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Conserved domains on  [gi|568967112|ref|XP_006513494|]
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histone-lysine N-methyltransferase, H3 lysine-79 specific isoform X4 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CC_DOT1L cd20902
coiled coil domain of disruptor of telomeric-silencing 1-like (DOT1L) and similar proteins; ...
 242-306 5.64e-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: 124.73  E-value: 5.64e-34
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568967112  242 ALQKLLESFRIQYLQFLAYTKTPQYKANLQQLLDQEKEKNTQLLGTAQQLFGHCQAQKEEIRRLF 306
Cdd:cd20902     1 ALQKLLESFKIQYLQFLAYMKTPQYKASLQQQIEQEKEKNKQLTGKAQQLEKQIQALQKEGVRLL 65
AdoMet_MTases super family cl17173
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 9-78 1.63e-31

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.).


The actual alignment was detected with superfamily member pfam08123:

Pssm-ID: 473071  Cd Length: 205  Bit Score: 123.18  E-value: 1.63e-31
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112     9 EVDHQLKERFANMKEGGRIVSSKPFAPLNFRINSRNLSDIGTIMRVVELSPLKGSVSWTGKPVSYYLHTI 78
Cdd:pfam08123  136 ELNLQLKEMLQDLKDGCKIISLKSFVPLNYRINFRNLSDIFNILKVEELKLPEGSVSWTSRGVEYYISTV 205
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
267-420 3.84e-11

Uncharacterized protein, contains DUF3084 domain [Function unknown];


:

Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 66.85  E-value: 3.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112  267 KANLQQLLDQEKEKNTQLLGTAQQLfghcQAQKEEIRRLfQQKLDELgvkaltYNDLIQAQKEISAHNQQL---REQSEQ 343
Cdd:COG4372    44 QEELEQLREELEQAREELEQLEEEL----EQARSELEQL-EEELEEL------NEQLQAAQAELAQAQEELeslQEEAEE 112

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568967112  344 LEKDNSELRSQsLRLLRARCEELRLDWSTL--SLENLRKEKQALRSQISEKQRHCLELQISIVELEKTQRQQELLQLKS 420
Cdd:COG4372   113 LQEELEELQKE-RQDLEQQRKQLEAQIAELqsEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLK 190
PHA03307 super family cl33723
transcriptional regulator ICP4; Provisional
 542-886 2.05e-04

transcriptional regulator ICP4; Provisional


The actual alignment was detected with superfamily member PHA03307:

Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 46.32  E-value: 2.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112  542 RHLSQDHTGASKAATSEPHPRPEHPKESSLPyqSPGLSNSMKLSPQDPPLASPATSPltsekGSEKGVKERAYSSHGETI 621
Cdd:PHA03307   76 GTEAPANESRSTPTWSLSTLAPASPAREGSP--TPPGPSSPDPPPPTPPPASPPPSP-----APDLSEMLRPVGSPGPPP 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112  622 TSLPVSIPLSTVQPNKLPVSIPLASVVLPSRAERARSTPSPVPQPRDSSAtlekqtgasahgaggagagsrSLAVAPTGF 701
Cdd:PHA03307  149 AASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTP---------------------PAAASPRPP 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112  702 YAGSVAISGALASSPAPL---ASGMESAVFDESSGPSSLFATMGSRSTPPQHPPLLSQSRNSGPASPAHqltASPRLSVT 778
Cdd:PHA03307  208 RRSSPISASASSPAPAPGrsaADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWN---GPSSRPGP 284

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112  779 TQGSLPDTSKGELPSDPAFSDPESEAKRRIVFSISVGASSKQSPSTRHSPLTSG---TRGDCVQSHGQDS---------- 845
Cdd:PHA03307  285 ASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGaavSPGPSPSRSPSPSrppppadpss 364

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 568967112  846 RKRSRRKRASAGTPSLSTGVSPKRRALPTVAGLFTQSSGSP 886
Cdd:PHA03307  365 PRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATG 405
 
Name Accession Description Interval E-value
CC_DOT1L cd20902
coiled coil domain of disruptor of telomeric-silencing 1-like (DOT1L) and similar proteins; ...
 242-306 5.64e-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: 124.73  E-value: 5.64e-34
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568967112  242 ALQKLLESFRIQYLQFLAYTKTPQYKANLQQLLDQEKEKNTQLLGTAQQLFGHCQAQKEEIRRLF 306
Cdd:cd20902     1 ALQKLLESFKIQYLQFLAYMKTPQYKASLQQQIEQEKEKNKQLTGKAQQLEKQIQALQKEGVRLL 65
DOT1 pfam08123
Histone methylation protein DOT1; The DOT1 domain regulates gene expression by methylating ...
 9-78 1.63e-31

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: 123.18  E-value: 1.63e-31
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112     9 EVDHQLKERFANMKEGGRIVSSKPFAPLNFRINSRNLSDIGTIMRVVELSPLKGSVSWTGKPVSYYLHTI 78
Cdd:pfam08123  136 ELNLQLKEMLQDLKDGCKIISLKSFVPLNYRINFRNLSDIFNILKVEELKLPEGSVSWTSRGVEYYISTV 205
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
267-420 3.84e-11

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 66.85  E-value: 3.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112  267 KANLQQLLDQEKEKNTQLLGTAQQLfghcQAQKEEIRRLfQQKLDELgvkaltYNDLIQAQKEISAHNQQL---REQSEQ 343
Cdd:COG4372    44 QEELEQLREELEQAREELEQLEEEL----EQARSELEQL-EEELEEL------NEQLQAAQAELAQAQEELeslQEEAEE 112

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568967112  344 LEKDNSELRSQsLRLLRARCEELRLDWSTL--SLENLRKEKQALRSQISEKQRHCLELQISIVELEKTQRQQELLQLKS 420
Cdd:COG4372   113 LQEELEELQKE-RQDLEQQRKQLEAQIAELqsEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLK 190
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 271-420 3.39e-08

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: 58.49  E-value: 3.39e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112   271 QQLLDQEKEKNTQLLGTAQQLfghcqaqKEEIRRLFQQKLDELgVKAL------TYNDLIQAQKEISAHNQ---QLREQS 341
Cdd:TIGR04523  273 QKELEQNNKKIKELEKQLNQL-------KSEISDLNNQKEQDW-NKELkselknQEKKLEEIQNQISQNNKiisQLNEQI 344

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112   342 EQLEKD--NSELRSQSL-RLLRARCEELRL-----DWSTLSLENLRKEKQALRSQIS--EKQRHCLELQISIVELEKTQR 411
Cdd:TIGR04523  345 SQLKKEltNSESENSEKqRELEEKQNEIEKlkkenQSYKQEIKNLESQINDLESKIQnqEKLNQQKDEQIKKLQQEKELL 424


                   ....*....
gi 568967112   412 QQELLQLKS 420
Cdd:TIGR04523  425 EKEIERLKE 433
MscS_porin pfam12795
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...
 235-420 4.09e-06

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: 49.61  E-value: 4.09e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112   235 LVAPTPPALQKLLESFRIQYL-QFLAytktpQYKANLQQLLDQEKEKNTQLLGTAQQLFGhCQAQKEEIRRLFQQKLDEL 313
Cdd:pfam12795   63 LQAKAEAAPKEILASLSLEELeQRLL-----QTSAQLQELQNQLAQLNSQLIELQTRPER-AQQQLSEARQRLQQIRNRL 136

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112   314 GVKALTYNDLIQAQK-EISAHNQQLREQSEQLEKdnsELRSQSLRLLRARceeLRLDWSTLSLENLRKEKQALRSQISEK 392
Cdd:pfam12795  137 NGPAPPGEPLSEAQRwALQAELAALKAQIDMLEQ---ELLSNNNRQDLLK---ARRDLLTLRIQRLEQQLQALQELLNEK 210

                          170       180
                   ....*....|....*....|....*...
gi 568967112   393 QRhclelqisiVELEKTQRQQELLQLKS 420
Cdd:pfam12795  211 RL---------QEAEQAVAQTEQLAEEA 229
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 542-886 2.05e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 46.32  E-value: 2.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112  542 RHLSQDHTGASKAATSEPHPRPEHPKESSLPyqSPGLSNSMKLSPQDPPLASPATSPltsekGSEKGVKERAYSSHGETI 621
Cdd:PHA03307   76 GTEAPANESRSTPTWSLSTLAPASPAREGSP--TPPGPSSPDPPPPTPPPASPPPSP-----APDLSEMLRPVGSPGPPP 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112  622 TSLPVSIPLSTVQPNKLPVSIPLASVVLPSRAERARSTPSPVPQPRDSSAtlekqtgasahgaggagagsrSLAVAPTGF 701
Cdd:PHA03307  149 AASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTP---------------------PAAASPRPP 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112  702 YAGSVAISGALASSPAPL---ASGMESAVFDESSGPSSLFATMGSRSTPPQHPPLLSQSRNSGPASPAHqltASPRLSVT 778
Cdd:PHA03307  208 RRSSPISASASSPAPAPGrsaADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWN---GPSSRPGP 284

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112  779 TQGSLPDTSKGELPSDPAFSDPESEAKRRIVFSISVGASSKQSPSTRHSPLTSG---TRGDCVQSHGQDS---------- 845
Cdd:PHA03307  285 ASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGaavSPGPSPSRSPSPSrppppadpss 364

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 568967112  846 RKRSRRKRASAGTPSLSTGVSPKRRALPTVAGLFTQSSGSP 886
Cdd:PHA03307  365 PRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATG 405
STAT5_CCD cd16855
Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family ...
 243-403 8.34e-04

Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family consists of the coiled-coil (alpha) domain of the STAT5 proteins (Signal Transducer and Activator of Transcription 5, or Signal Transduction And Transcription 5) which include STAT5A and STAT5B, both of which are >90% identical despite being encoded by separate genes. The coiled-coil domain (CCD) of STAT5A and STAT5B appears to be required for constitutive nuclear localization signals (NLS) function; small deletions within the CCD can abrogate nuclear import. Studies show that the CCD binds to the importin-alpha3 NLS adapter in most cells. STAT5A and STAT5B regulate erythropoiesis, lymphopoiesis, and the maintenance of the hematopoietic stem cell population. STAT5A and STAT5B have overlapping and redundant functions; both isoforms can be activated by the same set of cytokines, but some cytokines preferentially activate either STAT5A or STAT5B, e.g. during pregnancy and lactation, STAT5A rather than STAT5B is required for the production of luminal progenitor cells from mammary stem cells and is essential for the differentiation of milk producing alveolar cells during pregnancy. STAT5 has been found to be constitutively phosphorylated in cancer cells, and therefore constantly activated, either by aberrant cell signaling expression or by mutations. It differentially regulates cellular behavior in human mammary carcinoma. Prolactin (PRL) in the prostate gland can induce growth and survival of prostate cancer cells and tissues through the activation of STAT5, its downstream target; PRL expression and STAT5 activation correlates with disease severity. STAT5A and STAT5B are central signaling molecules in leukemias driven by Abelson fusion tyrosine kinases, displaying unique nuclear shuttling mechanisms and having a key role in resistance of leukemic cells against treatment with tyrosine kinase inhibitors (TKI). In addition, STAT5A and STAT5B promote survival of leukemic stem cells. STAT5 is a key transcription factor for IL-3-mediated inhibition of RANKL-induced osteoclastogenesis via the induction of the expression of Id genes. Autosomal recessive STAT5B mutations are associated with severe growth failure, insulin-like growth factor (IGF) deficiency and growth hormone insensitivity (GHI) syndrome. STAT5B deficiency can lead to potentially fatal primary immunodeficiency.


Pssm-ID: 341080 [Multi-domain]  Cd Length: 194  Bit Score: 42.25  E-value: 8.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112  243 LQKLLESFRIQYlQFLayTKtpqYKANLQQLLDQEKEKNTQLLGTAQQlfghcqaQKEEIRRLFQQKLDELGVKALTynd 322
Cdd:cd16855    27 LQQKQESFVIQY-QES--QK---IQAQLQQLQQQPQNERIELEQQLQQ-------QKEQLEQLLNAKAQELLQLRME--- 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112  323 LIQAQKEISAHNQQLreQSEQLEKdnsEL----RSQ-----------SLRLLRARCEELrLD--WSTlslenlrkekqal 385
Cdd:cd16855    91 LADKFKKTIQLLSKL--QSRVLDE---ELiqwkRQQqlagngapfesNLDTIQEWCESL-AEiiWQN------------- 151

                         170
                  ....*....|....*...
gi 568967112  386 RSQISEKQRHCLELQISI 403
Cdd:cd16855   152 RQQIKRAERLKQKLPIPL 169
PRK11281 PRK11281
mechanosensitive channel MscK;
238-415 9.23e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 44.13  E-value: 9.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112  238 PTPPALQKLLESFRIQYLQflaytkTPQYKA---NLQQLL------DQEKEKNTQLLGTAQQLFGHCQAQKEEIRRL--- 305
Cdd:PRK11281   36 PTEADVQAQLDALNKQKLL------EAEDKLvqqDLEQTLalldkiDRQKEETEQLKQQLAQAPAKLRQAQAELEALkdd 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112  306 ----FQQKLDELGVKAL------TYNDLIQAQKEISAHNQQLREQSEQLEKDNSELRSQSLRLlrarcEELRldwstlsl 375
Cdd:PRK11281  110 ndeeTRETLSTLSLRQLesrlaqTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRL-----QQIR-------- 176

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 568967112  376 eNLRKEKQALRSQISEKQRHCLELQISIVELEKTQRQQEL 415
Cdd:PRK11281  177 -NLLKGGKVGGKALRPSQRVLLQAEQALLNAQNDLQRKSL 215
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 300-408 1.64e-03

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: 42.31  E-value: 1.64e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112    300 EEIRRLFQQKLDELGVKALTYNDLIQAqkeISAHNQQLREQSEQLEKDNSELRSQSLRLLRARCEELRLDWSTLS----- 374
Cdd:smart00787  150 DENLEGLKEDYKLLMKELELLNSIKPK---LRDRKDALEEELRQLKQLEDELEDCDPTELDRAKEKLKKLLQEIMikvkk 226

                            90       100       110
                    ....*....|....*....|....*....|....
gi 568967112    375 LENLRKEKQALRSQISEKQRHCLELQISIVELEK 408
Cdd:smart00787  227 LEELEEELQELESKIEDLTNKKSELNTEIAEAEK 260
 
Name Accession Description Interval E-value
CC_DOT1L cd20902
coiled coil domain of disruptor of telomeric-silencing 1-like (DOT1L) and similar proteins; ...
 242-306 5.64e-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: 124.73  E-value: 5.64e-34
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568967112  242 ALQKLLESFRIQYLQFLAYTKTPQYKANLQQLLDQEKEKNTQLLGTAQQLFGHCQAQKEEIRRLF 306
Cdd:cd20902     1 ALQKLLESFKIQYLQFLAYMKTPQYKASLQQQIEQEKEKNKQLTGKAQQLEKQIQALQKEGVRLL 65
DOT1 pfam08123
Histone methylation protein DOT1; The DOT1 domain regulates gene expression by methylating ...
 9-78 1.63e-31

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: 123.18  E-value: 1.63e-31
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112     9 EVDHQLKERFANMKEGGRIVSSKPFAPLNFRINSRNLSDIGTIMRVVELSPLKGSVSWTGKPVSYYLHTI 78
Cdd:pfam08123  136 ELNLQLKEMLQDLKDGCKIISLKSFVPLNYRINFRNLSDIFNILKVEELKLPEGSVSWTSRGVEYYISTV 205
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
267-420 3.84e-11

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 66.85  E-value: 3.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112  267 KANLQQLLDQEKEKNTQLLGTAQQLfghcQAQKEEIRRLfQQKLDELgvkaltYNDLIQAQKEISAHNQQL---REQSEQ 343
Cdd:COG4372    44 QEELEQLREELEQAREELEQLEEEL----EQARSELEQL-EEELEEL------NEQLQAAQAELAQAQEELeslQEEAEE 112

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568967112  344 LEKDNSELRSQsLRLLRARCEELRLDWSTL--SLENLRKEKQALRSQISEKQRHCLELQISIVELEKTQRQQELLQLKS 420
Cdd:COG4372   113 LQEELEELQKE-RQDLEQQRKQLEAQIAELqsEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLK 190
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
267-420 9.96e-10

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 62.23  E-value: 9.96e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112  267 KANLQQLLDQEKEKNTQLLGTAQQLfghcQAQKEEIRRLfQQKLDelgvkaltyndliQAQKEISAHNQQLREQSEQLEK 346
Cdd:COG4372    30 SEQLRKALFELDKLQEELEQLREEL----EQAREELEQL-EEELE-------------QARSELEQLEEELEELNEQLQA 91

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568967112  347 DNSELRS--QSLRLLRARCEELRLDwstlsLENLRKEKQALRSQISEkqrhcLELQISIVELEKTQRQQELLQLKS 420
Cdd:COG4372    92 AQAELAQaqEELESLQEEAEELQEE-----LEELQKERQDLEQQRKQ-----LEAQIAELQSEIAEREEELKELEE 157
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 271-420 3.39e-08

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: 58.49  E-value: 3.39e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112   271 QQLLDQEKEKNTQLLGTAQQLfghcqaqKEEIRRLFQQKLDELgVKAL------TYNDLIQAQKEISAHNQ---QLREQS 341
Cdd:TIGR04523  273 QKELEQNNKKIKELEKQLNQL-------KSEISDLNNQKEQDW-NKELkselknQEKKLEEIQNQISQNNKiisQLNEQI 344

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112   342 EQLEKD--NSELRSQSL-RLLRARCEELRL-----DWSTLSLENLRKEKQALRSQIS--EKQRHCLELQISIVELEKTQR 411
Cdd:TIGR04523  345 SQLKKEltNSESENSEKqRELEEKQNEIEKlkkenQSYKQEIKNLESQINDLESKIQnqEKLNQQKDEQIKKLQQEKELL 424


                   ....*....
gi 568967112   412 QQELLQLKS 420
Cdd:TIGR04523  425 EKEIERLKE 433
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 265-453 1.20e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.48  E-value: 1.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112  265 QYKANLQQLLDQEKEKNTQLLGTAQQLfGHCQAQKEEIRRLFQQKLDELGVKALTYNDLIQAQKEISAHNQQLREQSEQL 344
Cdd:COG1196   313 ELEERLEELEEELAELEEELEELEEEL-EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112  345 EKDNSELRSQSLRLLRARcEELRLDwstlsLENLRKEKQALRSQISEKQRHCLELQISIVELEKTQRQQELLQLKScvpp 424
Cdd:COG1196   392 LRAAAELAAQLEELEEAE-EALLER-----LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL---- 461

                         170       180
                  ....*....|....*....|....*....
gi 568967112  425 dDALSLHLRGKGALGRELEADAGRLRLEL 453
Cdd:COG1196   462 -LELLAELLEEAALLEAALAELLEELAEA 489
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
265-418 2.52e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 55.54  E-value: 2.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112  265 QYKANLQQLLDQEKEKNT------------QLLGTAQQLFGHCQAQKEEIRRL--FQQKLDELGVKALTYNDLIQAQKEI 330
Cdd:COG4717    89 EYAELQEELEELEEELEEleaeleelreelEKLEKLLQLLPLYQELEALEAELaeLPERLEELEERLEELRELEEELEEL 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112  331 SAHNQQLREQSEQLEKDNSELRSQSLRLLRARCEELRLDwstlsLENLRKEKQALRSQISEKQRHCLELQISIVELEKTQ 410
Cdd:COG4717   169 EAELAELQEELEELLEQLSLATEEELQDLAEELEELQQR-----LAELEEELEEAQEELEELEEELEQLENELEAAALEE 243


                  ....*...
gi 568967112  411 RQQELLQL 418
Cdd:COG4717   244 RLKEARLL 251
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 265-419 5.28e-07

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 54.68  E-value: 5.28e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112   265 QYKANLQQLLDQEKEKNTQLLGTAQQLFGhCQAQKEEIRRLFQQKLDELGVKALTYNDLIQAQKEISAHNQQLREQSEQL 344
Cdd:TIGR02168  236 ELREELEELQEELKEAEEELEELTAELQE-LEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANL 314

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568967112   345 EKDNSELRSQSLRLLRARcEELRLDWSTLS--LENLRKEKQALRSQISEKQRHCLELQISIVELEK--TQRQQELLQLK 419
Cdd:TIGR02168  315 ERQLEELEAQLEELESKL-DELAEELAELEekLEELKEELESLEAELEELEAELEELESRLEELEEqlETLRSKVAQLE 392
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 247-420 2.64e-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: 52.33  E-value: 2.64e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112   247 LESFRIQYLQFLAYTKTPQYKANLQQLLDQeKEKNTQLLGTAQQLFGHCQAQKEEIRRLFQQKLDELGVKALTYNDLIQA 326
Cdd:TIGR04523  194 NKLLKLELLLSNLKKKIQKNKSLESQISEL-KKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEK 272

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112   327 QKEISAHNQQLREQSEQLEKDNSELRSqslrlLRARCEElrlDWSTL---SLENLRKEKQALRSQISEKQRHCLEL--QI 401
Cdd:TIGR04523  273 QKELEQNNKKIKELEKQLNQLKSEISD-----LNNQKEQ---DWNKElksELKNQEKKLEEIQNQISQNNKIISQLneQI 344

                          170       180       190
                   ....*....|....*....|....*....|...
gi 568967112   402 SIVELEKT--------------QRQQELLQLKS 420
Cdd:TIGR04523  345 SQLKKELTnsesensekqreleEKQNEIEKLKK 377
MscS_porin pfam12795
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...
 235-420 4.09e-06

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: 49.61  E-value: 4.09e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112   235 LVAPTPPALQKLLESFRIQYL-QFLAytktpQYKANLQQLLDQEKEKNTQLLGTAQQLFGhCQAQKEEIRRLFQQKLDEL 313
Cdd:pfam12795   63 LQAKAEAAPKEILASLSLEELeQRLL-----QTSAQLQELQNQLAQLNSQLIELQTRPER-AQQQLSEARQRLQQIRNRL 136

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112   314 GVKALTYNDLIQAQK-EISAHNQQLREQSEQLEKdnsELRSQSLRLLRARceeLRLDWSTLSLENLRKEKQALRSQISEK 392
Cdd:pfam12795  137 NGPAPPGEPLSEAQRwALQAELAALKAQIDMLEQ---ELLSNNNRQDLLK---ARRDLLTLRIQRLEQQLQALQELLNEK 210

                          170       180
                   ....*....|....*....|....*...
gi 568967112   393 QRhclelqisiVELEKTQRQQELLQLKS 420
Cdd:pfam12795  211 RL---------QEAEQAVAQTEQLAEEA 229
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 265-417 5.09e-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: 51.21  E-value: 5.09e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112   265 QYKANLQQLLDQEKEKNTQL------LGTAQQLFGHCQAQKEEIRRLFQQKLDELGVKALTYNDLIQAQKEISAHNQQLR 338
Cdd:TIGR02168  306 ILRERLANLERQLEELEAQLeeleskLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLR 385

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112   339 EQSEQLEKDNSELRSQsLRLLRARCEELrldwsTLSLENLRKEKQALRSQISEKQRHCLELQISIV--ELEKTQRQQELL 416
Cdd:TIGR02168  386 SKVAQLELQIASLNNE-IERLEARLERL-----EDRRERLQQEIEELLKKLEEAELKELQAELEELeeELEELQEELERL 459


                   .
gi 568967112   417 Q 417
Cdd:TIGR02168  460 E 460
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 249-452 8.23e-06

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: 50.89  E-value: 8.23e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112   249 SFRIQYLQFLAYTKTPQYKANLQQLLDQEKEKNTQLlgtaqQLFGHCQAQKEEIRRLFQQKLDELGVKALTyndLIQAQK 328
Cdd:pfam15921  425 NMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESL-----EKVSSLTAQLESTKEMLRKVVEELTAKKMT---LESSER 496

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112   329 EISAHNQQLREQSEQLEKDNSE---LRSQ----------------SLRLLRARCEELRLDWSTLS--LENLRKEKQALRS 387
Cdd:pfam15921  497 TVSDLTASLQEKERAIEATNAEitkLRSRvdlklqelqhlknegdHLRNVQTECEALKLQMAEKDkvIEILRQQIENMTQ 576

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568967112   388 QISEKQRHCLELQISIVELEK--TQRQQELLQLKscVPPDDalslhlrgKGALGRELEADAGRLRLE 452
Cdd:pfam15921  577 LVGQHGRTAGAMQVEKAQLEKeiNDRRLELQEFK--ILKDK--------KDAKIRELEARVSDLELE 633
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 270-454 1.48e-05

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.06  E-value: 1.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112   270 LQQLLDQEKEKNTQLLGTAQQLFGHCQAQKEEIRRLfQQKLDELGVKALTY--------NDLIQAQKEISAHNQQLREQS 341
Cdd:TIGR02168  773 AEEELAEAEAEIEELEAQIEQLKEELKALREALDEL-RAELTLLNEEAANLrerlesleRRIAATERRLEDLEEQIEELS 851

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112   342 EQLEKDNSELRSQSLRL----------------LRARCEELRLDWSTLS--LENLRKEKQALRSQISEKQrhcleLQISI 403
Cdd:TIGR02168  852 EDIESLAAEIEELEELIeeleseleallnerasLEEALALLRSELEELSeeLRELESKRSELRRELEELR-----EKLAQ 926

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 568967112   404 VELEKTQRQQELLQLKS------CVPPDDALSLHLRGKGALgRELEADAGRLRLELD 454
Cdd:TIGR02168  927 LELRLEGLEVRIDNLQErlseeySLTLEEAEALENKIEDDE-EEARRRLKRLENKIK 982
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
300-422 1.77e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.38  E-value: 1.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112  300 EEIRRLfQQKLDELGVKALTYNDLIQAQKEISAHNQQLREQSEQLEKDNSELRSQ-SLRLLRARCEELR--LDWSTLSLE 376
Cdd:COG4717    71 KELKEL-EEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLlQLLPLYQELEALEaeLAELPERLE 149

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 568967112  377 NLRKEKQA---LRSQISEKQRHCLELQISIVELEKTQRQQELLQLKSCV 422
Cdd:COG4717   150 ELEERLEElreLEEELEELEAELAELQEELEELLEQLSLATEEELQDLA 198
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
304-417 2.18e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 48.75  E-value: 2.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112  304 RLFQQKLDELGVKALTYNDLIQAQKEISAHNQQLREQSEQLEKDNSELRSQSLRLLRARcEEL-----RLDWSTLSLENL 378
Cdd:COG4372    14 SLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQAR-SELeqleeELEELNEQLQAA 92

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 568967112  379 RKEKQALRSQISEKQRHCLELQIsivELEKTQRQQELLQ 417
Cdd:COG4372    93 QAELAQAQEELESLQEEAEELQE---ELEELQKERQDLE 128
flagell_FliJ TIGR02473
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ...
 270-394 2.47e-05

flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly every case, in the midst of other flagellar biosynthesis genes in bacgterial genomes. Typically the fliJ gene is found adjacent to the gene for the flagellum-specific ATPase FliI. Sequence scoring in the gray zone between trusted and noise cutoffs include both probable FliJ proteins and components of bacterial type III secretion systems.


Pssm-ID: 131526 [Multi-domain]  Cd Length: 141  Bit Score: 45.77  E-value: 2.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112   270 LQQLLD---QEKEKNTQLLGTAQQLFGHCQAQkeeIRRLFQQKlDELGVKALTYNDLIQAQKEISAHNQQLReqseQLEK 346
Cdd:TIGR02473    4 LQKLLDlreKEEEQAKLELAKAQAEFERLETQ---LQQLIKYR-EEYEQQALEKVGAGTSALELSNYQRFIR----QLDQ 75

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 568967112   347 DNSELRsQSLRLLRARCEELRLDWSTL-----SLENLrKEKQALRSQISEKQR 394
Cdd:TIGR02473   76 RIQQQQ-QELALLQQEVEAKRERLLEArrelkALEKL-KEKKQKEYRAEEAKR 126
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 270-414 2.59e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 48.22  E-value: 2.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112  270 LQQLLDQEKEKNTQLLGTAQQLfghcqAQKEEIRRLFQQKLDELGVKALTY------------NDLIQAQKEISAHNQQL 337
Cdd:COG4942    95 LRAELEAQKEELAELLRALYRL-----GRQPPLALLLSPEDFLDAVRRLQYlkylaparreqaEELRADLAELAALRAEL 169

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568967112  338 REQSEQLEKDNSELRSQSLRLLRARCEELRLdwstlsLENLRKEKQALRSQISEKQRHCLELQISIVELEKTQRQQE 414
Cdd:COG4942   170 EAERAELEALLAELEEERAALEALKAERQKL------LARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 242-452 2.67e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.16  E-value: 2.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112  242 ALQKLLESFRIQyLQFLAYTktpQYKANLQQLLDQEKEKNTQLLGTAQQLfGHCQAQKEEIRRLFQQKLDELGVKALTYN 321
Cdd:COG1196   217 ELKEELKELEAE-LLLLKLR---ELEAELEELEAELEELEAELEELEAEL-AELEAELEELRLELEELELELEEAQAEEY 291

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112  322 DLIQAQKEISAHNQQLREQSEQLEKDNSELRSQsLRLLRARCEEL--RLDWSTLSLENLRKEKQALRSQISEKQRHCLEL 399
Cdd:COG1196   292 ELLAELARLEQDIARLEERRRELEERLEELEEE-LAELEEELEELeeELEELEEELEEAEEELEEAEAELAEAEEALLEA 370

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568967112  400 QISIVELEKT--QRQQELLQLKScvppdDALSLHLRGKGALGRELEADAGRLRLE 452
Cdd:COG1196   371 EAELAEAEEEleELAEELLEALR-----AAAELAAQLEELEEAEEALLERLERLE 420
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 259-453 2.75e-05

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: 48.91  E-value: 2.75e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112   259 AYTKTPQYKANLQQLLDQEKEKNTQLLGtaqqlfghCQAQKEEIRRLFQQKLDELGVkaltyndliqAQKEISAhnqqLR 338
Cdd:TIGR02169  665 GILFSRSEPAELQRLRERLEGLKRELSS--------LQSELRRIENRLDELSQELSD----------ASRKIGE----IE 722

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112   339 EQSEQLEKDnselrsqsLRLLRARCEELRLDWSTLS--LENLRKEKQALRSQISEKQRHCLELQISIVELEKTQRQQELL 416
Cdd:TIGR02169  723 KEIEQLEQE--------EEKLKERLEELEEDLSSLEqeIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIP 794

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 568967112   417 QLkscvppDDALS----LHLRGKGALgRELEADAGRLRLEL 453
Cdd:TIGR02169  795 EI------QAELSkleeEVSRIEARL-REIEQKLNRLTLEK 828
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 265-443 5.67e-05

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: 47.81  E-value: 5.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112   265 QYKANLQQLLDQEKEKnTQLLGTAQQLFgHC------------QAQKEEIRRL------FQQKLDELGVKALTYNDLIQ- 325
Cdd:pfam05557   80 LKKKYLEALNKKLNEK-ESQLADAREVI-SClknelselrrqiQRAELELQSTnseleeLQERLDLLKAKASEAEQLRQn 157

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112   326 ---AQKEISAHNQQLRE----------QSEQLEKDNSELRS-----QSLRLLRARCEELRLDWSTLSLenLRKEKQALRS 387
Cdd:pfam05557  158 lekQQSSLAEAEQRIKElefeiqsqeqDSEIVKNSKSELARipeleKELERLREHNKHLNENIENKLL--LKEEVEDLKR 235

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 568967112   388 QIS--EKQRHclelQISIVELEKTQRQQEllqLKSCVPPDDALSLHLRGKGALGRELE 443
Cdd:pfam05557  236 KLEreEKYRE----EAATLELEKEKLEQE---LQSWVKLAQDTGLNLRSPEDLSRRIE 286
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 296-464 7.73e-05

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.36  E-value: 7.73e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112   296 QAQKEE-IRRLF--QQKLDELgvkaltyNDLIqaqKEISAHNQQLREQSEQLEKdnselrsqsLRLLRARCEELRLDWST 372
Cdd:TIGR02168  171 KERRKEtERKLErtRENLDRL-------EDIL---NELERQLKSLERQAEKAER---------YKELKAELRELELALLV 231

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112   373 LSLENLRKEKQALRSQISEKQRHCLELQisiveLEKTQRQQELLQLKSCVPPDDALSLHLRGK----GALGRELEADAGR 448
Cdd:TIGR02168  232 LRLEELREELEELQEELKEAEEELEELT-----AELQELEEKLEELRLEVSELEEEIEELQKElyalANEISRLEQQKQI 306

                          170
                   ....*....|....*.
gi 568967112   449 LRLELDCAKISLPHLS 464
Cdd:TIGR02168  307 LRERLANLERQLEELE 322
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
268-417 9.41e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.07  E-value: 9.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112  268 ANLQQLLDQEKEKNTQLLgtaqqlfghCQAQKEEIRRLFQQK----LDELGVKALTYNDLIQAQKEISAHNQQLREQSEQ 343
Cdd:COG4717   347 EELQELLREAEELEEELQ---------LEELEQEIAALLAEAgvedEEELRAALEQAEEYQELKEELEELEEQLEELLGE 417

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568967112  344 LEkdnSELRSQSLRLLRARceelrldwstlsLENLRKEKQALRSQISEKQRHCLELQISIVELEKTQRQQELLQ 417
Cdd:COG4717   418 LE---ELLEALDEEELEEE------------LEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQ 476
MscS_porin pfam12795
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...
 267-419 9.52e-05

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: 45.76  E-value: 9.52e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112   267 KANLQQLLDQEKEKNTQLLGTAQQLFGHCQAQKEEIRRL-------------FQQKLDELGVKA-------LTYNDLIQA 326
Cdd:pfam12795    4 ELEKAKLDEAAKKKLLQDLQQALSLLDKIDASKQRAAAYqkalddapaelreLRQELAALQAKAeaapkeiLASLSLEEL 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112   327 QKEISAHNQQLREQSEQLEKDNSELRSQSLRLLRARCE-----------ELRLDWSTLSLENLRK--------EKQALRS 387
Cdd:pfam12795   84 EQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQlsearqrlqqiRNRLNGPAPPGEPLSEaqrwalqaELAALKA 163

                          170       180       190
                   ....*....|....*....|....*....|..
gi 568967112   388 QISEKQrhcLELQISIVELEKTQRQQELLQLK 419
Cdd:pfam12795  164 QIDMLE---QELLSNNNRQDLLKARRDLLTLR 192
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 276-460 1.25e-04

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 46.71  E-value: 1.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112   276 QEKEKNTQLL----GTAQQLFGHCQAQKEEIRRLFQQKLDELgvKALtyndLIQAQKEISAHNQQLREQSEqLEKDNSEL 351
Cdd:pfam01576  204 QELEKAKRKLegesTDLQEQIAELQAQIAELRAQLAKKEEEL--QAA----LARLEEETAQKNNALKKIRE-LEAQISEL 276

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112   352 RS--QSLRLLRARCEELRLDwstlslenLRKEKQALRSQISEKQRHCLELQisivELeKTQRQQELLQLKSCVPPD---- 425
Cdd:pfam01576  277 QEdlESERAARNKAEKQRRD--------LGEELEALKTELEDTLDTTAAQQ----EL-RSKREQEVTELKKALEEEtrsh 343

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 568967112   426 DALSLHLRGKGA-----LGRELEaDAGRLRLELDCAKISL 460
Cdd:pfam01576  344 EAQLQEMRQKHTqaleeLTEQLE-QAKRNKANLEKAKQAL 382
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 267-420 1.31e-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: 1.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112   267 KANLQQLLDQEKEKNTQLLGTAQQLfghcQAQKE----EIRRLFQQKLD----------ELGVKALTYNDLiqaQKEISA 332
Cdd:TIGR04523  393 INDLESKIQNQEKLNQQKDEQIKKL----QQEKEllekEIERLKETIIKnnseikdltnQDSVKELIIKNL---DNTRES 465

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112   333 HNQQLREQSEQLEKDNSELRSQSlrllrarcEELRLDwsTLSLENLRKEKQALRSQISE--KQRHCLELQISIVELEKTQ 410
Cdd:TIGR04523  466 LETQLKVLSRSINKIKQNLEQKQ--------KELKSK--EKELKKLNEEKKELEEKVKDltKKISSLKEKIEKLESEKKE 535

                          170
                   ....*....|
gi 568967112   411 RQQELLQLKS 420
Cdd:TIGR04523  536 KESKISDLED 545
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
247-391 1.36e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 46.30  E-value: 1.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112  247 LESFRIQYLQFLAYTKTPQYKANLQQLLDQEKEKNTQLLGTAQQlfghcQAQKEEIRRLfQQKLDELgvkaltYNDLIQA 326
Cdd:COG4717   384 EEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE-----EELEEELEEL-EEELEEL------EEELEEL 451

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568967112  327 QKEISAHNQQLreqsEQLEKDN--SELRsQSLRLLRARCEELRLDWSTLSL---------ENLRKEKQ-ALRSQISE 391
Cdd:COG4717   452 REELAELEAEL----EQLEEDGelAELL-QELEELKAELRELAEEWAALKLalelleearEEYREERLpPVLERASE 523
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 542-886 2.05e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 46.32  E-value: 2.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112  542 RHLSQDHTGASKAATSEPHPRPEHPKESSLPyqSPGLSNSMKLSPQDPPLASPATSPltsekGSEKGVKERAYSSHGETI 621
Cdd:PHA03307   76 GTEAPANESRSTPTWSLSTLAPASPAREGSP--TPPGPSSPDPPPPTPPPASPPPSP-----APDLSEMLRPVGSPGPPP 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112  622 TSLPVSIPLSTVQPNKLPVSIPLASVVLPSRAERARSTPSPVPQPRDSSAtlekqtgasahgaggagagsrSLAVAPTGF 701
Cdd:PHA03307  149 AASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTP---------------------PAAASPRPP 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112  702 YAGSVAISGALASSPAPL---ASGMESAVFDESSGPSSLFATMGSRSTPPQHPPLLSQSRNSGPASPAHqltASPRLSVT 778
Cdd:PHA03307  208 RRSSPISASASSPAPAPGrsaADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWN---GPSSRPGP 284

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112  779 TQGSLPDTSKGELPSDPAFSDPESEAKRRIVFSISVGASSKQSPSTRHSPLTSG---TRGDCVQSHGQDS---------- 845
Cdd:PHA03307  285 ASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGaavSPGPSPSRSPSPSrppppadpss 364

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 568967112  846 RKRSRRKRASAGTPSLSTGVSPKRRALPTVAGLFTQSSGSP 886
Cdd:PHA03307  365 PRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATG 405
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 259-453 3.88e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.05  E-value: 3.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112   259 AYTKTPQYKANLQQLLDQEKEKNTQLLGTAQQLFGH---CQAQKEEIRRLFQQKLDELGVKALTYNDLIQAQKEISAH-- 333
Cdd:TIGR02168  703 LRKELEELEEELEQLRKELEELSRQISALRKDLARLeaeVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAea 782

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112   334 ---------------NQQLREQSEQLEKDNSELRS--QSLRLLRARCEELRLDWSTL------SLENLRKEKQALRSQIS 390
Cdd:TIGR02168  783 eieeleaqieqlkeeLKALREALDELRAELTLLNEeaANLRERLESLERRIAATERRledleeQIEELSEDIESLAAEIE 862

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568967112   391 EKQRHCLELQISIVEL--EKTQRQQELLQLKSCVppdDALSLHLRGKGALGRELEADAGRLRLEL 453
Cdd:TIGR02168  863 ELEELIEELESELEALlnERASLEEALALLRSEL---EELSEELRELESKRSELRRELEELREKL 924
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 274-420 4.89e-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: 44.63  E-value: 4.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112   274 LDQEKEKNTQLlgtaQQLFghcqaqKEEIRRLfQQKLDELGVKaltYNDLIQAQKEISAHNQQLREQSEQLEKDNSELRS 353
Cdd:TIGR04523  129 LEKQKKENKKN----IDKF------LTEIKKK-EKELEKLNNK---YNDLKKQKEELENELNLLEKEKLNIQKNIDKIKN 194

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568967112   354 QSLRLlrarceELRLdwstLSLENLRKEKQALRSQISEkqrhcLELQISIVELEKTQRQQELLQLKS 420
Cdd:TIGR04523  195 KLLKL------ELLL----SNLKKKIQKNKSLESQISE-----LKKQNNQLKDNIEKKQQEINEKTT 246
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
272-454 5.30e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.91  E-value: 5.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112  272 QLLDQEKEKNTQLLGTAQQLFGHCQAQKEEIRRLFQQKLDELgvkaltynDLIQAQKEISAHNQQLreqsEQLEKDNSEL 351
Cdd:COG4913   620 AELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEI--------DVASAEREIAELEAEL----ERLDASSDDL 687

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112  352 RSqslrllrarceelrldwstlslenLRKEKQALRSQIS--EKQRHCLELQISIVELEKTQRQQELLQLKSCV---PPDD 426
Cdd:COG4913   688 AA------------------------LEEQLEELEAELEelEEELDELKGEIGRLEKELEQAEEELDELQDRLeaaEDLA 743

                         170       180
                  ....*....|....*....|....*....
gi 568967112  427 ALSLHLRGKGALGREL-EADAGRLRLELD 454
Cdd:COG4913   744 RLELRALLEERFAAALgDAVERELRENLE 772
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 272-417 7.81e-04

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: 41.84  E-value: 7.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112   272 QLLDQE---KEKNTQLLGTAQQLFGHCQAQKEEIRRLFQQKLDELGVKALTYN-DLIQAQKEISAHNQQLREQSEQLEKD 347
Cdd:pfam08614   11 RLLDRTallEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQLReELAELYRSRGELAQRLVDLNEELQEL 90

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568967112   348 NSELRSQS--LRLLRARCEEL--RLDWSTLSLENLRKEKQALRSQISEkqrhcLELQISIVE--LEKTQRQ-QELLQ 417
Cdd:pfam08614   91 EKKLREDErrLAALEAERAQLeeKLKDREEELREKRKLNQDLQDELVA-----LQLQLNMAEekLRKLEKEnRELVE 162
STAT5_CCD cd16855
Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family ...
 243-403 8.34e-04

Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family consists of the coiled-coil (alpha) domain of the STAT5 proteins (Signal Transducer and Activator of Transcription 5, or Signal Transduction And Transcription 5) which include STAT5A and STAT5B, both of which are >90% identical despite being encoded by separate genes. The coiled-coil domain (CCD) of STAT5A and STAT5B appears to be required for constitutive nuclear localization signals (NLS) function; small deletions within the CCD can abrogate nuclear import. Studies show that the CCD binds to the importin-alpha3 NLS adapter in most cells. STAT5A and STAT5B regulate erythropoiesis, lymphopoiesis, and the maintenance of the hematopoietic stem cell population. STAT5A and STAT5B have overlapping and redundant functions; both isoforms can be activated by the same set of cytokines, but some cytokines preferentially activate either STAT5A or STAT5B, e.g. during pregnancy and lactation, STAT5A rather than STAT5B is required for the production of luminal progenitor cells from mammary stem cells and is essential for the differentiation of milk producing alveolar cells during pregnancy. STAT5 has been found to be constitutively phosphorylated in cancer cells, and therefore constantly activated, either by aberrant cell signaling expression or by mutations. It differentially regulates cellular behavior in human mammary carcinoma. Prolactin (PRL) in the prostate gland can induce growth and survival of prostate cancer cells and tissues through the activation of STAT5, its downstream target; PRL expression and STAT5 activation correlates with disease severity. STAT5A and STAT5B are central signaling molecules in leukemias driven by Abelson fusion tyrosine kinases, displaying unique nuclear shuttling mechanisms and having a key role in resistance of leukemic cells against treatment with tyrosine kinase inhibitors (TKI). In addition, STAT5A and STAT5B promote survival of leukemic stem cells. STAT5 is a key transcription factor for IL-3-mediated inhibition of RANKL-induced osteoclastogenesis via the induction of the expression of Id genes. Autosomal recessive STAT5B mutations are associated with severe growth failure, insulin-like growth factor (IGF) deficiency and growth hormone insensitivity (GHI) syndrome. STAT5B deficiency can lead to potentially fatal primary immunodeficiency.


Pssm-ID: 341080 [Multi-domain]  Cd Length: 194  Bit Score: 42.25  E-value: 8.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112  243 LQKLLESFRIQYlQFLayTKtpqYKANLQQLLDQEKEKNTQLLGTAQQlfghcqaQKEEIRRLFQQKLDELGVKALTynd 322
Cdd:cd16855    27 LQQKQESFVIQY-QES--QK---IQAQLQQLQQQPQNERIELEQQLQQ-------QKEQLEQLLNAKAQELLQLRME--- 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112  323 LIQAQKEISAHNQQLreQSEQLEKdnsEL----RSQ-----------SLRLLRARCEELrLD--WSTlslenlrkekqal 385
Cdd:cd16855    91 LADKFKKTIQLLSKL--QSRVLDE---ELiqwkRQQqlagngapfesNLDTIQEWCESL-AEiiWQN------------- 151

                         170
                  ....*....|....*...
gi 568967112  386 RSQISEKQRHCLELQISI 403
Cdd:cd16855   152 RQQIKRAERLKQKLPIPL 169
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 257-470 8.43e-04

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: 44.19  E-value: 8.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112   257 FLAYTKTPQYKANLQQLLDQEKEKNTQLLGTAQQLFGHCQAQKEEIRRLFQ--QKLDELGVKAL-------TYNDLIQAQ 327
Cdd:TIGR00618  465 AQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNParQDIDNPGPLTRrmqrgeqTYAQLETSE 544

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112   328 KEISAHNQQLREQSEQLEKDNSELRSQSLRLLRARCEelrldwSTLSLENLRKEKQALRSQIS-----------EKQRHC 396
Cdd:TIGR00618  545 EDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNR------SKEDIPNLQNITVRLQDLTEklseaedmlacEQHALL 618

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112   397 LELQISIVELEKTQRQQEL---LQLKSCVPPDDALSL---HLRGKGALGRELEADAGRLR-LELDCAKISLPHLSSMSPE 469
Cdd:TIGR00618  619 RKLQPEQDLQDVRLHLQQCsqeLALKLTALHALQLTLtqeRVREHALSIRVLPKELLASRqLALQKMQSEKEQLTYWKEM 698


                   .
gi 568967112   470 L 470
Cdd:TIGR00618  699 L 699
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 265-417 9.21e-04

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: 43.73  E-value: 9.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112   265 QYKANLQQLLDqEKEKNTQLLGTAQQLFGHCQAQKEEIRRL------FQQKLDELG--------VKALTYNDLIQAQKEI 330
Cdd:pfam07888  203 QRDTQVLQLQD-TITTLTQKLTTAHRKEAENEALLEELRSLqerlnaSERKVEGLGeelssmaaQRDRTQAELHQARLQA 281

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112   331 SAHNQQL-------RE-------------QSEQLEKDNSELRSQSLRLLRARCEELRLDWSTLSLEnLRKEKQALRSQIS 390
Cdd:pfam07888  282 AQLTLQLadaslalREgrarwaqeretlqQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVE-LGREKDCNRVQLS 360

                          170       180       190
                   ....*....|....*....|....*....|..
gi 568967112   391 EKQRHCLELQISIVELEKTQRQ-----QELLQ 417
Cdd:pfam07888  361 ESRRELQELKASLRVAQKEKEQlqaekQELLE 392
PRK11281 PRK11281
mechanosensitive channel MscK;
238-415 9.23e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 44.13  E-value: 9.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112  238 PTPPALQKLLESFRIQYLQflaytkTPQYKA---NLQQLL------DQEKEKNTQLLGTAQQLFGHCQAQKEEIRRL--- 305
Cdd:PRK11281   36 PTEADVQAQLDALNKQKLL------EAEDKLvqqDLEQTLalldkiDRQKEETEQLKQQLAQAPAKLRQAQAELEALkdd 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112  306 ----FQQKLDELGVKAL------TYNDLIQAQKEISAHNQQLREQSEQLEKDNSELRSQSLRLlrarcEELRldwstlsl 375
Cdd:PRK11281  110 ndeeTRETLSTLSLRQLesrlaqTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRL-----QQIR-------- 176

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 568967112  376 eNLRKEKQALRSQISEKQRHCLELQISIVELEKTQRQQEL 415
Cdd:PRK11281  177 -NLLKGGKVGGKALRPSQRVLLQAEQALLNAQNDLQRKSL 215
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 499-888 1.01e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 44.01  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112  499 ASPLDQEVVPCTPSHSGRPRLEKLSGLALPDYTRLSPAKIVLRRHLSQDHTGASKAATSEPHPRPEHPKESSLPYQSPGL 578
Cdd:PHA03307   59 AAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEML 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112  579 SNSMKLSPQDPPLASPATSPLTSEKGSEKgvkeraysshgetiTSLPVSIPLSTVQPNKLPVSIPLASVvlPSRAERARS 658
Cdd:PHA03307  139 RPVGSPGPPPAASPPAAGASPAAVASDAA--------------SSRQAALPLSSPEETARAPSSPPAEP--PPSTPPAAA 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112  659 TPSPVPQPRDSSATLEKQTGASAHGAGGAGAGSRSLAVAPTGFYAGSVAISGALASSPAPLASGMESAVFDESSGPSSLF 738
Cdd:PHA03307  203 SPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRP 282

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112  739 ATMGSRSTPPQHPPLLSQSRNSGPASPAHQLTASPRLSVTTQGSLPDTSKGELPSDPAFSDPESEAKRRivfSISVGASS 818
Cdd:PHA03307  283 GPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSP---SPSRPPPP 359

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112  819 KQSPSTRHSPLTSGTRGDCVQSHGQDSRKRSRRKRASAGTPSLSTGVSPKRRALPTVAGLFTQSSGSPLN 888
Cdd:PHA03307  360 ADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATGRFPAGRPRPSPLDAGAASGAFYAR 429
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 261-505 1.10e-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: 43.80  E-value: 1.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112   261 TKTPQYKanlqQLLDQEKEKNTQLLGTAQQLFGHCQAQKEEIRRLFQQKLDELGVKALTYNDLIQAQKEISAHNQQLREQ 340
Cdd:TIGR00618  173 FPLDQYT----QLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQK 248

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112   341 SEQLEKDNSelRSQSLRLLRARCEELRLDWSTLSLENLRKEKQALRSQISEKQRHCL-----------ELQISIVELEKT 409
Cdd:TIGR00618  249 REAQEEQLK--KQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTqieqqaqrihtELQSKMRSRAKL 326

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112   410 --QRQQELLQLKSCVPPDDALSLHLRGKGALGRELEADAGRlRLELDCAKISLPHLSSMSPELSmnghaASYELCNAASR 487
Cdd:TIGR00618  327 lmKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSI-REISCQQHTLTQHIHTLQQQKT-----TLTQKLQSLCK 400

                          250
                   ....*....|....*...
gi 568967112   488 PSSKQNTPQYLASPLDQE 505
Cdd:TIGR00618  401 ELDILQREQATIDTRTSA 418
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 265-420 1.34e-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: 1.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112   265 QYKANLQQLLDQEKEKNTQLlgtaqqlfghcQAQKEEIrrlfQQKLDELGVKALTYNDLIQAQKEISAHNQQLREQSEQL 344
Cdd:TIGR04523  381 SYKQEIKNLESQINDLESKI-----------QNQEKLN----QQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDL 445

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112   345 EKDNSELRsqslrllrarceelrldwstLSLENLRKEKQALRSQISEkqrhcLELQISIVE--LEKTQRQ-----QELLQ 417
Cdd:TIGR04523  446 TNQDSVKE--------------------LIIKNLDNTRESLETQLKV-----LSRSINKIKqnLEQKQKElkskeKELKK 500


                   ...
gi 568967112   418 LKS 420
Cdd:TIGR04523  501 LNE 503
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 271-419 1.42e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 42.60  E-value: 1.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112   271 QQLLDQEKEKNTQLLGTAQQLFGHCQAQKEEIR-RLFQQKLDELGVKaltyNDLIQAQKEI-------SAHNQQLREQSE 342
Cdd:pfam13868  175 REEIEEEKEREIARLRAQQEKAQDEKAERDELRaKLYQEEQERKERQ----KEREEAEKKArqrqelqQAREEQIELKER 250

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112   343 QLEKDNSELRSQSLRLLRARCEELRLDwstlsLENLRKEKQ-------ALRSQISEKQRHCL-ELQISIVELEKTQRQQE 414
Cdd:pfam13868  251 RLAEEAEREEEEFERMLRKQAEDEEIE-----QEEAEKRRMkrlehrrELEKQIEEREEQRAaEREEELEEGERLREEEA 325


                   ....*
gi 568967112   415 LLQLK 419
Cdd:pfam13868  326 ERRER 330
PRK10246 PRK10246
exonuclease subunit SbcC; Provisional
 258-417 1.55e-03

exonuclease subunit SbcC; Provisional


Pssm-ID: 182330 [Multi-domain]  Cd Length: 1047  Bit Score: 43.25  E-value: 1.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112  258 LAYTKTPQYKANLQQLLDQEKEKNTQLLGTAQQL------FGHCQAQKEEIRRLFQQKLDELGVKALTYNDLIQAQKEIS 331
Cdd:PRK10246  280 LAALSLAQPARQLRPHWERIQEQSAALAHTRQQIeevntrLQSTMALRARIRHHAAKQSAELQAQQQSLNTWLAEHDRFR 359

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112  332 AHNQQL---REQSEQLEKDNSELRSQSLRLLRARCEELRLDWSTLSL---------------ENLRKEKQALRSQISEKQ 393
Cdd:PRK10246  360 QWNNELagwRAQFSQQTSDREQLRQWQQQLTHAEQKLNALPAITLTLtadevaaalaqhaeqRPLRQRLVALHGQIVPQQ 439

                         170       180
                  ....*....|....*....|....*.
gi 568967112  394 RHCLELQISIVEL--EKTQRQQELLQ 417
Cdd:PRK10246  440 KRLAQLQVAIQNVtqEQTQRNAALNE 465
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 300-408 1.64e-03

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: 42.31  E-value: 1.64e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112    300 EEIRRLFQQKLDELGVKALTYNDLIQAqkeISAHNQQLREQSEQLEKDNSELRSQSLRLLRARCEELRLDWSTLS----- 374
Cdd:smart00787  150 DENLEGLKEDYKLLMKELELLNSIKPK---LRDRKDALEEELRQLKQLEDELEDCDPTELDRAKEKLKKLLQEIMikvkk 226

                            90       100       110
                    ....*....|....*....|....*....|....
gi 568967112    375 LENLRKEKQALRSQISEKQRHCLELQISIVELEK 408
Cdd:smart00787  227 LEELEEELQELESKIEDLTNKKSELNTEIAEAEK 260
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 324-463 2.01e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 42.85  E-value: 2.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112   324 IQAQKEISAHNQQLREQSEQLEKDNSELRSQSLRLL-----RARCEElRLDWSTLSLENLRKEKQALRSQISEKQRHCLE 398
Cdd:pfam01576  457 IKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRqledeRNSLQE-QLEEEEEAKRNVERQLSTLQAQLSDMKKKLEE 535

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568967112   399 LQISIVELEKTQR--QQELlqlkscvppdDALSLHLRGKGALGRELEADAGRLRLELDCAKISLPHL 463
Cdd:pfam01576  536 DAGTLEALEEGKKrlQREL----------EALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQ 592
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 270-391 2.04e-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: 43.02  E-value: 2.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112  270 LQQLLDQEKEKNTQLLGTAQQLFGHCQAQKEEIRrlfqQKLDELGVKALTYndlIQAQKEIsahnQQLREQSEQLEKDNS 349
Cdd:COG3096   558 LLAELEAQLEELEEQAAEAVEQRSELRQQLEQLR----ARIKELAARAPAW---LAAQDAL----ERLREQSGEALADSQ 626

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 568967112  350 ELRSQSLRLLRarceelRLDWSTLSLENLRKEKQALRSQISE 391
Cdd:COG3096   627 EVTAAMQQLLE------REREATVERDELAARKQALESQIER 662
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 289-419 2.04e-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: 42.75  E-value: 2.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112   289 QQLFGHCQAQKEEIRRLfQQKLDELGVK--ALTYnDLIQAQKEIsahnQQLREQSEQLEkDNSELRSQSLRLLRARCEEL 366
Cdd:TIGR02169  794 PEIQAELSKLEEEVSRI-EARLREIEQKlnRLTL-EKEYLEKEI----QELQEQRIDLK-EQIKSIEKEIENLNGKKEEL 866

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 568967112   367 --RLDWSTLSLENLRKEKQALRSQISEKQRHCLELQISIVELEkTQRQQELLQLK 419
Cdd:TIGR02169  867 eeELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELE-AQIEKKRKRLS 920
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
242-454 3.29e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 3.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112  242 ALQKLLESFRIQYlqflaYTKTPQYKANLQQLLDQEKEKntqllgtAQQLFGHCQAQKEE--IRRLF-QQKLDELGVKAL 318
Cdd:COG4913   159 ALKARLKKQGVEF-----FDSFSAYLARLRRRLGIGSEK-------ALRLLHKTQSFKPIgdLDDFVrEYMLEEPDTFEA 226

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112  319 -------------TYNDLIQAQK------EISAHNQQLREQSEQLEKdNSELRS--------QSLRLLRARCEELRLDWS 371
Cdd:COG4913   227 adalvehfddlerAHEALEDAREqiellePIRELAERYAAARERLAE-LEYLRAalrlwfaqRRLELLEAELEELRAELA 305

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112  372 TL---------SLENLRKEKQALRSQISE-----KQRhcLELQISIVELEKTQRQQELLQLKSCV------PPDDA---L 428
Cdd:COG4913   306 RLeaelerleaRLDALREELDELEAQIRGnggdrLEQ--LEREIERLERELEERERRRARLEALLaalglpLPASAeefA 383

                         250       260
                  ....*....|....*....|....*.
gi 568967112  429 SLHLRGKGALgRELEADAGRLRLELD 454
Cdd:COG4913   384 ALRAEAAALL-EALEEELEALEEALA 408
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 270-400 3.85e-03

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


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 41.60  E-value: 3.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112   270 LQQLLDQEKEKNTQLLGTAQQLFGHCQAQKEEIRRLfQQKLDELGVKAltynDLIQAQK-EISAhnqqLREQSEQLEK-- 346
Cdd:pfam05622   64 LQKQLEQLQEENFRLETARDDYRIKCEELEKEVLEL-QHRNEELTSLA----EEAQALKdEMDI----LRESSDKVKKle 134

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568967112   347 -----------DNSELRSQsLRLLrarcEELRLDW--STLSLENLRKEKQALRSQISEKQRHCLELQ 400
Cdd:pfam05622  135 atvetykkkleDLGDLRRQ-VKLL----EERNAEYmqRTLQLEEELKKANALRGQLETYKRQVQELH 196
CENP-F_leu_zip pfam10473
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ...
 325-419 7.39e-03

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: 38.43  E-value: 7.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112   325 QAQKEISAHNQ-QLREQSEQLEKDNSELRSQsLRLLRARCEELRLDwstlsLENLRKEKQALRSQISEKQRHCLELQISI 403
Cdd:pfam10473   30 ERELEMSEENQeLAILEAENSKAEVETLKAE-IEEMAQNLRDLELD-----LVTLRSEKENLTKELQKKQERVSELESLN 103

                           90
                   ....*....|....*...
gi 568967112   404 VELEK--TQRQQELLQLK 419
Cdd:pfam10473  104 SSLENllEEKEQEKVQMK 121
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
 299-400 7.70e-03

TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.


Pssm-ID: 462316 [Multi-domain]  Cd Length: 129  Bit Score: 38.00  E-value: 7.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112   299 KEEIRRLfQQKLDELGVKALTYNDLIQAQKEISAHNQQ------------------LREQSEQLEKDNSELRSQsLRLLR 360
Cdd:pfam07926    7 QSEIKRL-KEEAADAEAQLQKLQEDLEKQAEIAREAQQnyerelvlhaedikalqaLREELNELKAEIAELKAE-AESAK 84

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 568967112   361 ARCEELRLDWStlslenlrKEKQALRSQISEKQRHCLELQ 400
Cdd:pfam07926   85 AELEESEESWE--------EQKKELEKELSELEKRIEDLN 116
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
 264-414 8.26e-03

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 40.81  E-value: 8.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112  264 PQYKANLQQLLDQEKEK-------------NTQLLGTAQQLFghcqaqkeEIRRLFQQKLDELGVKALTYNDLIQAQKEI 330
Cdd:PRK10929   78 PKLSAELRQQLNNERDEprsvppnmstdalEQEILQVSSQLL--------EKSRQAQQEQDRAREISDSLSQLPQQQTEA 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112  331 sahNQQLREQSEQL-----------EKDNSELRSQSLRLlRARCEELRLdwSTLSLENlRKEKQALRSQISEKQRHCLEL 399
Cdd:PRK10929  150 ---RRQLNEIERRLqtlgtpntplaQAQLTALQAESAAL-KALVDELEL--AQLSANN-RQELARLRSELAKKRSQQLDA 222

                         170
                  ....*....|....*.
gi 568967112  400 QISIVE-LEKTQRQQE 414
Cdd:PRK10929  223 YLQALRnQLNSQRQRE 238
CENP-F_leu_zip pfam10473
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ...
 326-406 9.29e-03

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: 38.05  E-value: 9.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112   326 AQKEISAHNQQLREQSE---QLEKDNSELRS------QSLRLLRARCEELrlDWSTLSLENLRKEKQALRSQISEKQRHC 396
Cdd:pfam10473   50 SKAEVETLKAEIEEMAQnlrDLELDLVTLRSekenltKELQKKQERVSEL--ESLNSSLENLLEEKEQEKVQMKEESKTA 127

                           90
                   ....*....|.
gi 568967112   397 LE-LQISIVEL 406
Cdd:pfam10473  128 VEmLQTQLKEL 138
HAP1_N pfam04849
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ...
 264-413 1.00e-02

HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.


Pssm-ID: 461455 [Multi-domain]  Cd Length: 309  Bit Score: 40.01  E-value: 1.00e-02
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112   264 PQYKAnLQQLLDQEKEKNTQLLGTAQQLFGHCQAQKEEirrlfQQKLdelgvkaltyndLIQAQKEISAHNQQLREQSEQ 343
Cdd:pfam04849  164 VQLDA-LQEKLRGLEEENLKLRSEASHLKTETDTYEEK-----EQQL------------MSDCVEQLSEANQQMAELSEE 225

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967112   344 LEKDNSELRSQ-----SLRL----LRARCEELRLDWSTLSLE-NLRKEKQ-ALRSQISE-KQRH--CLELQISIVELEKT 409
Cdd:pfam04849  226 LARKMEENLRQqeeitSLLAqivdLQHKCKELGIENEELQQHlQASKEAQrQLTSELQElQDRYaeCLGMLHEAQEELKE 305


                   ....
gi 568967112   410 QRQQ 413
Cdd:pfam04849  306 LRKK 309
 
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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