|
Name |
Accession |
Description |
Interval |
E-value |
| LETM1_RBD |
pfam07766 |
LETM1-like, RBD; Members of this entry are inner mitochondrial membrane proteins which play a ... |
198-429 |
1.05e-121 |
|
LETM1-like, RBD; Members of this entry are inner mitochondrial membrane proteins which play a role in potassium and hydrogen ion exchange. Deletion of LETM1 is thought to be involved in the development of Wolf-Hirschhorn syndrome in humans. This entry represents the ribosome-binding domain (RBD) of LETM1/MDM38 proteins.
Pssm-ID: 462258 [Multi-domain] Cd Length: 229 Bit Score: 364.11 E-value: 1.05e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113680846 198 LSRRERRQFLRTCADVFRLLPFLVFIIVPFMEFLLPVALKLFPNMLPSTFETQSKKEERLKKELRVKLEMAKFLQDTIEE 277
Cdd:pfam07766 1 LTRREREQLRRTTRDLFRLVPFSVFIIVPFAELLLPVLLKLFPNLLPSTFWSKKQKEEKLKKRLKARLEVAKFLQETVEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113680846 278 IAlrnKASKGNVTEEFSTFFQKIRDSGEIPSNEQIIRFSKLFEDELTLDNLTRPQLVALCKLLELQSIGTNNFLRFQLIM 357
Cdd:pfam07766 81 SL---SDETTELKEEFKEFFKKVRSGGEPPSNEEILKVAKLFKDDLTLDNLSRPQLVALCKYMNLTPFGTDNLLRYRLRH 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 113680846 358 KLRAIRADDKLIAEEGVDSLTANELQAACRVRGMRALGVTEERLREQLKQWLELHLNQHIPTSLLLLSRAMF 429
Cdd:pfam07766 158 KLLEIKRDDRAIAREGVDSLSLEELQSACYSRGIRPLGLSEERLREWLQQWLDLSLNLKVPSSLLLLSRAVL 229
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
422-644 |
5.69e-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: 49.38 E-value: 5.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113680846 422 LLLSRAMFLPDTLSPADQLKTTLQNLPEIMAKEAQVKVAELDFSKVDNKTKLETTLQEEAAIRQENRERELERLADAAEK 501
Cdd:COG4942 4 LLLLALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113680846 502 AKEQTQSQEAEVLEVEGERRVDAEHAL---------SSVDVAIHSETLRDTAPVLEGIKG-EEITKEEIDMLSDACTKLK 571
Cdd:COG4942 84 ELAELEKEIAELRAELEAQKEELAELLralyrlgrqPPLALLLSPEDFLDAVRRLQYLKYlAPARREQAEELRADLAELA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 113680846 572 EQKNLLTKEKEELEDLKDDVQEYSEDLEEIKRELSKTGQEKAVEESKASQRLsKRVNRMIGRMDKIITELEKD 644
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAEL-AELQQEAEELEALIARLEAE 235
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
453-645 |
1.08e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.37 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113680846 453 KEAQVKVAElDFSKVDNKTKLETTLQEEAAIRQENRERELERLADAAEKAKEQTQSQEAEVLEV----EGERRVDAEHAL 528
Cdd:PTZ00121 1535 KADEAKKAE-EKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVmklyEEEKKMKAEEAK 1613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113680846 529 SSVDVAIHSETLRDTAPVLEGI------------KGEEITKEEidmlSDACTKLKEQKNLLTKEKEELEDLKDDVQEYSE 596
Cdd:PTZ00121 1614 KAEEAKIKAEELKKAEEEKKKVeqlkkkeaeekkKAEELKKAE----EENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKK 1689
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 113680846 597 DLEEIKRELSKTGQ-----EKAVEESKASQRLSKRVNRMIGRMDKIITELEKDK 645
Cdd:PTZ00121 1690 AAEALKKEAEEAKKaeelkKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDK 1743
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
454-632 |
1.59e-04 |
|
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: 45.44 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113680846 454 EAQVKVAELDFSKVDNK-TKLETTLQEEAAIR-------QENRERELERLADAAEKAKE-----QTQSQEAEVLEVEGER 520
Cdd:TIGR02169 321 EERLAKLEAEIDKLLAEiEELEREIEEERKRRdklteeyAELKEELEDLRAELEEVDKEfaetrDELKDYREKLEKLKRE 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113680846 521 RVDAEHALSSVDVAIH--SETLRDTAPVLEGIKG-----EEITKEEIDMLSDACTKLKEQKNLLTKEKEELEDLKDDVQE 593
Cdd:TIGR02169 401 INELKRELDRLQEELQrlSEELADLNAAIAGIEAkinelEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDR 480
|
170 180 190
....*....|....*....|....*....|....*....
gi 113680846 594 YSEDLEEIKRELSKTgqEKAVEESKASQRLSKRVNRMIG 632
Cdd:TIGR02169 481 VEKELSKLQRELAEA--EAQARASEERVRGGRAVEEVLK 517
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
483-647 |
1.06e-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: 42.42 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113680846 483 IRQENRERELERLADaAEKAKEQTQSQEAEVLEVEGERRVD-AEHALSSVDVAIHSETLRDTAPVLEGIKGEEITKEEID 561
Cdd:pfam17380 353 IRQEERKRELERIRQ-EEIAMEISRMRELERLQMERQQKNErVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEE 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113680846 562 MLSDACTKLKEQKnlltkeKEELEDLKDDVQEYSEDLEEIKRELSKTGQEK-AVEESKASQRLSKRVNRMI------GRM 634
Cdd:pfam17380 432 ARQREVRRLEEER------AREMERVRLEEQERQQQVERLRQQEEERKRKKlELEKEKRDRKRAEEQRRKIlekeleERK 505
|
170
....*....|...
gi 113680846 635 DKIITELEKDKMV 647
Cdd:pfam17380 506 QAMIEEERKRKLL 518
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| LETM1_RBD |
pfam07766 |
LETM1-like, RBD; Members of this entry are inner mitochondrial membrane proteins which play a ... |
198-429 |
1.05e-121 |
|
LETM1-like, RBD; Members of this entry are inner mitochondrial membrane proteins which play a role in potassium and hydrogen ion exchange. Deletion of LETM1 is thought to be involved in the development of Wolf-Hirschhorn syndrome in humans. This entry represents the ribosome-binding domain (RBD) of LETM1/MDM38 proteins.
Pssm-ID: 462258 [Multi-domain] Cd Length: 229 Bit Score: 364.11 E-value: 1.05e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113680846 198 LSRRERRQFLRTCADVFRLLPFLVFIIVPFMEFLLPVALKLFPNMLPSTFETQSKKEERLKKELRVKLEMAKFLQDTIEE 277
Cdd:pfam07766 1 LTRREREQLRRTTRDLFRLVPFSVFIIVPFAELLLPVLLKLFPNLLPSTFWSKKQKEEKLKKRLKARLEVAKFLQETVEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113680846 278 IAlrnKASKGNVTEEFSTFFQKIRDSGEIPSNEQIIRFSKLFEDELTLDNLTRPQLVALCKLLELQSIGTNNFLRFQLIM 357
Cdd:pfam07766 81 SL---SDETTELKEEFKEFFKKVRSGGEPPSNEEILKVAKLFKDDLTLDNLSRPQLVALCKYMNLTPFGTDNLLRYRLRH 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 113680846 358 KLRAIRADDKLIAEEGVDSLTANELQAACRVRGMRALGVTEERLREQLKQWLELHLNQHIPTSLLLLSRAMF 429
Cdd:pfam07766 158 KLLEIKRDDRAIAREGVDSLSLEELQSACYSRGIRPLGLSEERLREWLQQWLDLSLNLKVPSSLLLLSRAVL 229
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
422-644 |
5.69e-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: 49.38 E-value: 5.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113680846 422 LLLSRAMFLPDTLSPADQLKTTLQNLPEIMAKEAQVKVAELDFSKVDNKTKLETTLQEEAAIRQENRERELERLADAAEK 501
Cdd:COG4942 4 LLLLALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113680846 502 AKEQTQSQEAEVLEVEGERRVDAEHAL---------SSVDVAIHSETLRDTAPVLEGIKG-EEITKEEIDMLSDACTKLK 571
Cdd:COG4942 84 ELAELEKEIAELRAELEAQKEELAELLralyrlgrqPPLALLLSPEDFLDAVRRLQYLKYlAPARREQAEELRADLAELA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 113680846 572 EQKNLLTKEKEELEDLKDDVQEYSEDLEEIKRELSKTGQEKAVEESKASQRLsKRVNRMIGRMDKIITELEKD 644
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAEL-AELQQEAEELEALIARLEAE 235
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
453-645 |
1.08e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.37 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113680846 453 KEAQVKVAElDFSKVDNKTKLETTLQEEAAIRQENRERELERLADAAEKAKEQTQSQEAEVLEV----EGERRVDAEHAL 528
Cdd:PTZ00121 1535 KADEAKKAE-EKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVmklyEEEKKMKAEEAK 1613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113680846 529 SSVDVAIHSETLRDTAPVLEGI------------KGEEITKEEidmlSDACTKLKEQKNLLTKEKEELEDLKDDVQEYSE 596
Cdd:PTZ00121 1614 KAEEAKIKAEELKKAEEEKKKVeqlkkkeaeekkKAEELKKAE----EENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKK 1689
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 113680846 597 DLEEIKRELSKTGQ-----EKAVEESKASQRLSKRVNRMIGRMDKIITELEKDK 645
Cdd:PTZ00121 1690 AAEALKKEAEEAKKaeelkKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDK 1743
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
452-645 |
4.40e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.44 E-value: 4.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113680846 452 AKEAQVKVAELDFSKVDNKTKLETTLQEEAAIRQEN-RERELERLADAAEKAKEQTQSQEAEVLEVEGER----RVDAEH 526
Cdd:PTZ00121 1175 AKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEeRKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKaeeeRNNEEI 1254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113680846 527 ALSSVDVAIHSETLRDTAPVLEGIKGEEITKEEIDMLSDACTKLKEQKNL-----LTKEKEELEDLKDDVQEYSEDLEEI 601
Cdd:PTZ00121 1255 RKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKAdeakkKAEEAKKADEAKKKAEEAKKKADAA 1334
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 113680846 602 KR---ELSKTGQEKAVEESKASQRLSKRVNRmiGRMDKIITELEKDK 645
Cdd:PTZ00121 1335 KKkaeEAKKAAEAAKAEAEAAADEAEAAEEK--AEAAEKKKEEAKKK 1379
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
468-643 |
5.19e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 5.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113680846 468 DNKTKLEtTLQEEAAIRQENRERELERLADAAEKAKEQTQSQEA-EVLEVEGERRVD---AEHALSSVDVAIhsETLRDT 543
Cdd:COG4913 607 DNRAKLA-ALEAELAELEEELAEAEERLEALEAELDALQERREAlQRLAEYSWDEIDvasAEREIAELEAEL--ERLDAS 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113680846 544 APVLEGIKGE-EITKEEIDMLSDACTKLKEQKNLLTKEKEELEDLKDDVQEYSEDLEEIKRELSKTGQEKAVE------- 615
Cdd:COG4913 684 SDDLAALEEQlEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAaalgdav 763
|
170 180
....*....|....*....|....*...
gi 113680846 616 ESKASQRLSKRVNRMIGRMDKIITELEK 643
Cdd:COG4913 764 ERELRENLEERIDALRARLNRAEEELER 791
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
449-623 |
5.88e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.85 E-value: 5.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113680846 449 EIMAKEAQVKVAELDFSKVDNKTKLETTLQEEAAIRQENRERELERLADAAEKAKEQTQSQEAEVLEVEGERRvDAEHAL 528
Cdd:COG1196 282 ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE-EAEAEL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113680846 529 SSVDVAIhSETLRDTAPVLEGIkgEEITKEEIDMLSDACTKLKEQKNLLTKEKEELEDLKDDVQEYSEDLEEIKRELSKT 608
Cdd:COG1196 361 AEAEEAL-LEAEAELAEAEEEL--EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437
|
170
....*....|....*
gi 113680846 609 GQEKAVEESKASQRL 623
Cdd:COG1196 438 EEEEEALEEAAEEEA 452
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
397-654 |
7.97e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.49 E-value: 7.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113680846 397 TEERLREQLKQWLEL--HLNQHIPTSLLLLsramflPDTLSPadqlkttlqnlpEIMAKEAQVKVAELDFSKVDNKTKLE 474
Cdd:PRK04863 859 QEQQQRSQLEQAKEGlsALNRLLPRLNLLA------DETLAD------------RVEEIREQLDEAEEAKRFVQQHGNAL 920
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113680846 475 TTLQEEAAIRQENRER--ELERLADAAEKAKEQTQSQEAEVLEVEgERRvdaeHALSSVDVAihsETLRDTAPVLEGIKG 552
Cdd:PRK04863 921 AQLEPIVSVLQSDPEQfeQLKQDYQQAQQTQRDAKQQAFALTEVV-QRR----AHFSYEDAA---EMLAKNSDLNEKLRQ 992
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113680846 553 EEITKEEidMLSDACTKLKEQKNLLTKEKEELEDLKDDVQEYSEDLEEIKRELSKTG-QEKAVEESKASQR---LSKRVN 628
Cdd:PRK04863 993 RLEQAEQ--ERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGvPADSGAEERARARrdeLHARLS 1070
|
250 260
....*....|....*....|....*.
gi 113680846 629 RMIGRmdkiITELEKDKMVLDGQMDS 654
Cdd:PRK04863 1071 ANRSR----RNQLEKQLTFCEAEMDN 1092
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
452-625 |
1.00e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113680846 452 AKEAQVKVAELDFSKVDNKTKLETTLQEEAAIRQENRERELERLADAAEKAKEQTQSQEA----------EVLEVEGERR 521
Cdd:PTZ00121 1492 AEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELkkaeelkkaeEKKKAEEAKK 1571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113680846 522 V--DAEHALSSVDVAIHSETLRDTAPVLEGIKGEEITKEEIDMLSDACTKLKEQKNlLTKEKEELEDLKDDVQEYSEDLE 599
Cdd:PTZ00121 1572 AeeDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK-AEEEKKKVEQLKKKEAEEKKKAE 1650
|
170 180
....*....|....*....|....*.
gi 113680846 600 EIKRELSKTGQEKAVEESKASQRLSK 625
Cdd:PTZ00121 1651 ELKKAEEENKIKAAEEAKKAEEDKKK 1676
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
453-629 |
1.55e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.31 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113680846 453 KEAQVKVAELDFSKVDNKTKLETTLQEEAAIRQENRERELERLADAAEKAKEQTQSQEAEVLEVEgERRVDAEHALSSVd 532
Cdd:COG1196 220 EELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELE-EAQAEEYELLAEL- 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113680846 533 vaihSETLRDTAPVLEGIKGEEITKEEIDmlsdacTKLKEQKNLLTKEKEELEDLKDDVQEYSEDLEEIKRELSKTGQEK 612
Cdd:COG1196 298 ----ARLEQDIARLEERRRELEERLEELE------EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367
|
170
....*....|....*..
gi 113680846 613 AVEESKASQRLSKRVNR 629
Cdd:COG1196 368 LEAEAELAEAEEELEEL 384
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
454-632 |
1.59e-04 |
|
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: 45.44 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113680846 454 EAQVKVAELDFSKVDNK-TKLETTLQEEAAIR-------QENRERELERLADAAEKAKE-----QTQSQEAEVLEVEGER 520
Cdd:TIGR02169 321 EERLAKLEAEIDKLLAEiEELEREIEEERKRRdklteeyAELKEELEDLRAELEEVDKEfaetrDELKDYREKLEKLKRE 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113680846 521 RVDAEHALSSVDVAIH--SETLRDTAPVLEGIKG-----EEITKEEIDMLSDACTKLKEQKNLLTKEKEELEDLKDDVQE 593
Cdd:TIGR02169 401 INELKRELDRLQEELQrlSEELADLNAAIAGIEAkinelEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDR 480
|
170 180 190
....*....|....*....|....*....|....*....
gi 113680846 594 YSEDLEEIKRELSKTgqEKAVEESKASQRLSKRVNRMIG 632
Cdd:TIGR02169 481 VEKELSKLQRELAEA--EAQARASEERVRGGRAVEEVLK 517
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
453-643 |
1.63e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113680846 453 KEAQVKVAELDFSKVDNKTKLETTLQEEAAirqeNRERELERLADAAEKAKEQtqsqEAEVLEVEGERRvDAEHALSSVD 532
Cdd:PRK03918 506 KELEEKLKKYNLEELEKKAEEYEKLKEKLI----KLKGEIKSLKKELEKLEEL----KKKLAELEKKLD-ELEEELAELL 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113680846 533 VAIHSETLRDTAPVLEGIKGEEITKEEIDMLSDACTKLKEQKNLLTKEKEELEDLKDDVQEYSEDLEEIKRELSKTGQEK 612
Cdd:PRK03918 577 KELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKY 656
|
170 180 190
....*....|....*....|....*....|.
gi 113680846 613 AVEESKASQRLSKRVNRMIGRMDKIITELEK 643
Cdd:PRK03918 657 SEEEYEELREEYLELSRELAGLRAELEELEK 687
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
470-626 |
2.06e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.93 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113680846 470 KTKLETTLQEEAAIRQENRERELERLADAAEKAKEQTQSQEAEVLEVEGERRVdAEHALSSVDVAIHSETLRDTAPVLEG 549
Cdd:COG1196 219 KEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEE-LRLELEELELELEEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 113680846 550 IKGEEITKEEIDMLSDACTKLKEQKNLLTKEKEELEDLKDDVQEYSEDLEEIKRELSKTGQEKAVEESKASQRLSKR 626
Cdd:COG1196 298 ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
427-643 |
2.62e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113680846 427 AMFLPDTLSPADQLKTTLQNLPEIMAKEAQVKvAELDfsKVDNKtkLETTLQEEAAIRQENR--ERELERLADAAEKAKE 504
Cdd:COG3883 5 ALAAPTPAFADPQIQAKQKELSELQAELEAAQ-AELD--ALQAE--LEELNEEYNELQAELEalQAEIDKLQAEIAEAEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113680846 505 QTQSQEAEVleveGERRVDA---EHALSSVDVAIHSETLRDtapVLEGIKG-EEITKEEIDMLSDactkLKEQKNLLTKE 580
Cdd:COG3883 80 EIEERREEL----GERARALyrsGGSVSYLDVLLGSESFSD---FLDRLSAlSKIADADADLLEE----LKADKAELEAK 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 113680846 581 KEELEDLKDDVQEYSEDLEEIKRELsktgQEKAVEESKASQRLSKRVNRMIGRMDKIITELEK 643
Cdd:COG3883 149 KAELEAKLAELEALKAELEAAKAEL----EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAA 207
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
454-645 |
3.36e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113680846 454 EAQVKVAELDFSKVDNKTKLETTLQE---EAAIRQENRERELERLADAAEKAKEQTQS-----QEAEVLEVEGErrvdaE 525
Cdd:PRK02224 481 EAELEDLEEEVEEVEERLERAEDLVEaedRIERLEERREDLEELIAERRETIEEKRERaeelrERAAELEAEAE-----E 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113680846 526 HALSSVDVAIHSETLRDTAPVLEGIKGEeiTKEEIDMLSDACTKLKEQKNL------LTKEKEELEDLKDDVQEYSEDLE 599
Cdd:PRK02224 556 KREAAAEAEEEAEEAREEVAELNSKLAE--LKERIESLERIRTLLAAIADAedeierLREKREALAELNDERRERLAEKR 633
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 113680846 600 EIKRELSKTGQEKAVEESKASQrlsKRVNRMIGRMDKIITELEKDK 645
Cdd:PRK02224 634 ERKRELEAEFDEARIEEAREDK---ERAEEYLEQVEEKLDELREER 676
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
490-629 |
4.58e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 4.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113680846 490 RELERLADAAEKAKEQtqsqeAEVLEVEGERRVDAEHALSSVDVAihsETLRDTAPVLEGIKGEEITKEEIDMLSDACTK 569
Cdd:COG4913 235 DDLERAHEALEDAREQ-----IELLEPIRELAERYAAARERLAEL---EYLRAALRLWFAQRRLELLEAELEELRAELAR 306
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 113680846 570 LKEQKNLLTKEKEELEDLKDDVQEY-----SEDLEEIKRELSKTGQEKAvEESKASQRLSKRVNR 629
Cdd:COG4913 307 LEAELERLEARLDALREELDELEAQirgngGDRLEQLEREIERLERELE-ERERRRARLEALLAA 370
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
441-709 |
7.20e-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: 7.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113680846 441 KTTLQNLPEIMAKEAQVKVAELDFSK--VDNKTKLettLQEEAAIrqenrERELERLADAAEKAKEQTQSQEAEVLEVEG 518
Cdd:TIGR01612 1161 KAISNDDPEEIEKKIENIVTKIDKKKniYDEIKKL---LNEIAEI-----EKDKTSLEEVKGINLSYGKNLGKLFLEKID 1232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113680846 519 ERRVDAEHALSSVDVAIHS-ETLRDTAPVLEGIKGEEI-TKEEIDMLSDACTKLKEQKNLLTKEKEELEDLKDD----VQ 592
Cdd:TIGR01612 1233 EEKKKSEHMIKAMEAYIEDlDEIKEKSPEIENEMGIEMdIKAEMETFNISHDDDKDHHIISKKHDENISDIREKslkiIE 1312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113680846 593 EYSE--DLEEIKRELSKTGQEKAVEESKASQRLSKRVNRM-IGRMDKIITELEKDKmvldgqmdsETTPPIGENLISIN- 668
Cdd:TIGR01612 1313 DFSEesDINDIKKELQKNLLDAQKHNSDINLYLNEIANIYnILKLNKIKKIIDEVK---------EYTKEIEENNKNIKd 1383
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 113680846 669 ELITVMKQIQNIPEH-KLLSIADALDENKDGKiDIDDVIKVV 709
Cdd:TIGR01612 1384 ELDKSEKLIKKIKDDiNLEECKSKIESTLDDK-DIDECIKKI 1424
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
487-642 |
7.57e-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: 7.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113680846 487 NRERELERLADAAEKAKEQTQSQEAEVLEVEGERRvDAEHALSSVDVAIHSET--LRDTAPVLEGIKGEEITKEE-IDML 563
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELE-ELEEELEQLRKELEELSrqISALRKDLARLEAEVEQLEErIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113680846 564 SDACTKLKEQKNLLTKEKEEL-----------EDLKDDVQEYSEDLEEIKRELSKTgQEKAVEESKASQRLSKRVNRMIG 632
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAeeelaeaeaeiEELEAQIEQLKEELKALREALDEL-RAELTLLNEEAANLRERLESLER 831
|
170
....*....|
gi 113680846 633 RMDKIITELE 642
Cdd:TIGR02168 832 RIAATERRLE 841
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
439-716 |
8.36e-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: 42.70 E-value: 8.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113680846 439 QLKTTLQNLP-EIMAKEAQVKvaELDFSKVDNKTKLETTLQEEAAIRQ--ENRERELERLADAAEKAKEQTQ--SQEAEV 513
Cdd:TIGR04523 437 KNNSEIKDLTnQDSVKELIIK--NLDNTRESLETQLKVLSRSINKIKQnlEQKQKELKSKEKELKKLNEEKKelEEKVKD 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113680846 514 LEVEGERRVDAEHALSSVDVAIHSE--TLRDTAPVLEGIKGEEITKEEIDMLSDACTKLKEQKNLLTKEKEELEDLkddV 591
Cdd:TIGR04523 515 LTKKISSLKEKIEKLESEKKEKESKisDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQEL---I 591
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113680846 592 QEYSEDLEEIKRELSKtgQEKAVEESKASQRLSKRVNRmigRMDKIITELEKDKmvldgqmdsettppigenlisiNELI 671
Cdd:TIGR04523 592 DQKEKEKKDLIKEIEE--KEKKISSLEKELEKAKKENE---KLSSIIKNIKSKK----------------------NKLK 644
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 113680846 672 TVMKQIQNIPEHKLLSIADALDENKDGKIDIDDVIKVVELIDKED 716
Cdd:TIGR04523 645 QEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDWLKEL 689
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
483-647 |
1.06e-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: 42.42 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113680846 483 IRQENRERELERLADaAEKAKEQTQSQEAEVLEVEGERRVD-AEHALSSVDVAIHSETLRDTAPVLEGIKGEEITKEEID 561
Cdd:pfam17380 353 IRQEERKRELERIRQ-EEIAMEISRMRELERLQMERQQKNErVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEE 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113680846 562 MLSDACTKLKEQKnlltkeKEELEDLKDDVQEYSEDLEEIKRELSKTGQEK-AVEESKASQRLSKRVNRMI------GRM 634
Cdd:pfam17380 432 ARQREVRRLEEER------AREMERVRLEEQERQQQVERLRQQEEERKRKKlELEKEKRDRKRAEEQRRKIlekeleERK 505
|
170
....*....|...
gi 113680846 635 DKIITELEKDKMV 647
Cdd:pfam17380 506 QAMIEEERKRKLL 518
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
469-645 |
1.60e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113680846 469 NKTKLETTLQEEAAIRQENRE-----RELERLADAAEKAKEQTQSQEAEVLEVEGERRvDAEHALSSVDVAI-----HSE 538
Cdd:PRK03918 198 KEKELEEVLREINEISSELPElreelEKLEKEVKELEELKEEIEELEKELESLEGSKR-KLEEKIRELEERIeelkkEIE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113680846 539 TLRDTAPVLEGIKGEEI-----------TKEEIDMLSDACTKLKEQKNLLTKEKEELEDLKDDVQEYSEDLEEIKRELSK 607
Cdd:PRK03918 277 ELEEKVKELKELKEKAEeyiklsefyeeYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEE 356
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 113680846 608 -TGQEKAVEESKAS----QRLSKRV-NRMIGRMDKIITELEKDK 645
Cdd:PRK03918 357 lEERHELYEEAKAKkeelERLKKRLtGLTPEKLEKELEELEKAK 400
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
457-627 |
4.31e-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: 4.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113680846 457 VKVAELDFSKVDNKTKLETTLQEEAAIRQE--NRERELERLADAAEKAKEQTQSQEAEVLEVEgERRVDAEHALSSVdva 534
Cdd:COG1579 10 LDLQELDSELDRLEHRLKELPAELAELEDElaALEARLEAAKTELEDLEKEIKRLELEIEEVE-ARIKKYEEQLGNV--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113680846 535 ihsETLRDtapvLEGIKGE-EITKEEIDMLSDACTKLKEQ----KNLLTKEKEELEDLKDDVQEYSEDLEEIKRELSKTG 609
Cdd:COG1579 86 ---RNNKE----YEALQKEiESLKRRISDLEDEILELMERieelEEELAELEAELAELEAELEEKKAELDEELAELEAEL 158
|
170
....*....|....*...
gi 113680846 610 QEKAVEESKASQRLSKRV 627
Cdd:COG1579 159 EELEAEREELAAKIPPEL 176
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
452-684 |
4.69e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.51 E-value: 4.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113680846 452 AKEAQVKVAELDFSKVDNKTKLETTLQEEAAIRQENRERELERLADAAEKAKEQTQSQEAEVLEVEGERRVDAEHALSSV 531
Cdd:PTZ00121 1400 AEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKA 1479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113680846 532 DVAIHSETLRDTAPVLEGIKGEEITKEEIDMLSDACTKLKEQKNLLTKEKEELEDLKDDVQEYSE--DLEEIKR--ELSK 607
Cdd:PTZ00121 1480 EEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEkkKADELKKaeELKK 1559
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 113680846 608 TGQEKAVEESKasqRLSKRVNrMIGRMDKIITELEKDKMVLDGQMDSETTPPIGENLISINELITVMKQIQNIPEHK 684
Cdd:PTZ00121 1560 AEEKKKAEEAK---KAEEDKN-MALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEK 1632
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
452-646 |
5.11e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.51 E-value: 5.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113680846 452 AKEAQVKVAEL----DFSKVDNKTKLETTLQ-EEAAIRQENRERELERLADAAEKAKEQTQSQE--------------AE 512
Cdd:PTZ00121 1505 AAEAKKKADEAkkaeEAKKADEAKKAEEAKKaDEAKKAEEKKKADELKKAEELKKAEEKKKAEEakkaeedknmalrkAE 1584
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113680846 513 VLEVEGERRVDAEHALSSVDVAIHSETLRDTAPvlEGIKGEEITKEE-----IDMLSDACTKLKEQKNLLTKEKEEL--- 584
Cdd:PTZ00121 1585 EAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEE--AKIKAEELKKAEeekkkVEQLKKKEAEEKKKAEELKKAEEENkik 1662
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 113680846 585 -EDLKDDVQEYSEDLEEIKR--ELSKTGQE---KAVEESKASQRLSKRVNRMIGRMDKIITELEKDKM 646
Cdd:PTZ00121 1663 aAEEAKKAEEDKKKAEEAKKaeEDEKKAAEalkKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKI 1730
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
441-625 |
5.24e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.51 E-value: 5.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113680846 441 KTTLQNLPEIMAKEAQVKVAElDFSKVDNKTKLETTLQ-EEAAIRQENRERELERLADAAEKAKEQTQSQEA-------- 511
Cdd:PTZ00121 1105 KTETGKAEEARKAEEAKKKAE-DARKAEEARKAEDARKaEEARKAEDAKRVEIARKAEDARKAEEARKAEDAkkaeaark 1183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113680846 512 --------EVLEVEGERRVDAEHALSSVDVAIHSETLRDTAPVLEGIKGEEITKEEidmlSDACTKLKEQKNLLTKEKEE 583
Cdd:PTZ00121 1184 aeevrkaeELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDA----EEAKKAEEERNNEEIRKFEE 1259
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 113680846 584 LEDLKDDVQEYSEDLEEIKR--ELSKTGQEKAVEESKASQRLSK 625
Cdd:PTZ00121 1260 ARMAHFARRQAAIKAEEARKadELKKAEEKKKADEAKKAEEKKK 1303
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
437-637 |
5.25e-03 |
|
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: 40.43 E-value: 5.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113680846 437 ADQLKTTLQNLPEIMAkEAQVKVAELDFSKVDNKTKLETTLQEEAAIRQE--NRERELERLADAAEKAKEQTQSQEAEVL 514
Cdd:TIGR02168 735 LARLEAEVEQLEERIA-QLSKELTELEAEIEELEERLEEAEEELAEAEAEieELEAQIEQLKEELKALREALDELRAELT 813
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113680846 515 EVEGERRVDAEHALSSV-DVAIHSETLRDTAPVLEGIKGE-EITKEEIDMLSDACTKLKEQKNLLTKEKEELEDLKDDVQ 592
Cdd:TIGR02168 814 LLNEEAANLRERLESLErRIAATERRLEDLEEQIEELSEDiESLAAEIEELEELIEELESELEALLNERASLEEALALLR 893
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 113680846 593 EYSEDLEEIKRELSKtgqeKAVEESKASQRLSKRVNRMIGRMDKI 637
Cdd:TIGR02168 894 SELEELSEELRELES----KRSELRRELEELREKLAQLELRLEGL 934
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
449-660 |
6.46e-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: 6.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113680846 449 EIMAKEAQVKVAELDFSKVDNKTKLETTLQEEAAIRQENRERELERLadaaeKAKEQTQSQEAEVLEVEGERRVDAEHAL 528
Cdd:pfam17380 405 KILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERV-----RLEEQERQQQVERLRQQEEERKRKKLEL 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113680846 529 SSVDvaihsetlRDTAPVLEgiKGEEITKEEIDMLSDACTKLKEQKNLLTKEKEELEDLKDDVQEYSEDLEEIKRelskt 608
Cdd:pfam17380 480 EKEK--------RDRKRAEE--QRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRK----- 544
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 113680846 609 gqEKAVEESKASQRLSKRVNRMIGRMDKIITELEKDKMVLDG---QMDSETTPPI 660
Cdd:pfam17380 545 --QQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESekaRAEYEATTPI 597
|
|
| ElaB |
COG4575 |
Membrane-anchored ribosome-binding protein ElaB, inhibits growth in stationary phase, YqjD ... |
578-635 |
7.26e-03 |
|
Membrane-anchored ribosome-binding protein ElaB, inhibits growth in stationary phase, YqjD/DUF883 family [Translation, ribosomal structure and biogenesis];
Pssm-ID: 443632 [Multi-domain] Cd Length: 108 Bit Score: 36.84 E-value: 7.26e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 113680846 578 TKEKEELEDLKDDVQEYSEDLEEIKRELSKTGQEKAveeSKASQRLSKRVNRMIGRMD 635
Cdd:COG4575 8 TSVEDSKEDLEADLKALVDDLEELLKSTADDAGEKA---AELREKAEAALDEARERLS 62
|
|
| PRK02292 |
PRK02292 |
V-type ATP synthase subunit E; Provisional |
473-604 |
9.88e-03 |
|
V-type ATP synthase subunit E; Provisional
Pssm-ID: 235026 [Multi-domain] Cd Length: 188 Bit Score: 38.05 E-value: 9.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113680846 473 LETTLQEeaaIRQENRERELERLADAAEKAKEQTQSQEAEVLEVEGERRVDAEHalssvdvaihsetlrdtapvlegikg 552
Cdd:PRK02292 3 LETVVED---IRDEARARASEIRAEADEEAEEIIAEAEADAEEILEDREAEAER-------------------------- 53
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 113680846 553 eEITKEEIDMLSDActKLKEQKNLLTKEKEELEDLKDDVQEYSEDLEEIKRE 604
Cdd:PRK02292 54 -EIEQLREQELSSA--KLEAKRERLNARKEVLEDVRNQVEDEIASLDGDKRE 102
|
|
|