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Conserved domains on  [gi|755534310|ref|XP_011241693|]
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histone-lysine N-methyltransferase, H3 lysine-79 specific isoform X2 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DOT1 pfam08123
Histone methylation protein DOT1; The DOT1 domain regulates gene expression by methylating ...
 115-317 2.93e-107

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: 339.28  E-value: 2.93e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310   115 YNHSV-TDPEKLNNYEPFSPEVYGETSFDLVAQMIDEIKMTEDDLFVDLGSGVGQVVLQVAAATNCKHHYGVEKADIPAK 193
Cdd:pfam08123    1 YSRSVsPDANKLNHYKAFSNEVYGELLPEFLSDVLDKCNLGPQDVFVDLGSGVGNCVLQAALEFGCKLSFGCEIMDNASN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310   194 YAETMDREFRKWMKWYGKKHAEYTLERGDFLSEEWRERI-ANTSVIFVNNFAFGPEVDHQLKERFANMKEGGRIVSSKPF 272
Cdd:pfam08123   81 LAELQDEEFKKRCKLFGKKLGKIEFIRGSFLDNERVEEIiPEADVILVNNFAFDPELNLQLKEMLQDLKDGCKIISLKSF 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 755534310   273 APLNFRINSRNLSDIGTIMRVVELSPLKGSVSWTGKPVSYYLHTI 317
Cdd:pfam08123  161 VPLNYRINFRNLSDIFNILKVEELKLPEGSVSWTSRGVEYYISTV 205
CC_DOT1L cd20902
coiled coil domain of disruptor of telomeric-silencing 1-like (DOT1L) and similar proteins; ...
 481-545 7.50e-34

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


:

Pssm-ID: 411016 [Multi-domain]  Cd Length: 65  Bit Score: 124.73  E-value: 7.50e-34
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755534310  481 ALQKLLESFRIQYLQFLAYTKTPQYKANLQQLLDQEKEKNTQLLGTAQQLFGHCQAQKEEIRRLF 545
Cdd:cd20902     1 ALQKLLESFKIQYLQFLAYMKTPQYKASLQQQIEQEKEKNKQLTGKAQQLEKQIQALQKEGVRLL 65
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
506-659 3.27e-10

Uncharacterized protein, contains DUF3084 domain [Function unknown];


:

Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 63.77  E-value: 3.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310  506 KANLQQLLDQEKEKNTQLLGTAQQLfghcQAQKEEIRRLfQQKLDELgvkaltYNDLIQAQKEISAHNQQL---REQSEQ 582
Cdd:COG4372    44 QEELEQLREELEQAREELEQLEEEL----EQARSELEQL-EEELEEL------NEQLQAAQAELAQAQEELeslQEEAEE 112

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755534310  583 LEKDNSELRSQsLRLLRARCEELRLDWSTL--SLENLRKEKQALRSQISEKQRHCLELQISIVELEKTQRQQELLQLKS 659
Cdd:COG4372   113 LQEELEELQKE-RQDLEQQRKQLEAQIAELqsEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLK 190
PHA03307 super family cl33723
transcriptional regulator ICP4; Provisional
 781-1125 6.34e-06

transcriptional regulator ICP4; Provisional


The actual alignment was detected with superfamily member PHA03307:

Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 51.33  E-value: 6.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310  781 RHLSQDHTGASKAATSEPHPRPEHPKESSLPyqSPGLSNSMKLSPQDPPLASPATSPltsekGSEKGVKERAYSSHGETI 860
Cdd:PHA03307   76 GTEAPANESRSTPTWSLSTLAPASPAREGSP--TPPGPSSPDPPPPTPPPASPPPSP-----APDLSEMLRPVGSPGPPP 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310  861 TSLPVSIPLSTVQPNKLPVSIPLASVVLPSRAERARSTPSPVPQPRDSSAtlekqtgasahgaggagagsrSLAVAPTGF 940
Cdd:PHA03307  149 AASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTP---------------------PAAASPRPP 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310  941 YAGSVAISGALASSPAPL---ASGMESAVFDESSGPSSLFATMGSRSTPPQHPPLLSQSRNSGPASPAHqltASPRLSVT 1017
Cdd:PHA03307  208 RRSSPISASASSPAPAPGrsaADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWN---GPSSRPGP 284

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310 1018 TQGSLPDTSKGELPSDPAFSDPESEAKRRIVFSISVGASSKQSPSTRHSPLTSG---TRGDCVQSHGQDS---------- 1084
Cdd:PHA03307  285 ASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGaavSPGPSPSRSPSPSrppppadpss 364

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 755534310 1085 RKRSRRKRASAGTPSLSTGVSPKRRALPTVAGLFTQSSGSP 1125
Cdd:PHA03307  365 PRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATG 405
Herpes_BLLF1 super family cl37540
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 942-1314 1.29e-03

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


The actual alignment was detected with superfamily member pfam05109:

Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 43.37  E-value: 1.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310   942 AGSVAISGALASSPAPLASGMESAVFDESSgPSSLFATMGSRSTPPQhPPLLSQSRNSgpASPAHQLTaSPRLSVTTQgs 1021
Cdd:pfam05109  479 AGTTSGASPVTPSPSPRDNGTESKAPDMTS-PTSAVTTPTPNATSPT-PAVTTPTPNA--TSPTLGKT-SPTSAVTTP-- 551

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310  1022 lpdTSKGELPSdPAFSDPESEAkrrivfsiSVGASSKQSPStrhSPLTSGTRGDCVQSHGQDSRKRSRRKRASAGTPSLS 1101
Cdd:pfam05109  552 ---TPNATSPT-PAVTTPTPNA--------TIPTLGKTSPT---SAVTTPTPNATSPTVGETSPQANTTNHTLGGTSSTP 616

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310  1102 TGVSPKRRALPTV-AGLFTQSSGSPLNLNSMVSNINQPLEITaisspesslksspTPYQDHDQPPVLRKERPLGLTNGAH 1180
Cdd:pfam05109  617 VVTSPPKNATSAVtTGQHNITSSSTSSMSLRPSSISETLSPS-------------TSDNSTSHMPLLTSAHPTGGENITQ 683

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310  1181 YSPLTSDE----------EPGSEDE---PSSARIERKIATISLESKSPPKTLENGGGLVGRKSAPSSEPINSSKWKSTFS 1247
Cdd:pfam05109  684 VTPASTSThhvstsspapRPGTTSQasgPGNSSTSTKPGEVNVTKGTPPKNATSPQAPSGQKTAVPTVTSTGGKANSTTG 763

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755534310  1248 PISDLGL-AKAVDSPLQAGSALSHSPLFSFRPSLE-EPAAEAKLptHPRKSFAG---SLGAAEGPSPGTNPP 1314
Cdd:pfam05109  764 GKHTTGHgARTSTEPTTDYGGDSTTPRTRYNATTYlPPSTSSKL--RPRWTFTSppvTTAQATVPVPPTSQP 833
 
Name Accession Description Interval E-value
DOT1 pfam08123
Histone methylation protein DOT1; The DOT1 domain regulates gene expression by methylating ...
 115-317 2.93e-107

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: 339.28  E-value: 2.93e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310   115 YNHSV-TDPEKLNNYEPFSPEVYGETSFDLVAQMIDEIKMTEDDLFVDLGSGVGQVVLQVAAATNCKHHYGVEKADIPAK 193
Cdd:pfam08123    1 YSRSVsPDANKLNHYKAFSNEVYGELLPEFLSDVLDKCNLGPQDVFVDLGSGVGNCVLQAALEFGCKLSFGCEIMDNASN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310   194 YAETMDREFRKWMKWYGKKHAEYTLERGDFLSEEWRERI-ANTSVIFVNNFAFGPEVDHQLKERFANMKEGGRIVSSKPF 272
Cdd:pfam08123   81 LAELQDEEFKKRCKLFGKKLGKIEFIRGSFLDNERVEEIiPEADVILVNNFAFDPELNLQLKEMLQDLKDGCKIISLKSF 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 755534310   273 APLNFRINSRNLSDIGTIMRVVELSPLKGSVSWTGKPVSYYLHTI 317
Cdd:pfam08123  161 VPLNYRINFRNLSDIFNILKVEELKLPEGSVSWTSRGVEYYISTV 205
CC_DOT1L cd20902
coiled coil domain of disruptor of telomeric-silencing 1-like (DOT1L) and similar proteins; ...
 481-545 7.50e-34

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


Pssm-ID: 411016 [Multi-domain]  Cd Length: 65  Bit Score: 124.73  E-value: 7.50e-34
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755534310  481 ALQKLLESFRIQYLQFLAYTKTPQYKANLQQLLDQEKEKNTQLLGTAQQLFGHCQAQKEEIRRLF 545
Cdd:cd20902     1 ALQKLLESFKIQYLQFLAYMKTPQYKASLQQQIEQEKEKNKQLTGKAQQLEKQIQALQKEGVRLL 65
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
506-659 3.27e-10

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 63.77  E-value: 3.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310  506 KANLQQLLDQEKEKNTQLLGTAQQLfghcQAQKEEIRRLfQQKLDELgvkaltYNDLIQAQKEISAHNQQL---REQSEQ 582
Cdd:COG4372    44 QEELEQLREELEQAREELEQLEEEL----EQARSELEQL-EEELEEL------NEQLQAAQAELAQAQEELeslQEEAEE 112

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755534310  583 LEKDNSELRSQsLRLLRARCEELRLDWSTL--SLENLRKEKQALRSQISEKQRHCLELQISIVELEKTQRQQELLQLKS 659
Cdd:COG4372   113 LQEELEELQKE-RQDLEQQRKQLEAQIAELqsEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLK 190
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 510-659 3.52e-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: 3.52e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310   510 QQLLDQEKEKNTQLLGTAQQLfghcqaqKEEIRRLFQQKLDELgVKAL------TYNDLIQAQKEISAHNQ---QLREQS 580
Cdd:TIGR04523  273 QKELEQNNKKIKELEKQLNQL-------KSEISDLNNQKEQDW-NKELkselknQEKKLEEIQNQISQNNKiisQLNEQI 344

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310   581 EQLEKD--NSELRSQSL-RLLRARCEELRL-----DWSTLSLENLRKEKQALRSQIS--EKQRHCLELQISIVELEKTQR 650
Cdd:TIGR04523  345 SQLKKEltNSESENSEKqRELEEKQNEIEKlkkenQSYKQEIKNLESQINDLESKIQnqEKLNQQKDEQIKKLQQEKELL 424


                   ....*....
gi 755534310   651 QQELLQLKS 659
Cdd:TIGR04523  425 EKEIERLKE 433
MscS_porin pfam12795
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...
 474-659 1.96e-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: 50.76  E-value: 1.96e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310   474 LVAPTPPALQKLLESFRIQYL-QFLAytktpQYKANLQQLLDQEKEKNTQLLGTAQQLFGhCQAQKEEIRRLFQQKLDEL 552
Cdd:pfam12795   63 LQAKAEAAPKEILASLSLEELeQRLL-----QTSAQLQELQNQLAQLNSQLIELQTRPER-AQQQLSEARQRLQQIRNRL 136

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310   553 GVKALTYNDLIQAQK-EISAHNQQLREQSEQLEKdnsELRSQSLRLLRARceeLRLDWSTLSLENLRKEKQALRSQISEK 631
Cdd:pfam12795  137 NGPAPPGEPLSEAQRwALQAELAALKAQIDMLEQ---ELLSNNNRQDLLK---ARRDLLTLRIQRLEQQLQALQELLNEK 210

                          170       180
                   ....*....|....*....|....*...
gi 755534310   632 QRhclelqisiVELEKTQRQQELLQLKS 659
Cdd:pfam12795  211 RL---------QEAEQAVAQTEQLAEEA 229
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 781-1125 6.34e-06

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 51.33  E-value: 6.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310  781 RHLSQDHTGASKAATSEPHPRPEHPKESSLPyqSPGLSNSMKLSPQDPPLASPATSPltsekGSEKGVKERAYSSHGETI 860
Cdd:PHA03307   76 GTEAPANESRSTPTWSLSTLAPASPAREGSP--TPPGPSSPDPPPPTPPPASPPPSP-----APDLSEMLRPVGSPGPPP 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310  861 TSLPVSIPLSTVQPNKLPVSIPLASVVLPSRAERARSTPSPVPQPRDSSAtlekqtgasahgaggagagsrSLAVAPTGF 940
Cdd:PHA03307  149 AASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTP---------------------PAAASPRPP 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310  941 YAGSVAISGALASSPAPL---ASGMESAVFDESSGPSSLFATMGSRSTPPQHPPLLSQSRNSGPASPAHqltASPRLSVT 1017
Cdd:PHA03307  208 RRSSPISASASSPAPAPGrsaADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWN---GPSSRPGP 284

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310 1018 TQGSLPDTSKGELPSDPAFSDPESEAKRRIVFSISVGASSKQSPSTRHSPLTSG---TRGDCVQSHGQDS---------- 1084
Cdd:PHA03307  285 ASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGaavSPGPSPSRSPSPSrppppadpss 364

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 755534310 1085 RKRSRRKRASAGTPSLSTGVSPKRRALPTVAGLFTQSSGSP 1125
Cdd:PHA03307  365 PRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATG 405
PRK11281 PRK11281
mechanosensitive channel MscK;
477-654 8.50e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 44.13  E-value: 8.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310  477 PTPPALQKLLESFRIQYLQflaytkTPQYKA---NLQQLL------DQEKEKNTQLLGTAQQLFGHCQAQKEEIRRL--- 544
Cdd:PRK11281   36 PTEADVQAQLDALNKQKLL------EAEDKLvqqDLEQTLalldkiDRQKEETEQLKQQLAQAPAKLRQAQAELEALkdd 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310  545 ----FQQKLDELGVKAL------TYNDLIQAQKEISAHNQQLREQSEQLEKDNSELRSQSLRLlrarcEELRldwstlsl 614
Cdd:PRK11281  110 ndeeTRETLSTLSLRQLesrlaqTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRL-----QQIR-------- 176

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 755534310  615 eNLRKEKQALRSQISEKQRHCLELQISIVELEKTQRQQEL 654
Cdd:PRK11281  177 -NLLKGGKVGGKALRPSQRVLLQAEQALLNAQNDLQRKSL 215
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 942-1314 1.29e-03

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 43.37  E-value: 1.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310   942 AGSVAISGALASSPAPLASGMESAVFDESSgPSSLFATMGSRSTPPQhPPLLSQSRNSgpASPAHQLTaSPRLSVTTQgs 1021
Cdd:pfam05109  479 AGTTSGASPVTPSPSPRDNGTESKAPDMTS-PTSAVTTPTPNATSPT-PAVTTPTPNA--TSPTLGKT-SPTSAVTTP-- 551

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310  1022 lpdTSKGELPSdPAFSDPESEAkrrivfsiSVGASSKQSPStrhSPLTSGTRGDCVQSHGQDSRKRSRRKRASAGTPSLS 1101
Cdd:pfam05109  552 ---TPNATSPT-PAVTTPTPNA--------TIPTLGKTSPT---SAVTTPTPNATSPTVGETSPQANTTNHTLGGTSSTP 616

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310  1102 TGVSPKRRALPTV-AGLFTQSSGSPLNLNSMVSNINQPLEITaisspesslksspTPYQDHDQPPVLRKERPLGLTNGAH 1180
Cdd:pfam05109  617 VVTSPPKNATSAVtTGQHNITSSSTSSMSLRPSSISETLSPS-------------TSDNSTSHMPLLTSAHPTGGENITQ 683

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310  1181 YSPLTSDE----------EPGSEDE---PSSARIERKIATISLESKSPPKTLENGGGLVGRKSAPSSEPINSSKWKSTFS 1247
Cdd:pfam05109  684 VTPASTSThhvstsspapRPGTTSQasgPGNSSTSTKPGEVNVTKGTPPKNATSPQAPSGQKTAVPTVTSTGGKANSTTG 763

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755534310  1248 PISDLGL-AKAVDSPLQAGSALSHSPLFSFRPSLE-EPAAEAKLptHPRKSFAG---SLGAAEGPSPGTNPP 1314
Cdd:pfam05109  764 GKHTTGHgARTSTEPTTDYGGDSTTPRTRYNATTYlPPSTSSKL--RPRWTFTSppvTTAQATVPVPPTSQP 833
STAT5_CCD cd16855
Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family ...
 482-642 1.68e-03

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: 41.48  E-value: 1.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310  482 LQKLLESFRIQYlQFLayTKtpqYKANLQQLLDQEKEKNTQLLGTAQQlfghcqaQKEEIRRLFQQKLDELGVKALTynd 561
Cdd:cd16855    27 LQQKQESFVIQY-QES--QK---IQAQLQQLQQQPQNERIELEQQLQQ-------QKEQLEQLLNAKAQELLQLRME--- 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310  562 LIQAQKEISAHNQQLreQSEQLEKdnsEL----RSQ-----------SLRLLRARCEELrLD--WSTlslenlrkekqal 624
Cdd:cd16855    91 LADKFKKTIQLLSKL--QSRVLDE---ELiqwkRQQqlagngapfesNLDTIQEWCESL-AEiiWQN------------- 151

                         170
                  ....*....|....*...
gi 755534310  625 RSQISEKQRHCLELQISI 642
Cdd:cd16855   152 RQQIKRAERLKQKLPIPL 169
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 539-647 1.70e-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: 1.70e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310    539 EEIRRLFQQKLDELGVKALTYNDLIQAqkeISAHNQQLREQSEQLEKDNSELRSQSLRLLRARCEELRLDWSTLS----- 613
Cdd:smart00787  150 DENLEGLKEDYKLLMKELELLNSIKPK---LRDRKDALEEELRQLKQLEDELEDCDPTELDRAKEKLKKLLQEIMikvkk 226

                            90       100       110
                    ....*....|....*....|....*....|....
gi 755534310    614 LENLRKEKQALRSQISEKQRHCLELQISIVELEK 647
Cdd:smart00787  227 LEELEEELQELESKIEDLTNKKSELNTEIAEAEK 260
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 159-267 2.21e-03

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


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 39.34  E-value: 2.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310  159 FVDLGSGVGQvVLQVAAATNCKHHYGVEKADIPAKYAETmdrefrkwmKWYGKKHAEYTLERGDFlsEEWRERIANT-SV 237
Cdd:cd02440     2 VLDLGCGTGA-LALALASGPGARVTGVDISPVALELARK---------AAAALLADNVEVLKGDA--EELPPEADESfDV 69

                          90       100       110
                  ....*....|....*....|....*....|..
gi 755534310  238 IFVNN-FAFGPEVDHQLKERFAN-MKEGGRIV 267
Cdd:cd02440    70 IISDPpLHHLVEDLARFLEEARRlLKPGGVLV 101
 
Name Accession Description Interval E-value
DOT1 pfam08123
Histone methylation protein DOT1; The DOT1 domain regulates gene expression by methylating ...
 115-317 2.93e-107

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: 339.28  E-value: 2.93e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310   115 YNHSV-TDPEKLNNYEPFSPEVYGETSFDLVAQMIDEIKMTEDDLFVDLGSGVGQVVLQVAAATNCKHHYGVEKADIPAK 193
Cdd:pfam08123    1 YSRSVsPDANKLNHYKAFSNEVYGELLPEFLSDVLDKCNLGPQDVFVDLGSGVGNCVLQAALEFGCKLSFGCEIMDNASN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310   194 YAETMDREFRKWMKWYGKKHAEYTLERGDFLSEEWRERI-ANTSVIFVNNFAFGPEVDHQLKERFANMKEGGRIVSSKPF 272
Cdd:pfam08123   81 LAELQDEEFKKRCKLFGKKLGKIEFIRGSFLDNERVEEIiPEADVILVNNFAFDPELNLQLKEMLQDLKDGCKIISLKSF 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 755534310   273 APLNFRINSRNLSDIGTIMRVVELSPLKGSVSWTGKPVSYYLHTI 317
Cdd:pfam08123  161 VPLNYRINFRNLSDIFNILKVEELKLPEGSVSWTSRGVEYYISTV 205
CC_DOT1L cd20902
coiled coil domain of disruptor of telomeric-silencing 1-like (DOT1L) and similar proteins; ...
 481-545 7.50e-34

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


Pssm-ID: 411016 [Multi-domain]  Cd Length: 65  Bit Score: 124.73  E-value: 7.50e-34
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755534310  481 ALQKLLESFRIQYLQFLAYTKTPQYKANLQQLLDQEKEKNTQLLGTAQQLFGHCQAQKEEIRRLF 545
Cdd:cd20902     1 ALQKLLESFKIQYLQFLAYMKTPQYKASLQQQIEQEKEKNKQLTGKAQQLEKQIQALQKEGVRLL 65
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
506-659 3.27e-10

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 63.77  E-value: 3.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310  506 KANLQQLLDQEKEKNTQLLGTAQQLfghcQAQKEEIRRLfQQKLDELgvkaltYNDLIQAQKEISAHNQQL---REQSEQ 582
Cdd:COG4372    44 QEELEQLREELEQAREELEQLEEEL----EQARSELEQL-EEELEEL------NEQLQAAQAELAQAQEELeslQEEAEE 112

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755534310  583 LEKDNSELRSQsLRLLRARCEELRLDWSTL--SLENLRKEKQALRSQISEKQRHCLELQISIVELEKTQRQQELLQLKS 659
Cdd:COG4372   113 LQEELEELQKE-RQDLEQQRKQLEAQIAELqsEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLK 190
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
506-659 8.23e-09

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 59.53  E-value: 8.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310  506 KANLQQLLDQEKEKNTQLLGTAQQLfghcQAQKEEIRRLFQQkldelgvkaltyndLIQAQKEISAHNQQLREQSEQLEK 585
Cdd:COG4372    30 SEQLRKALFELDKLQEELEQLREEL----EQAREELEQLEEE--------------LEQARSELEQLEEELEELNEQLQA 91

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755534310  586 DNSELRS--QSLRLLRARCEELRLDwstlsLENLRKEKQALRSQISEkqrhcLELQISIVELEKTQRQQELLQLKS 659
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 ...
 510-659 3.52e-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: 3.52e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310   510 QQLLDQEKEKNTQLLGTAQQLfghcqaqKEEIRRLFQQKLDELgVKAL------TYNDLIQAQKEISAHNQ---QLREQS 580
Cdd:TIGR04523  273 QKELEQNNKKIKELEKQLNQL-------KSEISDLNNQKEQDW-NKELkselknQEKKLEEIQNQISQNNKiisQLNEQI 344

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310   581 EQLEKD--NSELRSQSL-RLLRARCEELRL-----DWSTLSLENLRKEKQALRSQIS--EKQRHCLELQISIVELEKTQR 650
Cdd:TIGR04523  345 SQLKKEltNSESENSEKqRELEEKQNEIEKlkkenQSYKQEIKNLESQINDLESKIQnqEKLNQQKDEQIKKLQQEKELL 424


                   ....*....
gi 755534310   651 QQELLQLKS 659
Cdd:TIGR04523  425 EKEIERLKE 433
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 504-692 2.08e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.10  E-value: 2.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310  504 QYKANLQQLLDQEKEKNTQLLGTAQQLfGHCQAQKEEIRRLFQQKLDELGVKALTYNDLIQAQKEISAHNQQLREQSEQL 583
Cdd:COG1196   313 ELEERLEELEEELAELEEELEELEEEL-EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310  584 EKDNSELRSQSLRLLRARcEELRLDwstlsLENLRKEKQALRSQISEKQRHCLELQISIVELEKTQRQQELLQLKScvpp 663
Cdd:COG1196   392 LRAAAELAAQLEELEEAE-EALLER-----LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL---- 461

                         170       180
                  ....*....|....*....|....*....
gi 755534310  664 dDALSLHLRGKGALGRELEADAGRLRLEL 692
Cdd:COG1196   462 -LELLAELLEEAALLEAALAELLEELAEA 489
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
504-657 4.36e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 54.77  E-value: 4.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310  504 QYKANLQQLLDQEKEKNT------------QLLGTAQQLFGHCQAQKEEIRRL--FQQKLDELGVKALTYNDLIQAQKEI 569
Cdd:COG4717    89 EYAELQEELEELEEELEEleaeleelreelEKLEKLLQLLPLYQELEALEAELaeLPERLEELEERLEELRELEEELEEL 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310  570 SAHNQQLREQSEQLEKDNSELRSQSLRLLRARCEELRLDwstlsLENLRKEKQALRSQISEKQRHCLELQISIVELEKTQ 649
Cdd:COG4717   169 EAELAELQEELEELLEQLSLATEEELQDLAEELEELQQR-----LAELEEELEEAQEELEELEEELEQLENELEAAALEE 243


                  ....*...
gi 755534310  650 RQQELLQL 657
Cdd:COG4717   244 RLKEARLL 251
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 504-658 1.01e-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: 53.91  E-value: 1.01e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310   504 QYKANLQQLLDQEKEKNTQLLGTAQQLFGhCQAQKEEIRRLFQQKLDELGVKALTYNDLIQAQKEISAHNQQLREQSEQL 583
Cdd:TIGR02168  236 ELREELEELQEELKEAEEELEELTAELQE-LEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANL 314

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755534310   584 EKDNSELRSQSLRLLRARcEELRLDWSTLS--LENLRKEKQALRSQISEKQRHCLELQISIVELEK--TQRQQELLQLK 658
Cdd:TIGR02168  315 ERQLEELEAQLEELESKL-DELAEELAELEekLEELKEELESLEAELEELEAELEELESRLEELEEqlETLRSKVAQLE 392
MscS_porin pfam12795
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...
 474-659 1.96e-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: 50.76  E-value: 1.96e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310   474 LVAPTPPALQKLLESFRIQYL-QFLAytktpQYKANLQQLLDQEKEKNTQLLGTAQQLFGhCQAQKEEIRRLFQQKLDEL 552
Cdd:pfam12795   63 LQAKAEAAPKEILASLSLEELeQRLL-----QTSAQLQELQNQLAQLNSQLIELQTRPER-AQQQLSEARQRLQQIRNRL 136

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310   553 GVKALTYNDLIQAQK-EISAHNQQLREQSEQLEKdnsELRSQSLRLLRARceeLRLDWSTLSLENLRKEKQALRSQISEK 631
Cdd:pfam12795  137 NGPAPPGEPLSEAQRwALQAELAALKAQIDMLEQ---ELLSNNNRQDLLK---ARRDLLTLRIQRLEQQLQALQELLNEK 210

                          170       180
                   ....*....|....*....|....*...
gi 755534310   632 QRhclelqisiVELEKTQRQQELLQLKS 659
Cdd:pfam12795  211 RL---------QEAEQAVAQTEQLAEEA 229
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 486-659 2.73e-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: 2.73e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310   486 LESFRIQYLQFLAYTKTPQYKANLQQLLDQeKEKNTQLLGTAQQLFGHCQAQKEEIRRLFQQKLDELGVKALTYNDLIQA 565
Cdd:TIGR04523  194 NKLLKLELLLSNLKKKIQKNKSLESQISEL-KKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEK 272

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310   566 QKEISAHNQQLREQSEQLEKDNSELRSqslrlLRARCEElrlDWSTL---SLENLRKEKQALRSQISEKQRHCLEL--QI 640
Cdd:TIGR04523  273 QKELEQNNKKIKELEKQLNQLKSEISD-----LNNQKEQ---DWNKElksELKNQEKKLEEIQNQISQNNKIISQLneQI 344

                          170       180       190
                   ....*....|....*....|....*....|...
gi 755534310   641 SIVELEKT--------------QRQQELLQLKS 659
Cdd:TIGR04523  345 SQLKKELTnsesensekqreleEKQNEIEKLKK 377
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 781-1125 6.34e-06

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 51.33  E-value: 6.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310  781 RHLSQDHTGASKAATSEPHPRPEHPKESSLPyqSPGLSNSMKLSPQDPPLASPATSPltsekGSEKGVKERAYSSHGETI 860
Cdd:PHA03307   76 GTEAPANESRSTPTWSLSTLAPASPAREGSP--TPPGPSSPDPPPPTPPPASPPPSP-----APDLSEMLRPVGSPGPPP 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310  861 TSLPVSIPLSTVQPNKLPVSIPLASVVLPSRAERARSTPSPVPQPRDSSAtlekqtgasahgaggagagsrSLAVAPTGF 940
Cdd:PHA03307  149 AASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTP---------------------PAAASPRPP 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310  941 YAGSVAISGALASSPAPL---ASGMESAVFDESSGPSSLFATMGSRSTPPQHPPLLSQSRNSGPASPAHqltASPRLSVT 1017
Cdd:PHA03307  208 RRSSPISASASSPAPAPGrsaADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWN---GPSSRPGP 284

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310 1018 TQGSLPDTSKGELPSDPAFSDPESEAKRRIVFSISVGASSKQSPSTRHSPLTSG---TRGDCVQSHGQDS---------- 1084
Cdd:PHA03307  285 ASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGaavSPGPSPSRSPSPSrppppadpss 364

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 755534310 1085 RKRSRRKRASAGTPSLSTGVSPKRRALPTVAGLFTQSSGSP 1125
Cdd:PHA03307  365 PRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATG 405
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 488-691 6.73e-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: 6.73e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310   488 SFRIQYLQFLAYTKTPQYKANLQQLLDQEKEKNTQLlgtaqQLFGHCQAQKEEIRRLFQQKLDELGVKALTyndLIQAQK 567
Cdd:pfam15921  425 NMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESL-----EKVSSLTAQLESTKEMLRKVVEELTAKKMT---LESSER 496

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310   568 EISAHNQQLREQSEQLEKDNSE---LRSQ----------------SLRLLRARCEELRLDWSTLS--LENLRKEKQALRS 626
Cdd:pfam15921  497 TVSDLTASLQEKERAIEATNAEitkLRSRvdlklqelqhlknegdHLRNVQTECEALKLQMAEKDkvIEILRQQIENMTQ 576

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755534310   627 QISEKQRHCLELQISIVELEK--TQRQQELLQLKscVPPDDalslhlrgKGALGRELEADAGRLRLE 691
Cdd:pfam15921  577 LVGQHGRTAGAMQVEKAQLEKeiNDRRLELQEFK--ILKDK--------KDAKIRELEARVSDLELE 633
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 504-656 9.61e-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: 50.44  E-value: 9.61e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310   504 QYKANLQQLLDQEKEKNTQL------LGTAQQLFGHCQAQKEEIRRLFQQKLDELGVKALTYNDLIQAQKEISAHNQQLR 577
Cdd:TIGR02168  306 ILRERLANLERQLEELEAQLeeleskLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLR 385

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310   578 EQSEQLEKDNSELRSQsLRLLRARCEELrldwsTLSLENLRKEKQALRSQISEKQRHCLELQISIV--ELEKTQRQQELL 655
Cdd:TIGR02168  386 SKVAQLELQIASLNNE-IERLEARLERL-----EDRRERLQQEIEELLKKLEEAELKELQAELEELeeELEELQEELERL 459


                   .
gi 755534310   656 Q 656
Cdd:TIGR02168  460 E 460
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 509-653 2.57e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 48.22  E-value: 2.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310  509 LQQLLDQEKEKNTQLLGTAQQLfghcqAQKEEIRRLFQQKLDELGVKALTY------------NDLIQAQKEISAHNQQL 576
Cdd:COG4942    95 LRAELEAQKEELAELLRALYRL-----GRQPPLALLLSPEDFLDAVRRLQYlkylaparreqaEELRADLAELAALRAEL 169

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755534310  577 REQSEQLEKDNSELRSQSLRLLRARCEELRLdwstlsLENLRKEKQALRSQISEKQRHCLELQISIVELEKTQRQQE 653
Cdd:COG4942   170 EAERAELEALLAELEEERAALEALKAERQKL------LARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
539-661 2.86e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.61  E-value: 2.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310  539 EEIRRLfQQKLDELGVKALTYNDLIQAQKEISAHNQQLREQSEQLEKDNSELRSQ-SLRLLRARCEELR--LDWSTLSLE 615
Cdd:COG4717    71 KELKEL-EEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLlQLLPLYQELEALEaeLAELPERLE 149

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 755534310  616 NLRKEKQA---LRSQISEKQRHCLELQISIVELEKTQRQQELLQLKSCV 661
Cdd:COG4717   150 ELEERLEElreLEEELEELEAELAELQEELEELLEQLSLATEEELQDLA 198
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 509-693 3.38e-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: 48.90  E-value: 3.38e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310   509 LQQLLDQEKEKNTQLLGTAQQLFGHCQAQKEEIRRLfQQKLDELGVKALTY--------NDLIQAQKEISAHNQQLREQS 580
Cdd:TIGR02168  773 AEEELAEAEAEIEELEAQIEQLKEELKALREALDEL-RAELTLLNEEAANLrerlesleRRIAATERRLEDLEEQIEELS 851

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310   581 EQLEKDNSELRSQSLRL----------------LRARCEELRLDWSTLS--LENLRKEKQALRSQISEKQrhcleLQISI 642
Cdd:TIGR02168  852 EDIESLAAEIEELEELIeeleseleallnerasLEEALALLRSELEELSeeLRELESKRSELRRELEELR-----EKLAQ 926

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 755534310   643 VELEKTQRQQELLQLKS------CVPPDDALSLHLRGKGALgRELEADAGRLRLELD 693
Cdd:TIGR02168  927 LELRLEGLEVRIDNLQErlseeySLTLEEAEALENKIEDDE-EEARRRLKRLENKIK 982
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 481-691 4.44e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.39  E-value: 4.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310  481 ALQKLLESFRIQyLQFLAYTktpQYKANLQQLLDQEKEKNTQLLGTAQQLfGHCQAQKEEIRRLFQQKLDELGVKALTYN 560
Cdd:COG1196   217 ELKEELKELEAE-LLLLKLR---ELEAELEELEAELEELEAELEELEAEL-AELEAELEELRLELEELELELEEAQAEEY 291

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310  561 DLIQAQKEISAHNQQLREQSEQLEKDNSELRSQsLRLLRARCEEL--RLDWSTLSLENLRKEKQALRSQISEKQRHCLEL 638
Cdd:COG1196   292 ELLAELARLEQDIARLEERRRELEERLEELEEE-LAELEEELEELeeELEELEEELEEAEEELEEAEAELAEAEEALLEA 370

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 755534310  639 QISIVELEKT--QRQQELLQLKScvppdDALSLHLRGKGALGRELEADAGRLRLE 691
Cdd:COG1196   371 EAELAEAEEEleELAEELLEALR-----AAAELAAQLEELEEAEEALLERLERLE 420
MscS_porin pfam12795
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...
 478-658 4.80e-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: 46.53  E-value: 4.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310   478 TPPALQKLLESFRiQYLQFLAYTKTPQYKAN-LQQLLDQekekntqllgTAQQLfghcQAQKEEIRRLFQQKLDELgVKA 556
Cdd:pfam12795   11 DEAAKKKLLQDLQ-QALSLLDKIDASKQRAAaYQKALDD----------APAEL----RELRQELAALQAKAEAAP-KEI 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310   557 LTYNDLIQAQKEISAHNQQLREQSEQLEKDNSELRSQSLRLLRARCE-----------ELRLDWSTLSLENLRK------ 619
Cdd:pfam12795   75 LASLSLEELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQlsearqrlqqiRNRLNGPAPPGEPLSEaqrwal 154

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 755534310   620 --EKQALRSQISEKQrhcLELQISIVELEKTQRQQELLQLK 658
Cdd:pfam12795  155 qaELAALKAQIDMLE---QELLSNNNRQDLLKARRDLLTLR 192
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 498-692 5.90e-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: 48.14  E-value: 5.90e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310   498 AYTKTPQYKANLQQLLDQEKEKNTQLLGtaqqlfghCQAQKEEIRRLFQQKLDELGVkaltyndliqAQKEISAhnqqLR 577
Cdd:TIGR02169  665 GILFSRSEPAELQRLRERLEGLKRELSS--------LQSELRRIENRLDELSQELSD----------ASRKIGE----IE 722

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310   578 EQSEQLEKDnselrsqsLRLLRARCEELRLDWSTLS--LENLRKEKQALRSQISEKQRHCLELQISIVELEKTQRQQELL 655
Cdd:TIGR02169  723 KEIEQLEQE--------EEKLKERLEELEEDLSSLEqeIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIP 794

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 755534310   656 QLkscvppDDALS----LHLRGKGALgRELEADAGRLRLEL 692
Cdd:TIGR02169  795 EI------QAELSkleeEVSRIEARL-REIEQKLNRLTLEK 828
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 738-1127 6.13e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 47.86  E-value: 6.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310  738 ASPLDQEVVPCTPSHSGRPRLEKLSGLALPDYTRLSPAKIVLRRHLSQDHTGASKAATSEPHPRPEHPKESSLPYQSPGL 817
Cdd:PHA03307   59 AAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEML 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310  818 SNSMKLSPQDPPLASPATSPLTSEKGSEKGVKERAY--SSHGETITSL-------PVSIPLSTVQPNKLPVSIPLASVVL 888
Cdd:PHA03307  139 RPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALplSSPEETARAPssppaepPPSTPPAAASPRPPRRSSPISASAS 218

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310  889 PSRAERARSTPSPVPQPRDSSATLEKQTGASAHGAGGAGAGSrSLAVAPTGFYAGSVAISGALASSPAPLASGmesavfD 968
Cdd:PHA03307  219 SPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRP-APITLPTRIWEASGWNGPSSRPGPASSSSS------P 291

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310  969 ESSGPSSLFATMGSRSTPPQHPPLLSQS--RNSGPASPAHQlTASPRLSVTTQGSLPDTSkGELPSDPAFSDPESEAKRr 1046
Cdd:PHA03307  292 RERSPSPSPSSPGSGPAPSSPRASSSSSssRESSSSSTSSS-SESSRGAAVSPGPSPSRS-PSPSRPPPPADPSSPRKR- 368

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310 1047 ivfsisvGASSKQSPSTRHSPLTSGTRGdcvqshgqdsrkrSRRKRASAGTPSLSTGVSPKRRALPTVAGLFTQSSGSPL 1126
Cdd:PHA03307  369 -------PRPSRAPSSPAASAGRPTRRR-------------ARAAVAGRARRRDATGRFPAGRPRPSPLDAGAASGAFYA 428


                  .
gi 755534310 1127 N 1127
Cdd:PHA03307  429 R 429
flagell_FliJ TIGR02473
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ...
 509-633 8.22e-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: 44.23  E-value: 8.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310   509 LQQLLD---QEKEKNTQLLGTAQQLFGHCQAQKEEIRrlfqQKLDELGVKALTYNDLIQAQKEISAHNQQLReqseQLEK 585
Cdd:TIGR02473    4 LQKLLDlreKEEEQAKLELAKAQAEFERLETQLQQLI----KYREEYEQQALEKVGAGTSALELSNYQRFIR----QLDQ 75

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 755534310   586 DNSELRsQSLRLLRARCEELRLDWSTL-----SLENLrKEKQALRSQISEKQR 633
Cdd:TIGR02473   76 RIQQQQ-QELALLQQEVEAKRERLLEArrelkALEKL-KEKKQKEYRAEEAKR 126
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
543-656 8.39e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.82  E-value: 8.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310  543 RLFQQKLDELGVKALTYNDLIQAQKEISAHNQQLREQSEQLEKDNSELRSQSLRLLRARcEEL-----RLDWSTLSLENL 617
Cdd:COG4372    14 SLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQAR-SELeqleeELEELNEQLQAA 92

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 755534310  618 RKEKQALRSQISEKQRHCLELQIsivELEKTQRQQELLQ 656
Cdd:COG4372    93 QAELAQAQEELESLQEEAEELQE---ELEELQKERQDLE 128
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 506-659 1.36e-04

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 46.55  E-value: 1.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310   506 KANLQQLLDQEKEKNTQLLGTAQQLfghcQAQKE----EIRRLFQQKLD----------ELGVKALTYNDLiqaQKEISA 571
Cdd:TIGR04523  393 INDLESKIQNQEKLNQQKDEQIKKL----QQEKEllekEIERLKETIIKnnseikdltnQDSVKELIIKNL---DNTRES 465

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310   572 HNQQLREQSEQLEKDNSELRSQSlrllrarcEELRLDwsTLSLENLRKEKQALRSQISE--KQRHCLELQISIVELEKTQ 649
Cdd:TIGR04523  466 LETQLKVLSRSINKIKQNLEQKQ--------KELKSK--EKELKKLNEEKKELEEKVKDltKKISSLKEKIEKLESEKKE 535

                          170
                   ....*....|
gi 755534310   650 RQQELLQLKS 659
Cdd:TIGR04523  536 KESKISDLED 545
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 504-682 1.55e-04

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


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 46.27  E-value: 1.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310   504 QYKANLQQLLDQEKEKnTQLLGTAQQLFgHC------------QAQKEEIRRL------FQQKLDELGVKALTYNDLIQ- 564
Cdd:pfam05557   80 LKKKYLEALNKKLNEK-ESQLADAREVI-SClknelselrrqiQRAELELQSTnseleeLQERLDLLKAKASEAEQLRQn 157

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310   565 ---AQKEISAHNQQLRE----------QSEQLEKDNSELRS-----QSLRLLRARCEELRLDWSTLSLenLRKEKQALRS 626
Cdd:pfam05557  158 lekQQSSLAEAEQRIKElefeiqsqeqDSEIVKNSKSELARipeleKELERLREHNKHLNENIENKLL--LKEEVEDLKR 235

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 755534310   627 QIS--EKQRHclelQISIVELEKTQRQQEllqLKSCVPPDDALSLHLRGKGALGRELE 682
Cdd:pfam05557  236 KLEreEKYRE----EAATLELEKEKLEQE---LQSWVKLAQDTGLNLRSPEDLSRRIE 286
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
502-656 1.56e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 46.30  E-value: 1.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310  502 TPQYKANLQQLLDQEKEKNTQLLGTAQQLfgHCQAQKEEIRRLFQQK----LDELGVKALTYNDLIQAQKEISAHNQQLR 577
Cdd:COG4717   335 SPEELLELLDRIEELQELLREAEELEEEL--QLEELEQEIAALLAEAgvedEEELRAALEQAEEYQELKEELEELEEQLE 412

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755534310  578 EQSEQLEkdnSELRSQSLRLLRARceelrldwstlsLENLRKEKQALRSQISEKQRHCLELQISIVELEKTQRQQELLQ 656
Cdd:COG4717   413 ELLGELE---ELLEALDEEELEEE------------LEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQ 476
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 535-703 1.79e-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: 46.20  E-value: 1.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310   535 QAQKEE-IRRLF--QQKLDELgvkaltyNDLIqaqKEISAHNQQLREQSEQLEKdnselrsqsLRLLRARCEELRLDWST 611
Cdd:TIGR02168  171 KERRKEtERKLErtRENLDRL-------EDIL---NELERQLKSLERQAEKAER---------YKELKAELRELELALLV 231

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310   612 LSLENLRKEKQALRSQISEKQRHCLELQisiveLEKTQRQQELLQLKSCVPPDDALSLHLRGK----GALGRELEADAGR 687
Cdd:TIGR02168  232 LRLEELREELEELQEELKEAEEELEELT-----AELQELEEKLEELRLEVSELEEEIEELQKElyalANEISRLEQQKQI 306

                          170
                   ....*....|....*.
gi 755534310   688 LRLELDCAKISLPHLS 703
Cdd:TIGR02168  307 LRERLANLERQLEELE 322
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
486-630 2.83e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.53  E-value: 2.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310  486 LESFRIQYLQFLAYTKTPQYKANLQQLLDQEKEKNTQLLGTAQQlfghcQAQKEEIRRLfQQKLDELgvkaltYNDLIQA 565
Cdd:COG4717   384 EEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE-----EELEEELEEL-EEELEEL------EEELEEL 451

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755534310  566 QKEISAHNQQLreqsEQLEKDN--SELRsQSLRLLRARCEELRLDWSTLSL---------ENLRKEKQ-ALRSQISE 630
Cdd:COG4717   452 REELAELEAEL----EQLEEDGelAELL-QELEELKAELRELAEEWAALKLalelleearEEYREERLpPVLERASE 523
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 515-699 3.74e-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: 45.17  E-value: 3.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310   515 QEKEKNTQLL----GTAQQLFGHCQAQKEEIRRLFQQKLDELgvKALtyndLIQAQKEISAHNQQLREQSEqLEKDNSEL 590
Cdd:pfam01576  204 QELEKAKRKLegesTDLQEQIAELQAQIAELRAQLAKKEEEL--QAA----LARLEEETAQKNNALKKIRE-LEAQISEL 276

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310   591 RS--QSLRLLRARCEELRLDwstlslenLRKEKQALRSQISEKQRHCLELQisivELeKTQRQQELLQLKSCVPPD---- 664
Cdd:pfam01576  277 QEdlESERAARNKAEKQRRD--------LGEELEALKTELEDTLDTTAAQQ----EL-RSKREQEVTELKKALEEEtrsh 343

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 755534310   665 DALSLHLRGKGA-----LGRELEaDAGRLRLELDCAKISL 699
Cdd:pfam01576  344 EAQLQEMRQKHTqaleeLTEQLE-QAKRNKANLEKAKQAL 382
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 513-659 5.07e-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: 5.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310   513 LDQEKEKNTQLlgtaQQLFghcqaqKEEIRRLfQQKLDELGVKaltYNDLIQAQKEISAHNQQLREQSEQLEKDNSELRS 592
Cdd:TIGR04523  129 LEKQKKENKKN----IDKF------LTEIKKK-EKELEKLNNK---YNDLKKQKEELENELNLLEKEKLNIQKNIDKIKN 194

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755534310   593 QSLRLlrarceELRLdwstLSLENLRKEKQALRSQISEkqrhcLELQISIVELEKTQRQQELLQLKS 659
Cdd:TIGR04523  195 KLLKL------ELLL----SNLKKKIQKNKSLESQISE-----LKKQNNQLKDNIEKKQQEINEKTT 246
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
511-693 6.02e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.52  E-value: 6.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310  511 QLLDQEKEKNTQLLGTAQQLFGHCQAQKEEIRRLFQQKLDELgvkaltynDLIQAQKEISAHNQQLreqsEQLEKDNSEL 590
Cdd:COG4913   620 AELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEI--------DVASAEREIAELEAEL----ERLDASSDDL 687

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310  591 RSqslrllrarceelrldwstlslenLRKEKQALRSQIS--EKQRHCLELQISIVELEKTQRQQELLQLKSCV---PPDD 665
Cdd:COG4913   688 AA------------------------LEEQLEELEAELEelEEELDELKGEIGRLEKELEQAEEELDELQDRLeaaEDLA 743

                         170       180
                  ....*....|....*....|....*....
gi 755534310  666 ALSLHLRGKGALGREL-EADAGRLRLELD 693
Cdd:COG4913   744 RLELRALLEERFAAALgDAVERELRENLE 772
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 504-656 6.60e-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: 6.60e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310   504 QYKANLQQLLDqEKEKNTQLLGTAQQLFGHCQAQKEEIRRL------FQQKLDELG--------VKALTYNDLIQAQKEI 569
Cdd:pfam07888  203 QRDTQVLQLQD-TITTLTQKLTTAHRKEAENEALLEELRSLqerlnaSERKVEGLGeelssmaaQRDRTQAELHQARLQA 281

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310   570 SAHNQQL-------RE-------------QSEQLEKDNSELRSQSLRLLRARCEELRLDWSTLSLEnLRKEKQALRSQIS 629
Cdd:pfam07888  282 AQLTLQLadaslalREgrarwaqeretlqQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVE-LGREKDCNRVQLS 360

                          170       180       190
                   ....*....|....*....|....*....|..
gi 755534310   630 EKQRHCLELQISIVELEKTQRQ-----QELLQ 656
Cdd:pfam07888  361 ESRRELQELKASLRVAQKEKEQlqaekQELLE 392
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 498-692 7.90e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 44.28  E-value: 7.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310   498 AYTKTPQYKANLQQLLDQEKEKNTQLLGTAQQLFGH---CQAQKEEIRRLFQQKLDELGVKALTYNDLIQAQKEISAH-- 572
Cdd:TIGR02168  703 LRKELEELEEELEQLRKELEELSRQISALRKDLARLeaeVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAea 782

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310   573 ---------------NQQLREQSEQLEKDNSELRS--QSLRLLRARCEELRLDWSTL------SLENLRKEKQALRSQIS 629
Cdd:TIGR02168  783 eieeleaqieqlkeeLKALREALDELRAELTLLNEeaANLRERLESLERRIAATERRledleeQIEELSEDIESLAAEIE 862

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755534310   630 EKQRHCLELQISIVEL--EKTQRQQELLQLKSCVppdDALSLHLRGKGALGRELEADAGRLRLEL 692
Cdd:TIGR02168  863 ELEELIEELESELEALlnERASLEEALALLRSEL---EELSEELRELESKRSELRRELEELREKL 924
PRK11281 PRK11281
mechanosensitive channel MscK;
477-654 8.50e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 44.13  E-value: 8.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310  477 PTPPALQKLLESFRIQYLQflaytkTPQYKA---NLQQLL------DQEKEKNTQLLGTAQQLFGHCQAQKEEIRRL--- 544
Cdd:PRK11281   36 PTEADVQAQLDALNKQKLL------EAEDKLvqqDLEQTLalldkiDRQKEETEQLKQQLAQAPAKLRQAQAELEALkdd 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310  545 ----FQQKLDELGVKAL------TYNDLIQAQKEISAHNQQLREQSEQLEKDNSELRSQSLRLlrarcEELRldwstlsl 614
Cdd:PRK11281  110 ndeeTRETLSTLSLRQLesrlaqTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRL-----QQIR-------- 176

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 755534310  615 eNLRKEKQALRSQISEKQRHCLELQISIVELEKTQRQQEL 654
Cdd:PRK11281  177 -NLLKGGKVGGKALRPSQRVLLQAEQALLNAQNDLQRKSL 215
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 511-656 8.54e-04

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


Pssm-ID: 462536 [Multi-domain]  Cd Length: 176  Bit Score: 41.84  E-value: 8.54e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310   511 QLLDQE---KEKNTQLLGTAQQLFGHCQAQKEEIRRLFQQKLDELGVKALTYN-DLIQAQKEISAHNQQLREQSEQLEKD 586
Cdd:pfam08614   11 RLLDRTallEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQLReELAELYRSRGELAQRLVDLNEELQEL 90

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755534310   587 NSELRSQS--LRLLRARCEEL--RLDWSTLSLENLRKEKQALRSQISEkqrhcLELQISIVE--LEKTQRQ-QELLQ 656
Cdd:pfam08614   91 EKKLREDErrLAALEAERAQLeeKLKDREEELREKRKLNQDLQDELVA-----LQLQLNMAEekLRKLEKEnRELVE 162
PRK10246 PRK10246
exonuclease subunit SbcC; Provisional
 497-656 1.00e-03

exonuclease subunit SbcC; Provisional


Pssm-ID: 182330 [Multi-domain]  Cd Length: 1047  Bit Score: 44.02  E-value: 1.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310  497 LAYTKTPQYKANLQQLLDQEKEKNTQLLGTAQQL------FGHCQAQKEEIRRLFQQKLDELGVKALTYNDLIQAQKEIS 570
Cdd:PRK10246  280 LAALSLAQPARQLRPHWERIQEQSAALAHTRQQIeevntrLQSTMALRARIRHHAAKQSAELQAQQQSLNTWLAEHDRFR 359

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310  571 AHNQQL---REQSEQLEKDNSELRSQSLRLLRARCEELRLDWSTLSL---------------ENLRKEKQALRSQISEKQ 632
Cdd:PRK10246  360 QWNNELagwRAQFSQQTSDREQLRQWQQQLTHAEQKLNALPAITLTLtadevaaalaqhaeqRPLRQRLVALHGQIVPQQ 439

                         170       180
                  ....*....|....*....|....*.
gi 755534310  633 RHCLELQISIVEL--EKTQRQQELLQ 656
Cdd:PRK10246  440 KRLAQLQVAIQNVtqEQTQRNAALNE 465
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 496-709 1.15e-03

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 43.80  E-value: 1.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310   496 FLAYTKTPQYKANLQQLLDQEKEKNTQLLGTAQQLFGHCQAQKEEIRRLFQ--QKLDELGVKAL-------TYNDLIQAQ 566
Cdd:TIGR00618  465 AQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNParQDIDNPGPLTRrmqrgeqTYAQLETSE 544

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310   567 KEISAHNQQLREQSEQLEKDNSELRSQSLRLLRARCEelrldwSTLSLENLRKEKQALRSQIS-----------EKQRHC 635
Cdd:TIGR00618  545 EDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNR------SKEDIPNLQNITVRLQDLTEklseaedmlacEQHALL 618

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310   636 LELQISIVELEKTQRQQ---ELLQLKSCVPPDDALSL---HLRGKGALGRELEADAGRLR-LELDCAKISLPHLSSMSPE 708
Cdd:TIGR00618  619 RKLQPEQDLQDVRLHLQqcsQELALKLTALHALQLTLtqeRVREHALSIRVLPKELLASRqLALQKMQSEKEQLTYWKEM 698


                   .
gi 755534310   709 L 709
Cdd:TIGR00618  699 L 699
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 942-1314 1.29e-03

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 43.37  E-value: 1.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310   942 AGSVAISGALASSPAPLASGMESAVFDESSgPSSLFATMGSRSTPPQhPPLLSQSRNSgpASPAHQLTaSPRLSVTTQgs 1021
Cdd:pfam05109  479 AGTTSGASPVTPSPSPRDNGTESKAPDMTS-PTSAVTTPTPNATSPT-PAVTTPTPNA--TSPTLGKT-SPTSAVTTP-- 551

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310  1022 lpdTSKGELPSdPAFSDPESEAkrrivfsiSVGASSKQSPStrhSPLTSGTRGDCVQSHGQDSRKRSRRKRASAGTPSLS 1101
Cdd:pfam05109  552 ---TPNATSPT-PAVTTPTPNA--------TIPTLGKTSPT---SAVTTPTPNATSPTVGETSPQANTTNHTLGGTSSTP 616

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310  1102 TGVSPKRRALPTV-AGLFTQSSGSPLNLNSMVSNINQPLEITaisspesslksspTPYQDHDQPPVLRKERPLGLTNGAH 1180
Cdd:pfam05109  617 VVTSPPKNATSAVtTGQHNITSSSTSSMSLRPSSISETLSPS-------------TSDNSTSHMPLLTSAHPTGGENITQ 683

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310  1181 YSPLTSDE----------EPGSEDE---PSSARIERKIATISLESKSPPKTLENGGGLVGRKSAPSSEPINSSKWKSTFS 1247
Cdd:pfam05109  684 VTPASTSThhvstsspapRPGTTSQasgPGNSSTSTKPGEVNVTKGTPPKNATSPQAPSGQKTAVPTVTSTGGKANSTTG 763

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755534310  1248 PISDLGL-AKAVDSPLQAGSALSHSPLFSFRPSLE-EPAAEAKLptHPRKSFAG---SLGAAEGPSPGTNPP 1314
Cdd:pfam05109  764 GKHTTGHgARTSTEPTTDYGGDSTTPRTRYNATTYlPPSTSSKL--RPRWTFTSppvTTAQATVPVPPTSQP 833
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 504-659 1.39e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 43.47  E-value: 1.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310   504 QYKANLQQLLDQEKEKNTQLlgtaqqlfghcQAQKEEIrrlfQQKLDELGVKALTYNDLIQAQKEISAHNQQLREQSEQL 583
Cdd:TIGR04523  381 SYKQEIKNLESQINDLESKI-----------QNQEKLN----QQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDL 445

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310   584 EKDNSELRsqslrllrarceelrldwstLSLENLRKEKQALRSQISEkqrhcLELQISIVE--LEKTQRQ-----QELLQ 656
Cdd:TIGR04523  446 TNQDSVKE--------------------LIIKNLDNTRESLETQLKV-----LSRSINKIKqnLEQKQKElkskeKELKK 500


                   ...
gi 755534310   657 LKS 659
Cdd:TIGR04523  501 LNE 503
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 500-744 1.45e-03

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 43.42  E-value: 1.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310   500 TKTPQYKanlqQLLDQEKEKNTQLLGTAQQLFGHCQAQKEEIRRLFQQKLDELGVKALTYNDLIQAQKEISAHNQQLREQ 579
Cdd:TIGR00618  173 FPLDQYT----QLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQK 248

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310   580 SEQLEKDNSelRSQSLRLLRARCEELRLDWSTLSLENLRKEKQALRSQISEKQRHCL-----------ELQISIVELEKT 648
Cdd:TIGR00618  249 REAQEEQLK--KQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTqieqqaqrihtELQSKMRSRAKL 326

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310   649 --QRQQELLQLKSCVPPDDALSLHLRGKGALGRELEADAGRlRLELDCAKISLPHLSSMSPELSmnghaASYELCNAASR 726
Cdd:TIGR00618  327 lmKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSI-REISCQQHTLTQHIHTLQQQKT-----TLTQKLQSLCK 400

                          250
                   ....*....|....*...
gi 755534310   727 PSSKQNTPQYLASPLDQE 744
Cdd:TIGR00618  401 ELDILQREQATIDTRTSA 418
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 510-658 1.47e-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: 1.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310   510 QQLLDQEKEKNTQLLGTAQQLFGHCQAQKEEIR-RLFQQKLDELGVKaltyNDLIQAQKEI-------SAHNQQLREQSE 581
Cdd:pfam13868  175 REEIEEEKEREIARLRAQQEKAQDEKAERDELRaKLYQEEQERKERQ----KEREEAEKKArqrqelqQAREEQIELKER 250

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310   582 QLEKDNSELRSQSLRLLRARCEELRLDwstlsLENLRKEKQ-------ALRSQISEKQRHCL-ELQISIVELEKTQRQQE 653
Cdd:pfam13868  251 RLAEEAEREEEEFERMLRKQAEDEEIE-----QEEAEKRRMkrlehrrELEKQIEEREEQRAaEREEELEEGERLREEEA 325


                   ....*
gi 755534310   654 LLQLK 658
Cdd:pfam13868  326 ERRER 330
STAT5_CCD cd16855
Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family ...
 482-642 1.68e-03

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: 41.48  E-value: 1.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310  482 LQKLLESFRIQYlQFLayTKtpqYKANLQQLLDQEKEKNTQLLGTAQQlfghcqaQKEEIRRLFQQKLDELGVKALTynd 561
Cdd:cd16855    27 LQQKQESFVIQY-QES--QK---IQAQLQQLQQQPQNERIELEQQLQQ-------QKEQLEQLLNAKAQELLQLRME--- 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310  562 LIQAQKEISAHNQQLreQSEQLEKdnsEL----RSQ-----------SLRLLRARCEELrLD--WSTlslenlrkekqal 624
Cdd:cd16855    91 LADKFKKTIQLLSKL--QSRVLDE---ELiqwkRQQqlagngapfesNLDTIQEWCESL-AEiiWQN------------- 151

                         170
                  ....*....|....*...
gi 755534310  625 RSQISEKQRHCLELQISI 642
Cdd:cd16855   152 RQQIKRAERLKQKLPIPL 169
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 539-647 1.70e-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: 1.70e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310    539 EEIRRLFQQKLDELGVKALTYNDLIQAqkeISAHNQQLREQSEQLEKDNSELRSQSLRLLRARCEELRLDWSTLS----- 613
Cdd:smart00787  150 DENLEGLKEDYKLLMKELELLNSIKPK---LRDRKDALEEELRQLKQLEDELEDCDPTELDRAKEKLKKLLQEIMikvkk 226

                            90       100       110
                    ....*....|....*....|....*....|....
gi 755534310    614 LENLRKEKQALRSQISEKQRHCLELQISIVELEK 647
Cdd:smart00787  227 LEELEEELQELESKIEDLTNKKSELNTEIAEAEK 260
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 509-630 2.09e-03

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


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 43.02  E-value: 2.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310  509 LQQLLDQEKEKNTQLLGTAQQLFGHCQAQKEEIRrlfqQKLDELGVKALTYndlIQAQKEIsahnQQLREQSEQLEKDNS 588
Cdd:COG3096   558 LLAELEAQLEELEEQAAEAVEQRSELRQQLEQLR----ARIKELAARAPAW---LAAQDAL----ERLREQSGEALADSQ 626

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 755534310  589 ELRSQSLRLLRarceelRLDWSTLSLENLRKEKQALRSQISE 630
Cdd:COG3096   627 EVTAAMQQLLE------REREATVERDELAARKQALESQIER 662
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 159-267 2.21e-03

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


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 39.34  E-value: 2.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310  159 FVDLGSGVGQvVLQVAAATNCKHHYGVEKADIPAKYAETmdrefrkwmKWYGKKHAEYTLERGDFlsEEWRERIANT-SV 237
Cdd:cd02440     2 VLDLGCGTGA-LALALASGPGARVTGVDISPVALELARK---------AAAALLADNVEVLKGDA--EELPPEADESfDV 69

                          90       100       110
                  ....*....|....*....|....*....|..
gi 755534310  238 IFVNN-FAFGPEVDHQLKERFAN-MKEGGRIV 267
Cdd:cd02440    70 IISDPpLHHLVEDLARFLEEARRlLKPGGVLV 101
PHA03247 PHA03247
large tegument protein UL36; Provisional
 799-1318 3.77e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 3.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310  799 HPRPEHPKESSLPYQSPGLSNSMKLSPQD----PPLASPATSPLTSEKGSEKgVKERAYS-SHG-ETITSLPVSIPlstv 872
Cdd:PHA03247 2477 APVYRRPAEARFPFAAGAAPDPGGGGPPDpdapPAPSRLAPAILPDEPVGEP-VHPRMLTwIRGlEELASDDAGDP---- 2551

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310  873 qpnklpvSIPLASVVLPSRAERARSTPSPVPQPRDSSATLEKQTGASAHGAGGAGAgsrslAVAPTGFYAGSVAisgalA 952
Cdd:PHA03247 2552 -------PPPLPPAAPPAAPDRSVPPPRPAPRPSEPAVTSRARRPDAPPQSARPRA-----PVDDRGDPRGPAP-----P 2614

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310  953 SSPAPLASGMESAVFDESSGPSSLFATMGSRSTPPQHPPLLSQSRNSGPASPAHQLTASPRLSVTTQGSLPDTSKGELPS 1032
Cdd:PHA03247 2615 SPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGS 2694

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310 1033 DPAFSDPESEAKrrivfsisvgasskqSPSTRHSPLTSGTRGDCVQSHGQDSRKRSRRKRASAGTPS-LSTGVSPKRRAL 1111
Cdd:PHA03247 2695 LTSLADPPPPPP---------------TPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAgPATPGGPARPAR 2759

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310 1112 PTVaglftqSSGSPlnlnsmvsninqpleitaisspesslksSPTPYQDHDQPPVLRKERPLGLTNGAHYSPLTSDEEPG 1191
Cdd:PHA03247 2760 PPT------TAGPP----------------------------APAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPA 2805

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310 1192 SEDEPSSARIERKIATISLESKSPPKTlenggglvgrksapSSEPINSSKWKSTFSPISDLGLAKAVDSPlqagsalshs 1271
Cdd:PHA03247 2806 DPPAAVLAPAAALPPAASPAGPLPPPT--------------SAQPTAPPPPPGPPPPSLPLGGSVAPGGD---------- 2861

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*..
gi 755534310 1272 plFSFRPSLEEPAAEAKLPTHPRKSFAGSLGAAEGPSPGTNPPNGLA 1318
Cdd:PHA03247 2862 --VRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPE 2906
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 528-658 3.89e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.98  E-value: 3.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310   528 QQLFGHCQAQKEEIRRLfQQKLDELGVK--ALTYnDLIQAQKEIsahnQQLREQSEQLeKDNSELRSQSLRLLRARCEEL 605
Cdd:TIGR02169  794 PEIQAELSKLEEEVSRI-EARLREIEQKlnRLTL-EKEYLEKEI----QELQEQRIDL-KEQIKSIEKEIENLNGKKEEL 866

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 755534310   606 --RLDWSTLSLENLRKEKQALRSQISEKQRHCLELQISIVELEkTQRQQELLQLK 658
Cdd:TIGR02169  867 eeELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELE-AQIEKKRKRLS 920
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 563-702 4.08e-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: 42.08  E-value: 4.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310   563 IQAQKEISAHNQQLREQSEQLEKDNSELRSQSLRLL-----RARCEElRLDWSTLSLENLRKEKQALRSQISEKQRHCLE 637
Cdd:pfam01576  457 IKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRqledeRNSLQE-QLEEEEEAKRNVERQLSTLQAQLSDMKKKLEE 535

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755534310   638 LQISIVELEKTQR--QQELlqlkscvppdDALSLHLRGKGALGRELEADAGRLRLELDCAKISLPHL 702
Cdd:pfam01576  536 DAGTLEALEEGKKrlQREL----------EALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQ 592
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
481-693 4.14e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.82  E-value: 4.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310  481 ALQKLLESFRIQYlqflaYTKTPQYKANLQQLLDQEKEKntqllgtAQQLFGHCQAQKEE--IRRLF-QQKLDELGVKAL 557
Cdd:COG4913   159 ALKARLKKQGVEF-----FDSFSAYLARLRRRLGIGSEK-------ALRLLHKTQSFKPIgdLDDFVrEYMLEEPDTFEA 226

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310  558 -------------TYNDLIQAQK------EISAHNQQLREQSEQLEKdNSELRS--------QSLRLLRARCEELRLDWS 610
Cdd:COG4913   227 adalvehfddlerAHEALEDAREqiellePIRELAERYAAARERLAE-LEYLRAalrlwfaqRRLELLEAELEELRAELA 305

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310  611 TL---------SLENLRKEKQALRSQISE-----KQRhcLELQISIVELEKTQRQQELLQLKSCV------PPDDA---L 667
Cdd:COG4913   306 RLeaelerleaRLDALREELDELEAQIRGnggdrLEQ--LEREIERLERELEERERRRARLEALLaalglpLPASAeefA 383

                         250       260
                  ....*....|....*....|....*.
gi 755534310  668 SLHLRGKGALgRELEADAGRLRLELD 693
Cdd:COG4913   384 ALRAEAAALL-EALEEELEALEEALA 408
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
 503-653 5.65e-03

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 41.58  E-value: 5.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310  503 PQYKANLQQLLDQEKEK-------------NTQLLGTAQQLFghcqaqkeEIRRLFQQKLDELGVKALTYNDLIQAQKEI 569
Cdd:PRK10929   78 PKLSAELRQQLNNERDEprsvppnmstdalEQEILQVSSQLL--------EKSRQAQQEQDRAREISDSLSQLPQQQTEA 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310  570 sahNQQLREQSEQL-----------EKDNSELRSQSLRLlRARCEELRLdwSTLSLENlRKEKQALRSQISEKQRHCLEL 638
Cdd:PRK10929  150 ---RRQLNEIERRLqtlgtpntplaQAQLTALQAESAAL-KALVDELEL--AQLSANN-RQELARLRSELAKKRSQQLDA 222

                         170
                  ....*....|....*.
gi 755534310  639 QISIVE-LEKTQRQQE 653
Cdd:PRK10929  223 YLQALRnQLNSQRQRE 238
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 509-639 7.69e-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: 40.83  E-value: 7.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310   509 LQQLLDQEKEKNTQLLGTAQQLFGHCQAQKEEIRRLfQQKLDELGVKAltynDLIQAQK-EISAhnqqLREQSEQLEK-- 585
Cdd:pfam05622   64 LQKQLEQLQEENFRLETARDDYRIKCEELEKEVLEL-QHRNEELTSLA----EEAQALKdEMDI----LRESSDKVKKle 134

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755534310   586 -----------DNSELRSQsLRLLrarcEELRLDW--STLSLENLRKEKQALRSQISEKQRHCLELQ 639
Cdd:pfam05622  135 atvetykkkleDLGDLRRQ-VKLL----EERNAEYmqRTLQLEEELKKANALRGQLETYKRQVQELH 196
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
481-656 8.72e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.77  E-value: 8.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310  481 ALQKLLESFRIQYLQFLAYTKTPQYKANLQQLLDQEKEKNTQLLGTaqqlfghcQAQKEEIRRLFQQKLDELGvkALTYN 560
Cdd:COG3206   193 EAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEA--------EARLAALRAQLGSGPDALP--ELLQS 262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534310  561 DLIQA-QKEISAHNQQLREQSEQLEKDNS---ELRSQSLRLLRARCEELRLDWSTLS--LENLRKEKQALRSQISEKQRH 634
Cdd:COG3206   263 PVIQQlRAQLAELEAELAELSARYTPNHPdviALRAQIAALRAQLQQEAQRILASLEaeLEALQAREASLQAQLAQLEAR 342

                         170       180
                  ....*....|....*....|..
gi 755534310  635 CLELQISIVELEKTQRQQELLQ 656
Cdd:COG3206   343 LAELPELEAELRRLEREVEVAR 364
 
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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