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Conserved domains on  [gi|729737607|ref|XP_010564931|]
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PREDICTED: histone-lysine N-methyltransferase, H3 lysine-79 specific [Haliaeetus leucocephalus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DOT1 pfam08123
Histone methylation protein DOT1; The DOT1 domain regulates gene expression by methylating ...
 91-293 1.69e-106

Histone methylation protein DOT1; The DOT1 domain regulates gene expression by methylating histone H3. H3 methylation by DOT1 has been shown to be required for the DNA damage checkpoint in yeast.


:

Pssm-ID: 149273  Cd Length: 205  Bit Score: 337.35  E-value: 1.69e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607    91 YNHSV-TDPEKLNNYEPFSPEVYGETSFDLVAQMIDEIKMTEDDLFVDLGSGVGQVVLQVAAATNCKHHYGVEKADIPAK 169
Cdd:pfam08123    1 YSRSVsPDANKLNHYKAFSNEVYGELLPEFLSDVLDKCNLGPQDVFVDLGSGVGNCVLQAALEFGCKLSFGCEIMDNASN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607   170 YAETMDREFRKWMKWYGKKHAEYTLERGDFLSEEWRERI-ANTSVIFVNNFAFGPEVDHQLKERFANMKEGGRIVSSKPF 248
Cdd:pfam08123   81 LAELQDEEFKKRCKLFGKKLGKIEFIRGSFLDNERVEEIiPEADVILVNNFAFDPELNLQLKEMLQDLKDGCKIISLKSF 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 729737607   249 APLNFRINSRNLSDIGTIMRVVELSPLKGSVSWTGKPVSYYLHTI 293
Cdd:pfam08123  161 VPLNYRINFRNLSDIFNILKVEELKLPEGSVSWTSRGVEYYISTV 205
CC_DOT1L cd20902
coiled coil domain of disruptor of telomeric-silencing 1-like (DOT1L) and similar proteins; ...
 450-514 3.09e-34

coiled coil domain of disruptor of telomeric-silencing 1-like (DOT1L) and similar proteins; This family contains DOT1L (disruptor of telomeric-silencing 1-like), a non-SET domain histone lysine methyltransferase (HKMT) that catalyzes monomethylation, dimethylation, and trimethylation of nucleosomal H3K79. DOT1L is recruited to the homeobox A by AF10 (ALL1-Fused gene from chromosome 10 protein), one of the mixed-lineage leukemia 1 (MLL1)-fusion partners that function in acute myeloid leukemia (ALL). Aberration of the MLL gene is implicated in acute leukemia; chromosomal translocations of MLL1 generate oncogenic chimeric proteins, containing the non-catalytic N-terminal portion of MLL1 fused with many partners such as AF10. The aberrant recruitment of DOT1L by MLL fusions and the resulting H3K79 methylation are thought to affect gene expression by altering chromatin accessibility. AF10 and DOT1L interact through their coiled coil domains.


:

Pssm-ID: 411016 [Multi-domain]  Cd Length: 65  Bit Score: 125.88  E-value: 3.09e-34
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 729737607  450 ALQKLLDSFKIQYMQFMAYMKTPQYKASLQQLLEQEKEKNAQLLGTAQQLFTHCQAQKEEIKRLF 514
Cdd:cd20902     1 ALQKLLESFKIQYLQFLAYMKTPQYKASLQQQIEQEKEKNKQLTGKAQQLEKQIQALQKEGVRLL 65
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
475-628 4.81e-08

Uncharacterized protein, contains DUF3084 domain [Function unknown];


:

Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 57.22  E-value: 4.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607  475 KASLQQLLEQEKEKNAQLLGTAQQLfthcQAQKEEIKRLFQQkldelgvkaltyndLIQAQKEISAHNQQLKEQTKQLEK 554
Cdd:COG4372    30 SEQLRKALFELDKLQEELEQLREEL----EQAREELEQLEEE--------------LEQARSELEQLEEELEELNEQLQA 91

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 729737607  555 DNSELR--NQSLQLLKARCEELKLDwstlsLENLLKEKQALKNQISEkqkhcLELQISIVELEKSQRQQELMQLKS 628
Cdd:COG4372    92 AQAELAqaQEELESLQEEAEELQEE-----LEELQKERQDLEQQRKQ-----LEAQIAELQSEIAEREEELKELEE 157
PRK14708 super family cl31733
flagellin; Provisional
 1112-1407 2.44e-03

flagellin; Provisional


The actual alignment was detected with superfamily member PRK14708:

Pssm-ID: 173171 [Multi-domain]  Cd Length: 888  Bit Score: 42.59  E-value: 2.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607 1112 VSSLSQNS-LFAFRPSSEDSLAIDAKITAHTRKSIAMPSS------GAD----GLSPSTNSTNGFTYNGGLST--DIGLH 1178
Cdd:PRK14708  199 ISSLTNGStATATGPAAGDSITVNGKTITFTTAGAATADSngnytiGLDqtltALLATIDTINGNTTNPSVVTagKLELH 278

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607 1179 SfidGASLPHKASDVT--TSNCSLGFQSQRSKDVGVSETNPFLNKRQL----EGLSSTKGEDLNRSGVKGKEIgeiSIRT 1252
Cdd:PRK14708  279 S---GTNSPLTISDNAggAVLAKLGLGAQVTTTAGTTAAANISATTQLfnthGGLSTTAIADGTTLTVNGKTI---TFKT 352

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607 1253 GGSSEKNSLQHN----GKVGK-GRDRDVEFKNGHNLFISAAVssGGLLNGKSLSTAVSSAGNpASSVQTHHPflNTLTTG 1327
Cdd:PRK14708  353 SDAPQGNNILTGsgvlGRIGTdGNGNSTIYLGTQNTFTNATV--GDVLTAIDLANGVKSATI-SNGVATIST--NAGQTA 427

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607 1328 SQFPLGPMALQ----ANLNSVTNSSVLQSLfnSMPAAASLVHVSSAATRLTNSHTMGNF----SPGVTGGTVGGIFNHAV 1399
Cdd:PRK14708  428 SIVTAGIVTIQsstgADLNVTGPTDLLKNL--GLTTSTGSGPLTLTKQRTTSGTTMGTLiadgSTLNVNGKTITFKNAAV 505


                  ....*...
gi 729737607 1400 PSASSPHQ 1407
Cdd:PRK14708  506 PTASASHT 513
 
Name Accession Description Interval E-value
DOT1 pfam08123
Histone methylation protein DOT1; The DOT1 domain regulates gene expression by methylating ...
 91-293 1.69e-106

Histone methylation protein DOT1; The DOT1 domain regulates gene expression by methylating histone H3. H3 methylation by DOT1 has been shown to be required for the DNA damage checkpoint in yeast.


Pssm-ID: 149273  Cd Length: 205  Bit Score: 337.35  E-value: 1.69e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607    91 YNHSV-TDPEKLNNYEPFSPEVYGETSFDLVAQMIDEIKMTEDDLFVDLGSGVGQVVLQVAAATNCKHHYGVEKADIPAK 169
Cdd:pfam08123    1 YSRSVsPDANKLNHYKAFSNEVYGELLPEFLSDVLDKCNLGPQDVFVDLGSGVGNCVLQAALEFGCKLSFGCEIMDNASN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607   170 YAETMDREFRKWMKWYGKKHAEYTLERGDFLSEEWRERI-ANTSVIFVNNFAFGPEVDHQLKERFANMKEGGRIVSSKPF 248
Cdd:pfam08123   81 LAELQDEEFKKRCKLFGKKLGKIEFIRGSFLDNERVEEIiPEADVILVNNFAFDPELNLQLKEMLQDLKDGCKIISLKSF 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 729737607   249 APLNFRINSRNLSDIGTIMRVVELSPLKGSVSWTGKPVSYYLHTI 293
Cdd:pfam08123  161 VPLNYRINFRNLSDIFNILKVEELKLPEGSVSWTSRGVEYYISTV 205
CC_DOT1L cd20902
coiled coil domain of disruptor of telomeric-silencing 1-like (DOT1L) and similar proteins; ...
 450-514 3.09e-34

coiled coil domain of disruptor of telomeric-silencing 1-like (DOT1L) and similar proteins; This family contains DOT1L (disruptor of telomeric-silencing 1-like), a non-SET domain histone lysine methyltransferase (HKMT) that catalyzes monomethylation, dimethylation, and trimethylation of nucleosomal H3K79. DOT1L is recruited to the homeobox A by AF10 (ALL1-Fused gene from chromosome 10 protein), one of the mixed-lineage leukemia 1 (MLL1)-fusion partners that function in acute myeloid leukemia (ALL). Aberration of the MLL gene is implicated in acute leukemia; chromosomal translocations of MLL1 generate oncogenic chimeric proteins, containing the non-catalytic N-terminal portion of MLL1 fused with many partners such as AF10. The aberrant recruitment of DOT1L by MLL fusions and the resulting H3K79 methylation are thought to affect gene expression by altering chromatin accessibility. AF10 and DOT1L interact through their coiled coil domains.


Pssm-ID: 411016 [Multi-domain]  Cd Length: 65  Bit Score: 125.88  E-value: 3.09e-34
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 729737607  450 ALQKLLDSFKIQYMQFMAYMKTPQYKASLQQLLEQEKEKNAQLLGTAQQLFTHCQAQKEEIKRLF 514
Cdd:cd20902     1 ALQKLLESFKIQYLQFLAYMKTPQYKASLQQQIEQEKEKNKQLTGKAQQLEKQIQALQKEGVRLL 65
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
475-628 4.81e-08

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 57.22  E-value: 4.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607  475 KASLQQLLEQEKEKNAQLLGTAQQLfthcQAQKEEIKRLFQQkldelgvkaltyndLIQAQKEISAHNQQLKEQTKQLEK 554
Cdd:COG4372    30 SEQLRKALFELDKLQEELEQLREEL----EQAREELEQLEEE--------------LEQARSELEQLEEELEELNEQLQA 91

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 729737607  555 DNSELR--NQSLQLLKARCEELKLDwstlsLENLLKEKQALKNQISEkqkhcLELQISIVELEKSQRQQELMQLKS 628
Cdd:COG4372    92 AQAELAqaQEELESLQEEAEELQEE-----LEELQKERQDLEQQRKQ-----LEAQIAELQSEIAEREEELKELEE 157
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 473-625 1.30e-07

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 56.52  E-value: 1.30e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607   473 QYKASLQQLLEQEKEKNAQLLGTAQQLF-THCQAQKEEIKRLFQQKLDELgvkaLTYNDLIQAQKEISAHNQQLKE---Q 548
Cdd:TIGR00618  725 NASSSLGSDLAAREDALNQSLKELMHQArTVLKARTEAHFNNNEEVTAAL----QTGAELSHLAAEIQFFNRLREEdthL 800

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 729737607   549 TKQLEKDNSELRNQSLQLLKARCEELKLDWStlSLENLLKEKQALKNQISEKQKHcLElqisivelEKSQRQQELMQ 625
Cdd:TIGR00618  801 LKTLEAEIGQEIPSDEDILNLQCETLVQEEE--QFLSRLEEKSATLGEITHQLLK-YE--------ECSKQLAQLTQ 866
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 475-649 3.51e-06

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 51.90  E-value: 3.51e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607   475 KASLQQLLEQEKEKN------AQLLGTAQ-QLFTHCQAQKEEIKRLFQQKLDELGVKALTYNDLIQAQKEISAHNQQLKE 547
Cdd:pfam02463  196 KLQELKLKEQAKKALeyyqlkEKLELEEEyLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENK 275

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607   548 QTKQLEKDNSELRNQ-SLQLLKARCEELKLDWSTLSLEnllKEKQALKNQISEKQKHCLELQISIVELEKSQRQQELMQL 626
Cdd:pfam02463  276 EEEKEKKLQEEELKLlAKEEEELKSELLKLERRKVDDE---EKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKRE 352

                          170       180
                   ....*....|....*....|...
gi 729737607   627 KSYTPSDESLSVQLRNKNHLSRD 649
Cdd:pfam02463  353 AEEEEEEELEKLQEKLEQLEEEL 375
PRK11281 PRK11281
mechanosensitive channel MscK;
446-623 1.60e-05

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 49.91  E-value: 1.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607  446 PTPPALQKLLDSFKIQYMQfmaymkTPQYKASLQQL---------LEQEKEKNAQLLGTAQQLFTHCQAQKEEIKRL--- 513
Cdd:PRK11281   36 PTEADVQAQLDALNKQKLL------EAEDKLVQQDLeqtlalldkIDRQKEETEQLKQQLAQAPAKLRQAQAELEALkdd 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607  514 ----FQQKLDELGVKAL------TYNDLIQAQKEISAHNQQLKEQTKQLEKDNSELRNQSLQLLKarceelkldwstlsL 583
Cdd:PRK11281  110 ndeeTRETLSTLSLRQLesrlaqTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQ--------------I 175

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 729737607  584 ENLLKEKQALKNQISEKQKHCLELQISIVELEKSQRQQEL 623
Cdd:PRK11281  176 RNLLKGGKVGGKALRPSQRVLLQAEQALLNAQNDLQRKSL 215
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 491-647 4.91e-04

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 44.24  E-value: 4.91e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607    491 QLLGTAQQLFTHCQAQKEEIKRL--FQQKLDELGVKaltyndliqaqkeISAHNQQLKEQTKQLEKDNSELRNQSLQLLK 568
Cdd:smart00787  141 LLEGLKEGLDENLEGLKEDYKLLmkELELLNSIKPK-------------LRDRKDALEEELRQLKQLEDELEDCDPTELD 207

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607    569 ARCEELKLDWSTLS-----LENLLKEKQALKNQISEKQKHCLELQISIVELEKSqrqqeLMQLKSYTPSD-ESLSVQLRN 642
Cdd:smart00787  208 RAKEKLKKLLQEIMikvkkLEELEEELQELESKIEDLTNKKSELNTEIAEAEKK-----LEQCRGFTFKEiEKLKEQLKL 282


                    ....*
gi 729737607    643 KNHLS 647
Cdd:smart00787  283 LQSLT 287
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 135-243 2.27e-03

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 39.34  E-value: 2.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607  135 FVDLGSGVGQvVLQVAAATNCKHHYGVEKADIPAKYAETmdrefrkwmKWYGKKHAEYTLERGDFlsEEWRERIANT-SV 213
Cdd:cd02440     2 VLDLGCGTGA-LALALASGPGARVTGVDISPVALELARK---------AAAALLADNVEVLKGDA--EELPPEADESfDV 69

                          90       100       110
                  ....*....|....*....|....*....|..
gi 729737607  214 IFVNN-FAFGPEVDHQLKERFAN-MKEGGRIV 243
Cdd:cd02440    70 IISDPpLHHLVEDLARFLEEARRlLKPGGVLV 101
PRK14708 PRK14708
flagellin; Provisional
 1112-1407 2.44e-03

flagellin; Provisional


Pssm-ID: 173171 [Multi-domain]  Cd Length: 888  Bit Score: 42.59  E-value: 2.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607 1112 VSSLSQNS-LFAFRPSSEDSLAIDAKITAHTRKSIAMPSS------GAD----GLSPSTNSTNGFTYNGGLST--DIGLH 1178
Cdd:PRK14708  199 ISSLTNGStATATGPAAGDSITVNGKTITFTTAGAATADSngnytiGLDqtltALLATIDTINGNTTNPSVVTagKLELH 278

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607 1179 SfidGASLPHKASDVT--TSNCSLGFQSQRSKDVGVSETNPFLNKRQL----EGLSSTKGEDLNRSGVKGKEIgeiSIRT 1252
Cdd:PRK14708  279 S---GTNSPLTISDNAggAVLAKLGLGAQVTTTAGTTAAANISATTQLfnthGGLSTTAIADGTTLTVNGKTI---TFKT 352

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607 1253 GGSSEKNSLQHN----GKVGK-GRDRDVEFKNGHNLFISAAVssGGLLNGKSLSTAVSSAGNpASSVQTHHPflNTLTTG 1327
Cdd:PRK14708  353 SDAPQGNNILTGsgvlGRIGTdGNGNSTIYLGTQNTFTNATV--GDVLTAIDLANGVKSATI-SNGVATIST--NAGQTA 427

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607 1328 SQFPLGPMALQ----ANLNSVTNSSVLQSLfnSMPAAASLVHVSSAATRLTNSHTMGNF----SPGVTGGTVGGIFNHAV 1399
Cdd:PRK14708  428 SIVTAGIVTIQsstgADLNVTGPTDLLKNL--GLTTSTGSGPLTLTKQRTTSGTTMGTLiadgSTLNVNGKTITFKNAAV 505


                  ....*...
gi 729737607 1400 PSASSPHQ 1407
Cdd:PRK14708  506 PTASASHT 513
 
Name Accession Description Interval E-value
DOT1 pfam08123
Histone methylation protein DOT1; The DOT1 domain regulates gene expression by methylating ...
 91-293 1.69e-106

Histone methylation protein DOT1; The DOT1 domain regulates gene expression by methylating histone H3. H3 methylation by DOT1 has been shown to be required for the DNA damage checkpoint in yeast.


Pssm-ID: 149273  Cd Length: 205  Bit Score: 337.35  E-value: 1.69e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607    91 YNHSV-TDPEKLNNYEPFSPEVYGETSFDLVAQMIDEIKMTEDDLFVDLGSGVGQVVLQVAAATNCKHHYGVEKADIPAK 169
Cdd:pfam08123    1 YSRSVsPDANKLNHYKAFSNEVYGELLPEFLSDVLDKCNLGPQDVFVDLGSGVGNCVLQAALEFGCKLSFGCEIMDNASN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607   170 YAETMDREFRKWMKWYGKKHAEYTLERGDFLSEEWRERI-ANTSVIFVNNFAFGPEVDHQLKERFANMKEGGRIVSSKPF 248
Cdd:pfam08123   81 LAELQDEEFKKRCKLFGKKLGKIEFIRGSFLDNERVEEIiPEADVILVNNFAFDPELNLQLKEMLQDLKDGCKIISLKSF 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 729737607   249 APLNFRINSRNLSDIGTIMRVVELSPLKGSVSWTGKPVSYYLHTI 293
Cdd:pfam08123  161 VPLNYRINFRNLSDIFNILKVEELKLPEGSVSWTSRGVEYYISTV 205
CC_DOT1L cd20902
coiled coil domain of disruptor of telomeric-silencing 1-like (DOT1L) and similar proteins; ...
 450-514 3.09e-34

coiled coil domain of disruptor of telomeric-silencing 1-like (DOT1L) and similar proteins; This family contains DOT1L (disruptor of telomeric-silencing 1-like), a non-SET domain histone lysine methyltransferase (HKMT) that catalyzes monomethylation, dimethylation, and trimethylation of nucleosomal H3K79. DOT1L is recruited to the homeobox A by AF10 (ALL1-Fused gene from chromosome 10 protein), one of the mixed-lineage leukemia 1 (MLL1)-fusion partners that function in acute myeloid leukemia (ALL). Aberration of the MLL gene is implicated in acute leukemia; chromosomal translocations of MLL1 generate oncogenic chimeric proteins, containing the non-catalytic N-terminal portion of MLL1 fused with many partners such as AF10. The aberrant recruitment of DOT1L by MLL fusions and the resulting H3K79 methylation are thought to affect gene expression by altering chromatin accessibility. AF10 and DOT1L interact through their coiled coil domains.


Pssm-ID: 411016 [Multi-domain]  Cd Length: 65  Bit Score: 125.88  E-value: 3.09e-34
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 729737607  450 ALQKLLDSFKIQYMQFMAYMKTPQYKASLQQLLEQEKEKNAQLLGTAQQLFTHCQAQKEEIKRLF 514
Cdd:cd20902     1 ALQKLLESFKIQYLQFLAYMKTPQYKASLQQQIEQEKEKNKQLTGKAQQLEKQIQALQKEGVRLL 65
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
475-628 4.81e-08

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 57.22  E-value: 4.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607  475 KASLQQLLEQEKEKNAQLLGTAQQLfthcQAQKEEIKRLFQQkldelgvkaltyndLIQAQKEISAHNQQLKEQTKQLEK 554
Cdd:COG4372    30 SEQLRKALFELDKLQEELEQLREEL----EQAREELEQLEEE--------------LEQARSELEQLEEELEELNEQLQA 91

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 729737607  555 DNSELR--NQSLQLLKARCEELKLDwstlsLENLLKEKQALKNQISEkqkhcLELQISIVELEKSQRQQELMQLKS 628
Cdd:COG4372    92 AQAELAqaQEELESLQEEAEELQEE-----LEELQKERQDLEQQRKQ-----LEAQIAELQSEIAEREEELKELEE 157
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 473-625 1.30e-07

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 56.52  E-value: 1.30e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607   473 QYKASLQQLLEQEKEKNAQLLGTAQQLF-THCQAQKEEIKRLFQQKLDELgvkaLTYNDLIQAQKEISAHNQQLKE---Q 548
Cdd:TIGR00618  725 NASSSLGSDLAAREDALNQSLKELMHQArTVLKARTEAHFNNNEEVTAAL----QTGAELSHLAAEIQFFNRLREEdthL 800

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 729737607   549 TKQLEKDNSELRNQSLQLLKARCEELKLDWStlSLENLLKEKQALKNQISEKQKHcLElqisivelEKSQRQQELMQ 625
Cdd:TIGR00618  801 LKTLEAEIGQEIPSDEDILNLQCETLVQEEE--QFLSRLEEKSATLGEITHQLLK-YE--------ECSKQLAQLTQ 866
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 476-622 1.94e-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: 52.07  E-value: 1.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607  476 ASLQQLLEQEKEKNAQLLGTAQQLfthcqAQKEEIKRLFQQKLDELGVKALTY------------NDLIQAQKEISAHNQ 543
Cdd:COG4942    93 AELRAELEAQKEELAELLRALYRL-----GRQPPLALLLSPEDFLDAVRRLQYlkylaparreqaEELRADLAELAALRA 167

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 729737607  544 QLKEQTKQLEKDNSELRNQSLQLLKARCEELKLdwstlsLENLLKEKQALKNQISEKQKHCLELQISIVELEKSQRQQE 622
Cdd:COG4942   168 ELEAERAELEALLAELEEERAALEALKAERQKL------LARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 473-622 2.05e-06

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.63  E-value: 2.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607  473 QYKASLQQLLEQEKEKNAQLLGTAQQLfTHCQAQKEEIKRLFQQKLDELGVKALTYNDLIQAQKEISAHNQQLKEQTKQL 552
Cdd:COG1196   313 ELEERLEELEEELAELEEELEELEEEL-EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607  553 EKDNSELRNQSLQLLKARcEELKLDwstlsLENLLKEKQALKNQISEKQKHCLELQISIVELEKSQRQQE 622
Cdd:COG1196   392 LRAAAELAAQLEELEEAE-EALLER-----LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE 455
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
473-648 2.07e-06

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 52.46  E-value: 2.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607  473 QYKASLQQL--LEQEKEKNAQLLGTAQQLFTHCQAQKEEIKRLfQQKLDELGvKALTYNDLIQAQKEISAHNQQLKEQTK 550
Cdd:COG4717    72 ELKELEEELkeAEEKEEEYAELQEELEELEEELEELEAELEEL-REELEKLE-KLLQLLPLYQELEALEAELAELPERLE 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607  551 QLEKDNSELRNQSLQL--LKARCEELKLDWSTLSLENLLKEKQALKNQISEKQKhcLELQISIVELEKSQRQQELMQLKS 628
Cdd:COG4717   150 ELEERLEELRELEEELeeLEAELAELQEELEELLEQLSLATEEELQDLAEELEE--LQQRLAELEEELEEAQEELEELEE 227

                         170       180
                  ....*....|....*....|
gi 729737607  629 YTPSDESLSVQLRNKNHLSR 648
Cdd:COG4717   228 ELEQLENELEAAALEERLKE 247
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 473-662 3.40e-06

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: 51.98  E-value: 3.40e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607   473 QYKASLQQLLEQEKEKNAQLLGTAQQLFThCQAQKEEIKRLFQQKLDELGVKALTYNDLIQAQKEISAHNQQLKEQTKQL 552
Cdd:TIGR02168  236 ELREELEELQEELKEAEEELEELTAELQE-LEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANL 314

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607   553 EKDNSELrNQSLQLLKARCEELKLDWSTLS--LENLLKEKQALKNQISEKQKHCLELQISIVELEK--SQRQQELMQLKS 628
Cdd:TIGR02168  315 ERQLEEL-EAQLEELESKLDELAEELAELEekLEELKEELESLEAELEELEAELEELESRLEELEEqlETLRSKVAQLEL 393

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 729737607   629 ytpSDESLSVQL-RNKNHLSRdPEADHGRFQLELE 662
Cdd:TIGR02168  394 ---QIASLNNEIeRLEARLER-LEDRRERLQQEIE 424
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 475-649 3.51e-06

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 51.90  E-value: 3.51e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607   475 KASLQQLLEQEKEKN------AQLLGTAQ-QLFTHCQAQKEEIKRLFQQKLDELGVKALTYNDLIQAQKEISAHNQQLKE 547
Cdd:pfam02463  196 KLQELKLKEQAKKALeyyqlkEKLELEEEyLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENK 275

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607   548 QTKQLEKDNSELRNQ-SLQLLKARCEELKLDWSTLSLEnllKEKQALKNQISEKQKHCLELQISIVELEKSQRQQELMQL 626
Cdd:pfam02463  276 EEEKEKKLQEEELKLlAKEEEELKSELLKLERRKVDDE---EKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKRE 352

                          170       180
                   ....*....|....*....|...
gi 729737607   627 KSYTPSDESLSVQLRNKNHLSRD 649
Cdd:pfam02463  353 AEEEEEEELEKLQEKLEQLEEEL 375
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 470-648 4.32e-06

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: 51.56  E-value: 4.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607   470 KTPQYKASLQQLLEQEKEKNAQLLGTAQQLFTHCQAQKEEIKRLF--QQKLDELGVKALTYNDLIQAQK-EISAHNQQ-- 544
Cdd:TIGR04523  226 QNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSekQKELEQNNKKIKELEKQLNQLKsEISDLNNQke 305

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607   545 ------LKEQTKQLEKDNSELRNQ------SLQLLKARCEELKLDWSTLSLENL-----LKEKQA----LKNQISEKQKH 603
Cdd:TIGR04523  306 qdwnkeLKSELKNQEKKLEEIQNQisqnnkIISQLNEQISQLKKELTNSESENSekqreLEEKQNeiekLKKENQSYKQE 385

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 729737607   604 CLELQISIVELE-KSQRQQELMQLKsytpsDESLSVQLRNKNHLSR 648
Cdd:TIGR04523  386 IKNLESQINDLEsKIQNQEKLNQQK-----DEQIKKLQQEKELLEK 426
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 475-627 6.33e-06

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.09  E-value: 6.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607  475 KASLQQLLEQEKEKNAQLLGTAQQLFTHCQAQKEEIKRLFQQKLDELGVKALTYNDLIQAQKEISAHNQQLKEQTKQLEK 554
Cdd:COG1196   304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 729737607  555 DNSELRNQSLQLLKARCEELKLDwstLSLENLLKEKQALKNQISEKQKHCLELQISIVELEKSQRQQELMQLK 627
Cdd:COG1196   384 LAEELLEALRAAAELAAQLEELE---EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
473-628 7.00e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 50.29  E-value: 7.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607  473 QYKASLQQLLEQEKEKNAQLLGTAQQLfthcqaqkEEIKRLFQQKLDELGvkaltyndliQAQKEIsahnQQLKEQTKQL 552
Cdd:COG4372    56 QAREELEQLEEELEQARSELEQLEEEL--------EELNEQLQAAQAELA----------QAQEEL----ESLQEEAEEL 113

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 729737607  553 EKDNSELRNQsLQLLKARCEELKLDWSTLSLENLLKEKQ--ALKNQISEKQKHCLELQISIVELEKSQRQQELMQLKS 628
Cdd:COG4372   114 QEELEELQKE-RQDLEQQRKQLEAQIAELQSEIAEREEElkELEEQLESLQEELAALEQELQALSEAEAEQALDELLK 190
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
480-626 7.74e-06

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 50.68  E-value: 7.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607  480 QLLEQEKEKNAQLLGTAQQLFTHCQAQKEEIKRLFQQKLDELgvkaltynDLIQAQKEISAHNQQLkeqtKQLEKDNSEL 559
Cdd:COG4913   620 AELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEI--------DVASAEREIAELEAEL----ERLDASSDDL 687

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 729737607  560 RNqslqlLKARCEELKLDWSTLS--LENLLKEKQALKNQISEKQKHCLELQISIVELEKSQRQQELMQL 626
Cdd:COG4913   688 AA-----LEEQLEELEAELEELEeeLDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALL 751
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 477-644 9.43e-06

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: 50.40  E-value: 9.43e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607   477 SLQQLLEQEKEKNAQLLGTAQQLFTHCQAQKEEIKRLFQQKLDELGVKALTYNDLIQAQKEISAHNQQLKEQTKQLEKDN 556
Cdd:TIGR04523  215 SLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLK 294

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607   557 SE---LRNQSLQ-LLKarceELKLDwstlsLENLLKEKQALKNQISEKQKHCLELQISIVELEKsqrqqELMQLKSytpS 632
Cdd:TIGR04523  295 SEisdLNNQKEQdWNK----ELKSE-----LKNQEKKLEEIQNQISQNNKIISQLNEQISQLKK-----ELTNSES---E 357

                          170
                   ....*....|..
gi 729737607   633 DESLSVQLRNKN 644
Cdd:TIGR04523  358 NSEKQRELEEKQ 369
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 221-622 1.58e-05

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 49.74  E-value: 1.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607   221 FGPEvDHQLKERfanmkeggriVSSKPFAPLNFRINSRNLsdIGTIMRVVELSPLKGSVSWTGKPVSyylhtidrTILEN 300
Cdd:pfam17380   45 FDPE-DRVCKER----------LDSRVFKPMRKYETAKTI--ITTPAPIPSSYPVSAEVSPPGAPAA--------APEEF 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607   301 YFSSLKnPKLREEQEAARRRQQRESKSNTTTPTKVQENKDSGAEEEKAAANSV---KKPSPSKARKKKLSKKGRKMAGRK 377
Cdd:pfam17380  104 VFSTIR-PKSRKPKARTRGKKRKTTTTMIQTTTPMMVTTSSSALEMTTTPKIVifaSKKNASGGNRSGEQRKQIQLIRRR 182

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607   378 RGRPKKMNTANTERKTkknqTALELLHAQ---TVSQTSSSSPQDAYKSPHS--PYYQLPPKVQRHSSNQLLVTPTPPALQ 452
Cdd:pfam17380  183 RGNHSAFTRPGRPRTT----TPMPVTHATrfvPGIQMSTVAPKEVQGMPHTlaPYEKMERRKESFNLAEDVTTMTPEYTV 258

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607   453 KL------LDSFKIQYMQFMAYMKT-------PQYKASLQQLLEQEKEKNAQLLGTAQQLFTHCQAQKEEIKRlfqqkld 519
Cdd:pfam17380  259 RYngqtmtENEFLNQLLHIVQHQKAvserqqqEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDR------- 331

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607   520 elgvkaltyndliqaQKEISAHNQQLK-EQTKQLEKDNSELRNQSLQllKARCEELKLDWSTL-SLENLLKEKQ------ 591
Cdd:pfam17380  332 ---------------QAAIYAEQERMAmERERELERIRQEERKRELE--RIRQEEIAMEISRMrELERLQMERQqknerv 394

                          410       420       430
                   ....*....|....*....|....*....|....*..
gi 729737607   592 ------ALKNQISEKQKHcLELQISIVELEKSQRQQE 622
Cdd:pfam17380  395 rqeleaARKVKILEEERQ-RKIQQQKVEMEQIRAEQE 430
PRK11281 PRK11281
mechanosensitive channel MscK;
446-623 1.60e-05

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 49.91  E-value: 1.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607  446 PTPPALQKLLDSFKIQYMQfmaymkTPQYKASLQQL---------LEQEKEKNAQLLGTAQQLFTHCQAQKEEIKRL--- 513
Cdd:PRK11281   36 PTEADVQAQLDALNKQKLL------EAEDKLVQQDLeqtlalldkIDRQKEETEQLKQQLAQAPAKLRQAQAELEALkdd 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607  514 ----FQQKLDELGVKAL------TYNDLIQAQKEISAHNQQLKEQTKQLEKDNSELRNQSLQLLKarceelkldwstlsL 583
Cdd:PRK11281  110 ndeeTRETLSTLSLRQLesrlaqTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQ--------------I 175

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 729737607  584 ENLLKEKQALKNQISEKQKHCLELQISIVELEKSQRQQEL 623
Cdd:PRK11281  176 RNLLKGGKVGGKALRPSQRVLLQAEQALLNAQNDLQRKSL 215
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 479-635 1.64e-05

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: 49.63  E-value: 1.64e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607   479 QQLLEQEKEKNAQLLGTAQQLFTHCQA---QKEEIKRLFQQKLDELGVKALTYNDLIQAQKEISAHNQQLKEQTKQLEKD 555
Cdd:TIGR04523  369 QNEIEKLKKENQSYKQEIKNLESQINDlesKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQ 448

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607   556 NSELR-------------NQSLQLLKARCEELKLDWSTLS---------LENLLKEKQALKNQISE--KQKHCLELQISI 611
Cdd:TIGR04523  449 DSVKEliiknldntreslETQLKVLSRSINKIKQNLEQKQkelkskekeLKKLNEEKKELEEKVKDltKKISSLKEKIEK 528

                          170       180
                   ....*....|....*....|....
gi 729737607   612 VELEKSQRQQELMQLKSYTPSDES 635
Cdd:TIGR04523  529 LESEKKEKESKISDLEDELNKDDF 552
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 476-622 4.06e-05

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 48.15  E-value: 4.06e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607   476 ASLQQLLEQEKEKNAQL---LGTAQQLFTHCQAQKEEIkrlfQQKLDELGVKAltyNDLIQAQKEISAHNQQLKEQTKQL 552
Cdd:pfam05622  307 TELQQLLEDANRRKNELetqNRLANQRILELQQQVEEL----QKALQEQGSKA---EDSSLLKQKLEEHLEKLHEAQSEL 379

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607   553 EKDN---SELRNQSLQLLKARCEEL-----KLDWSTLSLENLLK-----------------------EKQALKNQISEKQ 601
Cdd:pfam05622  380 QKKKeqiEELEPKQDSNLAQKIDELqealrKKDEDMKAMEERYKkyvekaksviktldpkqnpasppEIQALKNQLLEKD 459

                          170       180
                   ....*....|....*....|.
gi 729737607   602 KHCLELQISiVELEKSQRQQE 622
Cdd:pfam05622  460 KKIEHLERD-FEKSKLQREQE 479
HALZ pfam02183
Homeobox associated leucine zipper;
550-599 4.07e-05

Homeobox associated leucine zipper;


Pssm-ID: 460477 [Multi-domain]  Cd Length: 42  Bit Score: 42.12  E-value: 4.07e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 729737607   550 KQLEKDNSelrnqslqLLKARCEELKLDWstlslENLLKEKQALKNQISE 599
Cdd:pfam02183    1 KQLERDYD--------VLKASYDALKSDF-----DSLKKENQKLQAELQE 37
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 479-628 4.36e-05

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.39  E-value: 4.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607  479 QQLLEQEKEKNAQLLGTAQQLFTHCQAQKEEIKRLFQQKLDELGVKALTYN----DLIQAQKEISAHNQQLKEQTKQLEK 554
Cdd:COG1196   241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYellaELARLEQDIARLEERRRELEERLEE 320

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 729737607  555 DNSELR--NQSLQLLKARCEELKLDwstlsLENLLKEKQALKNQISEKQKHCLELQISIVELEK--SQRQQELMQLKS 628
Cdd:COG1196   321 LEEELAelEEELEELEEELEELEEE-----LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEelEELAEELLEALR 393
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
476-625 4.37e-05

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.23  E-value: 4.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607  476 ASLQQLLEQEKEKNAQLLgtaqqlfthCQAQKEEIKRLFQQK----LDELGVKALTYNDLIQAQKEISAHNQQLKEQTKQ 551
Cdd:COG4717   347 EELQELLREAEELEEELQ---------LEELEQEIAALLAEAgvedEEELRAALEQAEEYQELKEELEELEEQLEELLGE 417

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 729737607  552 LEkdnSELRNQSLQLLKARCEELKLDWSTLS--LENLLKEKQALKNQISEkqkhclelqisiveLEKSQRQQELMQ 625
Cdd:COG4717   418 LE---ELLEALDEEELEEELEELEEELEELEeeLEELREELAELEAELEQ--------------LEEDGELAELLQ 476
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 451-626 6.36e-05

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 47.81  E-value: 6.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607   451 LQKLLDSFKIQYMQFMAYMKTpqYKASLQQLLEQEKeknAQLLGTAQQL--FTHCQAQKEEIKRLFQQKLDELGVKALTy 528
Cdd:pfam15921  417 LRRELDDRNMEVQRLEALLKA--MKSECQGQMERQM---AAIQGKNESLekVSSLTAQLESTKEMLRKVVEELTAKKMT- 490

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607   529 ndLIQAQKEISAHNQQLKEQTKQLEKDNSE---------LRNQSLQLLKARCEELKldwstlsleNLLKEKQALKNQISE 599
Cdd:pfam15921  491 --LESSERTVSDLTASLQEKERAIEATNAEitklrsrvdLKLQELQHLKNEGDHLR---------NVQTECEALKLQMAE 559

                          170       180
                   ....*....|....*....|....*..
gi 729737607   600 KQKhclelqisIVELEKsQRQQELMQL 626
Cdd:pfam15921  560 KDK--------VIEILR-QQIENMTQL 577
COG5124 COG5124
Protein predicted to be involved in meiotic recombination [Cell division and chromosome ...
 469-668 1.21e-04

Protein predicted to be involved in meiotic recombination [Cell division and chromosome partitioning / General function prediction only];


Pssm-ID: 227453 [Multi-domain]  Cd Length: 209  Bit Score: 44.95  E-value: 1.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607  469 MKTPQYKASLQQLLEQEKE----KNAQLLGTAQQLFTHCqaqkeeIKRLFQQKLDElgvkaltynDLIQAQK-EISAHNQ 543
Cdd:COG5124     6 LSLAEKRRRLEAIFHDSKDffqlKEVEKLGSKKQIVLMT------VKDLLQQLVDD---------GVVSVEKcGTSNIYW 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607  544 QLKEQTKQLEKDnselrnqSLQLLKARCEELKLDWSTLSlENLLKEKQALKNQISEKQKHCLELQI-SIVELEKSQRQQE 622
Cdd:COG5124    71 SFKSQTLQKLYD-------SSELLKKKIQEVKQDIATYK-EEIDKEKATRRKKFTEGQKNYNREALlEKRKKEQDEIKKK 142

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 729737607  623 LMQLKSYTPSDESLSVQLRNKNHLSRDPEADHGRFQLELECSKFPM 668
Cdd:COG5124   143 LNSLQKIEPIRWDAAKIQEKKKKVHLNKTTDNIEILIDYLCKKFFL 188
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 475-628 1.42e-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: 46.55  E-value: 1.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607   475 KASLQQLLEQEKEKNAQLLGTAQQLFTHCQAQKEEIKRLFQQKLD----------ELGVKALTYNDL---IQAQK----- 536
Cdd:TIGR04523  393 INDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKnnseikdltnQDSVKELIIKNLdntRESLEtqlkv 472

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607   537 ---EISAHNQQLKEQTKQLEKDNSELRN---------QSLQLLKARCEELKLDWSTLSLENLLKE--------------- 589
Cdd:TIGR04523  473 lsrSINKIKQNLEQKQKELKSKEKELKKlneekkeleEKVKDLTKKISSLKEKIEKLESEKKEKEskisdledelnkddf 552

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 729737607   590 ---KQALKNQISEKQKHCLELQISIVELEKSQRQ-QELMQLKS 628
Cdd:TIGR04523  553 elkKENLEKEIDEKNKEIEELKQTQKSLKKKQEEkQELIDQKE 595
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
512-628 1.45e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.05  E-value: 1.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607  512 RLFQQKLDELGVKALTYNDLIQAQKEISAHNQQLKEQTKQLEKDNSELRNQSLQLLKARcEEL-----KLDWSTLSLENL 586
Cdd:COG4372    14 SLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQAR-SELeqleeELEELNEQLQAA 92

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 729737607  587 LKEKQALKNQISEKQKHCLELQISIVELEKSQR--QQELMQLKS 628
Cdd:COG4372    93 QAELAQAQEELESLQEEAEELQEELEELQKERQdlEQQRKQLEA 136
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
476-642 1.59e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 46.30  E-value: 1.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607  476 ASLQQLLEQEKEKNAQLLGTAQQLFThcQAQKEEIKRLfQQKLDELGVKALTYNDLIQAQKEIsahNQQLKEQTKQLEKD 555
Cdd:COG4717    41 AFIRAMLLERLEKEADELFKPQGRKP--ELNLKELKEL-EEELKEAEEKEEEYAELQEELEEL---EEELEELEAELEEL 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607  556 NSELRN----QSLQLLKARCEELK--LDWSTLSLENLLKEKQALKN---QISEKQKHCLELQISIVELEKSQRQQELMQL 626
Cdd:COG4717   115 REELEKleklLQLLPLYQELEALEaeLAELPERLEELEERLEELREleeELEELEAELAELQEELEELLEQLSLATEEEL 194

                         170
                  ....*....|....*.
gi 729737607  627 KSYTPSDESLSVQLRN 642
Cdd:COG4717   195 QDLAEELEELQQRLAE 210
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 467-662 2.07e-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: 46.21  E-value: 2.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607   467 AYMKTPQYKASLQQLLEQEKEKNAQLLGtaqqlfthCQAQKEEIKRLFQQKLDELgvkaltyndliqaqkeisahnQQLK 546
Cdd:TIGR02169  665 GILFSRSEPAELQRLRERLEGLKRELSS--------LQSELRRIENRLDELSQEL---------------------SDAS 715

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607   547 EQTKQLEKDNSELrNQSLQLLKARCEELKLDWSTLS--LENLLKEKQALKNQISEKQKHCLELQISIVELEKSQRQQELM 624
Cdd:TIGR02169  716 RKIGEIEKEIEQL-EQEEEKLKERLEELEEDLSSLEqeIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIP 794

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 729737607   625 QLksyTPSDESLSVQLRNKNHLSRDPEADHGRFQLELE 662
Cdd:TIGR02169  795 EI---QAELSKLEEEVSRIEARLREIEQKLNRLTLEKE 829
CENP-F_leu_zip pfam10473
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ...
 534-614 3.40e-04

Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance.


Pssm-ID: 463102 [Multi-domain]  Cd Length: 140  Bit Score: 42.28  E-value: 3.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607   534 AQKEISAHNQQ---LKEQTKQLEKDNSELR------NQSLQLLKARCEELKLdwSTLSLENLLKEKQALKNQISEKQKHC 604
Cdd:pfam10473   50 SKAEVETLKAEieeMAQNLRDLELDLVTLRsekenlTKELQKKQERVSELES--LNSSLENLLEEKEQEKVQMKEESKTA 127

                           90
                   ....*....|.
gi 729737607   605 LE-LQISIVEL 614
Cdd:pfam10473  128 VEmLQTQLKEL 138
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 479-622 3.80e-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: 3.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607  479 QQLLEQEKEKNAQLLGTAQQLFthcQAQKEEIkrlfQQKLDELGvkaltyNDLIQAQKEISAHNQQLKEQTKQLEKDNSE 558
Cdd:COG1196   216 RELKEELKELEAELLLLKLREL---EAELEEL----EAELEELE------AELEELEAELAELEAELEELRLELEELELE 282

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 729737607  559 L--RNQSLQLLKARCEEL--KLDWSTLSLENLLKEKQALKNQISEKQKHCLELQISIVELEKSQRQQE 622
Cdd:COG1196   283 LeeAQAEEYELLAELARLeqDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE 350
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 473-648 4.44e-04

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 44.73  E-value: 4.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607   473 QYKASLQQLLEQEKEKNAQLLgTAQQLFT---------HCQAQKEEI--------KRLFQQKLDELGVKALTYNDLIQ-- 533
Cdd:pfam05557   80 LKKKYLEALNKKLNEKESQLA-DAREVISclknelselRRQIQRAELelqstnseLEELQERLDLLKAKASEAEQLRQnl 158

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607   534 --AQKEISAHNQQLKEqtkqLEKDNsELRNQSLQLLKARCEELkldwstLSLENLLKEKQALK------------NQISE 599
Cdd:pfam05557  159 ekQQSSLAEAEQRIKE----LEFEI-QSQEQDSEIVKNSKSEL------ARIPELEKELERLRehnkhlnenienKLLLK 227

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 729737607   600 KQKHCLEL----------QISIVELEKSQRQQElmqLKSYTPSDESLSVQLRNKNHLSR 648
Cdd:pfam05557  228 EEVEDLKRklereekyreEAATLELEKEKLEQE---LQSWVKLAQDTGLNLRSPEDLSR 283
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 491-647 4.91e-04

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 44.24  E-value: 4.91e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607    491 QLLGTAQQLFTHCQAQKEEIKRL--FQQKLDELGVKaltyndliqaqkeISAHNQQLKEQTKQLEKDNSELRNQSLQLLK 568
Cdd:smart00787  141 LLEGLKEGLDENLEGLKEDYKLLmkELELLNSIKPK-------------LRDRKDALEEELRQLKQLEDELEDCDPTELD 207

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607    569 ARCEELKLDWSTLS-----LENLLKEKQALKNQISEKQKHCLELQISIVELEKSqrqqeLMQLKSYTPSD-ESLSVQLRN 642
Cdd:smart00787  208 RAKEKLKKLLQEIMikvkkLEELEEELQELESKIEDLTNKKSELNTEIAEAEKK-----LEQCRGFTFKEiEKLKEQLKL 282


                    ....*
gi 729737607    643 KNHLS 647
Cdd:smart00787  283 LQSLT 287
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
473-653 5.50e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.12  E-value: 5.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607  473 QYKASLQQLLEQEKEKNAQLlgtaQQLFTHCQAQKEEIKRLFQQkldelgvkaltYNDLIQAQKEISAHNQQLKEQTKQL 552
Cdd:COG4372    84 ELNEQLQAAQAELAQAQEEL----ESLQEEAEELQEELEELQKE-----------RQDLEQQRKQLEAQIAELQSEIAER 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607  553 EKDNSELRNQsLQLLKARCEELKLDWSTLSLENLLKEKQALKNQISEKQKHCLELQISIVELEKSQRQQELMQLKSYTPS 632
Cdd:COG4372   149 EEELKELEEQ-LESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSL 227

                         170       180
                  ....*....|....*....|.
gi 729737607  633 DESLSVQLRNKNHLSRDPEAD 653
Cdd:COG4372   228 EAKLGLALSALLDALELEEDK 248
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 499-628 6.52e-04

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.98  E-value: 6.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607  499 LFTHCQAQKEEIKRLfQQKLDELgvkaltyndliqaQKEISAHNQQLKEQTKQLEKDNSELRNQSLQLLKARCE----EL 574
Cdd:COG4942    11 LALAAAAQADAAAEA-EAELEQL-------------QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRiralEQ 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 729737607  575 KLDWSTLSLENLLKEKQALKNQISEKQKhclELQISIVELEKSQRQQELMQLKS 628
Cdd:COG4942    77 ELAALEAELAELEKEIAELRAELEAQKE---ELAELLRALYRLGRQPPLALLLS 127
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
478-607 6.66e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.37  E-value: 6.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607  478 LQQLLEQEKEKNAQL---LGTAQQLFTHCQAQ--KEEIKRLfQQKLDELgvkaltYNDLIQAQKEIsahnQQLKEQTKQL 552
Cdd:COG4717   397 YQELKEELEELEEQLeelLGELEELLEALDEEelEEELEEL-EEELEEL------EEELEELREEL----AELEAELEQL 465

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 729737607  553 EKDN--SELRnQSLQLLKARCEELKLDWSTLSL-ENLLkeKQALKNQISEKQKHCLEL 607
Cdd:COG4717   466 EEDGelAELL-QELEELKAELRELAEEWAALKLaLELL--EEAREEYREERLPPVLER 520
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
473-648 7.89e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.99  E-value: 7.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607  473 QYKASLQQLLEQEKEKNAQLLGTAQQLFTHCQAQKEEIKRLfQQKLDELG---VKALTYNDLIQAQKEIsahnQQLKEQT 549
Cdd:COG4717   367 ELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEEL-EEQLEELLgelEELLEALDEEELEEEL----EELEEEL 441

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607  550 KQLEKDNSELRNQsLQLLKARCEELKLDwstLSLENLLKEKQALKNQISEKQKHCLELQISIVELEK------SQRQQEL 623
Cdd:COG4717   442 EELEEELEELREE-LAELEAELEQLEED---GELAELLQELEELKAELRELAEEWAALKLALELLEEareeyrEERLPPV 517

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 729737607  624 MQL--------------KSYTPSDESLSVQLRNK-----NHLSR 648
Cdd:COG4717   518 LERaseyfsrltdgryrLIRIDEDLSLKVDTEDGrtrpvEELSR 561
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 475-627 9.10e-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: 44.28  E-value: 9.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607   475 KASLQQLLEQEKEKNAQLLGTAQQLFtHCQAQKEEIKRLFQQKLDElgvkaltYNDLIQAQKEISAHNQQLKEQTKQLEK 554
Cdd:TIGR02168  837 ERRLEDLEEQIEELSEDIESLAAEIE-ELEELIEELESELEALLNE-------RASLEEALALLRSELEELSEELRELES 908

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 729737607   555 DNSELRnQSLQLLKARCEELKLDWStlSLENLLKEKQAlknQISEKQKHCLELQI---SIVELEKSQRQQELMQLK 627
Cdd:TIGR02168  909 KRSELR-RELEELREKLAQLELRLE--GLEVRIDNLQE---RLSEEYSLTLEEAEaleNKIEDDEEEARRRLKRLE 978
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 480-628 1.12e-03

Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.


Pssm-ID: 462536 [Multi-domain]  Cd Length: 176  Bit Score: 41.46  E-value: 1.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607   480 QLLEQE---KEKNAQLLGTAQQLFTHCQAQKEEIKRLFQQKLDELGVKALTYN-DLIQAQKEISAHNQQLKEQTKQLEKD 555
Cdd:pfam08614   11 RLLDRTallEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQLReELAELYRSRGELAQRLVDLNEELQEL 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607   556 NSELRNQS--LQLLKARCEELKLdwSTLSLENLLKEKQALkNQI--SEKQKhcLELQISIVELEKSQRQQE-------LM 624
Cdd:pfam08614   91 EKKLREDErrLAALEAERAQLEE--KLKDREEELREKRKL-NQDlqDELVA--LQLQLNMAEEKLRKLEKEnrelverWM 165


                   ....
gi 729737607   625 QLKS 628
Cdd:pfam08614  166 KRKG 169
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 475-628 1.39e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 43.47  E-value: 1.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607   475 KASLQQLLEQEKEKNAQLLgtaqQLFTHCQAQKEEIKRLfQQKLDELGVKaltyndlIQA-QKEISAHNQQLKEQTKQLE 553
Cdd:TIGR04523  481 KQNLEQKQKELKSKEKELK----KLNEEKKELEEKVKDL-TKKISSLKEK-------IEKlESEKKEKESKISDLEDELN 548

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607   554 KDNSELRNQSL----QLLKARCEELKLDWSTL-----SLENLLKEKQA----LKNQISEKQKHCLEL--QISIVELEKSQ 618
Cdd:TIGR04523  549 KDDFELKKENLekeiDEKNKEIEELKQTQKSLkkkqeEKQELIDQKEKekkdLIKEIEEKEKKISSLekELEKAKKENEK 628

                          170
                   ....*....|
gi 729737607   619 RQQELMQLKS 628
Cdd:TIGR04523  629 LSSIIKNIKS 638
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 467-565 1.54e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 40.64  E-value: 1.54e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607    467 AYMKTPQYKASLQQLLEQEKEKNAQLlgtaqqlfthcQAQKEEIKRLfQQKLDELGVKaLTYNDLIQAQKEISAHNQQLK 546
Cdd:smart00935    9 ILQESPAGKAAQKQLEKEFKKRQAEL-----------EKLEKELQKL-KEKLQKDAAT-LSEAAREKKEKELQKKVQEFQ 75

                            90
                    ....*....|....*....
gi 729737607    547 EQTKQLEKDNSELRNQSLQ 565
Cdd:smart00935   76 RKQQKLQQDLQKRQQEELQ 94
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 472-665 1.63e-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: 43.13  E-value: 1.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607   472 PQYKASLQQLLEQEKEKNAQLLGTA-QQLFTHCQAQKEEIKRLfQQKLDELGVK--ALTYnDLIQAQKEIsahnQQLKEQ 548
Cdd:TIGR02169  768 EELEEDLHKLEEALNDLEARLSHSRiPEIQAELSKLEEEVSRI-EARLREIEQKlnRLTL-EKEYLEKEI----QELQEQ 841

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607   549 TKQLEKDNSELRnQSLQLLKARCEEL--KLDWSTLSLENLLKEKQALKNQISEKQKHCLELQISIVELEkSQRQQELMQL 626
Cdd:TIGR02169  842 RIDLKEQIKSIE-KEIENLNGKKEELeeELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELE-AQIEKKRKRL 919

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 729737607   627 KSYTPSDESLSVQL----RNKNHLSRDPEADHGRFQLELECSK 665
Cdd:TIGR02169  920 SELKAKLEALEEELseieDPKGEDEEIPEEELSLEDVQAELQR 962
MscS_porin pfam12795
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...
 473-628 1.83e-03

Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.


Pssm-ID: 432790 [Multi-domain]  Cd Length: 238  Bit Score: 41.90  E-value: 1.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607   473 QYKASLQQLLEQEKEKNAQLLGTAQQLfTHCQAQKEEIKRLFQQKLDELGVKALTYNDLIQAQK-EISAHNQQLKEQTKQ 551
Cdd:pfam12795   89 QTSAQLQELQNQLAQLNSQLIELQTRP-ERAQQQLSEARQRLQQIRNRLNGPAPPGEPLSEAQRwALQAELAALKAQIDM 167

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 729737607   552 LEKdnsELRNQSLQ--LLKARceelkLDWSTLSLENLLKEKQALKNQISEKQKhclelqisiVELEKSQRQQELMQLKS 628
Cdd:pfam12795  168 LEQ---ELLSNNNRqdLLKAR-----RDLLTLRIQRLEQQLQALQELLNEKRL---------QEAEQAVAQTEQLAEEA 229
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 135-243 2.27e-03

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 39.34  E-value: 2.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607  135 FVDLGSGVGQvVLQVAAATNCKHHYGVEKADIPAKYAETmdrefrkwmKWYGKKHAEYTLERGDFlsEEWRERIANT-SV 213
Cdd:cd02440     2 VLDLGCGTGA-LALALASGPGARVTGVDISPVALELARK---------AAAALLADNVEVLKGDA--EELPPEADESfDV 69

                          90       100       110
                  ....*....|....*....|....*....|..
gi 729737607  214 IFVNN-FAFGPEVDHQLKERFAN-MKEGGRIV 243
Cdd:cd02440    70 IISDPpLHHLVEDLARFLEEARRlLKPGGVLV 101
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 504-627 2.38e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.62  E-value: 2.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607  504 QAQKEEIKRLFQQKLDELGVKALTYNDLiQAQKEISAHNQQLKEQTKQLEKDNSELRNQSLQLLKARCEELKLDwstLSL 583
Cdd:COG1196   208 QAEKAERYRELKEELKELEAELLLLKLR-ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELE---LEL 283

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 729737607  584 ENLLKEKQALKNQISEkqkhcLELQISIVELEKSQRQQELMQLK 627
Cdd:COG1196   284 EEAQAEEYELLAELAR-----LEQDIARLEERRRELEERLEELE 322
PRK14708 PRK14708
flagellin; Provisional
 1112-1407 2.44e-03

flagellin; Provisional


Pssm-ID: 173171 [Multi-domain]  Cd Length: 888  Bit Score: 42.59  E-value: 2.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607 1112 VSSLSQNS-LFAFRPSSEDSLAIDAKITAHTRKSIAMPSS------GAD----GLSPSTNSTNGFTYNGGLST--DIGLH 1178
Cdd:PRK14708  199 ISSLTNGStATATGPAAGDSITVNGKTITFTTAGAATADSngnytiGLDqtltALLATIDTINGNTTNPSVVTagKLELH 278

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607 1179 SfidGASLPHKASDVT--TSNCSLGFQSQRSKDVGVSETNPFLNKRQL----EGLSSTKGEDLNRSGVKGKEIgeiSIRT 1252
Cdd:PRK14708  279 S---GTNSPLTISDNAggAVLAKLGLGAQVTTTAGTTAAANISATTQLfnthGGLSTTAIADGTTLTVNGKTI---TFKT 352

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607 1253 GGSSEKNSLQHN----GKVGK-GRDRDVEFKNGHNLFISAAVssGGLLNGKSLSTAVSSAGNpASSVQTHHPflNTLTTG 1327
Cdd:PRK14708  353 SDAPQGNNILTGsgvlGRIGTdGNGNSTIYLGTQNTFTNATV--GDVLTAIDLANGVKSATI-SNGVATIST--NAGQTA 427

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607 1328 SQFPLGPMALQ----ANLNSVTNSSVLQSLfnSMPAAASLVHVSSAATRLTNSHTMGNF----SPGVTGGTVGGIFNHAV 1399
Cdd:PRK14708  428 SIVTAGIVTIQsstgADLNVTGPTDLLKNL--GLTTSTGSGPLTLTKQRTTSGTTMGTLiadgSTLNVNGKTITFKNAAV 505


                  ....*...
gi 729737607 1400 PSASSPHQ 1407
Cdd:PRK14708  506 PTASASHT 513
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
472-628 2.46e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.59  E-value: 2.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607  472 PQYKASLQ-QLLEQEKEKNAQLLGTAQQLFTHCQAQKEEIK---RLFQQKLDELGVKALTyndliQAQKEISAHNQQLKE 547
Cdd:COG4913   282 RLWFAQRRlELLEAELEELRAELARLEAELERLEARLDALReelDELEAQIRGNGGDRLE-----QLEREIERLERELEE 356

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607  548 qtkqlekdnselRNQSLQLLKARCEELKL--DWSTLSLENLLKEKQALKNQISEKQKHC------LELQISIVELEKSQR 619
Cdd:COG4913   357 ------------RERRRARLEALLAALGLplPASAEEFAALRAEAAALLEALEEELEALeealaeAEAALRDLRRELREL 424


                  ....*....
gi 729737607  620 QQELMQLKS 628
Cdd:COG4913   425 EAEIASLER 433
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 470-640 2.71e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 42.63  E-value: 2.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607  470 KTPQYKASLQQLLEQEKEKNAQLLGTAQQLfTHCQAQK----EEIKRL------FQQKLDELGVKALTYNDLIQAqkeis 539
Cdd:COG3096   348 KIERYQEDLEELTERLEEQEEVVEEAAEQL-AEAEARLeaaeEEVDSLksqladYQQALDVQQTRAIQYQQAVQA----- 421

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607  540 ahnqqLKEQTKQLEKDNSELRNQSLQLLKARCEELKLDWSTLSLENLLKEKQALKNQISekqkHCLELQISIV-ELEKSQ 618
Cdd:COG3096   422 -----LEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFE----KAYELVCKIAgEVERSQ 492

                         170       180
                  ....*....|....*....|..
gi 729737607  619 RQQELMQLKSYTPSDESLSVQL 640
Cdd:COG3096   493 AWQTARELLRRYRSQQALAQRL 514
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 480-622 3.52e-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: 41.06  E-value: 3.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607  480 QLLEQEKEKNAQLLGTAQQLFTHCQAQKEEIKRLFQQKLDELGvkaltyndliQAQKEISAHNQQLKEQTKQLEKDNSEL 559
Cdd:COG1579    13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELE----------DLEKEIKRLELEIEEVEARIKKYEEQL 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 729737607  560 RNQSlqllKARceELkldwstlslENLLKEKQALKNQISEKQKHCLELQISIVELEKSQRQQE 622
Cdd:COG1579    83 GNVR----NNK--EY---------EALQKEIESLKRRISDLEDEILELMERIEELEEELAELE 130
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
505-662 3.60e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 3.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607  505 AQKEEIKRLFQQKLDELGvkaltyndliQAQKEISAHNQQLKEQTKQLEKDNSELrnQSLQLLKARCEELKLDwstlsLE 584
Cdd:PRK03918  186 KRTENIEELIKEKEKELE----------EVLREINEISSELPELREELEKLEKEV--KELEELKEEIEELEKE-----LE 248

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 729737607  585 NLLKEKQALKNQISEKQKHCLELQISIVELEKsqRQQELMQLKSYTPSDESLSVQLRNKNHLSRDPEADHGRFQLELE 662
Cdd:PRK03918  249 SLEGSKRKLEEKIRELEERIEELKKEIEELEE--KVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEIN 324
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 470-628 7.98e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 41.11  E-value: 7.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607   470 KTPQYKASLQQLLE--QEKEKNAQLLgtaQQLFTHCQAQKEEIKRL-FQQKLDELGVKALTY----NDLIQAQKEISAHN 542
Cdd:TIGR00618  237 QTQQSHAYLTQKREaqEEQLKKQQLL---KQLRARIEELRAQEAVLeETQERINRARKAAPLaahiKAVTQIEQQAQRIH 313

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607   543 QQLKEQTKQLEK----------DNSELRNQ--SLQLLKARCEELKlDWStlslenllkEKQALKNQISEKQK----HCLE 606
Cdd:TIGR00618  314 TELQSKMRSRAKllmkraahvkQQSSIEEQrrLLQTLHSQEIHIR-DAH---------EVATSIREISCQQHtltqHIHT 383

                          170       180
                   ....*....|....*....|..
gi 729737607   607 LQISIVELEksQRQQELMQLKS 628
Cdd:TIGR00618  384 LQQQKTTLT--QKLQSLCKELD 403
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 479-665 9.06e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 40.72  E-value: 9.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607   479 QQLLEQEKEKNAQLLGTA-QQLFTHCQAQKEEIK----RLFQQKLDELGVKALTYNDLIQAQKEISAHN----QQLKEQT 549
Cdd:TIGR00618  424 GQLAHAKKQQELQQRYAElCAAAITCTAQCEKLEkihlQESAQSLKEREQQLQTKEQIHLQETRKKAVVlarlLELQEEP 503

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607   550 KQLEKDNSELrNQSLQLL------KARCEELKLDWSTL--SLENL-------LKEKQALKNQISEKQKHCLELQISIVEL 614
Cdd:TIGR00618  504 CPLCGSCIHP-NPARQDIdnpgplTRRMQRGEQTYAQLetSEEDVyhqltseRKQRASLKEQMQEIQQSFSILTQCDNRS 582

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 729737607   615 EKS--QRQQELMQLKSYTPSDESLSVQLRNKNH---LSRDPEADHGRFQLEL-ECSK 665
Cdd:TIGR00618  583 KEDipNLQNITVRLQDLTEKLSEAEDMLACEQHallRKLQPEQDLQDVRLHLqQCSQ 639
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 438-641 9.52e-03

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 40.26  E-value: 9.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607   438 SSNQLLVTPTPPALQKLLDsfkiqymqfmaymKTPQYKASLQQLLE---QEKEKNAQLLGTAQQLFTHcqaQKEEIKRLF 514
Cdd:pfam07888   19 GTDMLLVVPRAELLQNRLE-------------ECLQERAELLQAQEaanRQREKEKERYKRDREQWER---QRRELESRV 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607   515 QQKLDELGVKALTYNDLIQAQKEISAHNQQLKEQT--------------KQLEKDNSELRNQSL--------------QL 566
Cdd:pfam07888   83 AELKEELRQSREKHEELEEKYKELSASSEELSEEKdallaqraaheariRELEEDIKTLTQRVLeretelermkerakKA 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607   567 LKARCEE--------LKLDWSTLSLENLLKEKQALKNQISEKQKHCLELQISIVELeksqrQQELMQLKSYTPSDESLSV 638
Cdd:pfam07888  163 GAQRKEEeaerkqlqAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTL-----TQKLTTAHRKEAENEALLE 237


                   ...
gi 729737607   639 QLR 641
Cdd:pfam07888  238 ELR 240
PRK12704 PRK12704
phosphodiesterase; Provisional
 504-634 9.84e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.53  E-value: 9.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737607  504 QAQKEEIKRLFQQKLDELGVKALTYND--LIQAQKEIsahnqqlKEQTKQLEKDNSElRNQSLQLLKARceeLKLDWSTL 581
Cdd:PRK12704   30 EAKIKEAEEEAKRILEEAKKEAEAIKKeaLLEAKEEI-------HKLRNEFEKELRE-RRNELQKLEKR---LLQKEENL 98

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 729737607  582 S--LENLLKEKQAL---KNQISEKQKHcLELQISIVELEKSQRQQELMQLKSYTpSDE 634
Cdd:PRK12704   99 DrkLELLEKREEELekkEKELEQKQQE-LEKKEEELEELIEEQLQELERISGLT-AEE 154
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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