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Conserved domains on  [gi|1720360855|ref|XP_030100834|]
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histone-lysine N-methyltransferase, H3 lysine-79 specific isoform X3 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AdoMet_MTases super family cl17173
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 2-101 1.86e-47

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: 169.02  E-value: 1.86e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855    2 LERGDFLSEEWRERI-ANTSVIFVNNFAFGPEVDHQLKERFANMKEGGRIVSSKPFAPLNFRINSRNLSDIGTIMRVVEL 80
Cdd:pfam08123  105 FIRGSFLDNERVEEIiPEADVILVNNFAFDPELNLQLKEMLQDLKDGCKIISLKSFVPLNYRINFRNLSDIFNILKVEEL 184

                           90       100
                   ....*....|....*....|.
gi 1720360855   81 SPLKGSVSWTGKPVSYYLHTI 101
Cdd:pfam08123  185 KLPEGSVSWTSRGVEYYISTV 205
CC_DOT1L cd20902
coiled coil domain of disruptor of telomeric-silencing 1-like (DOT1L) and similar proteins; ...
 265-329 3.56e-34

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


:

Pssm-ID: 411016 [Multi-domain]  Cd Length: 65  Bit Score: 125.50  E-value: 3.56e-34
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720360855  265 ALQKLLESFRIQYLQFLAYTKTPQYKANLQQLLDQEKEKNTQLLGTAQQLFGHCQAQKEEIRRLF 329
Cdd:cd20902      1 ALQKLLESFKIQYLQFLAYMKTPQYKASLQQQIEQEKEKNKQLTGKAQQLEKQIQALQKEGVRLL 65
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
290-443 3.48e-11

Uncharacterized protein, contains DUF3084 domain [Function unknown];


:

Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 66.85  E-value: 3.48e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  290 KANLQQLLDQEKEKNTQLLGTAQQLfghcQAQKEEIRRLfQQKLDELgvkaltYNDLIQAQKEISAHNQQL---REQSEQ 366
Cdd:COG4372     44 QEELEQLREELEQAREELEQLEEEL----EQARSELEQL-EEELEEL------NEQLQAAQAELAQAQEELeslQEEAEE 112

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720360855  367 LEKDNSELRSQsLRLLRARCEELRLDWSTL--SLENLRKEKQALRSQISEKQRHCLELQISIVELEKTQRQQELLQLKS 443
Cdd:COG4372    113 LQEELEELQKE-RQDLEQQRKQLEAQIAELqsEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLK 190
PHA03307 super family cl33723
transcriptional regulator ICP4; Provisional
 565-909 1.73e-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: 1.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  565 RHLSQDHTGASKAATSEPHPRPEHPKESSLPyqSPGLSNSMKLSPQDPPLASPATSPltsekGSEKGVKERAYSSHGETI 644
Cdd:PHA03307    76 GTEAPANESRSTPTWSLSTLAPASPAREGSP--TPPGPSSPDPPPPTPPPASPPPSP-----APDLSEMLRPVGSPGPPP 148

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  645 TSLPVSIPLSTVQPNKLPVSIPLASVVLPSRAERARSTPSPVPQPRDSSAtlekqtgasahgaggagagsrSLAVAPTGF 724
Cdd:PHA03307   149 AASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTP---------------------PAAASPRPP 207

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  725 YAGSVAISGALASSPAPL---ASGMESAVFDESSGPSSLFATMGSRSTPPQHPPLLSQSRNSGPASPAHqltASPRLSVT 801
Cdd:PHA03307   208 RRSSPISASASSPAPAPGrsaADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWN---GPSSRPGP 284

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  802 TQGSLPDTSKGELPSDPAFSDPESEAKRRIVFSISVGASSKQSPSTRHSPLTSG---TRGDCVQSHGQDS---------- 868
Cdd:PHA03307   285 ASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGaavSPGPSPSRSPSPSrppppadpss 364

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 1720360855  869 RKRSRRKRASAGTPSLSTGVSPKRRALPTVAGLFTQSSGSP 909
Cdd:PHA03307   365 PRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATG 405
 
Name Accession Description Interval E-value
DOT1 pfam08123
Histone methylation protein DOT1; The DOT1 domain regulates gene expression by methylating ...
 2-101 1.86e-47

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: 169.02  E-value: 1.86e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855    2 LERGDFLSEEWRERI-ANTSVIFVNNFAFGPEVDHQLKERFANMKEGGRIVSSKPFAPLNFRINSRNLSDIGTIMRVVEL 80
Cdd:pfam08123  105 FIRGSFLDNERVEEIiPEADVILVNNFAFDPELNLQLKEMLQDLKDGCKIISLKSFVPLNYRINFRNLSDIFNILKVEEL 184

                           90       100
                   ....*....|....*....|.
gi 1720360855   81 SPLKGSVSWTGKPVSYYLHTI 101
Cdd:pfam08123  185 KLPEGSVSWTSRGVEYYISTV 205
CC_DOT1L cd20902
coiled coil domain of disruptor of telomeric-silencing 1-like (DOT1L) and similar proteins; ...
 265-329 3.56e-34

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


Pssm-ID: 411016 [Multi-domain]  Cd Length: 65  Bit Score: 125.50  E-value: 3.56e-34
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720360855  265 ALQKLLESFRIQYLQFLAYTKTPQYKANLQQLLDQEKEKNTQLLGTAQQLFGHCQAQKEEIRRLF 329
Cdd:cd20902      1 ALQKLLESFKIQYLQFLAYMKTPQYKASLQQQIEQEKEKNKQLTGKAQQLEKQIQALQKEGVRLL 65
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
290-443 3.48e-11

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 66.85  E-value: 3.48e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  290 KANLQQLLDQEKEKNTQLLGTAQQLfghcQAQKEEIRRLfQQKLDELgvkaltYNDLIQAQKEISAHNQQL---REQSEQ 366
Cdd:COG4372     44 QEELEQLREELEQAREELEQLEEEL----EQARSELEQL-EEELEEL------NEQLQAAQAELAQAQEELeslQEEAEE 112

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720360855  367 LEKDNSELRSQsLRLLRARCEELRLDWSTL--SLENLRKEKQALRSQISEKQRHCLELQISIVELEKTQRQQELLQLKS 443
Cdd:COG4372    113 LQEELEELQKE-RQDLEQQRKQLEAQIAELqsEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLK 190
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 294-443 3.45e-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: 3.45e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  294 QQLLDQEKEKNTQLLGTAQQLfghcqaqKEEIRRLFQQKLDELgVKAL------TYNDLIQAQKEISAHNQ---QLREQS 364
Cdd:TIGR04523  273 QKELEQNNKKIKELEKQLNQL-------KSEISDLNNQKEQDW-NKELkselknQEKKLEEIQNQISQNNKiisQLNEQI 344

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  365 EQLEKD--NSELRSQSL-RLLRARCEELRL-----DWSTLSLENLRKEKQALRSQIS--EKQRHCLELQISIVELEKTQR 434
Cdd:TIGR04523  345 SQLKKEltNSESENSEKqRELEEKQNEIEKlkkenQSYKQEIKNLESQINDLESKIQnqEKLNQQKDEQIKKLQQEKELL 424


                   ....*....
gi 1720360855  435 QQELLQLKS 443
Cdd:TIGR04523  425 EKEIERLKE 433
MscS_porin pfam12795
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...
 258-443 3.04e-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: 50.38  E-value: 3.04e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  258 LVAPTPPALQKLLESFRIQYL-QFLAytktpQYKANLQQLLDQEKEKNTQLLGTAQQLFGhCQAQKEEIRRLFQQKLDEL 336
Cdd:pfam12795   63 LQAKAEAAPKEILASLSLEELeQRLL-----QTSAQLQELQNQLAQLNSQLIELQTRPER-AQQQLSEARQRLQQIRNRL 136

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  337 GVKALTYNDLIQAQK-EISAHNQQLREQSEQLEKdnsELRSQSLRLLRARceeLRLDWSTLSLENLRKEKQALRSQISEK 415
Cdd:pfam12795  137 NGPAPPGEPLSEAQRwALQAELAALKAQIDMLEQ---ELLSNNNRQDLLK---ARRDLLTLRIQRLEQQLQALQELLNEK 210

                          170       180
                   ....*....|....*....|....*...
gi 1720360855  416 QRhclelqisiVELEKTQRQQELLQLKS 443
Cdd:pfam12795  211 RL---------QEAEQAVAQTEQLAEEA 229
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 565-909 1.73e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 46.32  E-value: 1.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  565 RHLSQDHTGASKAATSEPHPRPEHPKESSLPyqSPGLSNSMKLSPQDPPLASPATSPltsekGSEKGVKERAYSSHGETI 644
Cdd:PHA03307    76 GTEAPANESRSTPTWSLSTLAPASPAREGSP--TPPGPSSPDPPPPTPPPASPPPSP-----APDLSEMLRPVGSPGPPP 148

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  645 TSLPVSIPLSTVQPNKLPVSIPLASVVLPSRAERARSTPSPVPQPRDSSAtlekqtgasahgaggagagsrSLAVAPTGF 724
Cdd:PHA03307   149 AASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTP---------------------PAAASPRPP 207

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  725 YAGSVAISGALASSPAPL---ASGMESAVFDESSGPSSLFATMGSRSTPPQHPPLLSQSRNSGPASPAHqltASPRLSVT 801
Cdd:PHA03307   208 RRSSPISASASSPAPAPGrsaADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWN---GPSSRPGP 284

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  802 TQGSLPDTSKGELPSDPAFSDPESEAKRRIVFSISVGASSKQSPSTRHSPLTSG---TRGDCVQSHGQDS---------- 868
Cdd:PHA03307   285 ASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGaavSPGPSPSRSPSPSrppppadpss 364

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 1720360855  869 RKRSRRKRASAGTPSLSTGVSPKRRALPTVAGLFTQSSGSP 909
Cdd:PHA03307   365 PRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATG 405
STAT5_CCD cd16855
Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family ...
 266-426 6.91e-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: 42.64  E-value: 6.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  266 LQKLLESFRIQYlQFLayTKtpqYKANLQQLLDQEKEKNTQLLGTAQQlfghcqaQKEEIRRLFQQKLDELGVKALTynd 345
Cdd:cd16855     27 LQQKQESFVIQY-QES--QK---IQAQLQQLQQQPQNERIELEQQLQQ-------QKEQLEQLLNAKAQELLQLRME--- 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  346 LIQAQKEISAHNQQLreQSEQLEKdnsEL----RSQ-----------SLRLLRARCEELrLD--WSTlslenlrkekqal 408
Cdd:cd16855     91 LADKFKKTIQLLSKL--QSRVLDE---ELiqwkRQQqlagngapfesNLDTIQEWCESL-AEiiWQN------------- 151

                          170
                   ....*....|....*...
gi 1720360855  409 RSQISEKQRHCLELQISI 426
Cdd:cd16855    152 RQQIKRAERLKQKLPIPL 169
PRK11281 PRK11281
mechanosensitive channel MscK;
261-438 9.39e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 44.13  E-value: 9.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  261 PTPPALQKLLESFRIQYLQflaytkTPQYKA---NLQQLL------DQEKEKNTQLLGTAQQLFGHCQAQKEEIRRL--- 328
Cdd:PRK11281    36 PTEADVQAQLDALNKQKLL------EAEDKLvqqDLEQTLalldkiDRQKEETEQLKQQLAQAPAKLRQAQAELEALkdd 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  329 ----FQQKLDELGVKAL------TYNDLIQAQKEISAHNQQLREQSEQLEKDNSELRSQSLRLlrarcEELRldwstlsl 398
Cdd:PRK11281   110 ndeeTRETLSTLSLRQLesrlaqTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRL-----QQIR-------- 176

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1720360855  399 eNLRKEKQALRSQISEKQRHCLELQISIVELEKTQRQQEL 438
Cdd:PRK11281   177 -NLLKGGKVGGKALRPSQRVLLQAEQALLNAQNDLQRKSL 215
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 323-431 1.67e-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: 1.67e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855   323 EEIRRLFQQKLDELGVKALTYNDLIQAqkeISAHNQQLREQSEQLEKDNSELRSQSLRLLRARCEELRLDWSTLS----- 397
Cdd:smart00787  150 DENLEGLKEDYKLLMKELELLNSIKPK---LRDRKDALEEELRQLKQLEDELEDCDPTELDRAKEKLKKLLQEIMikvkk 226

                            90       100       110
                    ....*....|....*....|....*....|....
gi 1720360855   398 LENLRKEKQALRSQISEKQRHCLELQISIVELEK 431
Cdd:smart00787  227 LEELEEELQELESKIEDLTNKKSELNTEIAEAEK 260
 
Name Accession Description Interval E-value
DOT1 pfam08123
Histone methylation protein DOT1; The DOT1 domain regulates gene expression by methylating ...
 2-101 1.86e-47

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: 169.02  E-value: 1.86e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855    2 LERGDFLSEEWRERI-ANTSVIFVNNFAFGPEVDHQLKERFANMKEGGRIVSSKPFAPLNFRINSRNLSDIGTIMRVVEL 80
Cdd:pfam08123  105 FIRGSFLDNERVEEIiPEADVILVNNFAFDPELNLQLKEMLQDLKDGCKIISLKSFVPLNYRINFRNLSDIFNILKVEEL 184

                           90       100
                   ....*....|....*....|.
gi 1720360855   81 SPLKGSVSWTGKPVSYYLHTI 101
Cdd:pfam08123  185 KLPEGSVSWTSRGVEYYISTV 205
CC_DOT1L cd20902
coiled coil domain of disruptor of telomeric-silencing 1-like (DOT1L) and similar proteins; ...
 265-329 3.56e-34

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


Pssm-ID: 411016 [Multi-domain]  Cd Length: 65  Bit Score: 125.50  E-value: 3.56e-34
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720360855  265 ALQKLLESFRIQYLQFLAYTKTPQYKANLQQLLDQEKEKNTQLLGTAQQLFGHCQAQKEEIRRLF 329
Cdd:cd20902      1 ALQKLLESFKIQYLQFLAYMKTPQYKASLQQQIEQEKEKNKQLTGKAQQLEKQIQALQKEGVRLL 65
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
290-443 3.48e-11

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 66.85  E-value: 3.48e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  290 KANLQQLLDQEKEKNTQLLGTAQQLfghcQAQKEEIRRLfQQKLDELgvkaltYNDLIQAQKEISAHNQQL---REQSEQ 366
Cdd:COG4372     44 QEELEQLREELEQAREELEQLEEEL----EQARSELEQL-EEELEEL------NEQLQAAQAELAQAQEELeslQEEAEE 112

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720360855  367 LEKDNSELRSQsLRLLRARCEELRLDWSTL--SLENLRKEKQALRSQISEKQRHCLELQISIVELEKTQRQQELLQLKS 443
Cdd:COG4372    113 LQEELEELQKE-RQDLEQQRKQLEAQIAELqsEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLK 190
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
290-443 9.70e-10

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 62.23  E-value: 9.70e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  290 KANLQQLLDQEKEKNTQLLGTAQQLfghcQAQKEEIRRLfQQKLDelgvkaltyndliQAQKEISAHNQQLREQSEQLEK 369
Cdd:COG4372     30 SEQLRKALFELDKLQEELEQLREEL----EQAREELEQL-EEELE-------------QARSELEQLEEELEELNEQLQA 91

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720360855  370 DNSELRS--QSLRLLRARCEELRLDwstlsLENLRKEKQALRSQISEkqrhcLELQISIVELEKTQRQQELLQLKS 443
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 ...
 294-443 3.45e-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: 3.45e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  294 QQLLDQEKEKNTQLLGTAQQLfghcqaqKEEIRRLFQQKLDELgVKAL------TYNDLIQAQKEISAHNQ---QLREQS 364
Cdd:TIGR04523  273 QKELEQNNKKIKELEKQLNQL-------KSEISDLNNQKEQDW-NKELkselknQEKKLEEIQNQISQNNKiisQLNEQI 344

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  365 EQLEKD--NSELRSQSL-RLLRARCEELRL-----DWSTLSLENLRKEKQALRSQIS--EKQRHCLELQISIVELEKTQR 434
Cdd:TIGR04523  345 SQLKKEltNSESENSEKqRELEEKQNEIEKlkkenQSYKQEIKNLESQINDLESKIQnqEKLNQQKDEQIKKLQQEKELL 424


                   ....*....
gi 1720360855  435 QQELLQLKS 443
Cdd:TIGR04523  425 EKEIERLKE 433
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 288-476 1.27e-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: 1.27e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  288 QYKANLQQLLDQEKEKNTQLLGTAQQLfGHCQAQKEEIRRLFQQKLDELGVKALTYNDLIQAQKEISAHNQQLREQSEQL 367
Cdd:COG1196    313 ELEERLEELEEELAELEEELEELEEEL-EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  368 EKDNSELRSQSLRLLRARcEELRLDwstlsLENLRKEKQALRSQISEKQRHCLELQISIVELEKTQRQQELLQLKScvpp 447
Cdd:COG1196    392 LRAAAELAAQLEELEEAE-EALLER-----LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL---- 461

                          170       180
                   ....*....|....*....|....*....
gi 1720360855  448 dDALSLHLRGKGALGRELEADAGRLRLEL 476
Cdd:COG1196    462 -LELLAELLEEAALLEAALAELLEELAEA 489
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
288-441 2.56e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 55.54  E-value: 2.56e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  288 QYKANLQQLLDQEKEKNT------------QLLGTAQQLFGHCQAQKEEIRRL--FQQKLDELGVKALTYNDLIQAQKEI 353
Cdd:COG4717     89 EYAELQEELEELEEELEEleaeleelreelEKLEKLLQLLPLYQELEALEAELaeLPERLEELEERLEELRELEEELEEL 168

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  354 SAHNQQLREQSEQLEKDNSELRSQSLRLLRARCEELRLDwstlsLENLRKEKQALRSQISEKQRHCLELQISIVELEKTQ 433
Cdd:COG4717    169 EAELAELQEELEELLEQLSLATEEELQDLAEELEELQQR-----LAELEEELEEAQEELEELEEELEQLENELEAAALEE 243


                   ....*...
gi 1720360855  434 RQQELLQL 441
Cdd:COG4717    244 RLKEARLL 251
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 288-442 5.42e-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: 5.42e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  288 QYKANLQQLLDQEKEKNTQLLGTAQQLFGhCQAQKEEIRRLFQQKLDELGVKALTYNDLIQAQKEISAHNQQLREQSEQL 367
Cdd:TIGR02168  236 ELREELEELQEELKEAEEELEELTAELQE-LEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANL 314

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720360855  368 EKDNSELRSQSLRLLRARcEELRLDWSTLS--LENLRKEKQALRSQISEKQRHCLELQISIVELEK--TQRQQELLQLK 442
Cdd:TIGR02168  315 ERQLEELEAQLEELESKL-DELAEELAELEekLEELKEELESLEAELEELEAELEELESRLEELEEqlETLRSKVAQLE 392
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 270-443 2.68e-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: 2.68e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  270 LESFRIQYLQFLAYTKTPQYKANLQQLLDQeKEKNTQLLGTAQQLFGHCQAQKEEIRRLFQQKLDELGVKALTYNDLIQA 349
Cdd:TIGR04523  194 NKLLKLELLLSNLKKKIQKNKSLESQISEL-KKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEK 272

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  350 QKEISAHNQQLREQSEQLEKDNSELRSqslrlLRARCEElrlDWSTL---SLENLRKEKQALRSQISEKQRHCLEL--QI 424
Cdd:TIGR04523  273 QKELEQNNKKIKELEKQLNQLKSEISD-----LNNQKEQ---DWNKElksELKNQEKKLEEIQNQISQNNKIISQLneQI 344

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1720360855  425 SIVELEKT--------------QRQQELLQLKS 443
Cdd:TIGR04523  345 SQLKKELTnsesensekqreleEKQNEIEKLKK 377
MscS_porin pfam12795
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...
 258-443 3.04e-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: 50.38  E-value: 3.04e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  258 LVAPTPPALQKLLESFRIQYL-QFLAytktpQYKANLQQLLDQEKEKNTQLLGTAQQLFGhCQAQKEEIRRLFQQKLDEL 336
Cdd:pfam12795   63 LQAKAEAAPKEILASLSLEELeQRLL-----QTSAQLQELQNQLAQLNSQLIELQTRPER-AQQQLSEARQRLQQIRNRL 136

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  337 GVKALTYNDLIQAQK-EISAHNQQLREQSEQLEKdnsELRSQSLRLLRARceeLRLDWSTLSLENLRKEKQALRSQISEK 415
Cdd:pfam12795  137 NGPAPPGEPLSEAQRwALQAELAALKAQIDMLEQ---ELLSNNNRQDLLK---ARRDLLTLRIQRLEQQLQALQELLNEK 210

                          170       180
                   ....*....|....*....|....*...
gi 1720360855  416 QRhclelqisiVELEKTQRQQELLQLKS 443
Cdd:pfam12795  211 RL---------QEAEQAVAQTEQLAEEA 229
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 288-440 5.18e-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: 5.18e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  288 QYKANLQQLLDQEKEKNTQL------LGTAQQLFGHCQAQKEEIRRLFQQKLDELGVKALTYNDLIQAQKEISAHNQQLR 361
Cdd:TIGR02168  306 ILRERLANLERQLEELEAQLeeleskLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLR 385

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  362 EQSEQLEKDNSELRSQsLRLLRARCEELrldwsTLSLENLRKEKQALRSQISEKQRHCLELQISIV--ELEKTQRQQELL 439
Cdd:TIGR02168  386 SKVAQLELQIASLNNE-IERLEARLERL-----EDRRERLQQEIEELLKKLEEAELKELQAELEELeeELEELQEELERL 459


                   .
gi 1720360855  440 Q 440
Cdd:TIGR02168  460 E 460
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 272-475 6.61e-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: 6.61e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  272 SFRIQYLQFLAYTKTPQYKANLQQLLDQEKEKNTQLlgtaqQLFGHCQAQKEEIRRLFQQKLDELGVKALTyndLIQAQK 351
Cdd:pfam15921  425 NMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESL-----EKVSSLTAQLESTKEMLRKVVEELTAKKMT---LESSER 496

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  352 EISAHNQQLREQSEQLEKDNSE---LRSQ----------------SLRLLRARCEELRLDWSTLS--LENLRKEKQALRS 410
Cdd:pfam15921  497 TVSDLTASLQEKERAIEATNAEitkLRSRvdlklqelqhlknegdHLRNVQTECEALKLQMAEKDkvIEILRQQIENMTQ 576

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720360855  411 QISEKQRHCLELQISIVELEK--TQRQQELLQLKscVPPDDalslhlrgKGALGRELEADAGRLRLE 475
Cdd:pfam15921  577 LVGQHGRTAGAMQVEKAQLEKeiNDRRLELQEFK--ILKDK--------KDAKIRELEARVSDLELE 633
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 293-477 1.50e-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: 1.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  293 LQQLLDQEKEKNTQLLGTAQQLFGHCQAQKEEIRRLfQQKLDELGVKALTY--------NDLIQAQKEISAHNQQLREQS 364
Cdd:TIGR02168  773 AEEELAEAEAEIEELEAQIEQLKEELKALREALDEL-RAELTLLNEEAANLrerlesleRRIAATERRLEDLEEQIEELS 851

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  365 EQLEKDNSELRSQSLRL----------------LRARCEELRLDWSTLS--LENLRKEKQALRSQISEKQrhcleLQISI 426
Cdd:TIGR02168  852 EDIESLAAEIEELEELIeeleseleallnerasLEEALALLRSELEELSeeLRELESKRSELRRELEELR-----EKLAQ 926

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720360855  427 VELEKTQRQQELLQLKS------CVPPDDALSLHLRGKGALgRELEADAGRLRLELD 477
Cdd:TIGR02168  927 LELRLEGLEVRIDNLQErlseeySLTLEEAEALENKIEDDE-EEARRRLKRLENKIK 982
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
323-445 1.80e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.38  E-value: 1.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  323 EEIRRLfQQKLDELGVKALTYNDLIQAQKEISAHNQQLREQSEQLEKDNSELRSQ-SLRLLRARCEELR--LDWSTLSLE 399
Cdd:COG4717     71 KELKEL-EEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLlQLLPLYQELEALEaeLAELPERLE 149

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1720360855  400 NLRKEKQA---LRSQISEKQRHCLELQISIVELEKTQRQQELLQLKSCV 445
Cdd:COG4717    150 ELEERLEElreLEEELEELEAELAELQEELEELLEQLSLATEEELQDLA 198
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
327-440 2.14e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 48.75  E-value: 2.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  327 RLFQQKLDELGVKALTYNDLIQAQKEISAHNQQLREQSEQLEKDNSELRSQSLRLLRARcEEL-----RLDWSTLSLENL 401
Cdd:COG4372     14 SLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQAR-SELeqleeELEELNEQLQAA 92

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1720360855  402 RKEKQALRSQISEKQRHCLELQIsivELEKTQRQQELLQ 440
Cdd:COG4372     93 QAELAQAQEELESLQEEAEELQE---ELEELQKERQDLE 128
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 293-437 2.37e-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: 48.61  E-value: 2.37e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  293 LQQLLDQEKEKNTQLLGTAQQLfghcqAQKEEIRRLFQQKLDELGVKALTY------------NDLIQAQKEISAHNQQL 360
Cdd:COG4942     95 LRAELEAQKEELAELLRALYRL-----GRQPPLALLLSPEDFLDAVRRLQYlkylaparreqaEELRADLAELAALRAEL 169

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720360855  361 REQSEQLEKDNSELRSQSLRLLRARCEELRLdwstlsLENLRKEKQALRSQISEKQRHCLELQISIVELEKTQRQQE 437
Cdd:COG4942    170 EAERAELEALLAELEEERAALEALKAERQKL------LARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
flagell_FliJ TIGR02473
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ...
 293-417 2.51e-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: 2.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  293 LQQLLD---QEKEKNTQLLGTAQQLFGHCQAQkeeIRRLFQQKlDELGVKALTYNDLIQAQKEISAHNQQLReqseQLEK 369
Cdd:TIGR02473    4 LQKLLDlreKEEEQAKLELAKAQAEFERLETQ---LQQLIKYR-EEYEQQALEKVGAGTSALELSNYQRFIR----QLDQ 75

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1720360855  370 DNSELRsQSLRLLRARCEELRLDWSTL-----SLENLrKEKQALRSQISEKQR 417
Cdd:TIGR02473   76 RIQQQQ-QELALLQQEVEAKRERLLEArrelkALEKL-KEKKQKEYRAEEAKR 126
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 265-475 2.69e-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: 2.69e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  265 ALQKLLESFRIQyLQFLAYTktpQYKANLQQLLDQEKEKNTQLLGTAQQLfGHCQAQKEEIRRLFQQKLDELGVKALTYN 344
Cdd:COG1196    217 ELKEELKELEAE-LLLLKLR---ELEAELEELEAELEELEAELEELEAEL-AELEAELEELRLELEELELELEEAQAEEY 291

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  345 DLIQAQKEISAHNQQLREQSEQLEKDNSELRSQsLRLLRARCEEL--RLDWSTLSLENLRKEKQALRSQISEKQRHCLEL 422
Cdd:COG1196    292 ELLAELARLEQDIARLEERRRELEERLEELEEE-LAELEEELEELeeELEELEEELEEAEEELEEAEAELAEAEEALLEA 370

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1720360855  423 QISIVELEKT--QRQQELLQLKScvppdDALSLHLRGKGALGRELEADAGRLRLE 475
Cdd:COG1196    371 EAELAEAEEEleELAEELLEALR-----AAAELAAQLEELEEAEEALLERLERLE 420
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 282-476 2.80e-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: 2.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  282 AYTKTPQYKANLQQLLDQEKEKNTQLLGtaqqlfghCQAQKEEIRRLFQQKLDELGVkaltyndliqAQKEISAhnqqLR 361
Cdd:TIGR02169  665 GILFSRSEPAELQRLRERLEGLKRELSS--------LQSELRRIENRLDELSQELSD----------ASRKIGE----IE 722

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  362 EQSEQLEKDnselrsqsLRLLRARCEELRLDWSTLS--LENLRKEKQALRSQISEKQRHCLELQISIVELEKTQRQQELL 439
Cdd:TIGR02169  723 KEIEQLEQE--------EEKLKERLEELEEDLSSLEqeIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIP 794

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1720360855  440 QLkscvppDDALS----LHLRGKGALgRELEADAGRLRLEL 476
Cdd:TIGR02169  795 EI------QAELSkleeEVSRIEARL-REIEQKLNRLTLEK 828
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 288-466 5.03e-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: 5.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  288 QYKANLQQLLDQEKEKnTQLLGTAQQLFgHC------------QAQKEEIRRL------FQQKLDELGVKALTYNDLIQ- 348
Cdd:pfam05557   80 LKKKYLEALNKKLNEK-ESQLADAREVI-SClknelselrrqiQRAELELQSTnseleeLQERLDLLKAKASEAEQLRQn 157

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  349 ---AQKEISAHNQQLRE----------QSEQLEKDNSELRS-----QSLRLLRARCEELRLDWSTLSLenLRKEKQALRS 410
Cdd:pfam05557  158 lekQQSSLAEAEQRIKElefeiqsqeqDSEIVKNSKSELARipeleKELERLREHNKHLNENIENKLL--LKEEVEDLKR 235

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720360855  411 QIS--EKQRHclelQISIVELEKTQRQQEllqLKSCVPPDDALSLHLRGKGALGRELE 466
Cdd:pfam05557  236 KLEreEKYRE----EAATLELEKEKLEQE---LQSWVKLAQDTGLNLRSPEDLSRRIE 286
MscS_porin pfam12795
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...
 290-442 7.17e-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: 46.14  E-value: 7.17e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  290 KANLQQLLDQEKEKNTQLLGTAQQLFGHCQAQKEEIRRL-------------FQQKLDELGVKA-------LTYNDLIQA 349
Cdd:pfam12795    4 ELEKAKLDEAAKKKLLQDLQQALSLLDKIDASKQRAAAYqkalddapaelreLRQELAALQAKAeaapkeiLASLSLEEL 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  350 QKEISAHNQQLREQSEQLEKDNSELRSQSLRLLRARCE-----------ELRLDWSTLSLENLRK--------EKQALRS 410
Cdd:pfam12795   84 EQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQlsearqrlqqiRNRLNGPAPPGEPLSEaqrwalqaELAALKA 163

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1720360855  411 QISEKQrhcLELQISIVELEKTQRQQELLQLK 442
Cdd:pfam12795  164 QIDMLE---QELLSNNNRQDLLKARRDLLTLR 192
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 319-487 7.93e-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: 7.93e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  319 QAQKEE-IRRLF--QQKLDELgvkaltyNDLIqaqKEISAHNQQLREQSEQLEKdnselrsqsLRLLRARCEELRLDWST 395
Cdd:TIGR02168  171 KERRKEtERKLErtRENLDRL-------EDIL---NELERQLKSLERQAEKAER---------YKELKAELRELELALLV 231

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  396 LSLENLRKEKQALRSQISEKQRHCLELQisiveLEKTQRQQELLQLKSCVPPDDALSLHLRGK----GALGRELEADAGR 471
Cdd:TIGR02168  232 LRLEELREELEELQEELKEAEEELEELT-----AELQELEEKLEELRLEVSELEEEIEELQKElyalANEISRLEQQKQI 306

                          170
                   ....*....|....*.
gi 1720360855  472 LRLELDCAKISLPHLS 487
Cdd:TIGR02168  307 LRERLANLERQLEELE 322
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
291-440 9.57e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.07  E-value: 9.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  291 ANLQQLLDQEKEKNTQLLgtaqqlfghCQAQKEEIRRLFQQK----LDELGVKALTYNDLIQAQKEISAHNQQLREQSEQ 366
Cdd:COG4717    347 EELQELLREAEELEEELQ---------LEELEQEIAALLAEAgvedEEELRAALEQAEEYQELKEELEELEEQLEELLGE 417

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720360855  367 LEkdnSELRSQSLRLLRARceelrldwstlsLENLRKEKQALRSQISEKQRHCLELQISIVELEKTQRQQELLQ 440
Cdd:COG4717    418 LE---ELLEALDEEELEEE------------LEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQ 476
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 299-483 1.04e-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: 47.09  E-value: 1.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  299 QEKEKNTQLL----GTAQQLFGHCQAQKEEIRRLFQQKLDELgvKALtyndLIQAQKEISAHNQQLREQSEqLEKDNSEL 374
Cdd:pfam01576  204 QELEKAKRKLegesTDLQEQIAELQAQIAELRAQLAKKEEEL--QAA----LARLEEETAQKNNALKKIRE-LEAQISEL 276

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  375 RS--QSLRLLRARCEELRLDwstlslenLRKEKQALRSQISEKQRHCLELQisivELeKTQRQQELLQLKSCVPPD---- 448
Cdd:pfam01576  277 QEdlESERAARNKAEKQRRD--------LGEELEALKTELEDTLDTTAAQQ----EL-RSKREQEVTELKKALEEEtrsh 343

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1720360855  449 DALSLHLRGKGA-----LGRELEaDAGRLRLELDCAKISL 483
Cdd:pfam01576  344 EAQLQEMRQKHTqaleeLTEQLE-QAKRNKANLEKAKQAL 382
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 290-443 1.34e-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: 1.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  290 KANLQQLLDQEKEKNTQLLGTAQQLfghcQAQKE----EIRRLFQQKLD----------ELGVKALTYNDLiqaQKEISA 355
Cdd:TIGR04523  393 INDLESKIQNQEKLNQQKDEQIKKL----QQEKEllekEIERLKETIIKnnseikdltnQDSVKELIIKNL---DNTRES 465

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  356 HNQQLREQSEQLEKDNSELRSQSlrllrarcEELRLDwsTLSLENLRKEKQALRSQISE--KQRHCLELQISIVELEKTQ 433
Cdd:TIGR04523  466 LETQLKVLSRSINKIKQNLEQKQ--------KELKSK--EKELKKLNEEKKELEEKVKDltKKISSLKEKIEKLESEKKE 535

                          170
                   ....*....|
gi 1720360855  434 RQQELLQLKS 443
Cdd:TIGR04523  536 KESKISDLED 545
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
270-414 1.38e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 46.30  E-value: 1.38e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  270 LESFRIQYLQFLAYTKTPQYKANLQQLLDQEKEKNTQLLGTAQQlfghcQAQKEEIRRLfQQKLDELgvkaltYNDLIQA 349
Cdd:COG4717    384 EEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE-----EELEEELEEL-EEELEEL------EEELEEL 451

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720360855  350 QKEISAHNQQLreqsEQLEKDN--SELRsQSLRLLRARCEELRLDWSTLSL---------ENLRKEKQ-ALRSQISE 414
Cdd:COG4717    452 REELAELEAEL----EQLEEDGelAELL-QELEELKAELRELAEEWAALKLalelleearEEYREERLpPVLERASE 523
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 565-909 1.73e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 46.32  E-value: 1.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  565 RHLSQDHTGASKAATSEPHPRPEHPKESSLPyqSPGLSNSMKLSPQDPPLASPATSPltsekGSEKGVKERAYSSHGETI 644
Cdd:PHA03307    76 GTEAPANESRSTPTWSLSTLAPASPAREGSP--TPPGPSSPDPPPPTPPPASPPPSP-----APDLSEMLRPVGSPGPPP 148

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  645 TSLPVSIPLSTVQPNKLPVSIPLASVVLPSRAERARSTPSPVPQPRDSSAtlekqtgasahgaggagagsrSLAVAPTGF 724
Cdd:PHA03307   149 AASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTP---------------------PAAASPRPP 207

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  725 YAGSVAISGALASSPAPL---ASGMESAVFDESSGPSSLFATMGSRSTPPQHPPLLSQSRNSGPASPAHqltASPRLSVT 801
Cdd:PHA03307   208 RRSSPISASASSPAPAPGrsaADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWN---GPSSRPGP 284

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  802 TQGSLPDTSKGELPSDPAFSDPESEAKRRIVFSISVGASSKQSPSTRHSPLTSG---TRGDCVQSHGQDS---------- 868
Cdd:PHA03307   285 ASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGaavSPGPSPSRSPSPSrppppadpss 364

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 1720360855  869 RKRSRRKRASAGTPSLSTGVSPKRRALPTVAGLFTQSSGSP 909
Cdd:PHA03307   365 PRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATG 405
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 282-476 3.91e-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: 3.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  282 AYTKTPQYKANLQQLLDQEKEKNTQLLGTAQQLFGH---CQAQKEEIRRLFQQKLDELGVKALTYNDLIQAQKEISAH-- 356
Cdd:TIGR02168  703 LRKELEELEEELEQLRKELEELSRQISALRKDLARLeaeVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAea 782

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  357 ---------------NQQLREQSEQLEKDNSELRS--QSLRLLRARCEELRLDWSTL------SLENLRKEKQALRSQIS 413
Cdd:TIGR02168  783 eieeleaqieqlkeeLKALREALDELRAELTLLNEeaANLRERLESLERRIAATERRledleeQIEELSEDIESLAAEIE 862

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720360855  414 EKQRHCLELQISIVEL--EKTQRQQELLQLKSCVppdDALSLHLRGKGALGRELEADAGRLRLEL 476
Cdd:TIGR02168  863 ELEELIEELESELEALlnERASLEEALALLRSEL---EELSEELRELESKRSELRRELEELREKL 924
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 297-443 4.98e-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: 4.98e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  297 LDQEKEKNTQLlgtaQQLFghcqaqKEEIRRLfQQKLDELGVKaltYNDLIQAQKEISAHNQQLREQSEQLEKDNSELRS 376
Cdd:TIGR04523  129 LEKQKKENKKN----IDKF------LTEIKKK-EKELEKLNNK---YNDLKKQKEELENELNLLEKEKLNIQKNIDKIKN 194

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720360855  377 QSLRLlrarceELRLdwstLSLENLRKEKQALRSQISEkqrhcLELQISIVELEKTQRQQELLQLKS 443
Cdd:TIGR04523  195 KLLKL------ELLL----SNLKKKIQKNKSLESQISE-----LKKQNNQLKDNIEKKQQEINEKTT 246
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
295-477 5.39e-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: 5.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  295 QLLDQEKEKNTQLLGTAQQLFGHCQAQKEEIRRLFQQKLDELgvkaltynDLIQAQKEISAHNQQLreqsEQLEKDNSEL 374
Cdd:COG4913    620 AELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEI--------DVASAEREIAELEAEL----ERLDASSDDL 687

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  375 RSqslrllrarceelrldwstlslenLRKEKQALRSQIS--EKQRHCLELQISIVELEKTQRQQELLQLKSCV---PPDD 449
Cdd:COG4913    688 AA------------------------LEEQLEELEAELEelEEELDELKGEIGRLEKELEQAEEELDELQDRLeaaEDLA 743

                          170       180
                   ....*....|....*....|....*....
gi 1720360855  450 ALSLHLRGKGALGREL-EADAGRLRLELD 477
Cdd:COG4913    744 RLELRALLEERFAAALgDAVERELRENLE 772
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 288-440 6.71e-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: 44.12  E-value: 6.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  288 QYKANLQQLLDqEKEKNTQLLGTAQQLFGHCQAQKEEIRRL------FQQKLDELG--------VKALTYNDLIQAQKEI 353
Cdd:pfam07888  203 QRDTQVLQLQD-TITTLTQKLTTAHRKEAENEALLEELRSLqerlnaSERKVEGLGeelssmaaQRDRTQAELHQARLQA 281

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  354 SAHNQQL-------RE-------------QSEQLEKDNSELRSQSLRLLRARCEELRLDWSTLSLEnLRKEKQALRSQIS 413
Cdd:pfam07888  282 AQLTLQLadaslalREgrarwaqeretlqQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVE-LGREKDCNRVQLS 360

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1720360855  414 EKQRHCLELQISIVELEKTQRQ-----QELLQ 440
Cdd:pfam07888  361 ESRRELQELKASLRVAQKEKEQlqaekQELLE 392
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 280-493 6.89e-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: 44.57  E-value: 6.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  280 FLAYTKTPQYKANLQQLLDQEKEKNTQLLGTAQQLFGHCQAQKEEIRRLFQ--QKLDELGVKAL-------TYNDLIQAQ 350
Cdd:TIGR00618  465 AQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNParQDIDNPGPLTRrmqrgeqTYAQLETSE 544

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  351 KEISAHNQQLREQSEQLEKDNSELRSQSLRLLRARCEelrldwSTLSLENLRKEKQALRSQIS-----------EKQRHC 419
Cdd:TIGR00618  545 EDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNR------SKEDIPNLQNITVRLQDLTEklseaedmlacEQHALL 618

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  420 LELQISIVELEKTQRQQ---ELLQLKSCVPPDDALSL---HLRGKGALGRELEADAGRLR-LELDCAKISLPHLSSMSPE 492
Cdd:TIGR00618  619 RKLQPEQDLQDVRLHLQqcsQELALKLTALHALQLTLtqeRVREHALSIRVLPKELLASRqLALQKMQSEKEQLTYWKEM 698


                   .
gi 1720360855  493 L 493
Cdd:TIGR00618  699 L 699
STAT5_CCD cd16855
Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family ...
 266-426 6.91e-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: 42.64  E-value: 6.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  266 LQKLLESFRIQYlQFLayTKtpqYKANLQQLLDQEKEKNTQLLGTAQQlfghcqaQKEEIRRLFQQKLDELGVKALTynd 345
Cdd:cd16855     27 LQQKQESFVIQY-QES--QK---IQAQLQQLQQQPQNERIELEQQLQQ-------QKEQLEQLLNAKAQELLQLRME--- 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  346 LIQAQKEISAHNQQLreQSEQLEKdnsEL----RSQ-----------SLRLLRARCEELrLD--WSTlslenlrkekqal 408
Cdd:cd16855     91 LADKFKKTIQLLSKL--QSRVLDE---ELiqwkRQQqlagngapfesNLDTIQEWCESL-AEiiWQN------------- 151

                          170
                   ....*....|....*...
gi 1720360855  409 RSQISEKQRHCLELQISI 426
Cdd:cd16855    152 RQQIKRAERLKQKLPIPL 169
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 295-440 7.64e-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: 42.23  E-value: 7.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  295 QLLDQE---KEKNTQLLGTAQQLFGHCQAQKEEIRRLFQQKLDELGVKALTYN-DLIQAQKEISAHNQQLREQSEQLEKD 370
Cdd:pfam08614   11 RLLDRTallEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQLReELAELYRSRGELAQRLVDLNEELQEL 90

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720360855  371 NSELRSQS--LRLLRARCEEL--RLDWSTLSLENLRKEKQALRSQISEkqrhcLELQISIVE--LEKTQRQ-QELLQ 440
Cdd:pfam08614   91 EKKLREDErrLAALEAERAQLeeKLKDREEELREKRKLNQDLQDELVA-----LQLQLNMAEekLRKLEKEnRELVE 162
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 522-911 8.23e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 44.39  E-value: 8.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  522 ASPLDQEVVPCTPSHSGRPRLEKLSGLALPDYTRLSPAKIVLRRHLSQDHTGASKAATSEPHPRPEHPKESSLPYQSPGL 601
Cdd:PHA03307    59 AAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEML 138

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  602 SNSMKLSPQDPPLASPATSPLTSEKGSEKgvkeraysshgetiTSLPVSIPLSTVQPNKLPVSIPLASVvlPSRAERARS 681
Cdd:PHA03307   139 RPVGSPGPPPAASPPAAGASPAAVASDAA--------------SSRQAALPLSSPEETARAPSSPPAEP--PPSTPPAAA 202

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  682 TPSPVPQPRDSSATLEKQTGASAHGAGGAGAGSRSLAVAPTGFYAGSVAISGALASSPAPLASGMESAVFDESSGPSSLF 761
Cdd:PHA03307   203 SPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRP 282

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  762 ATMGSRSTPPQHPPLLSQSRNSGPASPAHQLTASPRLSVTTQGSLPDTSKGELPSDPAFSDPESEAKRRivfSISVGASS 841
Cdd:PHA03307   283 GPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSP---SPSRPPPP 359

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  842 KQSPSTRHSPLTSGTRGDCVQSHGQDSRKRSRRKRASAGTPSLSTGVSPKRRALPTVAGLFTQSSGSPLN 911
Cdd:PHA03307   360 ADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATGRFPAGRPRPSPLDAGAASGAFYAR 429
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 284-528 8.58e-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: 8.58e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  284 TKTPQYKanlqQLLDQEKEKNTQLLGTAQQLFGHCQAQKEEIRRLFQQKLDELGVKALTYNDLIQAQKEISAHNQQLREQ 363
Cdd:TIGR00618  173 FPLDQYT----QLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQK 248

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  364 SEQLEKDNSelRSQSLRLLRARCEELRLDWSTLSLENLRKEKQALRSQISEKQRHCL-----------ELQISIVELEKT 432
Cdd:TIGR00618  249 REAQEEQLK--KQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTqieqqaqrihtELQSKMRSRAKL 326

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  433 --QRQQELLQLKSCVPPDDALSLHLRGKGALGRELEADAGRlRLELDCAKISLPHLSSMSPELSmnghaASYELCNAASR 510
Cdd:TIGR00618  327 lmKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSI-REISCQQHTLTQHIHTLQQQKT-----TLTQKLQSLCK 400

                          250
                   ....*....|....*...
gi 1720360855  511 PSSKQNTPQYLASPLDQE 528
Cdd:TIGR00618  401 ELDILQREQATIDTRTSA 418
PRK11281 PRK11281
mechanosensitive channel MscK;
261-438 9.39e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 44.13  E-value: 9.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  261 PTPPALQKLLESFRIQYLQflaytkTPQYKA---NLQQLL------DQEKEKNTQLLGTAQQLFGHCQAQKEEIRRL--- 328
Cdd:PRK11281    36 PTEADVQAQLDALNKQKLL------EAEDKLvqqDLEQTLalldkiDRQKEETEQLKQQLAQAPAKLRQAQAELEALkdd 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  329 ----FQQKLDELGVKAL------TYNDLIQAQKEISAHNQQLREQSEQLEKDNSELRSQSLRLlrarcEELRldwstlsl 398
Cdd:PRK11281   110 ndeeTRETLSTLSLRQLesrlaqTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRL-----QQIR-------- 176

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1720360855  399 eNLRKEKQALRSQISEKQRHCLELQISIVELEKTQRQQEL 438
Cdd:PRK11281   177 -NLLKGGKVGGKALRPSQRVLLQAEQALLNAQNDLQRKSL 215
PRK10246 PRK10246
exonuclease subunit SbcC; Provisional
 281-440 1.21e-03

exonuclease subunit SbcC; Provisional


Pssm-ID: 182330 [Multi-domain]  Cd Length: 1047  Bit Score: 43.64  E-value: 1.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  281 LAYTKTPQYKANLQQLLDQEKEKNTQLLGTAQQL------FGHCQAQKEEIRRLFQQKLDELGVKALTYNDLIQAQKEIS 354
Cdd:PRK10246   280 LAALSLAQPARQLRPHWERIQEQSAALAHTRQQIeevntrLQSTMALRARIRHHAAKQSAELQAQQQSLNTWLAEHDRFR 359

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  355 AHNQQL---REQSEQLEKDNSELRSQSLRLLRARCEELRLDWSTLSL---------------ENLRKEKQALRSQISEKQ 416
Cdd:PRK10246   360 QWNNELagwRAQFSQQTSDREQLRQWQQQLTHAEQKLNALPAITLTLtadevaaalaqhaeqRPLRQRLVALHGQIVPQQ 439

                          170       180
                   ....*....|....*....|....*.
gi 1720360855  417 RHCLELQISIVEL--EKTQRQQELLQ 440
Cdd:PRK10246   440 KRLAQLQVAIQNVtqEQTQRNAALNE 465
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 288-443 1.37e-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: 1.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  288 QYKANLQQLLDQEKEKNTQLlgtaqqlfghcQAQKEEIrrlfQQKLDELGVKALTYNDLIQAQKEISAHNQQLREQSEQL 367
Cdd:TIGR04523  381 SYKQEIKNLESQINDLESKI-----------QNQEKLN----QQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDL 445

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  368 EKDNSELRsqslrllrarceelrldwstLSLENLRKEKQALRSQISEkqrhcLELQISIVE--LEKTQRQ-----QELLQ 440
Cdd:TIGR04523  446 TNQDSVKE--------------------LIIKNLDNTRESLETQLKV-----LSRSINKIKqnLEQKQKElkskeKELKK 500


                   ...
gi 1720360855  441 LKS 443
Cdd:TIGR04523  501 LNE 503
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 294-442 1.45e-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: 1.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  294 QQLLDQEKEKNTQLLGTAQQLFGHCQAQKEEIR-RLFQQKLDELGVKaltyNDLIQAQKEI-------SAHNQQLREQSE 365
Cdd:pfam13868  175 REEIEEEKEREIARLRAQQEKAQDEKAERDELRaKLYQEEQERKERQ----KEREEAEKKArqrqelqQAREEQIELKER 250

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  366 QLEKDNSELRSQSLRLLRARCEELRLDwstlsLENLRKEKQ-------ALRSQISEKQRHCL-ELQISIVELEKTQRQQE 437
Cdd:pfam13868  251 RLAEEAEREEEEFERMLRKQAEDEEIE-----QEEAEKRRMkrlehrrELEKQIEEREEQRAaEREEELEEGERLREEEA 325


                   ....*
gi 1720360855  438 LLQLK 442
Cdd:pfam13868  326 ERRER 330
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 323-431 1.67e-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: 1.67e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855   323 EEIRRLFQQKLDELGVKALTYNDLIQAqkeISAHNQQLREQSEQLEKDNSELRSQSLRLLRARCEELRLDWSTLS----- 397
Cdd:smart00787  150 DENLEGLKEDYKLLMKELELLNSIKPK---LRDRKDALEEELRQLKQLEDELEDCDPTELDRAKEKLKKLLQEIMikvkk 226

                            90       100       110
                    ....*....|....*....|....*....|....
gi 1720360855   398 LENLRKEKQALRSQISEKQRHCLELQISIVELEK 431
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 ...
 347-486 1.86e-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: 1.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  347 IQAQKEISAHNQQLREQSEQLEKDNSELRSQSLRLL-----RARCEElRLDWSTLSLENLRKEKQALRSQISEKQRHCLE 421
Cdd:pfam01576  457 IKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRqledeRNSLQE-QLEEEEEAKRNVERQLSTLQAQLSDMKKKLEE 535

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720360855  422 LQISIVELEKTQR--QQELlqlkscvppdDALSLHLRGKGALGRELEADAGRLRLELDCAKISLPHL 486
Cdd:pfam01576  536 DAGTLEALEEGKKrlQREL----------EALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQ 592
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 293-414 1.95e-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: 1.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  293 LQQLLDQEKEKNTQLLGTAQQLFGHCQAQKEEIRrlfqQKLDELGVKALTYndlIQAQKEIsahnQQLREQSEQLEKDNS 372
Cdd:COG3096    558 LLAELEAQLEELEEQAAEAVEQRSELRQQLEQLR----ARIKELAARAPAW---LAAQDAL----ERLREQSGEALADSQ 626

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1720360855  373 ELRSQSLRLLRarceelRLDWSTLSLENLRKEKQALRSQISE 414
Cdd:COG3096    627 EVTAAMQQLLE------REREATVERDELAARKQALESQIER 662
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 312-442 2.08e-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: 2.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  312 QQLFGHCQAQKEEIRRLfQQKLDELGVK--ALTYnDLIQAQKEIsahnQQLREQSEQLEkDNSELRSQSLRLLRARCEEL 389
Cdd:TIGR02169  794 PEIQAELSKLEEEVSRI-EARLREIEQKlnRLTL-EKEYLEKEI----QELQEQRIDLK-EQIKSIEKEIENLNGKKEEL 866

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1720360855  390 --RLDWSTLSLENLRKEKQALRSQISEKQRHCLELQISIVELEkTQRQQELLQLK 442
Cdd:TIGR02169  867 eeELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELE-AQIEKKRKRLS 920
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 293-423 3.11e-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: 41.98  E-value: 3.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  293 LQQLLDQEKEKNTQLLGTAQQLFGHCQAQKEEIRRLfQQKLDELGVKAltynDLIQAQK-EISAhnqqLREQSEQLEK-- 369
Cdd:pfam05622   64 LQKQLEQLQEENFRLETARDDYRIKCEELEKEVLEL-QHRNEELTSLA----EEAQALKdEMDI----LRESSDKVKKle 134

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720360855  370 -----------DNSELRSQsLRLLrarcEELRLDW--STLSLENLRKEKQALRSQISEKQRHCLELQ 423
Cdd:pfam05622  135 atvetykkkleDLGDLRRQ-VKLL----EERNAEYmqRTLQLEEELKKANALRGQLETYKRQVQELH 196
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
265-477 3.34e-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: 3.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  265 ALQKLLESFRIQYlqflaYTKTPQYKANLQQLLDQEKEKntqllgtAQQLFGHCQAQKEE--IRRLF-QQKLDELGVKAL 341
Cdd:COG4913    159 ALKARLKKQGVEF-----FDSFSAYLARLRRRLGIGSEK-------ALRLLHKTQSFKPIgdLDDFVrEYMLEEPDTFEA 226

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  342 -------------TYNDLIQAQK------EISAHNQQLREQSEQLEKdNSELRS--------QSLRLLRARCEELRLDWS 394
Cdd:COG4913    227 adalvehfddlerAHEALEDAREqiellePIRELAERYAAARERLAE-LEYLRAalrlwfaqRRLELLEAELEELRAELA 305

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  395 TL---------SLENLRKEKQALRSQISE-----KQRhcLELQISIVELEKTQRQQELLQLKSCV------PPDDA---L 451
Cdd:COG4913    306 RLeaelerleaRLDALREELDELEAQIRGnggdrLEQ--LEREIERLERELEERERRRARLEALLaalglpLPASAeefA 383

                          250       260
                   ....*....|....*....|....*.
gi 1720360855  452 SLHLRGKGALgRELEADAGRLRLELD 477
Cdd:COG4913    384 ALRAEAAALL-EALEEELEALEEALA 408
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
 322-423 6.59e-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: 38.39  E-value: 6.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  322 KEEIRRLfQQKLDELGVKALTYNDLIQAQKEISAHNQQ------------------LREQSEQLEKDNSELRSQsLRLLR 383
Cdd:pfam07926    7 QSEIKRL-KEEAADAEAQLQKLQEDLEKQAEIAREAQQnyerelvlhaedikalqaLREELNELKAEIAELKAE-AESAK 84

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1720360855  384 ARCEELRLDWStlslenlrKEKQALRSQISEKQRHCLELQ 423
Cdd:pfam07926   85 AELEESEESWE--------EQKKELEKELSELEKRIEDLN 116
CENP-F_leu_zip pfam10473
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ...
 348-442 7.37e-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: 7.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  348 QAQKEISAHNQ-QLREQSEQLEKDNSELRSQsLRLLRARCEELRLDwstlsLENLRKEKQALRSQISEKQRHCLELQISI 426
Cdd:pfam10473   30 ERELEMSEENQeLAILEAENSKAEVETLKAE-IEEMAQNLRDLELD-----LVTLRSEKENLTKELQKKQERVSELESLN 103

                           90
                   ....*....|....*...
gi 1720360855  427 VELEK--TQRQQELLQLK 442
Cdd:pfam10473  104 SSLENllEEKEQEKVQMK 121
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
 287-437 8.40e-03

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 40.81  E-value: 8.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  287 PQYKANLQQLLDQEKEK-------------NTQLLGTAQQLFghcqaqkeEIRRLFQQKLDELGVKALTYNDLIQAQKEI 353
Cdd:PRK10929    78 PKLSAELRQQLNNERDEprsvppnmstdalEQEILQVSSQLL--------EKSRQAQQEQDRAREISDSLSQLPQQQTEA 149

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  354 sahNQQLREQSEQL-----------EKDNSELRSQSLRLlRARCEELRLdwSTLSLENlRKEKQALRSQISEKQRHCLEL 422
Cdd:PRK10929   150 ---RRQLNEIERRLqtlgtpntplaQAQLTALQAESAAL-KALVDELEL--AQLSANN-RQELARLRSELAKKRSQQLDA 222

                          170
                   ....*....|....*.
gi 1720360855  423 QISIVE-LEKTQRQQE 437
Cdd:PRK10929   223 YLQALRnQLNSQRQRE 238
HAP1_N pfam04849
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ...
 287-436 8.61e-03

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: 8.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  287 PQYKAnLQQLLDQEKEKNTQLLGTAQQLFGHCQAQKEEirrlfQQKLdelgvkaltyndLIQAQKEISAHNQQLREQSEQ 366
Cdd:pfam04849  164 VQLDA-LQEKLRGLEEENLKLRSEASHLKTETDTYEEK-----EQQL------------MSDCVEQLSEANQQMAELSEE 225

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  367 LEKDNSELRSQ-----SLRL----LRARCEELRLDWSTLSLE-NLRKEKQ-ALRSQISE-KQRH--CLELQISIVELEKT 432
Cdd:pfam04849  226 LARKMEENLRQqeeitSLLAqivdLQHKCKELGIENEELQQHlQASKEAQrQLTSELQElQDRYaeCLGMLHEAQEELKE 305


                   ....
gi 1720360855  433 QRQQ 436
Cdd:pfam04849  306 LRKK 309
CENP-F_leu_zip pfam10473
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ...
 349-429 8.67e-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: 8.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360855  349 AQKEISAHNQQLREQSE---QLEKDNSELRS------QSLRLLRARCEELrlDWSTLSLENLRKEKQALRSQISEKQRHC 419
Cdd:pfam10473   50 SKAEVETLKAEIEEMAQnlrDLELDLVTLRSekenltKELQKKQERVSEL--ESLNSSLENLLEEKEQEKVQMKEESKTA 127

                           90
                   ....*....|.
gi 1720360855  420 LE-LQISIVEL 429
Cdd:pfam10473  128 VEmLQTQLKEL 138
 
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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