|
Name |
Accession |
Description |
Interval |
E-value |
| Nsp1_C |
pfam05064 |
Nsp1-like C-terminal region; This family probably forms a coiled-coil. This important region ... |
535-630 |
1.23e-22 |
|
Nsp1-like C-terminal region; This family probably forms a coiled-coil. This important region of Nsp1 is involved in binding Nup82.
Pssm-ID: 461540 [Multi-domain] Cd Length: 114 Bit Score: 93.53 E-value: 1.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689895 535 PSEITGKTVEEIIKEWNTELQERTGRFRKQANAIAEWDKRILQNRDVLLRLEIEVAKVVETQSSLERQLELIETHQQEVD 614
Cdd:pfam05064 10 PSALKNKTLDDIINKWSTQLSKQSKEFETQAAKVNEWDRVLVENGDKISKLYSETLEAEQDQNRIDQQLDYVESQQDELE 89
|
90
....*....|....*.
gi 30689895 615 KALQSMEEEAERIYND 630
Cdd:pfam05064 90 SLLDNYEEQLEELLGD 105
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
541-723 |
6.65e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.13 E-value: 6.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689895 541 KTVEEIIKEWNTELQERTGRFRKQANAIAEWDKRILQNRDVLLRLEIEVAKVVETQSSLERQLELIETHQQEVDKALQSM 620
Cdd:COG4372 41 DKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEEL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689895 621 EEEAERIyNDERKSLLDDEAASTRDAMYEQSEL--VERELEHMTEQIRSIIQSVNANQGGELEAidgmsPLDVVVRILNN 698
Cdd:COG4372 121 QKERQDL-EQQRKQLEAQIAELQSEIAEREEELkeLEEQLESLQEELAALEQELQALSEAEAEQ-----ALDELLKEANR 194
|
170 180
....*....|....*....|....*..
gi 30689895 699 QLSSLMWI--DEKAEEFSSRIQKIALQ 723
Cdd:COG4372 195 NAEKEEELaeAEKLIESLPRELAEELL 221
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
538-666 |
7.40e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 49.47 E-value: 7.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689895 538 ITGKTVEEII-----KEWNTELQERTGRFRKQANAIAEWDKRILQNRDVLLRLEIEVakvvetqSSLERQLEliethqqE 612
Cdd:COG2433 373 IRGLSIEEALeelieKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEV-------EELEAELE-------E 438
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 30689895 613 VDKALQSMEEEAERIYNDERKSLLDDEAASTRDAMYE--QSEL--VERELEHMTEQIR 666
Cdd:COG2433 439 KDERIERLERELSEARSEERREIRKDREISRLDREIErlERELeeERERIEELKRKLE 496
|
|
| HrpE_YscL_not |
TIGR02499 |
type III secretion apparatus protein, HrpE/YscL family; This model is related to pfam06188, ... |
594-703 |
7.96e-05 |
|
type III secretion apparatus protein, HrpE/YscL family; This model is related to pfam06188, but is broader. pfam06188 describes HrpE-like proteins, components of bacterial type III secretion systems primarily in bacteria that infect plants. This model includes also the homologous proteins of animal pathogens, such as YscL of Yersinia pestis. This model excludes the related protein FliH of the bacterial flagellar apparatus (see pfam02108) [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274165 [Multi-domain] Cd Length: 166 Bit Score: 43.82 E-value: 7.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689895 594 ETQSSLERQLELIETHQQEVDKALQSMEEEAERI----YNDERKSLLDDEAASTRDAMYEQSELVERELEHMTEQIRSII 669
Cdd:TIGR02499 7 EDLAALAQAQAILAAARQRAEAILADAEEEAEASrqlgYEQGLEQFWQEAAAQLAEWQQEAEQLEASLEERLAELVLQAL 86
|
90 100 110
....*....|....*....|....*....|....
gi 30689895 670 QSVnanqggeleaIDGMSPLDVVVRILNNQLSSL 703
Cdd:TIGR02499 87 EQI----------LGEYDEPERLVRLLRQLLRAV 110
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
544-670 |
2.32e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.38 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689895 544 EEIIKEWNTELQERTGRF----RKQANAIAEWDKRILQNRDVLLR----LEIEVAKVVETQSSLERQLELIETHQQEVDK 615
Cdd:PRK12704 56 KEALLEAKEEIHKLRNEFekelRERRNELQKLEKRLLQKEENLDRklelLEKREEELEKKEKELEQKQQELEKKEEELEE 135
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 30689895 616 ALQSMEEEAERIYN---DERKSLLDDEaastrdamyeqselVERELEH-MTEQIRSIIQ 670
Cdd:PRK12704 136 LIEEQLQELERISGltaEEAKEILLEK--------------VEEEARHeAAVLIKEIEE 180
|
|
| PLN02217 |
PLN02217 |
probable pectinesterase/pectinesterase inhibitor |
426-531 |
3.64e-04 |
|
probable pectinesterase/pectinesterase inhibitor
Pssm-ID: 215130 [Multi-domain] Cd Length: 670 Bit Score: 43.92 E-value: 3.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689895 426 FGVTSSATNTTPASSAATFSTTGFGLASSTPATGSTNSFTGFAVPKTSTPASSSQPQTTSPAFSFSLPSstSTTAPATSS 505
Cdd:PLN02217 562 FAGNPGSTNSTPTGSAASSNTTFSSDSPSTVVAPSTSPPAGHLGSPPATPSKIVSPSTSPPASHLGSPS--TTPSSPESS 639
|
90 100 110
....*....|....*....|....*....|
gi 30689895 506 ATTTQTTLVVPSSS----GTSTAVAPVAGS 531
Cdd:PLN02217 640 IKVASTETASPESSikvaSTESSVSMVSMS 669
|
|
| PRK13042 |
PRK13042 |
superantigen-like protein SSL4; Reviewed; |
433-656 |
4.38e-04 |
|
superantigen-like protein SSL4; Reviewed;
Pssm-ID: 183854 [Multi-domain] Cd Length: 291 Bit Score: 43.08 E-value: 4.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689895 433 TNTTPASSAATFSTTGFGLASSTPATGSTNSFTGFAVPKTSTPasSSQPQTTSPAFSFSLPSSTSTTAPATSSATTTQTT 512
Cdd:PRK13042 4 TTIAKTSLALGLLTTGVITTTTQAANATTPSSTKVEAPQSTPP--STKVEAPQSKPNATTPPSTKVEAPQQTPNATTPSS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689895 513 LVVPSSSGTSTAVAPVAGSPKL---------PSEITGKTVEEIIKEWNTElqertgRFrkqANAIAEW-----------D 572
Cdd:PRK13042 82 TKVETPQSPTTKQVPTEINPKFkdlrayytkPSLEFKNEIGIILKKWTTI------RF---MNVVPDYfiykialvgkdD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689895 573 KR----ILQNRDVLLRLEievakvvETQSSLERQL--ELIETHQQEVD-KALQSMEEEAER--IYNDERKSLLDDEAAST 643
Cdd:PRK13042 153 KKygegVHRNVDVFVVLE-------ENKYNLEKYSvgGITKSNSKKVDhKAGVRITKEDNKgtISHDVSEFKITKEQISL 225
|
250
....*....|....
gi 30689895 644 RDAMYE-QSELVER 656
Cdd:PRK13042 226 KELDFKlRKQLIEK 239
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
550-725 |
8.45e-04 |
|
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: 42.90 E-value: 8.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689895 550 WNTELQERTGRFRKQANAI----AEWDKRI----LQNRDVLLRLEIEVAKVVETQsslERQLELIETHQQEVDKALQSME 621
Cdd:pfam12128 352 WQSELENLEERLKALTGKHqdvtAKYNRRRskikEQNNRDIAGIKDKLAKIREAR---DRQLAVAEDDLQALESELREQL 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689895 622 EEAERIYNDER---KSLLDDEAASTRDAMYEQSELVERE-----LEHMTEQIRSIIQSVNANQgGELEAIDGMSpldvvv 693
Cdd:pfam12128 429 EAGKLEFNEEEyrlKSRLGELKLRLNQATATPELLLQLEnfderIERAREEQEAANAEVERLQ-SELRQARKRR------ 501
|
170 180 190
....*....|....*....|....*....|..
gi 30689895 694 rilNNQLSSLMWIDEKAEEFSSRIQKIALQGS 725
Cdd:pfam12128 502 ---DQASEALRQASRRLEERQSALDELELQLF 530
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
544-714 |
9.31e-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: 42.74 E-value: 9.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689895 544 EEIIKEWNTELQERTGRFRKQANAIAEWDKRI--LQNR---------DVLLRLEIEVAKVVETQSSLERQLELIETHQQE 612
Cdd:TIGR02168 774 EEELAEAEAEIEELEAQIEQLKEELKALREALdeLRAEltllneeaaNLRERLESLERRIAATERRLEDLEEQIEELSED 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689895 613 VDKALQSMEEEAERI--YNDERKSLLDDeaastRDAMYEQSELVERELEHMTEQIRSIIQSVNANQGGELEAIDGMSPLD 690
Cdd:TIGR02168 854 IESLAAEIEELEELIeeLESELEALLNE-----RASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE 928
|
170 180
....*....|....*....|....
gi 30689895 691 VVVRILNNQLSSLmwIDEKAEEFS 714
Cdd:TIGR02168 929 LRLEGLEVRIDNL--QERLSEEYS 950
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Nsp1_C |
pfam05064 |
Nsp1-like C-terminal region; This family probably forms a coiled-coil. This important region ... |
535-630 |
1.23e-22 |
|
Nsp1-like C-terminal region; This family probably forms a coiled-coil. This important region of Nsp1 is involved in binding Nup82.
Pssm-ID: 461540 [Multi-domain] Cd Length: 114 Bit Score: 93.53 E-value: 1.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689895 535 PSEITGKTVEEIIKEWNTELQERTGRFRKQANAIAEWDKRILQNRDVLLRLEIEVAKVVETQSSLERQLELIETHQQEVD 614
Cdd:pfam05064 10 PSALKNKTLDDIINKWSTQLSKQSKEFETQAAKVNEWDRVLVENGDKISKLYSETLEAEQDQNRIDQQLDYVESQQDELE 89
|
90
....*....|....*.
gi 30689895 615 KALQSMEEEAERIYND 630
Cdd:pfam05064 90 SLLDNYEEQLEELLGD 105
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
541-723 |
6.65e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.13 E-value: 6.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689895 541 KTVEEIIKEWNTELQERTGRFRKQANAIAEWDKRILQNRDVLLRLEIEVAKVVETQSSLERQLELIETHQQEVDKALQSM 620
Cdd:COG4372 41 DKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEEL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689895 621 EEEAERIyNDERKSLLDDEAASTRDAMYEQSEL--VERELEHMTEQIRSIIQSVNANQGGELEAidgmsPLDVVVRILNN 698
Cdd:COG4372 121 QKERQDL-EQQRKQLEAQIAELQSEIAEREEELkeLEEQLESLQEELAALEQELQALSEAEAEQ-----ALDELLKEANR 194
|
170 180
....*....|....*....|....*..
gi 30689895 699 QLSSLMWI--DEKAEEFSSRIQKIALQ 723
Cdd:COG4372 195 NAEKEEELaeAEKLIESLPRELAEELL 221
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
538-666 |
7.40e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 49.47 E-value: 7.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689895 538 ITGKTVEEII-----KEWNTELQERTGRFRKQANAIAEWDKRILQNRDVLLRLEIEVakvvetqSSLERQLEliethqqE 612
Cdd:COG2433 373 IRGLSIEEALeelieKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEV-------EELEAELE-------E 438
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 30689895 613 VDKALQSMEEEAERIYNDERKSLLDDEAASTRDAMYE--QSEL--VERELEHMTEQIR 666
Cdd:COG2433 439 KDERIERLERELSEARSEERREIRKDREISRLDREIErlERELeeERERIEELKRKLE 496
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
541-719 |
6.18e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.05 E-value: 6.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689895 541 KTVEEIIKEWNTELQERTGRFRKQANAIAEWDKRILQNRDVLLRLEIEVAKVVETQSSLERQLELIETHQQEVDKALQSM 620
Cdd:COG4372 76 EQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKEL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689895 621 EEEAERI------YNDERKSLLDDEAASTRDAMYEQSELVERELEHMTEQIRSIIQSVNANQGGELEAIDGMSPLDVVVR 694
Cdd:COG4372 156 EEQLESLqeelaaLEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLAL 235
|
170 180
....*....|....*....|....*
gi 30689895 695 ILNNQLSSLMWIDEKAEEFSSRIQK 719
Cdd:COG4372 236 SALLDALELEEDKEELLEEVILKEI 260
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
541-684 |
6.76e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.47 E-value: 6.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689895 541 KTVEEIIKEWNTELQERTGRFRKQANAIAEWDKRILQNRDVLLRLEIEV----AKVVETQSSLERQLELIETHQQEVDKA 616
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELeeaqAEEYELLAELARLEQDIARLEERRREL 314
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30689895 617 LQSMEEEAERIYNDERKSLLDDEAASTRDAMYEQSELVERELEHMTEQIRSIIQSVNANQGGELEAID 684
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
544-682 |
7.68e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.08 E-value: 7.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689895 544 EEIIKEWNTELQERTGRFRKQANAIAEWDKRILQNRDVLLRLEIEVAKVVETQSSLERQLELIETHQQEVDKALQSMEEE 623
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30689895 624 AERIyNDERKSLLDDEAASTRDAMYEQSELV--ERELEHMTEQIRSIIQSVNANQGGELEA 682
Cdd:COG1196 430 LAEL-EEEEEEEEEALEEAAEEEAELEEEEEalLELLAELLEEAALLEAALAELLEELAEA 489
|
|
| HrpE_YscL_not |
TIGR02499 |
type III secretion apparatus protein, HrpE/YscL family; This model is related to pfam06188, ... |
594-703 |
7.96e-05 |
|
type III secretion apparatus protein, HrpE/YscL family; This model is related to pfam06188, but is broader. pfam06188 describes HrpE-like proteins, components of bacterial type III secretion systems primarily in bacteria that infect plants. This model includes also the homologous proteins of animal pathogens, such as YscL of Yersinia pestis. This model excludes the related protein FliH of the bacterial flagellar apparatus (see pfam02108) [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274165 [Multi-domain] Cd Length: 166 Bit Score: 43.82 E-value: 7.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689895 594 ETQSSLERQLELIETHQQEVDKALQSMEEEAERI----YNDERKSLLDDEAASTRDAMYEQSELVERELEHMTEQIRSII 669
Cdd:TIGR02499 7 EDLAALAQAQAILAAARQRAEAILADAEEEAEASrqlgYEQGLEQFWQEAAAQLAEWQQEAEQLEASLEERLAELVLQAL 86
|
90 100 110
....*....|....*....|....*....|....
gi 30689895 670 QSVnanqggeleaIDGMSPLDVVVRILNNQLSSL 703
Cdd:TIGR02499 87 EQI----------LGEYDEPERLVRLLRQLLRAV 110
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
543-723 |
1.20e-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: 45.82 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689895 543 VEEIIKEWNTELQ------ERTGRFRKQANAIAEWDKRILQNR-----DVLLRLEIEVAKVVETQSSLERQLELIETHQQ 611
Cdd:TIGR02168 191 LEDILNELERQLKslerqaEKAERYKELKAELRELELALLVLRleelrEELEELQEELKEAEEELEELTAELQELEEKLE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689895 612 EVDKALQSMEEEAE--------------------RIYNDERKSLLDDEAASTrdamyEQSELVERELEHMTE---QIRSI 668
Cdd:TIGR02168 271 ELRLEVSELEEEIEelqkelyalaneisrleqqkQILRERLANLERQLEELE-----AQLEELESKLDELAEelaELEEK 345
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 30689895 669 IQSVNANQGGELEAidgmspLDVVVRILNNQLSSLMWIDEKAEEFSSRIQKIALQ 723
Cdd:TIGR02168 346 LEELKEELESLEAE------LEELEAELEELESRLEELEEQLETLRSKVAQLELQ 394
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
544-670 |
2.32e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.38 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689895 544 EEIIKEWNTELQERTGRF----RKQANAIAEWDKRILQNRDVLLR----LEIEVAKVVETQSSLERQLELIETHQQEVDK 615
Cdd:PRK12704 56 KEALLEAKEEIHKLRNEFekelRERRNELQKLEKRLLQKEENLDRklelLEKREEELEKKEKELEQKQQELEKKEEELEE 135
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 30689895 616 ALQSMEEEAERIYN---DERKSLLDDEaastrdamyeqselVERELEH-MTEQIRSIIQ 670
Cdd:PRK12704 136 LIEEQLQELERISGltaEEAKEILLEK--------------VEEEARHeAAVLIKEIEE 180
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
553-666 |
3.08e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 3.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689895 553 ELQERTGRFRKQANAIAEWDKRILQNRDVLLRL------EIEVAKVVETQSSLERQLELIETHQQEVdKALQSMEEEAER 626
Cdd:COG4913 621 ELEEELAEAEERLEALEAELDALQERREALQRLaeyswdEIDVASAEREIAELEAELERLDASSDDL-AALEEQLEELEA 699
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 30689895 627 IYnderkslldDEAASTRDAMYEQSELVERELEHMTEQIR 666
Cdd:COG4913 700 EL---------EELEEELDELKGEIGRLEKELEQAEEELD 730
|
|
| PLN02217 |
PLN02217 |
probable pectinesterase/pectinesterase inhibitor |
426-531 |
3.64e-04 |
|
probable pectinesterase/pectinesterase inhibitor
Pssm-ID: 215130 [Multi-domain] Cd Length: 670 Bit Score: 43.92 E-value: 3.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689895 426 FGVTSSATNTTPASSAATFSTTGFGLASSTPATGSTNSFTGFAVPKTSTPASSSQPQTTSPAFSFSLPSstSTTAPATSS 505
Cdd:PLN02217 562 FAGNPGSTNSTPTGSAASSNTTFSSDSPSTVVAPSTSPPAGHLGSPPATPSKIVSPSTSPPASHLGSPS--TTPSSPESS 639
|
90 100 110
....*....|....*....|....*....|
gi 30689895 506 ATTTQTTLVVPSSS----GTSTAVAPVAGS 531
Cdd:PLN02217 640 IKVASTETASPESSikvaSTESSVSMVSMS 669
|
|
| PRK13042 |
PRK13042 |
superantigen-like protein SSL4; Reviewed; |
433-656 |
4.38e-04 |
|
superantigen-like protein SSL4; Reviewed;
Pssm-ID: 183854 [Multi-domain] Cd Length: 291 Bit Score: 43.08 E-value: 4.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689895 433 TNTTPASSAATFSTTGFGLASSTPATGSTNSFTGFAVPKTSTPasSSQPQTTSPAFSFSLPSSTSTTAPATSSATTTQTT 512
Cdd:PRK13042 4 TTIAKTSLALGLLTTGVITTTTQAANATTPSSTKVEAPQSTPP--STKVEAPQSKPNATTPPSTKVEAPQQTPNATTPSS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689895 513 LVVPSSSGTSTAVAPVAGSPKL---------PSEITGKTVEEIIKEWNTElqertgRFrkqANAIAEW-----------D 572
Cdd:PRK13042 82 TKVETPQSPTTKQVPTEINPKFkdlrayytkPSLEFKNEIGIILKKWTTI------RF---MNVVPDYfiykialvgkdD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689895 573 KR----ILQNRDVLLRLEievakvvETQSSLERQL--ELIETHQQEVD-KALQSMEEEAER--IYNDERKSLLDDEAAST 643
Cdd:PRK13042 153 KKygegVHRNVDVFVVLE-------ENKYNLEKYSvgGITKSNSKKVDhKAGVRITKEDNKgtISHDVSEFKITKEQISL 225
|
250
....*....|....
gi 30689895 644 RDAMYE-QSELVER 656
Cdd:PRK13042 226 KELDFKlRKQLIEK 239
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
541-684 |
7.27e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 7.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689895 541 KTVEEIIKEWNTElQERTGRFRKQANAIAEwdkRILQNRDVLLRLEIEVAKVVETQSSLERQLELIETHQQEVDKALQSM 620
Cdd:PRK02224 216 AELDEEIERYEEQ-REQARETRDEADEVLE---EHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEEL 291
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30689895 621 EEEAERIYNDERKSLLDDEAASTR-DAMYEQSELVERELehmtEQIRSIIQSVNANQGGELEAID 684
Cdd:PRK02224 292 EEERDDLLAEAGLDDADAEAVEARrEELEDRDEELRDRL----EECRVAAQAHNEEAESLREDAD 352
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
550-725 |
8.45e-04 |
|
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: 42.90 E-value: 8.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689895 550 WNTELQERTGRFRKQANAI----AEWDKRI----LQNRDVLLRLEIEVAKVVETQsslERQLELIETHQQEVDKALQSME 621
Cdd:pfam12128 352 WQSELENLEERLKALTGKHqdvtAKYNRRRskikEQNNRDIAGIKDKLAKIREAR---DRQLAVAEDDLQALESELREQL 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689895 622 EEAERIYNDER---KSLLDDEAASTRDAMYEQSELVERE-----LEHMTEQIRSIIQSVNANQgGELEAIDGMSpldvvv 693
Cdd:pfam12128 429 EAGKLEFNEEEyrlKSRLGELKLRLNQATATPELLLQLEnfderIERAREEQEAANAEVERLQ-SELRQARKRR------ 501
|
170 180 190
....*....|....*....|....*....|..
gi 30689895 694 rilNNQLSSLMWIDEKAEEFSSRIQKIALQGS 725
Cdd:pfam12128 502 ---DQASEALRQASRRLEERQSALDELELQLF 530
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
544-714 |
9.31e-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: 42.74 E-value: 9.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689895 544 EEIIKEWNTELQERTGRFRKQANAIAEWDKRI--LQNR---------DVLLRLEIEVAKVVETQSSLERQLELIETHQQE 612
Cdd:TIGR02168 774 EEELAEAEAEIEELEAQIEQLKEELKALREALdeLRAEltllneeaaNLRERLESLERRIAATERRLEDLEEQIEELSED 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689895 613 VDKALQSMEEEAERI--YNDERKSLLDDeaastRDAMYEQSELVERELEHMTEQIRSIIQSVNANQGGELEAIDGMSPLD 690
Cdd:TIGR02168 854 IESLAAEIEELEELIeeLESELEALLNE-----RASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE 928
|
170 180
....*....|....*....|....
gi 30689895 691 VVVRILNNQLSSLmwIDEKAEEFS 714
Cdd:TIGR02168 929 LRLEGLEVRIDNL--QERLSEEYS 950
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
541-676 |
1.89e-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: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689895 541 KTVEEIIKEWNTELQERTGRFRKQANAIAEWDKRILQNRDVLLRLEIEVAKVVETQSSLERQLELIETHQQEVDKALQSM 620
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEL 109
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 30689895 621 EEEAERIYNDERKSLL---DDEAASTRDAMYEQSelVERELEHMTEQIRSIIQSVNANQ 676
Cdd:COG4942 110 LRALYRLGRQPPLALLlspEDFLDAVRRLQYLKY--LAPARREQAEELRADLAELAALR 166
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
551-684 |
1.95e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.85 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689895 551 NTELQERTGRFRKQANAIAEWDKRILQNRDVLLRLEIEVAKVVETQSSLERQLELIETHQQEVDKALQSMEEEAERIYND 630
Cdd:COG1196 657 SAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREE 736
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 30689895 631 ERKSLLDDEAASTRDAMYEQSEL-----VERELEHMTEQIRSiIQSVNanqggeLEAID 684
Cdd:COG1196 737 LLEELLEEEELLEEEALEELPEPpdleeLERELERLEREIEA-LGPVN------LLAIE 788
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
544-670 |
2.16e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.46 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689895 544 EEIIKEWNTELQERTGRFRKQANAIAEWDKRILQNRDVLLRLEIEVAKVVETQSSLERQL-----ELIETHQQEVDKALQ 618
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRreleeRLEELEEELAELEEE 331
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 30689895 619 SMEEEAERIYNDERKSLLDDEAASTRDAMYEQSELVERELEHMTEQIRSIIQ 670
Cdd:COG1196 332 LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
541-723 |
2.67e-03 |
|
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: 41.21 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689895 541 KTVEEIIKEWNT---ELQERTGRFRKQANAIAEWD--KRILQNRDVLLRL-EIEvakvvetqsSLERQLELIETHQQEVD 614
Cdd:TIGR02169 180 EEVEENIERLDLiidEKRQQLERLRREREKAERYQalLKEKREYEGYELLkEKE---------ALERQKEAIERQLASLE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689895 615 KALQSMEEEAERIYND--ERKSLLDDEAASTRDAMYEQSELVERELEHMTEQIRSIIQSVNANQggeleaiDGMSPLDVV 692
Cdd:TIGR02169 251 EELEKLTEEISELEKRleEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKE-------RELEDAEER 323
|
170 180 190
....*....|....*....|....*....|.
gi 30689895 693 VRILNNQLSSLmwiDEKAEEFSSRIQKIALQ 723
Cdd:TIGR02169 324 LAKLEAEIDKL---LAEIEELEREIEEERKR 351
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
538-674 |
3.09e-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: 41.20 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689895 538 ITGKTVEEI--IKEWNTELQERTGRFRKQANAIAEWDKRILQNRDVLLRLEIEVAKVVETQSSLERQL----ELIETHQQ 611
Cdd:TIGR02168 661 ITGGSAKTNssILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQIsalrKDLARLEA 740
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689895 612 EVDKALQSMEEEAERI--YNDERKSLLDD--EAASTRDAMYEQSELVERELEHMTEQ---IRSIIQSVNA 674
Cdd:TIGR02168 741 EVEQLEERIAQLSKELteLEAEIEELEERleEAEEELAEAEAEIEELEAQIEQLKEElkaLREALDELRA 810
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
543-683 |
3.22e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.91 E-value: 3.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689895 543 VEEIIKEWNTELQERTGRFRKQANAIAEWDKRILQNRDVLLRLEIEVAKVVETQSSLERQLELIETHqqevdKALQSMEE 622
Cdd:COG1579 22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN-----KEYEALQK 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30689895 623 EAEriYNDERKSLLDDEAastRDAMyEQSELVERELEHMTEQIRSIIQSVNANQgGELEAI 683
Cdd:COG1579 97 EIE--SLKRRISDLEDEI---LELM-ERIEELEEELAELEAELAELEAELEEKK-AELDEE 150
|
|
| PHA03369 |
PHA03369 |
capsid maturational protease; Provisional |
468-624 |
3.52e-03 |
|
capsid maturational protease; Provisional
Pssm-ID: 223061 [Multi-domain] Cd Length: 663 Bit Score: 40.75 E-value: 3.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689895 468 AVPKTSTPASSSQPQTTSPAFSFSLPSSTSTTAPATSSATTTQTTLVVPS---SSGTSTAVAPVAGSPKLPSEiTGKTVE 544
Cdd:PHA03369 370 AAPQTHTGPADRQRPQRPDGIPYSVPARSPMTAYPPVPQFCGDPGLVSPYnpqSPGTSYGPEPVGPVPPQPTN-PYVMPI 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689895 545 EIIKEWNTELQERTGRFRKQanaiaewdKRILQNRDVLLRLEIEVAKVVETQSSLERQLELIeTHQQEVDKalqSMEEEA 624
Cdd:PHA03369 449 SMANMVYPGHPQEHGHERKR--------KRGGELKEELIETLKLVKKLKEEQESLAKELEAT-AHKSEIKK---IAESEF 516
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
565-683 |
5.10e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 5.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689895 565 ANAIAEWDK---RILQNRDVLLRLEIEVAKVVETQSSLERQLELIETHQQEVDKALQSMEEEAERIYN--DERKSLLDDE 639
Cdd:COG4913 667 EREIAELEAeleRLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDrlEAAEDLARLE 746
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 30689895 640 AASTRDAMYEQsELVERELEHMTEQIRSIIQSVNANQGGELEAI 683
Cdd:COG4913 747 LRALLEERFAA-ALGDAVERELRENLEERIDALRARLNRAEEEL 789
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
551-721 |
7.19e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 7.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689895 551 NTELQERTGRFRKQANAIAEWdKRILQNRDVLLRLEIEvakvvetqsSLERQLELIETHQQEVDKAlQSMEEEAERI-YN 629
Cdd:COG4717 301 GKEAEELQALPALEELEEEEL-EELLAALGLPPDLSPE---------ELLELLDRIEELQELLREA-EELEEELQLEeLE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689895 630 DERKSLLDDEAASTRDAMYEQSELVERELEhMTEQIRSIIQSVNANQGGELEAIDGMSPLDvvvriLNNQLSSL-MWIDE 708
Cdd:COG4717 370 QEIAALLAEAGVEDEEELRAALEQAEEYQE-LKEELEELEEQLEELLGELEELLEALDEEE-----LEEELEELeEELEE 443
|
170
....*....|...
gi 30689895 709 KAEEFSSRIQKIA 721
Cdd:COG4717 444 LEEELEELREELA 456
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
541-635 |
9.00e-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: 38.37 E-value: 9.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689895 541 KTVEEIIKEwnteLQERTGRFR--KQANA----IAEWDKRILQNRDVLLRLEIEVAKVVETQSSLERQLELIETH----Q 610
Cdd:COG1579 69 EEVEARIKK----YEEQLGNVRnnKEYEAlqkeIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAEleekK 144
|
90 100
....*....|....*....|....*
gi 30689895 611 QEVDKALQSMEEEAERIyNDERKSL 635
Cdd:COG1579 145 AELDEELAELEAELEEL-EAEREEL 168
|
|
| |
