|
Name |
Accession |
Description |
Interval |
E-value |
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1-609 |
0e+00 |
|
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: 873.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887585 1 MEEVDRILIHSLRQAGTDIDEDVQSVKQFTSELIVEAVVRCLRVIDPAVGNGLSHSLPPGMSARFRLGMSLAQACQDVGF 80
Cdd:pfam05667 1 MEEVDGIIIHSLRQIGCEIAEDVQSLKDFTTELLVEAVVRCLRVINPDLGINLPLTLPPGMSARFRVGTSLAQACQELGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887585 81 KGEIGYQTFLYSNEPEIRSLFMFLVERLPRESAEASDQPAGKSVLLQRAIAAQIKAQLSVPWLPPTCRLpvHRKTQSSGP 160
Cdd:pfam05667 81 RGEIGYQTFLYPNEPDIRKILMFLVEKLPRESSEAADQPVGKSAVLQRAIAAAIRSQLAAPWLPPECKP--HQRRQGSRA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887585 161 CHSFHAQPLSLPCSlKVSSRKQPKEVQEYWRNYLLPVTAQPSQPASVPASLLENHISELSAAQEWESEWNSQGLLSRLTP 240
Cdd:pfam05667 159 LRPFHTQTLVLPGR-KGKTLKNSKELKEFYSEYLPPVTAQPSSRASVVPSLLERNAAELAAAQEWEEEWNSQGLASRLTP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887585 241 EEYRSRKKARLQKRIEEQLRTAAQPRPDTH-GATRSTSDLAELLQSFGGASTGGDVLTKGTRFTHTEKFTFTQEPEKAVq 319
Cdd:pfam05667 238 EEYRKRKRTKLLKRIAEQLRSAALAGTEATsGASRSAQDLAELLSSFSGSSTTDTGLTKGSRFTHTEKLQFTNEAPAAT- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887585 320 qmaaaaSALPSSQQSEEDLKAQQEAELSALQQQLQQLSVQMEEVGGGIKQLTVSIQQVTDELQTREVTNAERENSVKIKR 399
Cdd:pfam05667 317 ------SSPPTKVETEEELQQQREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQYKVKK 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887585 400 QTIDLLPDAENNLLKLQSLVESSSKRVVQLASQWEKHRVPLIDEHRRLKELCSNRESESSRKLSEIKDLHDKIRQSAEEA 479
Cdd:pfam05667 391 KTLDLLPDAEENIAKLQALVDASAQRLVELAGQWEKHRVPLIEEYRALKEAKSNKEDESQRKLEEIKELREKIKEVAEEA 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887585 480 KKKESLYKQLLTEFETLSKDVSRSAYTIRILEIVGNIKKQKEEITKILSDTKDLQKEINGLTGKLDRTFAVTDELVFKDA 559
Cdd:pfam05667 471 KQKEELYKQLVAEYERLPKDVSRSAYTRRILEIVKNIKKQKEEITKILSDTKSLQKEINSLTGKLDRTFTVTDELVFKDA 550
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 70887585 560 KKDESVRKSYKYLAALHENCTQLIQTIEDTGTIMREIRDLEEQIETENGK 609
Cdd:pfam05667 551 KKDESVRKAYKYLAALHENCEQLIQTVEETGTIMREIRDLEEQIETESGK 600
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
396-638 |
1.53e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.60 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887585 396 KIKRQT--IDLLPDAENNLLKLQSLVESSSKRVVQLASQWEKhrvplidehrrLKELCSNRESESSRKLSEIKDLHDKIR 473
Cdd:PRK03918 149 KVVRQIlgLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTEN-----------IEELIKEKEKELEEVLREINEISSELP 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887585 474 QSAEEAKKKESLYKQLLTEFETLSKdvsrsaYTIRILEIVGNIKKQKEEITKILSDTKDLQKEINGLtgkldrtfavtdE 553
Cdd:PRK03918 218 ELREELEKLEKEVKELEELKEEIEE------LEKELESLEGSKRKLEEKIRELEERIEELKKEIEEL------------E 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887585 554 LVFKDAKKDESVRKSYKYLAALHENCTQLIQTIEDT-GTIMREIRDLEEQIETENGKrtVSNLEKILEDYKAIRQENSAL 632
Cdd:PRK03918 280 EKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRlSRLEEEINGIEERIKELEEK--EERLEELKKKLKELEKRLEEL 357
|
....*.
gi 70887585 633 AAKIRE 638
Cdd:PRK03918 358 EERHEL 363
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
398-638 |
6.22e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.12 E-value: 6.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887585 398 KRQTIDLLPDAENNLLKLQSLVESSSKRVVQLASQWEKhrvplideHRRLKELcSNRESESSRKLS--EIKDLHDKIRQS 475
Cdd:TIGR02168 174 RKETERKLERTRENLDRLEDILNELERQLKSLERQAEK--------AERYKEL-KAELRELELALLvlRLEELREELEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887585 476 AEEAKKKESLYKQLLTEFETLSKDVSRSaytirILEIvGNIKKQKEEITKILsdtKDLQKEINGLTGkldrtfavtdELV 555
Cdd:TIGR02168 245 QEELKEAEEELEELTAELQELEEKLEEL-----RLEV-SELEEEIEELQKEL---YALANEISRLEQ----------QKQ 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887585 556 FKDAKKDESVRKSYKYLAALHENCTQLIQTIEDTGTIMREIRDLEEQIETENGK-----RTVSNLEKILEDY-KAIRQEN 629
Cdd:TIGR02168 306 ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEleeleAELEELESRLEELeEQLETLR 385
|
....*....
gi 70887585 630 SALAAKIRE 638
Cdd:TIGR02168 386 SKVAQLELQ 394
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
312-560 |
1.63e-03 |
|
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: 41.29 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887585 312 QEPEKAVQQMAAAASALPSSQQSEEDLKAQ---QEAELSALQQQLQQLSVQMEEVGGGIKQLTVSIQQVTDELQTREVTN 388
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQlaaLERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887585 389 AERENSV-KIKRQTIDLLpdaennLLKLQSLVESSskRVVQLASQWEKHRVPLIDEHRRlkelcsnresessrklsEIKD 467
Cdd:COG4942 107 AELLRALyRLGRQPPLAL------LLSPEDFLDAV--RRLQYLKYLAPARREQAEELRA-----------------DLAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887585 468 LHDKIRQSAEEAKKKESLYKQLLTEFETLSKDVSRSAYTIRILEivGNIKKQKEEITKILSDTKDLQKEINGLTGKLDRT 547
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLE--KELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
250
....*....|...
gi 70887585 548 FAVTDELVFKDAK 560
Cdd:COG4942 240 AERTPAAGFAALK 252
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1-609 |
0e+00 |
|
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: 873.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887585 1 MEEVDRILIHSLRQAGTDIDEDVQSVKQFTSELIVEAVVRCLRVIDPAVGNGLSHSLPPGMSARFRLGMSLAQACQDVGF 80
Cdd:pfam05667 1 MEEVDGIIIHSLRQIGCEIAEDVQSLKDFTTELLVEAVVRCLRVINPDLGINLPLTLPPGMSARFRVGTSLAQACQELGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887585 81 KGEIGYQTFLYSNEPEIRSLFMFLVERLPRESAEASDQPAGKSVLLQRAIAAQIKAQLSVPWLPPTCRLpvHRKTQSSGP 160
Cdd:pfam05667 81 RGEIGYQTFLYPNEPDIRKILMFLVEKLPRESSEAADQPVGKSAVLQRAIAAAIRSQLAAPWLPPECKP--HQRRQGSRA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887585 161 CHSFHAQPLSLPCSlKVSSRKQPKEVQEYWRNYLLPVTAQPSQPASVPASLLENHISELSAAQEWESEWNSQGLLSRLTP 240
Cdd:pfam05667 159 LRPFHTQTLVLPGR-KGKTLKNSKELKEFYSEYLPPVTAQPSSRASVVPSLLERNAAELAAAQEWEEEWNSQGLASRLTP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887585 241 EEYRSRKKARLQKRIEEQLRTAAQPRPDTH-GATRSTSDLAELLQSFGGASTGGDVLTKGTRFTHTEKFTFTQEPEKAVq 319
Cdd:pfam05667 238 EEYRKRKRTKLLKRIAEQLRSAALAGTEATsGASRSAQDLAELLSSFSGSSTTDTGLTKGSRFTHTEKLQFTNEAPAAT- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887585 320 qmaaaaSALPSSQQSEEDLKAQQEAELSALQQQLQQLSVQMEEVGGGIKQLTVSIQQVTDELQTREVTNAERENSVKIKR 399
Cdd:pfam05667 317 ------SSPPTKVETEEELQQQREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQYKVKK 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887585 400 QTIDLLPDAENNLLKLQSLVESSSKRVVQLASQWEKHRVPLIDEHRRLKELCSNRESESSRKLSEIKDLHDKIRQSAEEA 479
Cdd:pfam05667 391 KTLDLLPDAEENIAKLQALVDASAQRLVELAGQWEKHRVPLIEEYRALKEAKSNKEDESQRKLEEIKELREKIKEVAEEA 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887585 480 KKKESLYKQLLTEFETLSKDVSRSAYTIRILEIVGNIKKQKEEITKILSDTKDLQKEINGLTGKLDRTFAVTDELVFKDA 559
Cdd:pfam05667 471 KQKEELYKQLVAEYERLPKDVSRSAYTRRILEIVKNIKKQKEEITKILSDTKSLQKEINSLTGKLDRTFTVTDELVFKDA 550
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 70887585 560 KKDESVRKSYKYLAALHENCTQLIQTIEDTGTIMREIRDLEEQIETENGK 609
Cdd:pfam05667 551 KKDESVRKAYKYLAALHENCEQLIQTVEETGTIMREIRDLEEQIETESGK 600
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
396-638 |
1.53e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.60 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887585 396 KIKRQT--IDLLPDAENNLLKLQSLVESSSKRVVQLASQWEKhrvplidehrrLKELCSNRESESSRKLSEIKDLHDKIR 473
Cdd:PRK03918 149 KVVRQIlgLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTEN-----------IEELIKEKEKELEEVLREINEISSELP 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887585 474 QSAEEAKKKESLYKQLLTEFETLSKdvsrsaYTIRILEIVGNIKKQKEEITKILSDTKDLQKEINGLtgkldrtfavtdE 553
Cdd:PRK03918 218 ELREELEKLEKEVKELEELKEEIEE------LEKELESLEGSKRKLEEKIRELEERIEELKKEIEEL------------E 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887585 554 LVFKDAKKDESVRKSYKYLAALHENCTQLIQTIEDT-GTIMREIRDLEEQIETENGKrtVSNLEKILEDYKAIRQENSAL 632
Cdd:PRK03918 280 EKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRlSRLEEEINGIEERIKELEEK--EERLEELKKKLKELEKRLEEL 357
|
....*.
gi 70887585 633 AAKIRE 638
Cdd:PRK03918 358 EERHEL 363
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
372-638 |
2.40e-06 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 50.70 E-value: 2.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887585 372 VSIQQVTDELQTREVTNAeRENSVKIKRqTIDLLPDAENNLLKLQSLVESSSKRvvqlasqwekhrvplidehrRLKELC 451
Cdd:PRK05771 31 VHIEDLKEELSNERLRKL-RSLLTKLSE-ALDKLRSYLPKLNPLREEKKKVSVK--------------------SLEELI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887585 452 SNRESESSRKLSEIKDLHDKIRQSAEEAKKKESLyKQLLTEFETLSKDVSRSAYTIRILEIVGNIKKQKEEITKILSDtK 531
Cdd:PRK05771 89 KDVEEELEKIEKEIKELEEEISELENEIKELEQE-IERLEPWGNFDLDLSLLLGFKYVSVFVGTVPEDKLEELKLESD-V 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887585 532 DLQKEINglTGKLDRTFAVTDElvFKDAKKDESVRKSYKYLAalhenctqliQTIEDTGTIMREIRDLEEQIETENGKRt 611
Cdd:PRK05771 167 ENVEYIS--TDKGYVYVVVVVL--KELSDEVEEELKKLGFER----------LELEEEGTPSELIREIKEELEEIEKER- 231
|
250 260
....*....|....*....|....*..
gi 70887585 612 vsnlEKILEDYKAIRQENSALAAKIRE 638
Cdd:PRK05771 232 ----ESLLEELKELAKKYLEELLALYE 254
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
440-639 |
9.73e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 9.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887585 440 LIDEHRRLKELCSNR---ESESSRKLSEIKDLHDKIRQ----SAEEAKKKESLYKQLLTEFETLSKDVSRsaytIRILEi 512
Cdd:PRK03918 544 LKKELEKLEELKKKLaelEKKLDELEEELAELLKELEElgfeSVEELEERLKELEPFYNEYLELKDAEKE----LEREE- 618
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887585 513 vGNIKKQKEEITKILSDTKDLQKEINGLTGKLDRTFAVTDELVFKDaKKDESVRKSyKYLAALHENCTQLIQTIEdtgTI 592
Cdd:PRK03918 619 -KELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEE-LREEYLELS-RELAGLRAELEELEKRRE---EI 692
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 70887585 593 MREIRDLEEQIET-ENGKRTVSNLEKILEDYKAIRQENSALAAKIREG 639
Cdd:PRK03918 693 KKTLEKLKEELEErEKAKKELEKLEKALERVEELREKVKKYKALLKER 740
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
246-638 |
1.74e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.13 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887585 246 RKKARLQKRIEEqLRTAAQPRPDTHGATRSTSDLAELLQSfggastgGDVLTKGTRFTHTEKFTFTQEPEKAVQQMAAAA 325
Cdd:PTZ00121 1503 KKAAEAKKKADE-AKKAEEAKKADEAKKAEEAKKADEAKK-------AEEKKKADELKKAEELKKAEEKKKAEEAKKAEE 1574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887585 326 SALPSSQQSEEDLKAQQEAELSALQQQLQQLSVQMEEVGGGiKQLTVSIQQVTDELQTREVTNAERENSVKIKRQTIDLL 405
Cdd:PTZ00121 1575 DKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKA-EEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELK 1653
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887585 406 PDAENNLLKLQSLV--ESSSKRVVQLASQWEkhrvplidEHRRLKELCSNRESESSRKLSEIKDLHDKIRQSAEEAKKKE 483
Cdd:PTZ00121 1654 KAEEENKIKAAEEAkkAEEDKKKAEEAKKAE--------EDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAE 1725
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887585 484 SLYKQLLTEFETLSKDVSRSAYTIRILEivGNIKK----QKEEITKILSDTKDLQKEINGLTGKLDRTFAVTDELVFKDA 559
Cdd:PTZ00121 1726 EENKIKAEEAKKEAEEDKKKAEEAKKDE--EEKKKiahlKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDI 1803
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887585 560 KKD-----ESVRKSYKYLAALHENCTQLIQTIEDTGTIMREIRDLEEQ----IETENGKRTVSNLEKILEDYKAIRQENS 630
Cdd:PTZ00121 1804 FDNfaniiEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKhkfnKNNENGEDGNKEADFNKEKDLKEDDEEE 1883
|
....*...
gi 70887585 631 ALAAKIRE 638
Cdd:PTZ00121 1884 IEEADEIE 1891
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
398-638 |
6.22e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.12 E-value: 6.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887585 398 KRQTIDLLPDAENNLLKLQSLVESSSKRVVQLASQWEKhrvplideHRRLKELcSNRESESSRKLS--EIKDLHDKIRQS 475
Cdd:TIGR02168 174 RKETERKLERTRENLDRLEDILNELERQLKSLERQAEK--------AERYKEL-KAELRELELALLvlRLEELREELEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887585 476 AEEAKKKESLYKQLLTEFETLSKDVSRSaytirILEIvGNIKKQKEEITKILsdtKDLQKEINGLTGkldrtfavtdELV 555
Cdd:TIGR02168 245 QEELKEAEEELEELTAELQELEEKLEEL-----RLEV-SELEEEIEELQKEL---YALANEISRLEQ----------QKQ 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887585 556 FKDAKKDESVRKSYKYLAALHENCTQLIQTIEDTGTIMREIRDLEEQIETENGK-----RTVSNLEKILEDY-KAIRQEN 629
Cdd:TIGR02168 306 ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEleeleAELEELESRLEELeEQLETLR 385
|
....*....
gi 70887585 630 SALAAKIRE 638
Cdd:TIGR02168 386 SKVAQLELQ 394
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
312-560 |
1.63e-03 |
|
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: 41.29 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887585 312 QEPEKAVQQMAAAASALPSSQQSEEDLKAQ---QEAELSALQQQLQQLSVQMEEVGGGIKQLTVSIQQVTDELQTREVTN 388
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQlaaLERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887585 389 AERENSV-KIKRQTIDLLpdaennLLKLQSLVESSskRVVQLASQWEKHRVPLIDEHRRlkelcsnresessrklsEIKD 467
Cdd:COG4942 107 AELLRALyRLGRQPPLAL------LLSPEDFLDAV--RRLQYLKYLAPARREQAEELRA-----------------DLAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887585 468 LHDKIRQSAEEAKKKESLYKQLLTEFETLSKDVSRSAYTIRILEivGNIKKQKEEITKILSDTKDLQKEINGLTGKLDRT 547
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLE--KELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
250
....*....|...
gi 70887585 548 FAVTDELVFKDAK 560
Cdd:COG4942 240 AERTPAAGFAALK 252
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
332-637 |
1.86e-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: 41.54 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887585 332 QQSEEDLKAQQEAELSALQQQLQQLSVQMEEVGGGIKQLTVSIQQVTDELQTREVTNAERENSVKIKRQTI-DLLPDAEN 410
Cdd:TIGR04523 302 NQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIeKLKKENQS 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887585 411 NLLKLQSLVESSSKRVVQLASQ-------------WEKHRVPLIDEHRRLKEL-------CSNRESESSRKLSEIKDLHD 470
Cdd:TIGR04523 382 YKQEIKNLESQINDLESKIQNQeklnqqkdeqikkLQQEKELLEKEIERLKETiiknnseIKDLTNQDSVKELIIKNLDN 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887585 471 KIRQSAEEAKKKESLYKQLLTEFETLSKDVSR-----SAYTIRILEIVGNIKKQKEEITKILSDTKDLQKEINGLTGKLD 545
Cdd:TIGR04523 462 TRESLETQLKVLSRSINKIKQNLEQKQKELKSkekelKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKIS 541
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887585 546 --RTFAVTDELVFKDAKKDESVRKSYKYLAALHENCTQLIQTIEDTGTIMR----EIRDLEEQIETENgkRTVSNLEKIL 619
Cdd:TIGR04523 542 dlEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDqkekEKKDLIKEIEEKE--KKISSLEKEL 619
|
330
....*....|....*...
gi 70887585 620 EDykaIRQENSALAAKIR 637
Cdd:TIGR04523 620 EK---AKKENEKLSSIIK 634
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
368-624 |
2.51e-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: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887585 368 KQLTVSIQQVTDELQTREVTNAERENSVKIKRQTIDLLPDAENNLLKLQSLVESSSKRVVQLASQWEKHRVPLIDEHRRL 447
Cdd:TIGR04523 36 KQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKND 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887585 448 KELCSNRESESSRKLSEIKDLHDKIRQSAEEAKKKESLYKQLLTEFETLSKDVSRSAYTIRILE--------IVGNIKKQ 519
Cdd:TIGR04523 116 KEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEkeklniqkNIDKIKNK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887585 520 KEEITKILSDTKDLQKEINGLTGKLDRTFAVTDELvfKDAKKDESVRKSYKYlAALHENCTQLIQTIEDTGTIMREIRDL 599
Cdd:TIGR04523 196 LLKLELLLSNLKKKIQKNKSLESQISELKKQNNQL--KDNIEKKQQEINEKT-TEISNTQTQLNQLKDEQNKIKKQLSEK 272
|
250 260
....*....|....*....|....*
gi 70887585 600 EEQIETENGKrtVSNLEKILEDYKA 624
Cdd:TIGR04523 273 QKELEQNNKK--IKELEKQLNQLKS 295
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
367-571 |
8.18e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 39.23 E-value: 8.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887585 367 IKQLTVSIQQVTDELQTREVTNAERENSVKikrqtidllpDAENNLLKLQSLVESSSKrvvqLASQWEKHRV-PLidehr 445
Cdd:PHA02562 229 AKTIKAEIEELTDELLNLVMDIEDPSAALN----------KLNTAAAKIKSKIEQFQK----VIKMYEKGGVcPT----- 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887585 446 rlkelCSNRESESSRKLSEIKDLHDKIRQSAEEAKKKESLYKQLLTEFETLSKdvsrsaytiRILEIVGNIKKQKEEITK 525
Cdd:PHA02562 290 -----CTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSK---------KLLELKNKISTNKQSLIT 355
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 70887585 526 ILSDTKDLQKEINGLTGK-LDRTFAVT---DELVFKDAKKDESVRKSYKY 571
Cdd:PHA02562 356 LVDKAKKVKAAIEELQAEfVDNAEELAklqDELDKIVKTKSELVKEKYHR 405
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
360-637 |
8.27e-03 |
|
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: 39.33 E-value: 8.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887585 360 MEEVGGGIKQLTVSIQQVTDELqtrEVTNAERENSVKIkrqtidLLPDAENNLLKLQSLVESSSKRVVQLASQWEKHRVP 439
Cdd:pfam15921 226 LRELDTEISYLKGRIFPVEDQL---EALKSESQNKIEL------LLQQHQDRIEQLISEHEVEITGLTEKASSARSQANS 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887585 440 LIDEHRRLKELCSNRESESSRKLSEIKDLHDKIRQSAEEAK-----KKESLYKQL------LTEFETLSKDVSRSAYTI- 507
Cdd:pfam15921 297 IQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKrmyedKIEELEKQLvlanseLTEARTERDQFSQESGNLd 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887585 508 -RILEIVGNIKKQKEEITKILSDTKDLQKE-------INGLTGKL-DRTFAVTDELVFKDAKKDESVRKSYKYLAALH-- 576
Cdd:pfam15921 377 dQLQKLLADLHKREKELSLEKEQNKRLWDRdtgnsitIDHLRRELdDRNMEVQRLEALLKAMKSECQGQMERQMAAIQgk 456
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 70887585 577 ----ENCTQLIQTIEDTGTIMREIRD--LEEQIETENGKRTVSNLEKIL-EDYKAIRQENSALaAKIR 637
Cdd:pfam15921 457 neslEKVSSLTAQLESTKEMLRKVVEelTAKKMTLESSERTVSDLTASLqEKERAIEATNAEI-TKLR 523
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
400-547 |
9.89e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 38.35 E-value: 9.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887585 400 QTIDLLPDAENNLLKlqslvessskRVVQLASQWEKhRVPLIDEHRRLKELcsnrESESSRKLSEIKDLHDKIRQSAEEA 479
Cdd:COG1340 126 QTEVLSPEEEKELVE----------KIKELEKELEK-AKKALEKNEKLKEL----RAELKELRKEAEEIHKKIKELAEEA 190
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 70887585 480 KKKESLYKQLLTEFETLSKdvSRSAYTIRILEIVGNIKKQKEEITKILSDTKDLQKEINGLTGKLDRT 547
Cdd:COG1340 191 QELHEEMIELYKEADELRK--EADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRAL 256
|
|
|