKKAEELKKAEEEN 1728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 213 QLSAQSLQEEREEVKRRMEEstARLLQLEEDLIgvtqKGLQKETELDCLKDRVKKLNLEKEALEgqlknEKDEKELYKIH 292
Cdd:PTZ00121 1729 KIKAEEAKKEAEEDKKKAEE--AKKDEEEKKKI----AHLKKEEEKKAEEIRKEKEAVIEEELD-----EEDEKRRMEVD 1797
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207119093 293 LKNREL-ENTKLSAELQMLKSVDVN--KENTIAQLKDELARVKSCLAEKEKQHRQLLANSSPSGES 355
Cdd:PTZ00121 1798 KKIKDIfDNFANIIEGGKEGNLVINdsKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGED 1863
|
|
| Zn-C2H2_CALCOCO1 |
cd21967 |
C2H2-type zinc binding domain found in calcium-binding and coiled-coil domain-containing ... |
790-816 |
6.37e-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: 6.37e-04
10 20
....*....|....*....|....*..
gi 1207119093 790 KICPMCSEQFPLDCDQQLFEKHVLTHF 816
Cdd:cd21967 1 KECPICKERFPLECDKDALEDHIDSHF 27
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
316-521 |
7.10e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 7.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 316 NKENTIAQLKDELARVKsclAEKEKQHRQLLANSSpsgESKALREQLRQKEEQLQATQQQANMLKAELRDSSNARDRSMA 395
Cdd:COG3883 20 AKQKELSELQAELEAAQ---AELDALQAELEELNE---EYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 396 ELYR---------------------IRVEA------------ETLKKGQADARAECSRLEQQLEEMKSSTQQEAQCKESD 442
Cdd:COG3883 94 ALYRsggsvsyldvllgsesfsdflDRLSAlskiadadadllEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207119093 443 VLAVAELQREVEDLRLRLQMAAEHYKDKYKECQKLQKQVVKFNEQQGVKRSPGSDAAAGPLSASPEASAPGSPSTSDAV 521
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAA 252
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
130-493 |
7.21e-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: 43.02 E-value: 7.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 130 PTEEELLTMEDEGGSDILVVTTKASYLEQKMEQIQQEKKELLENLDLLQKERDELIDEK-NRLEKEYEQERESSA-QLRK 207
Cdd:COG5185 138 IKVEKLDEIADIEASYGEVETGIIKDIFGKLTQELNQNLKKLEIFGLTLGLLKGISELKkAEPSGTVNSIKESETgNLGS 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 208 DVQELQLSAQSLQEEREEVKRRMEESTARLLQLEEDLIgvtQKGLQKETELDCLK-----DRVKKLNLEKEALEGQLKNE 282
Cdd:COG5185 218 ESTLLEKAKEIINIEEALKGFQDPESELEDLAQTSDKL---EKLVEQNTDLRLEKlgenaESSKRLNENANNLIKQFENT 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 283 KDE----KELYKIHLKNRELENTKLSAELqmLKSVDVNKENT---IAQLKDELARVKSCLAEKEKQHRQLLANSSPSGES 355
Cdd:COG5185 295 KEKiaeyTKSIDIKKATESLEEQLAAAEA--EQELEESKRETetgIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVEL 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 356 KALREQLRQKEEQLQAT-----------QQQANMLKAELRDSSNARDRSMAELYR-IRVEAETLKKGQADARAECSRLEQ 423
Cdd:COG5185 373 SKSSEELDSFKDTIESTkesldeipqnqRGYAQEILATLEDTLKAADRQIEELQRqIEQATSSNEEVSKLLNELISELNK 452
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 424 QLEEMKSSTQQEAQCKESDVlaVAELQREVEDLRLRLQMAAEHyKDKYKEcqKLQKQVVKFNEQQGVKRS 493
Cdd:COG5185 453 VMREADEESQSRLEEAYDEI--NRSVRSKKEDLNEELTQIESR-VSTLKA--TLEKLRAKLERQLEGVRS 517
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
169-409 |
7.61e-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: 7.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 169 ELLENLDLLQKERDELidEKNRleKEYEQERESSAQLRKDVQEL--QLSAQSLQEEREEVKRRMEESTARLLQLEEDLIG 246
Cdd:TIGR01612 1487 ELKEHIDKSKGCKDEA--DKNA--KAIEKNKELFEQYKKDVTELlnKYSALAIKNKFAKTKKDSEIIIKEIKDAHKKFIL 1562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 247 VTQKGLQKETELdclkdRVKKLNLEKEALegqlKNEKDEKELYKIHLKNRELENtklsaelQMLKSVDVNKentiaqlkd 326
Cdd:TIGR01612 1563 EAEKSEQKIKEI-----KKEKFRIEDDAA----KNDKSNKAAIDIQLSLENFEN-------KFLKISDIKK--------- 1617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 327 elaRVKSCLAEKEKQHRQL--LANSSPSGESKALREQLRQKEEQLQATQQQanmlKAELRDSSNARDRSMAELYRIRVEA 404
Cdd:TIGR01612 1618 ---KINDCLKETESIEKKIssFSIDSQDTELKENGDNLNSLQEFLESLKDQ----KKNIEDKKKELDELDSEIEKIEIDV 1690
|
....*
gi 1207119093 405 ETLKK 409
Cdd:TIGR01612 1691 DQHKK 1695
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
133-396 |
8.51e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 8.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 133 EELLTMEDEGGSDILVVTTKASYLEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLE--KEYEQERESSAQLRKDVQ 210
Cdd:PTZ00121 1537 DEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEvmKLYEEEKKMKAEEAKKAE 1616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 211 ELQLSAQSLQEEREEvkRRM----------EESTARLLQLEEDLIGVTQKGLQKETELDCLK-DRVKKLNLEKEALEGQL 279
Cdd:PTZ00121 1617 EAKIKAEELKKAEEE--KKKveqlkkkeaeEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKaEEAKKAEEDEKKAAEAL 1694
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 280 KNEKDEKelykihlknRELENTKLSAELQMLKSVDVNKENTIAQLKDELARVKsclAEKEKQHRQLLANSspSGESKALR 359
Cdd:PTZ00121 1695 KKEAEEA---------KKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKE---AEEDKKKAEEAKKD--EEEKKKIA 1760
|
250 260 270
....*....|....*....|....*....|....*..
gi 1207119093 360 EQLRQKEEQLQATQQQANMLKAELRDSSNARDRSMAE 396
Cdd:PTZ00121 1761 HLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVD 1797
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
146-398 |
8.63e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 42.99 E-value: 8.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 146 ILVVTTKaSYLEQKMEQIQQEkkELLENLDLLQKERDELIdekNRLEKEYEQERESSAQLRKDVQELQLsaqsLQEEREE 225
Cdd:PRK05771 9 VLIVTLK-SYKDEVLEALHEL--GVVHIEDLKEELSNERL---RKLRSLLTKLSEALDKLRSYLPKLNP----LREEKKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 226 VKRRMEESTARllQLEEDLIGVTQKGLQKETELDCLKDRVKKLNLEKEALEgQLKN-EKDEKELYKIHLKNRELENTKLS 304
Cdd:PRK05771 79 VSVKSLEELIK--DVEEELEKIEKEIKELEEEISELENEIKELEQEIERLE-PWGNfDLDLSLLLGFKYVSVFVGTVPED 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 305 AELQMLKSVDVNKENTIAQLKDELARVKSCLAEKEKQHRQLLANSS----PSGESKALREQLRQKEEQLQATQQQANMLK 380
Cdd:PRK05771 156 KLEELKLESDVENVEYISTDKGYVYVVVVVLKELSDEVEEELKKLGferlELEEEGTPSELIREIKEELEEIEKERESLL 235
|
250
....*....|....*...
gi 1207119093 381 AELRDSSNARDRSMAELY 398
Cdd:PRK05771 236 EELKELAKKYLEELLALY 253
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
156-237 |
1.04e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 41.35 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 156 LEQKMEQIQQEKKELLENLDL-LQKERDEL----IDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEEREEVKRRM 230
Cdd:COG1842 56 LERQLEELEAEAEKWEEKARLaLEKGREDLareaLERKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKK 135
|
....*..
gi 1207119093 231 EESTARL 237
Cdd:COG1842 136 DTLKARA 142
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
181-465 |
1.05e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.02 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 181 RDELIDEknrLEKEYEQERESSAQLRKDVQELQLSAQSL----------------QEEREEVKRRMEESTARLLQLEEDL 244
Cdd:PRK04863 784 REKRIEQ---LRAEREELAERYATLSFDVQKLQRLHQAFsrfigshlavafeadpEAELRQLNRRRVELERALADHESQE 860
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 245 IGVTQKglqketeLDCLKDRVKKLNlekeALEGQLKNEKDEkelykiHLKNR--ELENtKLSAELQMLKSVDVNkENTIA 322
Cdd:PRK04863 861 QQQRSQ-------LEQAKEGLSALN----RLLPRLNLLADE------TLADRveEIRE-QLDEAEEAKRFVQQH-GNALA 921
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 323 QLKDELarvkSCLAEKEKQHRQllansspsgeskaLREQLRQKEEQLQATQQQANMLK---------------AELRDSS 387
Cdd:PRK04863 922 QLEPIV----SVLQSDPEQFEQ-------------LKQDYQQAQQTQRDAKQQAFALTevvqrrahfsyedaaEMLAKNS 984
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207119093 388 NARDRSMAELYRIRVEAETLKKGQADARAECSRLEQQLEEMKSSTQQEAQckesdvlAVAELQREVEDLRLRLQMAAE 465
Cdd:PRK04863 985 DLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQ-------MLQELKQELQDLGVPADSGAE 1055
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
148-381 |
1.15e-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: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 148 VVTTKASYLEQKME----QIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQE-LQLSAQSLQEE 222
Cdd:pfam04012 8 LVRANIHEGLDKAEdpekMLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAaLTKGNEELARE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 223 REEVKRRMEESTARLlqleedligvtqkglqkETELDCLKDRVKKLNLEKEALEGQLKNEKDEKELYKIHLKNRelentk 302
Cdd:pfam04012 88 ALAEKKSLEKQAEAL-----------------ETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKARLKAA------ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207119093 303 lSAELQMLKSVDVNKENTIAqlkDELARVKSCLAEKEKQHRQllanSSPSGESKALREQLRQKEEQLQATQQQANMLKA 381
Cdd:pfam04012 145 -KAQEAVQTSLGSLSTSSAT---DSFERIEEKIEEREARADA----AAELASAVDLDAKLEQAGIQMEVSEDVLARLKA 215
|
|
| 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 1207119093 158 QKMEQIQQEKKELLEN-LDLLQKERDELIDEKNRLEKEYEQ--ERESSAQ--LRKDVQELQ-LSAQSLQEEREEVKRRME 231
Cdd:PRK12704 85 QKLEKRLLQKEENLDRkLELLEKREEELEKKEKELEQKQQEleKKEEELEelIEEQLQELErISGLTAEEAKEILLEKVE 164
|
.
gi 1207119093 232 E 232
Cdd:PRK12704 165 E 165
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
186-454 |
1.43e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.21 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 186 DEKNRLEKEYEQERESSAQlRKDVQELQlSAQSLQEEREEVKRRMEestarllQLEEDLIGVTQKGLQKETELDCLKDrv 265
Cdd:PRK11281 40 DVQAQLDALNKQKLLEAED-KLVQQDLE-QTLALLDKIDRQKEETE-------QLKQQLAQAPAKLRQAQAELEALKD-- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 266 kklnlekealegqlKNEKDEKELYKIhLKNRELENtKLSAELQMLKSV--DVNKENT-IAQLKDELARVKSCLAEKEK-- 340
Cdd:PRK11281 109 --------------DNDEETRETLST-LSLRQLES-RLAQTLDQLQNAqnDLAEYNSqLVSLQTQPERAQAALYANSQrl 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 341 -QHRQLLANSSPSGesKALREQLRQK-EEQLQATQQQANMLKAELRDSSN-------ARDRSMAELYRIRVEAETLKKGQ 411
Cdd:PRK11281 173 qQIRNLLKGGKVGG--KALRPSQRVLlQAEQALLNAQNDLQRKSLEGNTQlqdllqkQRDYLTARIQRLEHQLQLLQEAI 250
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1207119093 412 ADARAECSrlEQQLEEMKSstQQEAQCKESDVLAVAELQREVE 454
Cdd:PRK11281 251 NSKRLTLS--EKTVQEAQS--QDEAARIQANPLVAQELEINLQ 289
|
|
| Zn-C2H2_spn-F |
cd21971 |
C2H2-type zinc binding domain found in Drosophila melanogaster Spindle-F (Spn-F) and similar ... |
790-817 |
1.70e-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: 1.70e-03
10 20
....*....|....*....|....*...
gi 1207119093 790 KICPMCSEQFPLDCDQQLFEKHVLTHFD 817
Cdd:cd21971 2 RTCPMCGKQFSDQVSFHEFREHVEMHFI 29
|
|
| Zn-C2H2_CALCOCO2 |
cd21968 |
C2H2-type zinc binding domain found in calcium-binding and coiled-coil domain-containing ... |
790-817 |
1.76e-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: 36.27 E-value: 1.76e-03
10 20
....*....|....*....|....*...
gi 1207119093 790 KICPMCSEQFPlDCDQQLFEKHVLTHFD 817
Cdd:cd21968 1 FECPICSKIFE-ATSKQEFEDHVFCHSL 27
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
125-352 |
1.79e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 41.99 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 125 FRANSPTEEELLTMEDE--GGSDILVVTTKASYLEQKMEQIQQEKKELLEnldlLQKERDELIDEKNRLEKEYEQERESS 202
Cdd:COG5022 919 LIENLEFKTELIARLKKllNNIDLEEGPSIEYVKLPELNKLHEVESKLKE----TSEEYEDLLKKSTILVREGNKANSEL 994
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 203 AQLRKDVQELQLSAQSLQEEREEVKRRMEESTArlLQLEEDLIGVTQKGLQKETELDCLKdrvKKLNLEKEALEGQLKNE 282
Cdd:COG5022 995 KNFKKELAELSKQYGALQESTKQLKELPVEVAE--LQSASKIISSESTELSILKPLQKLK---GLLLLENNQLQARYKAL 1069
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207119093 283 KDEKELYKIHLKN-------RELENTKLSAELQMLKSVDVNKENTIAQLKDELARVKSClAEKEKQHRQLLANSSPS 352
Cdd:COG5022 1070 KLRRENSLLDDKQlyqlestENLLKTINVKDLEVTNRNLVKPANVLQFIVAQMIKLNLL-QEISKFLSQLVNTLEPV 1145
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
154-251 |
1.91e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.82 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 154 SYLEQKMEQIQQEkkelLEN----LDLLQKERDELIDEKNRLEKE--------YEQERESSAQLRKDVQELQLSAQSlqE 221
Cdd:PRK11281 202 ALLNAQNDLQRKS----LEGntqlQDLLQKQRDYLTARIQRLEHQlqllqeaiNSKRLTLSEKTVQEAQSQDEAARI--Q 275
|
90 100 110
....*....|....*....|....*....|
gi 1207119093 222 EREEVKRRMEEStarlLQLEEDLIGVTQKG 251
Cdd:PRK11281 276 ANPLVAQELEIN----LQLSQRLLKATEKL 301
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
158-558 |
1.93e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.87 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 158 QKMEQIQQEKKELLENLDLLQKERD---ELIDEKN--------RLEKEYEQERESSAQLRKDVQELQLSAQSLQEEREEV 226
Cdd:PRK04863 233 QDMEAALRENRMTLEAIRVTQSDRDlfkHLITESTnyvaadymRHANERRVHLEEALELRRELYTSRRQLAAEQYRLVEM 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 227 KRRMEESTARllqlEEDLigvtqkglqkETELDCLKDRvkkLNLEKEALEGQLKNEKDEKELYKIHLKNRE-LENTKLSA 305
Cdd:PRK04863 313 ARELAELNEA----ESDL----------EQDYQAASDH---LNLVQTALRQQEKIERYQADLEELEERLEEqNEVVEEAD 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 306 ELQMLKSVDVNK-ENTIAQLKDELARVKSCLAEKEK---QHRQ----------LLANSSPSGES-KALREQLRQKEEQLq 370
Cdd:PRK04863 376 EQQEENEARAEAaEEEVDELKSQLADYQQALDVQQTraiQYQQavqalerakqLCGLPDLTADNaEDWLEEFQAKEQEA- 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 371 atQQQANMLKAELRDSSNARDR---SMAELYRI-----RVEA-----ETLKK--------GQADA-RAECSRLEQQLEEM 428
Cdd:PRK04863 455 --TEELLSLEQKLSVAQAAHSQfeqAYQLVRKIagevsRSEAwdvarELLRRlreqrhlaEQLQQlRMRLSELEQRLRQQ 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 429 KSSTQQEAQCK---ESDVLAVAELQR-------EVEDLRLRLQMAAEHYKDKYKECQKLQKQVvkfneQQGVKRSPG--- 495
Cdd:PRK04863 533 QRAERLLAEFCkrlGKNLDDEDELEQlqeeleaRLESLSESVSEARERRMALRQQLEQLQARI-----QRLAARAPAwla 607
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207119093 496 SDAAAGPLSA-SPEASApgspsTSDAVLDAIIH--GRLKSSSKEldkNDKYRKCKQMLNEERERCS 558
Cdd:PRK04863 608 AQDALARLREqSGEEFE-----DSQDVTEYMQQllERERELTVE---RDELAARKQALDEEIERLS 665
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
161-291 |
1.95e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.74 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 161 EQIQQEKKELlenldllqkerDELIDEKNRLEKEYEQERESSAQLRKDV----QELQLSAQSLQEEREEVKRRMEESTAR 236
Cdd:PRK00409 509 KLIGEDKEKL-----------NELIASLEELERELEQKAEEAEALLKEAeklkEELEEKKEKLQEEEDKLLEEAEKEAQQ 577
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207119093 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 |
2.04e-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: 2.04e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207119093 171 LENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEEREEVKRRMEESTARL 237
Cdd:pfam06005 3 LELLEQLETKIQAAVDTIALLQMENEELKEENEELKEEANELEEENQQLKQERNQWQERIRGLLGKL 69
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
366-440 |
2.04e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 41.86 E-value: 2.04e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207119093 366 EEQLQATQQQANMLKAELRDSSNARDRSMAELYRIRVEAETLKKGQADARAECSRLEQQLEEMKS-STQQEAQCKE 440
Cdd:PRK11448 141 ENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEkAAETSQERKQ 216
|
|
| IpaC_SipC |
pfam09599 |
Salmonella-Shigella invasin protein C (IpaC_SipC); This entry represents a family of proteins ... |
247-436 |
2.14e-03 |
|
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: 41.12 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 247 VTQKGLQKETELDCLKDRVKKLNLEKEALEGQL-KNEKDEKELYKIHLKNRELENTKLSAELQMLKSVDVNKENTIAQlK 325
Cdd:pfam09599 134 IAGSALQVGITGVGAKKQMKGLSTERGALKKNLaKQAKLKQEHAEQKLELNGQNKVKLSADEVSHVKIKRNAGTSVLG-K 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 326 DELARVKSCLAEkekQHRQLLANSSPSGESKALREQLRQKEEQLQATQQQanMLKAELRDSSNArdrsmaelyrirveAE 405
Cdd:pfam09599 213 HEIDHSNERLSD---EHAAVLSSEAESLQHKIDMEQMAMEENLLKAQRKQ--MTGDLIMSGSAI--------------AG 273
|
170 180 190
....*....|....*....|....*....|.
gi 1207119093 406 TLKKGQADARAECSRLEQQLEEMKSSTQQEA 436
Cdd:pfam09599 274 NIAGASGQYAAALERSEQQISQASSRVASTA 304
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
156-244 |
2.23e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 41.86 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 156 LEQKMEQIQQEKKELLENLDLLQKERDELidekNRLEKEYEQERessAQLRKDVQELQLSAQSL-QEEREEVKRRMEEST 234
Cdd:PRK11448 154 LKQQLELQAREKAQSQALAEAQQQELVAL----EGLAAELEEKQ---QELEAQLEQLQEKAAETsQERKQKRKEITDQAA 226
|
90
....*....|
gi 1207119093 235 ARlLQLEEDL 244
Cdd:PRK11448 227 KR-LELSEEE 235
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
164-471 |
2.49e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 164 QQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQELqlsaQSLQEEREEVKRRMEESTARLLQLEED 243
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREEL----EQAREELEQLEEELEQARSELEQLEEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 244 LIGVTQKGLQKETELDCLKDRVKKLNLEKEALEGQLKNEKDEKelykihlKNRELENTKLSAELQMLKSVDVNKENTIAQ 323
Cdd:COG4372 82 LEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKER-------QDLEQQRKQLEAQIAELQSEIAEREEELKE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 324 LKDELARVKSCLAEKEKQHRQLLANSSPSGESKALREQLRQKEEQLQATQQQANMLKAELRDSSNARDRSMAELYRIRVE 403
Cdd:COG4372 155 LEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLA 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207119093 404 AETLKKGQADARAECSRLEQQLEEMKSSTQQEAQcKESDVLAVAELQREVEDLRLRLQMAAEHYKDKY 471
Cdd:COG4372 235 LSALLDALELEEDKEELLEEVILKEIEELELAIL-VEKDTEEEELEIAALELEALEEAALELKLLALL 301
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
156-269 |
2.52e-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: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 156 LEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQE-------RESSAQLRKDVQELQLSAQSLQEEREEVKR 228
Cdd:pfam07926 6 LQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQNYERElvlhaedIKALQALREELNELKAEIAELKAEAESAKA 85
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1207119093 229 RMEESTARLLQLEEDLigvtqkglqkETELDCLKDRVKKLN 269
Cdd:pfam07926 86 ELEESEESWEEQKKEL----------EKELSELEKRIEDLN 116
|
|
| Zn-C2H2_TAX1BP1_rpt2 |
cd21970 |
second C2H2-type zinc binding domain found in tax1-binding protein 1 (TAX1BP1) and similar ... |
763-788 |
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 1207119093 763 KRCPLCEVIFPPHYDQSKFEEHVESH 788
Cdd:cd21970 1 KVCPMCSEQFPPDCDQQVFERHVQTH 26
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
198-446 |
2.87e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 41.21 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 198 ERESSAQLRKDVQELQLSAQSLQEEREEVKRRMEESTARLLQLE--EDLIGVT-QKGLQKETELDCLKDRVKKLNLEKEA 274
Cdd:pfam05622 5 AQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLEsgDDSGTPGgKKYLLLQKQLEQLQEENFRLETARDD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 275 LegQLKNEKDEKELYKIHLKNRELenTKLSAELQMLK-SVDVNKENTIAQLKDElARVKSC------LAEKEKQHRQLLA 347
Cdd:pfam05622 85 Y--RIKCEELEKEVLELQHRNEEL--TSLAEEAQALKdEMDILRESSDKVKKLE-ATVETYkkkledLGDLRRQVKLLEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 348 NSSPSGESKA-LREQLRQK---EEQLQATQQQANMLKAELRDSSNARDRSMAELYRIRVEAETLKKGQADARAECSRLEQ 423
Cdd:pfam05622 160 RNAEYMQRTLqLEEELKKAnalRGQLETYKRQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKERLIIERDTLRE 239
|
250 260
....*....|....*....|...
gi 1207119093 424 QLEEMKSSTQQEAQCKESDVLAV 446
Cdd:pfam05622 240 TNEELRCAQLQQAELSQADALLS 262
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
156-440 |
2.96e-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: 40.99 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 156 LEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYE-------------QERESsaqlRKDV--------QELQL 214
Cdd:pfam03148 48 LGERIQDITFWKSELEKELEELDEEIELLLEEKRRLEKALEaleeplhiaqeclTLREK----RQGIdlvhdeveKELLK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 215 SAQSLQEEREEVKRRMEESTARLLQLEEdligvtqkgLQKETELDcLKDRVKKLNLEKEALegQLKNEKDEKELY----K 290
Cdd:pfam03148 124 EVELIEGIQELLQRTLEQAWEQLRLLRA---------ARHKLEKD-LSDKKEALEIDEKCL--SLNNTSPNISYKpgptR 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 291 IHLKNRELE-------NTKLSAELQMLKS------VDVNKENTIAQLKDELARVKSCLAEKEKQHRQLLANsspsgeska 357
Cdd:pfam03148 192 IPPNSSTPEewekftqDNIERAEKERAASaqlrelIDSILEQTANDLRAQADAVNFALRKRIEETEDAKNK--------- 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 358 LREQLRQKEEQLQATQQQANMLKAELRDSSNA-----------RDRSMAEL------YRIRVEAETLKKGQAD-----AR 415
Cdd:pfam03148 263 LEWQLKKTLQEIAELEKNIEALEKAIRDKEAPlklaqtrlenrTYRPNVELcrdeaqYGLVDEVKELEETIEAlkqklAE 342
|
330 340
....*....|....*....|....*
gi 1207119093 416 AECSRleQQLEEMKSSTQQEAQCKE 440
Cdd:pfam03148 343 AEASL--QALERTRLRLEEDIAVKA 365
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
317-635 |
3.00e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 317 KENTIAQLKDELA-----RVKSCLAEKEKQHRQLLANSSPSGESKALREQLRQKEEQLQA--TQQQANMLKAE-LRDSSN 388
Cdd:PTZ00121 1077 KDFDFDAKEDNRAdeateEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAedARKAEEARKAEdAKRVEI 1156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 389 ARDRSMAELYRIRVEAETLKKGQADARAECSRLEQQLEEMKSSTQQEAQCKESDVLAVAELQREVEDLRLRLQMAAEHYK 468
Cdd:PTZ00121 1157 ARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAK 1236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 469 DKYKECQKLQKQVvkfNEQQGVKRSPGSDAAAGPLSASPEASApgspstsdavldaiihgrlKSSSKELDKNDKYRKCKQ 548
Cdd:PTZ00121 1237 KDAEEAKKAEEER---NNEEIRKFEEARMAHFARRQAAIKAEE-------------------ARKADELKKAEEKKKADE 1294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 549 MLNEERERcsmITDELTKmevKLREQMKTNEslrMQLAAEEDRYKSQVAEKGRELKELKDSlfVLTKEKEKLEGQLQKSV 628
Cdd:PTZ00121 1295 AKKAEEKK---KADEAKK---KAEEAKKADE---AKKKAEEAKKKADAAKKKAEEAKKAAE--AAKAEAEAAADEAEAAE 1363
|
....*..
gi 1207119093 629 NREEEQK 635
Cdd:PTZ00121 1364 EKAEAAE 1370
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
301-435 |
3.22e-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: 3.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 301 TKLSAELQMLKSVDVNKENTIAQLKDELARVKSCLAEKEKQHRQllansspsgESKALREQLRQKEEQLQATQQQANMLK 380
Cdd:pfam09787 43 TALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQE---------EAESSREQLQELEEQLATERSARREAE 113
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1207119093 381 AELRDSSNARDRSMAELYRIRVeaeTLKKGQADARAECSRLEQQL--EEMKSSTQQE 435
Cdd:pfam09787 114 AELERLQEELRYLEEELRRSKA---TLQSRIKDREAEIEKLRNQLtsKSQSSSSQSE 167
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
158-399 |
3.22e-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: 3.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 158 QKMEQIQQEKKELLENL------------DLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQELQlsAQSLQEeree 225
Cdd:pfam09787 14 QKAARILQSKEKLIASLkegsgvegldssTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELE--AQQQEE---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 226 vkrrMEESTARLLQLEEDLIGVTQKGLQKETELDCLKDrvkklnlEKEALEGQLKNEKDEkelYKIHLKNRELENTKLSA 305
Cdd:pfam09787 88 ----AESSREQLQELEEQLATERSARREAEAELERLQE-------ELRYLEEELRRSKAT---LQSRIKDREAEIEKLRN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 306 ELqMLKSvdvNKENTIAQLKDELARVKSCLAEKEKQHRQLlansspSGESKALREQLRQKEEQLQATQQQA----NMLKA 381
Cdd:pfam09787 154 QL-TSKS---QSSSSQSELENRLHQLTETLIQKQTMLEAL------STEKNSLVLQLERMEQQIKELQGEGsngtSINME 223
|
250
....*....|....*...
gi 1207119093 382 ELRDSSNARDRSMAELYR 399
Cdd:pfam09787 224 GISDGEGTRLRNVPGLFS 241
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
157-244 |
3.23e-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: 3.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 157 EQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEEREEVKRRMEESTAR 236
Cdd:pfam20492 33 EETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEEKEQLEAELAEAQEEIARLEEEVERKEEEARRLQEE 112
|
....*...
gi 1207119093 237 LLQLEEDL 244
Cdd:pfam20492 113 LEEAREEE 120
|
|
| EzrA |
COG4477 |
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome ... |
156-233 |
3.30e-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: 3.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 156 LEQKMEQIQQEKKELLENLD-------LLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEEREEVKR 228
Cdd:COG4477 352 LEKQIEELEKRYDEIDERIEeekvaysELQEELEEIEEQLEEIEEEQEEFSEKLKSLRKDELEAREKLDELKKKLREIKR 431
|
....*
gi 1207119093 229 RMEES 233
Cdd:COG4477 432 RLEKS 436
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
166-626 |
3.39e-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: 41.16 E-value: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 166 EKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEEREEVKRRMEESTARLLQLEEDLI 245
Cdd:TIGR04523 34 EEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 246 GVTQKGLQKETELDCLKDRVKKLNLEKEALEGQLKNEkdEKELYKIHLKNRELENTKLSAELQMLKsvdvnkentiaqLK 325
Cdd:TIGR04523 114 NDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKK--EKELEKLNNKYNDLKKQKEELENELNL------------LE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 326 DELARVK-----------------SCLAEKEKQHRQLLA--------NSSPSGESKALREQLRQKEEQLQATQQQANMLK 380
Cdd:TIGR04523 180 KEKLNIQknidkiknkllklelllSNLKKKIQKNKSLESqiselkkqNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLK 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 381 AELRDSSNARDRSMAELYRIRVEAETLKKGQADARAECSRLEQQLE-----EMKSS-TQQEAQCKESDVL------AVAE 448
Cdd:TIGR04523 260 DEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEqdwnkELKSElKNQEKKLEEIQNQisqnnkIISQ 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 449 LQREVEDLRLRLQMAAEHYKDKYKECQKLQKQVVKF-NEQQGVKRSpgsdaaagPLSASPEASAPGSPSTSDAVLDAIIH 527
Cdd:TIGR04523 340 LNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLkKENQSYKQE--------IKNLESQINDLESKIQNQEKLNQQKD 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 528 GRLKSSSKELDKNDK-YRKCKQMLNEERERCSMITDELTKMEVKLREQMKTNESLRMQLAAEEDRY---KSQVAEKGREL 603
Cdd:TIGR04523 412 EQIKKLQQEKELLEKeIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSInkiKQNLEQKQKEL 491
|
490 500
....*....|....*....|...
gi 1207119093 604 KELKDSLFVLTKEKEKLEGQLQK 626
Cdd:TIGR04523 492 KSKEKELKKLNEEKKELEEKVKD 514
|
|
| Zn-C2H2_CALCOCO1 |
cd21967 |
C2H2-type zinc binding domain found in calcium-binding and coiled-coil domain-containing ... |
763-789 |
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 1207119093 763 KRCPLCEVIFPPHYDQSKFEEHVESHW 789
Cdd:cd21967 1 KECPICKERFPLECDKDALEDHIDSHF 27
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
155-240 |
4.34e-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: 4.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 155 YLEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERessAQLRKDVQELQLSAQSLQEEREEVKRRMEEst 234
Cdd:COG1579 100 SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKK---AELDEELAELEAELEELEAEREELAAKIPP-- 174
|
....*.
gi 1207119093 235 aRLLQL 240
Cdd:COG1579 175 -ELLAL 179
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
163-486 |
4.53e-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: 40.81 E-value: 4.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 163 IQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQ--ERESSAQLRKDVQELQLSAQSLQEEREEVKRRMEESTARLLQL 240
Cdd:TIGR01612 498 ILMRMKDFKDIIDFMELYKPDEVPSKNIIGFDIDQniKAKLYKEIEAGLKESYELAKNWKKLIHEIKKELEEENEDSIHL 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 241 EEDLIGVTQKGLQketeldcLKDRVKKLNLEKEALEGQLKNEKDEKELYKihlknrelentklsaelqmlKSVDVNK--E 318
Cdd:TIGR01612 578 EKEIKDLFDKYLE-------IDDEIIYINKLKLELKEKIKNISDKNEYIK--------------------KAIDLKKiiE 630
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 319 NTIAQLkDELARVKSCLAEKEKQHRQLLANSSPSGESKALREQLRQKEEQLQATQQQANM----LKAELRDSSNARDRSM 394
Cdd:TIGR01612 631 NNNAYI-DELAKISPYQVPEHLKNKDKIYSTIKSELSKIYEDDIDALYNELSSIVKENAIdnteDKAKLDDLKSKIDKEY 709
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 395 AELYRIrvEAETLKKGQADARAECSRLEQQLEEMKSSTQQEAQckesdvlavAELQREVEDLRLRLQMAAEHYKDKYKEC 474
Cdd:TIGR01612 710 DKIQNM--ETATVELHLSNIENKKNELLDIIVEIKKHIHGEIN---------KDLNKILEDFKNKEKELSNKINDYAKEK 778
|
330
....*....|..
gi 1207119093 475 QKLQKQVVKFNE 486
Cdd:TIGR01612 779 DELNKYKSKISE 790
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
193-362 |
5.21e-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: 5.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 193 KEYEQERESSAQLRKDVQELQLSAQSLQEEREEVKRRMEESTARLLQLEEDLIGVTQKGLQKETELDCLKDRVKKLNLE- 271
Cdd:COG3096 522 AELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARa 601
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 272 ------KEALEgQLKNEKDEkelykihlknrELENTK-LSAELQMLksvdVNKENTIAQLKDELARVKSCLaekEKQHRQ 344
Cdd:COG3096 602 pawlaaQDALE-RLREQSGE-----------ALADSQeVTAAMQQL----LEREREATVERDELAARKQAL---ESQIER 662
|
170
....*....|....*....
gi 1207119093 345 LLANSSP-SGESKALREQL 362
Cdd:COG3096 663 LSQPGGAeDPRLLALAERL 681
|
|
| DUF3450 |
pfam11932 |
Protein of unknown function (DUF3450); This family of proteins are functionally ... |
146-232 |
5.51e-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: 39.14 E-value: 5.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 146 ILVVTTKASYLEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEEREE 225
Cdd:pfam11932 1 LLALLLASGALAATLDQALDLAEKAVAAAAQSQKKIDKWDDEKQELLAEYRALKAELESLEVYNRQLERLVASQEQEIAS 80
|
....*..
gi 1207119093 226 VKRRMEE 232
Cdd:pfam11932 81 LERQIEE 87
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
144-235 |
6.06e-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: 6.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 144 SDILVVTTKASYLEQKMEQIQQ-------EKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQELQLSA 216
Cdd:COG3883 119 DRLSALSKIADADADLLEELKAdkaeleaKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQL 198
|
90
....*....|....*....
gi 1207119093 217 QSLQEEREEVKRRMEESTA 235
Cdd:COG3883 199 AELEAELAAAEAAAAAAAA 217
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
151-383 |
6.28e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 40.28 E-value: 6.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 151 TKASYLEQKMEQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRK------DVQELQLSAQSLqeerE 224
Cdd:PRK11281 49 NKQKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEAlkddndEETRETLSTLSL----R 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 225 EVKRRMEESTARLLQLEEDLIGVTQK--GLQKETEldclkdRVKKL---NLEK-EALEGQLKNEKDEKELYKIHLKNrel 298
Cdd:PRK11281 125 QLESRLAQTLDQLQNAQNDLAEYNSQlvSLQTQPE------RAQAAlyaNSQRlQQIRNLLKGGKVGGKALRPSQRV--- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 299 entKLSAELQML--------KSVDVNKE-NTIAQLKDELARVKSCLAEKEKQHRQLLANSSPSGESKalrEQLRQKEEQL 369
Cdd:PRK11281 196 ---LLQAEQALLnaqndlqrKSLEGNTQlQDLLQKQRDYLTARIQRLEHQLQLLQEAINSKRLTLSE---KTVQEAQSQD 269
|
250
....*....|....*
gi 1207119093 370 QATQQQAN-MLKAEL 383
Cdd:PRK11281 270 EAARIQANpLVAQEL 284
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
161-290 |
6.37e-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: 6.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 161 EQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESsaqlrkDVQELQLSAQSLQEEREEVKRRMEESTARLLQL 240
Cdd:TIGR00618 774 LQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPS------DEDILNLQCETLVQEEEQFLSRLEEKSATLGEI 847
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1207119093 241 EEDLIGVTQKGLQKETeldcLKDRVKKLNLEKEALEG--QLKNEKDEKELYK 290
Cdd:TIGR00618 848 THQLLKYEECSKQLAQ----LTQEQAKIIQLSDKLNGinQIKIQFDGDALIK 895
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
159-242 |
6.80e-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: 6.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 159 KMEQIQ--QEKKELLENLDLLQKERDELIDEKN--------RLEKEYEQERESSAQLRKDVQELQLSAQSLQEEREEVKR 228
Cdd:COG0542 403 RMEIDSkpEELDELERRLEQLEIEKEALKKEQDeasferlaELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQ 482
|
90
....*....|....
gi 1207119093 229 RMEESTARLLQLEE 242
Cdd:COG0542 483 RYGKIPELEKELAE 496
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
152-352 |
6.85e-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: 6.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 152 KASYLEQKMEQIQQEKKELLENLDLLQKERDEliDEKNRLEKEYEQEREssaQLRKDVQELQLSAQSLQEEREEVKRR-- 229
Cdd:pfam17380 403 KVKILEEERQRKIQQQKVEMEQIRAEQEEARQ--REVRRLEEERAREME---RVRLEEQERQQQVERLRQQEEERKRKkl 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 230 -MEESTARLLQLEEDLIGVTQKGLQKETELDCLKDRVKKLnLEKEALEGQ--LKNEKDEKELYKIHLKNRELENTKLSAE 306
Cdd:pfam17380 478 eLEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKL-LEKEMEERQkaIYEEERRREAEEERRKQQEMEERRRIQE 556
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1207119093 307 lQMLKSVDVNKENTIAQLKDELARVkscLAEKEKQHRQLLANSSPS 352
Cdd:pfam17380 557 -QMRKATEERSRLEAMEREREMMRQ---IVESEKARAEYEATTPIT 598
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
156-248 |
8.52e-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: 8.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 156 LEQKMEQIQQEKKELLenldllqKERDELIDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEEREEVKRRMEESTA 235
Cdd:COG4026 140 LKEKIDEIAKEKEKLT-------KENEELESELEELREEYKKLREENSILEEEFDNIKSEYSDLKSRFEELLKKRLLEVF 212
|
90
....*....|...
gi 1207119093 236 RLLQLEEDLIGVT 248
Cdd:COG4026 213 SLEELWKELFPEE 225
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
161-639 |
9.33e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.74 E-value: 9.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 161 EQIQQEKKELLENLDLLQKERDELIDEKNRLEKEYEQERESSAQLRKDVQELQLSAQSLQEEREEVKRRMEES------- 233
Cdd:PTZ00121 1091 EATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDArkaeear 1170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 234 ---TARLLQLEEDLIGVTQKGLQKETELDCLKDRVKKLNLEKEALEG-QLKNEKDEKELYKIHLKNRELENTKLSAELQM 309
Cdd:PTZ00121 1171 kaeDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEArKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERN 1250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 310 LKSVDVNKENTIAQLKDELARVKSCLAEKEKQHRQllansspsGESKALREQLRQKEEQLQATQQQAnmlKAELRDSSNA 389
Cdd:PTZ00121 1251 NEEIRKFEEARMAHFARRQAAIKAEEARKADELKK--------AEEKKKADEAKKAEEKKKADEAKK---KAEEAKKADE 1319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 390 RDRSMAELYR----IRVEAETLKKGQADARAECSRLEQQLEEMKSSTQQEAQCKESDVLAVAELQREVEDLRL--RLQMA 463
Cdd:PTZ00121 1320 AKKKAEEAKKkadaAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKadEAKKK 1399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 464 AEHYKDKYKECQKLQKQVVKFNE--QQGVKRSPGSDAAAGPLSASPEASAPGSPSTSDAVLDAIIHGRLKSSSKELDKND 541
Cdd:PTZ00121 1400 AEEDKKKADELKKAAAAKKKADEakKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKA 1479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 542 KYRKCKQMLNEERERCSMITDELTKMEvklrEQMKTNESLRmqlAAEEDRYKSQV--AEKGRELKELKDSLFVLTKEKEK 619
Cdd:PTZ00121 1480 EEAKKADEAKKKAEEAKKKADEAKKAA----EAKKKADEAK---KAEEAKKADEAkkAEEAKKADEAKKAEEKKKADELK 1552
|
490 500
....*....|....*....|....*...
gi 1207119093 620 LEGQLQKS--------VNREEEQKDSNL 639
Cdd:PTZ00121 1553 KAEELKKAeekkkaeeAKKAEEDKNMAL 1580
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
155-433 |
9.42e-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: 39.34 E-value: 9.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 155 YLEQKMEQIQQEKKELLENLDllqKERDELIDEKNRLEKEYEQERESSaqlrkdvQELQLSAQSLQEEREEVKRRMEEST 234
Cdd:pfam05557 6 ESKARLSQLQNEKKQMELEHK---RARIELEKKASALKRQLDRESDRN-------QELQKRIRLLEKREAEAEEALREQA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 235 ARLLQLEEDLIGVTQKGLQKETEL-------DCLKDRVKKLNLEKEALEGQLKNEKDEKELYKIHL---KNRELENTKLS 304
Cdd:pfam05557 76 ELNRLKKKYLEALNKKLNEKESQLadareviSCLKNELSELRRQIQRAELELQSTNSELEELQERLdllKAKASEAEQLR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207119093 305 AELQMLKSVDVNKENTIAQLKDELARVKSCLAEKEKQHRQLLANSspsgESKALREQLRQKEEQLQATQQQANMLKAELR 384
Cdd:pfam05557 156 QNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELARIP----ELEKELERLREHNKHLNENIENKLLLKEEVE 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1207119093 385 DSSnardrsmAELYRIrveaETLKKGQADARAECSRLEQQLEEMKSSTQ 433
Cdd:pfam05557 232 DLK-------RKLERE----EKYREEAATLELEKEKLEQELQSWVKLAQ 269
|
|
| |
