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Conserved domains on  [gi|2462568124|ref|XP_054178322|]
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histone-lysine N-methyltransferase, H3 lysine-79 specific isoform X5 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CC_DOT1L cd20902
coiled coil domain of disruptor of telomeric-silencing 1-like (DOT1L) and similar proteins; ...
 193-257 1.93e-32

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: 120.49  E-value: 1.93e-32
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462568124  193 ALQKLLESFKIQYLQFLAYTKTPQYKASLQELLGQEKEKNAQLLGAAQQLLSHCQAQKEEIRRLF 257
Cdd:cd20902      1 ALQKLLESFKIQYLQFLAYMKTPQYKASLQQQIEQEKEKNKQLTGKAQQLEKQIQALQKEGVRLL 65
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
221-371 5.44e-10

Uncharacterized protein, contains DUF3084 domain [Function unknown];


:

Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 63.00  E-value: 5.44e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  221 LQELLGQEKEKNAQLLGAAQQLlshcQAQKEEIRRLfQQKLDELgvkaltYNDLIQAQKEISAHNQQL---REQSEQLEQ 297
Cdd:COG4372     47 LEQLREELEQAREELEQLEEEL----EQARSELEQL-EEELEEL------NEQLQAAQAELAQAQEELeslQEEAEELQE 115

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462568124  298 DNRALRGQsLQLLKARCEELQLDWATLSLEKLLKEKQ--ALKSQISEKQRHCLELQISIVELEKSQRQQELLQLKS 371
Cdd:COG4372    116 ELEELQKE-RQDLEQQRKQLEAQIAELQSEIAEREEElkELEEQLESLQEELAALEQELQALSEAEAEQALDELLK 190
AdoMet_MTases super family cl17173
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 1-27 3.06e-07

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


The actual alignment was detected with superfamily member pfam08123:

Pssm-ID: 473071  Cd Length: 205  Bit Score: 52.69  E-value: 3.06e-07
                           10        20
                   ....*....|....*....|....*..
gi 2462568124    1 MRVVELSPLKGSVSWTGKPVSYYLHTI 27
Cdd:pfam08123  179 LKVEELKLPEGSVSWTSRGVEYYISTV 205
PHA03307 super family cl33723
transcriptional regulator ICP4; Provisional
 502-834 2.86e-03

transcriptional regulator ICP4; Provisional


The actual alignment was detected with superfamily member PHA03307:

Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.47  E-value: 2.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  502 PGRPAASELHSRAEHTKENGLPYQSPSVPGSMKLSPQDPRPLSPGALQLAGEKSSEKGLRERAYGSSGElitSLPISIPL 581
Cdd:PHA03307    81 ANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPA---ASPPAAGA 157

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  582 STVQPNKLPVSIPLASVVLPSRAERARSTPSPvlQPRDPsstlekqiganahgaGSRSLALAPAGFSYAGSVAISGALAG 661
Cdd:PHA03307   158 SPAAVASDAASSRQAALPLSSPEETARAPSSP--PAEPP---------------PSTPPAAASPRPPRRSSPISASASSP 220

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  662 SPASLTPGAEPA--TLDESSSSGSLFATVGSRSSTPQ-HPLLLAQPRNSLPASPAHQ-----LSSSPRLGGAAQGPLPEA 733
Cdd:PHA03307   221 APAPGRSAADDAgaSSSDSSSSESSGCGWGPENECPLpRPAPITLPTRIWEASGWNGpssrpGPASSSSSPRERSPSPSP 300

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  734 SKGDLP--------SDSGFSDPESEAKRrivfTITTGAGSAKQSPSSKHSPLTASARGDCVPSHGQDSRRRGRRKRASAG 805
Cdd:PHA03307   301 SSPGSGpapsspraSSSSSSSRESSSSS----TSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPS 376

                          330       340
                   ....*....|....*....|....*....
gi 2462568124  806 TPSLSAGVSPKRRALPSVAGLFTQPSGSP 834
Cdd:PHA03307   377 SPAASAGRPTRRRARAAVAGRARRRDATG 405
 
Name Accession Description Interval E-value
CC_DOT1L cd20902
coiled coil domain of disruptor of telomeric-silencing 1-like (DOT1L) and similar proteins; ...
 193-257 1.93e-32

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: 120.49  E-value: 1.93e-32
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462568124  193 ALQKLLESFKIQYLQFLAYTKTPQYKASLQELLGQEKEKNAQLLGAAQQLLSHCQAQKEEIRRLF 257
Cdd:cd20902      1 ALQKLLESFKIQYLQFLAYMKTPQYKASLQQQIEQEKEKNKQLTGKAQQLEKQIQALQKEGVRLL 65
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
221-371 5.44e-10

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 63.00  E-value: 5.44e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  221 LQELLGQEKEKNAQLLGAAQQLlshcQAQKEEIRRLfQQKLDELgvkaltYNDLIQAQKEISAHNQQL---REQSEQLEQ 297
Cdd:COG4372     47 LEQLREELEQAREELEQLEEEL----EQARSELEQL-EEELEEL------NEQLQAAQAELAQAQEELeslQEEAEELQE 115

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462568124  298 DNRALRGQsLQLLKARCEELQLDWATLSLEKLLKEKQ--ALKSQISEKQRHCLELQISIVELEKSQRQQELLQLKS 371
Cdd:COG4372    116 ELEELQKE-RQDLEQQRKQLEAQIAELQSEIAEREEElkELEEQLESLQEELAALEQELQALSEAEAEQALDELLK 190
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 216-370 1.78e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 56.22  E-value: 1.78e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  216 QYKASLQELLgQEKEKNAQLLGAAQQLLSHCQAQKEEIRRLFQQKLDELGVKALTYNDLIQAQKEISAHNQQLREQSEQL 295
Cdd:TIGR02168  236 ELREELEELQ-EELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANL 314

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462568124  296 EQDNRALRGQsLQLLKARCEELQLDWATLS--LEKLLKEKQALKSQISEKQRHCLELQISIVELEK--SQRQQELLQLK 370
Cdd:TIGR02168  315 ERQLEELEAQ-LEELESKLDELAEELAELEekLEELKEELESLEAELEELEAELEELESRLEELEEqlETLRSKVAQLE 392
DOT1 pfam08123
Histone methylation protein DOT1; The DOT1 domain regulates gene expression by methylating ...
 1-27 3.06e-07

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: 52.69  E-value: 3.06e-07
                           10        20
                   ....*....|....*....|....*..
gi 2462568124    1 MRVVELSPLKGSVSWTGKPVSYYLHTI 27
Cdd:pfam08123  179 LKVEELKLPEGSVSWTSRGVEYYISTV 205
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 216-394 2.50e-06

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: 52.05  E-value: 2.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  216 QYKASLQELLGQEKEKNAQLLGAAQQLLS--------HCQAQKE--EIRRL------FQQKLDELGVKALTYNDLIQ--- 276
Cdd:pfam05557   80 LKKKYLEALNKKLNEKESQLADAREVISClknelselRRQIQRAelELQSTnseleeLQERLDLLKAKASEAEQLRQnle 159

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  277 -AQKEISAHNQQLREqseqLEQDNrALRGQSLQLLKARCEELqldwatLSLEKLLKEKQALK---SQISEKQRHCLEL-- 350
Cdd:pfam05557  160 kQQSSLAEAEQRIKE----LEFEI-QSQEQDSEIVKNSKSEL------ARIPELEKELERLRehnKHLNENIENKLLLke 228

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462568124  351 -----------------QISIVELEKSQRQQEllqLKSCVPPDDALSLHLRGKGALGRELE 394
Cdd:pfam05557  229 evedlkrklereekyreEAATLELEKEKLEQE---LQSWVKLAQDTGLNLRSPEDLSRRIE 286
PRK11281 PRK11281
mechanosensitive channel MscK;
189-366 1.01e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 47.21  E-value: 1.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  189 PTPPALQKLLESFKIQYLQFLAytKTPQYKASLQELlgqekekNAQLLGAAQQLLshcQAQkEEIRRL-------FQQKL 261
Cdd:PRK11281    52 KLLEAEDKLVQQDLEQTLALLD--KIDRQKEETEQL-------KQQLAQAPAKLR---QAQ-AELEALkddndeeTRETL 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  262 DELGVKAL------TYNDLIQAQKEISAHNQQLREQSEQLEQDNRALRGQSLQLLKarceelqldwatlsLEKLLKEKQA 335
Cdd:PRK11281   119 STLSLRQLesrlaqTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQ--------------IRNLLKGGKV 184

                          170       180       190
                   ....*....|....*....|....*....|.
gi 2462568124  336 LKSQISEKQRHCLELQISIVELEKSQRQQEL 366
Cdd:PRK11281   185 GGKALRPSQRVLLQAEQALLNAQNDLQRKSL 215
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 216-370 1.55e-03

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 41.66  E-value: 1.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  216 QYKASLQELLG--QEKEKNAQ------LLGAAQQLLSHCQAQKEEIRRLfQQKLDELGVKAltyNDLIQAQ----KEISA 283
Cdd:cd00176      4 QFLRDADELEAwlSEKEELLSstdygdDLESVEALLKKHEALEAELAAH-EERVEALNELG---EQLIEEGhpdaEEIQE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  284 HNQQLREQSEQLEQ--DNRALR-GQSLQLLK--ARCEELqLDW-----ATL----------SLEKLLKEKQALKSQISEK 343
Cdd:cd00176     80 RLEELNQRWEELRElaEERRQRlEEALDLQQffRDADDL-EQWleekeAALasedlgkdleSVEELLKKHKELEEELEAH 158

                          170       180
                   ....*....|....*....|....*..
gi 2462568124  344 QRHCLELQISIVELEKSQRQQELLQLK 370
Cdd:cd00176    159 EPRLKSLNELAEELLEEGHPDADEEIE 185
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 502-834 2.86e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.47  E-value: 2.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  502 PGRPAASELHSRAEHTKENGLPYQSPSVPGSMKLSPQDPRPLSPGALQLAGEKSSEKGLRERAYGSSGElitSLPISIPL 581
Cdd:PHA03307    81 ANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPA---ASPPAAGA 157

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  582 STVQPNKLPVSIPLASVVLPSRAERARSTPSPvlQPRDPsstlekqiganahgaGSRSLALAPAGFSYAGSVAISGALAG 661
Cdd:PHA03307   158 SPAAVASDAASSRQAALPLSSPEETARAPSSP--PAEPP---------------PSTPPAAASPRPPRRSSPISASASSP 220

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  662 SPASLTPGAEPA--TLDESSSSGSLFATVGSRSSTPQ-HPLLLAQPRNSLPASPAHQ-----LSSSPRLGGAAQGPLPEA 733
Cdd:PHA03307   221 APAPGRSAADDAgaSSSDSSSSESSGCGWGPENECPLpRPAPITLPTRIWEASGWNGpssrpGPASSSSSPRERSPSPSP 300

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  734 SKGDLP--------SDSGFSDPESEAKRrivfTITTGAGSAKQSPSSKHSPLTASARGDCVPSHGQDSRRRGRRKRASAG 805
Cdd:PHA03307   301 SSPGSGpapsspraSSSSSSSRESSSSS----TSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPS 376

                          330       340
                   ....*....|....*....|....*....
gi 2462568124  806 TPSLSAGVSPKRRALPSVAGLFTQPSGSP 834
Cdd:PHA03307   377 SPAASAGRPTRRRARAAVAGRARRRDATG 405
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 210-308 4.27e-03

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


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 39.10  E-value: 4.27e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124   210 AYTKTPQYKASLQELLGQEKEKNAQLlgaaqqllshcQAQKEEIRRLfQQKLDELGVKaLTYNDLIQAQKEISAHNQQLR 289
Cdd:smart00935    9 ILQESPAGKAAQKQLEKEFKKRQAEL-----------EKLEKELQKL-KEKLQKDAAT-LSEAAREKKEKELQKKVQEFQ 75

                            90
                    ....*....|....*....
gi 2462568124   290 EQSEQLEQDNRALRGQSLQ 308
Cdd:smart00935   76 RKQQKLQQDLQKRQQEELQ 94
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
 46-393 6.87e-03

Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.


Pssm-ID: 430783 [Multi-domain]  Cd Length: 618  Bit Score: 40.90  E-value: 6.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124   46 EEQEAARRRQQRESKSNAATPTKGPEGKVAGPADAPMDSGAEEEKAGAATVKKPSPSKARKKKLNKKGRKMAGR---KRG 122
Cdd:pfam09731   83 KEEKKQVKIPRQSGVSSEVAEEEKEATKDAAEAKAQLPKSEQEKEKALEEVLKEAISKAESATAVAKEAKDDAIqavKAH 162

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  123 RPKKMNTANPERKP--KKNQTALDALHA-----------QTVSQTAASSPQD--AYRSPHS---PFYQLPPSVQRHSPNP 184
Cdd:pfam09731  163 TDSLKEASDTAEISreKATDSALQKAEAlaeklkevinlAKQSEEEAAPPLLdaAPETPPKlpeHLDNVEEKVEKAQSLA 242

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  185 LLVAPtppaLQKLLESFKIQYLQFLAyTKTPQYKASLQELLGQEKEKNAQLLGAAQ-------QLLSHCQAQKE------ 251
Cdd:pfam09731  243 KLVDQ----YKELVASERIVFQQELV-SIFPDIIPVLKEDNLLSNDDLNSLIAHAHreidqlsKKLAELKKREEkhiera 317

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  252 -EIRRLFQQKLDELGVKALTY---NDLIQAQKEISAHNQQLREQSE-----QLEQDNRALRGQSLQLLKARCEELQLDWA 322
Cdd:pfam09731  318 lEKQKEELDKLAEELSARLEEvraADEAQLRLEFEREREEIRESYEeklrtELERQAEAHEEHLKDVLVEQEIELQREFL 397

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462568124  323 TLSLEKLLKEKQALKSQISE-----KQRHCLELQISIVELEKSQRQQelLQLkSCVPPDDAL--SLHLRGKGALGREL 393
Cdd:pfam09731  398 QDIKEKVEEERAGRLLKLNEllanlKGLEKATSSHSEVEDENRKAQQ--LWL-AVEALRSTLedGSADSRPRPLVREL 472
 
Name Accession Description Interval E-value
CC_DOT1L cd20902
coiled coil domain of disruptor of telomeric-silencing 1-like (DOT1L) and similar proteins; ...
 193-257 1.93e-32

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: 120.49  E-value: 1.93e-32
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462568124  193 ALQKLLESFKIQYLQFLAYTKTPQYKASLQELLGQEKEKNAQLLGAAQQLLSHCQAQKEEIRRLF 257
Cdd:cd20902      1 ALQKLLESFKIQYLQFLAYMKTPQYKASLQQQIEQEKEKNKQLTGKAQQLEKQIQALQKEGVRLL 65
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
221-371 5.44e-10

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 63.00  E-value: 5.44e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  221 LQELLGQEKEKNAQLLGAAQQLlshcQAQKEEIRRLfQQKLDELgvkaltYNDLIQAQKEISAHNQQL---REQSEQLEQ 297
Cdd:COG4372     47 LEQLREELEQAREELEQLEEEL----EQARSELEQL-EEELEEL------NEQLQAAQAELAQAQEELeslQEEAEELQE 115

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462568124  298 DNRALRGQsLQLLKARCEELQLDWATLSLEKLLKEKQ--ALKSQISEKQRHCLELQISIVELEKSQRQQELLQLKS 371
Cdd:COG4372    116 ELEELQKE-RQDLEQQRKQLEAQIAELQSEIAEREEElkELEEQLESLQEELAALEQELQALSEAEAEQALDELLK 190
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 218-405 6.84e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 57.25  E-value: 6.84e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  218 KASLQELLGQEKEKNAQLLGAAQQLLSHCQAQKEEIRRLFQQKLDELGVKALTYNDLIQAQKEISAHNQQLREQSEQLEQ 297
Cdd:COG1196    304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  298 DNRALRG--QSLQLLKARCEELQLDWATLS--LEKLLKEKQALKSQISEKQRHCLELQISIVELEKSQRQQELLQLKSCV 373
Cdd:COG1196    384 LAEELLEalRAAAELAAQLEELEEAEEALLerLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 2462568124  374 PPDDALSLHLRGK---GALGRELEPDASRLHLELD 405
Cdd:COG1196    464 LLAELLEEAALLEaalAELLEELAEAAARLLLLLE 498
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 216-370 1.78e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 56.22  E-value: 1.78e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  216 QYKASLQELLgQEKEKNAQLLGAAQQLLSHCQAQKEEIRRLFQQKLDELGVKALTYNDLIQAQKEISAHNQQLREQSEQL 295
Cdd:TIGR02168  236 ELREELEELQ-EELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANL 314

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462568124  296 EQDNRALRGQsLQLLKARCEELQLDWATLS--LEKLLKEKQALKSQISEKQRHCLELQISIVELEK--SQRQQELLQLK 370
Cdd:TIGR02168  315 ERQLEELEAQ-LEELESKLDELAEELAELEekLEELKEELESLEAELEELEAELEELESRLEELEEqlETLRSKVAQLE 392
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
205-369 2.19e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 55.69  E-value: 2.19e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  205 YLQFLAYTKTPQYKASLQELlGQEKEKNAQLLGAAQQLLSHCQAQKEEIRRLFQQKLDELgvkaltynDLIQAQKEISAH 284
Cdd:COG4913    603 VLGFDNRAKLAALEAELAEL-EEELAEAEERLEALEAELDALQERREALQRLAEYSWDEI--------DVASAEREIAEL 673

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  285 NQQLreqsEQLEQDNRALRGqslqlLKARCEELQLDWATLS--LEKLLKEKQALKSQISEKQRHCLELQISIVELEKSQR 362
Cdd:COG4913    674 EAEL----ERLDASSDDLAA-----LEEQLEELEAELEELEeeLDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLAR 744


                   ....*..
gi 2462568124  363 QQELLQL 369
Cdd:COG4913    745 LELRALL 751
DOT1 pfam08123
Histone methylation protein DOT1; The DOT1 domain regulates gene expression by methylating ...
 1-27 3.06e-07

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: 52.69  E-value: 3.06e-07
                           10        20
                   ....*....|....*....|....*..
gi 2462568124    1 MRVVELSPLKGSVSWTGKPVSYYLHTI 27
Cdd:pfam08123  179 LKVEELKLPEGSVSWTSRGVEYYISTV 205
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
216-369 1.08e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 53.23  E-value: 1.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  216 QYKASLQELLGQEKEKNA------------QLLGAAQQLLSHCQAQKEEIRRL--FQQKLDELGVKALTYNDLIQAQKEI 281
Cdd:COG4717     89 EYAELQEELEELEEELEEleaeleelreelEKLEKLLQLLPLYQELEALEAELaeLPERLEELEERLEELRELEEELEEL 168

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  282 SAHNQQLREQSEQLEQDNRALRGQSLQLLKARCEELQLDWATlsLEKLLKEKQALKSQISEKQRhclELQISIVELEKSQ 361
Cdd:COG4717    169 EAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAE--LEEELEEAQEELEELEEELE---QLENELEAAALEE 243


                   ....*...
gi 2462568124  362 RQQELLQL 369
Cdd:COG4717    244 RLKEARLL 251
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
202-400 1.43e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.00  E-value: 1.43e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  202 KIQYLQFLAyTKTPQYKASLQ-ELLGQEKEKNAQLLGAAQQLLSHCQAQ----KEEIRRLfQQKLDELGVKALTyndliQ 276
Cdd:COG4913    270 RLAELEYLR-AALRLWFAQRRlELLEAELEELRAELARLEAELERLEARldalREELDEL-EAQIRGNGGDRLE-----Q 342

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  277 AQKEISAHNQQLREQSEQLEQDNRALR--GQSLQLLKARCEELQLDWATLsLEKLLKEKQALksqisEKQRHCLELQISI 354
Cdd:COG4913    343 LEREIERLERELEERERRRARLEALLAalGLPLPASAEEFAALRAEAAAL-LEALEEELEAL-----EEALAEAEAALRD 416

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 2462568124  355 VELEKSQRQQELLQL---KSCVPPDdalSLHLRgkGALGRELEPDASRL 400
Cdd:COG4913    417 LRRELRELEAEIASLerrKSNIPAR---LLALR--DALAEALGLDEAEL 460
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 216-394 2.50e-06

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: 52.05  E-value: 2.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  216 QYKASLQELLGQEKEKNAQLLGAAQQLLS--------HCQAQKE--EIRRL------FQQKLDELGVKALTYNDLIQ--- 276
Cdd:pfam05557   80 LKKKYLEALNKKLNEKESQLADAREVISClknelselRRQIQRAelELQSTnseleeLQERLDLLKAKASEAEQLRQnle 159

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  277 -AQKEISAHNQQLREqseqLEQDNrALRGQSLQLLKARCEELqldwatLSLEKLLKEKQALK---SQISEKQRHCLEL-- 350
Cdd:pfam05557  160 kQQSSLAEAEQRIKE----LEFEI-QSQEQDSEIVKNSKSEL------ARIPELEKELERLRehnKHLNENIENKLLLke 228

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462568124  351 -----------------QISIVELEKSQRQQEllqLKSCVPPDDALSLHLRGKGALGRELE 394
Cdd:pfam05557  229 evedlkrklereekyreEAATLELEKEKLEQE---LQSWVKLAQDTGLNLRSPEDLSRRIE 286
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 216-366 2.90e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.98  E-value: 2.90e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  216 QYKASLQELLGQEKEKNAQLLGAAQQL------LSHCQAQKEEIRRLFQQKLDELGVKALTYNDLIQAQKEISAHNQQLR 289
Cdd:TIGR02168  306 ILRERLANLERQLEELEAQLEELESKLdelaeeLAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLR 385

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462568124  290 EQSEQLEQDNRALRGQsLQLLKARCEELQldwatLSLEKLLKEKQALKSQISEKQRHCLELQISIVELEKSQRQQEL 366
Cdd:TIGR02168  386 SKVAQLELQIASLNNE-IERLEARLERLE-----DRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEEL 456
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
251-373 2.92e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 51.69  E-value: 2.92e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  251 EEIRRLfQQKLDELGVKALTYNDLIQAQKEISAHNQQLREQSEQLEQDNRALRGQ-SLQLLKARCEELQLDWATLS--LE 327
Cdd:COG4717     71 KELKEL-EEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLlQLLPLYQELEALEAELAELPerLE 149

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2462568124  328 KLLKEKQALKS---QISEKQRHCLELQISIVELEKSQRQQELLQLKSCV 373
Cdd:COG4717    150 ELEERLEELREleeELEELEAELAELQEELEELLEQLSLATEEELQDLA 198
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 193-371 3.23e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.86  E-value: 3.23e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  193 ALQKLLESFKIQyLQFLAYTktpQYKASLQELLGQEKEKNAQLLGAAQQLlSHCQAQKEEIRRLFQQKLDELGVKALTYN 272
Cdd:COG1196    217 ELKEELKELEAE-LLLLKLR---ELEAELEELEAELEELEAELEELEAEL-AELEAELEELRLELEELELELEEAQAEEY 291

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  273 DLIQAQKEISAHNQQLREQSEQLEQDNRALRGQsLQLLKARCEEL--QLDWATLSLEKLLKEKQALKSQISEKQRHCLEL 350
Cdd:COG1196    292 ELLAELARLEQDIARLEERRRELEERLEELEEE-LAELEEELEELeeELEELEEELEEAEEELEEAEAELAEAEEALLEA 370

                          170       180
                   ....*....|....*....|...
gi 2462568124  351 QISIVELEK--SQRQQELLQLKS 371
Cdd:COG1196    371 EAELAEAEEelEELAEELLEALR 393
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 216-371 6.14e-06

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 50.79  E-value: 6.14e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  216 QYKASLQELlgqEKEKNAQLLGAAQQLLSHCQAQKEEIRrlfqqkldelgvkaltyNDLIQAQKEISAHNQQ---LREQS 292
Cdd:TIGR04523  292 QLKSEISDL---NNQKEQDWNKELKSELKNQEKKLEEIQ-----------------NQISQNNKIISQLNEQisqLKKEL 351

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  293 EQLEQDNRALRGQ------SLQLLKARCEELQLdwatlSLEKLLKEKQALKSQIS--EKQRHCLELQISIVELEKSQRQQ 364
Cdd:TIGR04523  352 TNSESENSEKQREleekqnEIEKLKKENQSYKQ-----EIKNLESQINDLESKIQnqEKLNQQKDEQIKKLQQEKELLEK 426


                   ....*..
gi 2462568124  365 ELLQLKS 371
Cdd:TIGR04523  427 EIERLKE 433
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 227-370 7.09e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.71  E-value: 7.09e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  227 QEKEKNAQLLGAAQQLLSHCQAQKEEIRRLFQQKLDELGVKALTYN-DLIQAQKEISAHNQQLREQSEQLEQDNRALRGQ 305
Cdd:COG1196    277 EELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEeELAELEEELEELEEELEELEEELEEAEEELEEA 356

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462568124  306 SLQLLKARCEELQldwATLSLEKLLKEKQALKSQISEKQRHCLELQISIVELEKSQRQQELLQLK 370
Cdd:COG1196    357 EAELAEAEEALLE---AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER 418
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 218-370 7.86e-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: 50.83  E-value: 7.86e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  218 KASLQELLGQEKEKNAQLLGAAQQLlSHCQAQKEEIRRLFQQKLDElgvkaltYNDLIQAQKEISAHNQQLREQSEQLEQ 297
Cdd:TIGR02168  837 ERRLEDLEEQIEELSEDIESLAAEI-EELEELIEELESELEALLNE-------RASLEEALALLRSELEELSEELRELES 908

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462568124  298 DNRALRgQSLQLLKARCEELQLDwatlsLEKLLKEKQALKSQISEKQRHCLELQI---SIVELEKSQRQQELLQLK 370
Cdd:TIGR02168  909 KRSELR-RELEELREKLAQLELR-----LEGLEVRIDNLQERLSEEYSLTLEEAEaleNKIEDDEEEARRRLKRLE 978
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
214-368 7.92e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 50.54  E-value: 7.92e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  214 TPQYKASLQELLGQEKEKNAQLLGAAQQLLshCQAQKEEIRRLFQQK----LDELGVKALTYNDLIQAQKEISAHNQQLR 289
Cdd:COG4717    335 SPEELLELLDRIEELQELLREAEELEEELQ--LEELEQEIAALLAEAgvedEEELRAALEQAEEYQELKEELEELEEQLE 412

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  290 EQSEQLEQdnrALRGQSLQLLKARCEELQLDWATLS--LEKLLKEKQALKSQISEkqrhclelqisiveLEKSQRQQELL 367
Cdd:COG4717    413 ELLGELEE---LLEALDEEELEEELEELEEELEELEeeLEELREELAELEAELEQ--------------LEEDGELAELL 475


                   .
gi 2462568124  368 Q 368
Cdd:COG4717    476 Q 476
Rootletin pfam15035
Ciliary rootlet component, centrosome cohesion;
203-370 9.38e-06

Ciliary rootlet component, centrosome cohesion;


Pssm-ID: 464459 [Multi-domain]  Cd Length: 190  Bit Score: 47.73  E-value: 9.38e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  203 IQYLQflayTKTPQYKASLQELLGQEKEKNAQLlgAAQQLLSHCQAQKEEIRRLFQQKLDELGVKALTYNDLIQAQKEIS 282
Cdd:pfam15035   18 VQKLQ----AKVLQYKKRCSELEQQLLEKTSEL--EKTELLLRKLTLEPRLQRLEREHSADLEEALIRLEEERQRSESLS 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  283 AHNQQLREQSEQLEQDNRALRgQSLQLLKArceelqlDWATLSLEKLLK------EKQALKSQISEKQRHCLELQISIVE 356
Cdd:pfam15035   92 QVNSLLREQLEQASRANEALR-EDLQKLTN-------DWERAREELEQKesewrkEEEAFNEYLSSEHSRLLSLWREVVA 163

                          170       180
                   ....*....|....*....|
gi 2462568124  357 LE------KSQRQQELLQLK 370
Cdd:pfam15035  164 VRrqftelKTATERDLSELK 183
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 222-371 1.00e-05

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 50.02  E-value: 1.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  222 QELLGQEKEKNaQLLGAAQQLLSHCQAQKEEIRRL--------------------FQQKLDELgvkALTYN----DLIQA 277
Cdd:TIGR04523  412 EQIKKLQQEKE-LLEKEIERLKETIIKNNSEIKDLtnqdsvkeliiknldntresLETQLKVL---SRSINkikqNLEQK 487

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  278 QKEISAHNQQ---LREQSEQLEQDNRALRGQSLQLL----KARCEELQLDWATLSLEKLLKE------KQALKSQISEKQ 344
Cdd:TIGR04523  488 QKELKSKEKElkkLNEEKKELEEKVKDLTKKISSLKekieKLESEKKEKESKISDLEDELNKddfelkKENLEKEIDEKN 567

                          170       180
                   ....*....|....*....|....*...
gi 2462568124  345 RHCLELQISIVELEKSQRQ-QELLQLKS 371
Cdd:TIGR04523  568 KEIEELKQTQKSLKKKQEEkQELIDQKE 595
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 210-371 1.10e-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: 50.07  E-value: 1.10e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  210 AYTKTPQYKASLQELlgQEKeknaqlLGAAQQLLSHCQAQKEEIRRLFQQKLDELgvKALTyNDLIQAQKEISAHNQQLR 289
Cdd:TIGR02169  665 GILFSRSEPAELQRL--RER------LEGLKRELSSLQSELRRIENRLDELSQEL--SDAS-RKIGEIEKEIEQLEQEEE 733

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  290 EQSEQLEQDNRALRG---------QSLQLLKARCEELQLDWATL--SLEKL--------LKEKQALKSQIsEKQRHCLEL 350
Cdd:TIGR02169  734 KLKERLEELEEDLSSleqeienvkSELKELEARIEELEEDLHKLeeALNDLearlshsrIPEIQAELSKL-EEEVSRIEA 812

                          170       180
                   ....*....|....*....|.
gi 2462568124  351 QISIVELEKSQRQQELLQLKS 371
Cdd:TIGR02169  813 RLREIEQKLNRLTLEKEYLEK 833
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 198-371 1.41e-05

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 49.63  E-value: 1.41e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  198 LESFKIQYLQFLAYTKTPQYKaSLQELLGQEKEKNAQLLGAAQQLLSHCQAQKEEIRRLFQQKLDELGVKALTYNDLIQA 277
Cdd:TIGR04523  194 NKLLKLELLLSNLKKKIQKNK-SLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEK 272

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  278 QKEISAHNQQLREQSEQLEQdnralrgqslqlLKARceelqldwatlsLEKLLKEKQA-----LKSQISEKQRHCLELQI 352
Cdd:TIGR04523  273 QKELEQNNKKIKELEKQLNQ------------LKSE------------ISDLNNQKEQdwnkeLKSELKNQEKKLEEIQN 328

                          170       180
                   ....*....|....*....|.
gi 2462568124  353 SIVELEK--SQRQQELLQLKS 371
Cdd:TIGR04523  329 QISQNNKiiSQLNEQISQLKK 349
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
255-371 1.86e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 48.75  E-value: 1.86e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  255 RLFQQKLDELGVKALTYNDLIQAQKEISAHNQQLREQSEQLEQDNRALRGQSLQLLKARcEEL-----QLDWATLSLEKL 329
Cdd:COG4372     14 SLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQAR-SELeqleeELEELNEQLQAA 92

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2462568124  330 LKEKQALKSQISEKQRHCLELQISIVELEKSQR--QQELLQLKS 371
Cdd:COG4372     93 QAELAQAQEELESLQEEAEELQEELEELQKERQdlEQQRKQLEA 136
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 222-365 2.91e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.78  E-value: 2.91e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  222 QELLGQEKEKNAQLLGAAQQLLshcQAQKEEIrrlfQQKLDELGvkaltyNDLIQAQKEISAHNQQLREQSEQLEQDNRA 301
Cdd:COG1196    216 RELKEELKELEAELLLLKLREL---EAELEEL----EAELEELE------AELEELEAELAELEAELEELRLELEELELE 282

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462568124  302 L--RGQSLQLLKARCEEL--QLDWATLSLEKLLKEKQALKSQISEKQRHCLELQISIVELEKSQRQQE 365
Cdd:COG1196    283 LeeAQAEEYELLAELARLeqDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE 350
DUF4686 pfam15742
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ...
 206-369 3.10e-05

Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.


Pssm-ID: 464838 [Multi-domain]  Cd Length: 384  Bit Score: 48.14  E-value: 3.10e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  206 LQFLAYTKTPQYKASLQELLGQEKEKNA----QLLGAAQQLLSHCQAQKEEIRRLFQQKLDElgvkaltynDLIQAQKEI 281
Cdd:pfam15742   97 LEVLKQAQSIKSQNSLQEKLAQEKSRVAdaeeKILELQQKLEHAHKVCLTDTCILEKKQLEE---------RIKEASENE 167

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  282 SAHNQQLREQSEQ---LEQDNRALRGQ--SLQLLKARCEE--LQLDWATLSLEKLLKEKQALKSQISEKQRHCLEL--QI 352
Cdd:pfam15742  168 AKLKQQYQEEQQKrklLDQNVNELQQQvrSLQDKEAQLEMtnSQQQLRIQQQEAQLKQLENEKRKSDEHLKSNQELseKL 247

                          170
                   ....*....|....*..
gi 2462568124  353 SIVELEKSQRQQELLQL 369
Cdd:pfam15742  248 SSLQQEKEALQEELQQV 264
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 219-365 4.02e-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: 47.84  E-value: 4.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  219 ASLQELLGQEKEKNAQLLGAAQQ--------LLSHCQAQKEEIRRL--FQQKLDELGVKAltyNDLIQAQKEISAHNQQL 288
Cdd:COG4942     93 AELRAELEAQKEELAELLRALYRlgrqpplaLLLSPEDFLDAVRRLqyLKYLAPARREQA---EELRADLAELAALRAEL 169

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462568124  289 REQSEQLEQDNRALRGQSLQLLKARCEELQLdwatlsLEKLLKEKQALKSQISEKQRHCLELQISIVELEKSQRQQE 365
Cdd:COG4942    170 EAERAELEALLAELEEERAALEALKAERQKL------LARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
MscS_porin pfam12795
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...
 193-371 6.32e-05

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


Pssm-ID: 432790 [Multi-domain]  Cd Length: 238  Bit Score: 46.14  E-value: 6.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  193 ALQKLLESF---------KIQYLQFLAYTKTPQY--KASLQELLGQEKEKNAQLLgAAQQLLSHCQAQKEEIR---RLFQ 258
Cdd:pfam12795   41 AYQKALDDApaelrelrqELAALQAKAEAAPKEIlaSLSLEELEQRLLQTSAQLQ-ELQNQLAQLNSQLIELQtrpERAQ 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  259 QKLDELgvkaltyndlIQAQKEISAHNQQLREQSEQLEQDNRALRGQSLQLLKARCEEL----------------QLDWA 322
Cdd:pfam12795  120 QQLSEA----------RQRLQQIRNRLNGPAPPGEPLSEAQRWALQAELAALKAQIDMLeqellsnnnrqdllkaRRDLL 189

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 2462568124  323 TLSLEKLLKEKQALKSQISEKQRhclelqisiVELEKSQRQQELLQLKS 371
Cdd:pfam12795  190 TLRIQRLEQQLQALQELLNEKRL---------QEAEQAVAQTEQLAEEA 229
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 218-370 7.18e-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: 47.76  E-value: 7.18e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  218 KASLQELLGQEKEKNAQL---LGAA--QQLLSHCQAQKEEIRRLfQQKLDELGVK--ALTYnDLIQAQKEIsahnQQLRE 290
Cdd:TIGR02169  767 IEELEEDLHKLEEALNDLearLSHSriPEIQAELSKLEEEVSRI-EARLREIEQKlnRLTL-EKEYLEKEI----QELQE 840

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  291 QSEQLEqDNRALRGQSLQLLKARCEEL--QLDWATLSLEKLLKEKQALKSQISEKQRHCLELQISIVELEkSQRQQELLQ 368
Cdd:TIGR02169  841 QRIDLK-EQIKSIEKEIENLNGKKEELeeELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELE-AQIEKKRKR 918


                   ..
gi 2462568124  369 LK 370
Cdd:TIGR02169  919 LS 920
PRK11281 PRK11281
mechanosensitive channel MscK;
189-366 1.01e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 47.21  E-value: 1.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  189 PTPPALQKLLESFKIQYLQFLAytKTPQYKASLQELlgqekekNAQLLGAAQQLLshcQAQkEEIRRL-------FQQKL 261
Cdd:PRK11281    52 KLLEAEDKLVQQDLEQTLALLD--KIDRQKEETEQL-------KQQLAQAPAKLR---QAQ-AELEALkddndeeTRETL 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  262 DELGVKAL------TYNDLIQAQKEISAHNQQLREQSEQLEQDNRALRGQSLQLLKarceelqldwatlsLEKLLKEKQA 335
Cdd:PRK11281   119 STLSLRQLesrlaqTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQ--------------IRNLLKGGKV 184

                          170       180       190
                   ....*....|....*....|....*....|.
gi 2462568124  336 LKSQISEKQRHCLELQISIVELEKSQRQQEL 366
Cdd:PRK11281   185 GGKALRPSQRVLLQAEQALLNAQNDLQRKSL 215
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
 218-351 1.01e-04

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


Pssm-ID: 462316 [Multi-domain]  Cd Length: 129  Bit Score: 43.40  E-value: 1.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  218 KASLQELLGQEKEKNAQLLGAAQQLLSHCQAQKEEIRRLfQQKldelgvkaltYNDLIQAQKEISAHNQQLREQSEQLEQ 297
Cdd:pfam07926    3 LSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREA-QQN----------YERELVLHAEDIKALQALREELNELKA 71

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462568124  298 DNRALRGQsLQLLKARCEELQLDWAtlslekllKEKQALKSQISEKQRHCLELQ 351
Cdd:pfam07926   72 EIAELKAE-AESAKAELEESEESWE--------EQKKELEKELSELEKRIEDLN 116
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
221-344 1.20e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 46.68  E-value: 1.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  221 LQELLGQEKEKNAQL---LGAAQQLLSHCQAQ--KEEIRRLfQQKLDELgvkaltYNDLIQAQKEISAHNQQLreqsEQL 295
Cdd:COG4717    397 YQELKEELEELEEQLeelLGELEELLEALDEEelEEELEEL-EEELEEL------EEELEELREELAELEAEL----EQL 465

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462568124  296 EQDNR--ALRgQSLQLLKARCEELQLDWATLSL-EKLLkeKQALKSQISEKQ 344
Cdd:COG4717    466 EEDGElaELL-QELEELKAELRELAEEWAALKLaLELL--EEAREEYREERL 514
Jnk-SapK_ap_N pfam09744
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ...
 240-345 1.45e-04

JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins conserved from yeasts to humans. Most of the proteins in this entry have an RhoGEF pfam00621 domain at their C-terminal end.


Pssm-ID: 462875 [Multi-domain]  Cd Length: 150  Bit Score: 43.76  E-value: 1.45e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  240 QQLLSHCQAQ-------KEEIRRLFQQKLDELGVKALTYNDLIQAQKEISAHNQQLREQSEQLEQDNRALRGQSLQLLKA 312
Cdd:pfam09744   39 ESLASRNQEHnveleelREDNEQLETQYEREKALRKRAEEELEEIEDQWEQETKDLLSQVESLEEENRRLEADHVSRLEE 118

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2462568124  313 RceELQLDWATLSLEKllKEKQALKS--QISEKQR 345
Cdd:pfam09744  119 K--EAELKKEYSKLHE--RETEVLRKlkEVVDRQR 149
CENP-F_leu_zip pfam10473
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ...
 218-357 2.25e-04

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


Pssm-ID: 463102 [Multi-domain]  Cd Length: 140  Bit Score: 42.67  E-value: 2.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  218 KASLQE-LLGQEKEKnaQLLGAAQ-QLLSHCQAQKEEIRRLfQQKLDELGVKaltyndLIQAQKEISAhnqqLREQSEQL 295
Cdd:pfam10473   19 ADSLKDkVENLEREL--EMSEENQeLAILEAENSKAEVETL-KAEIEEMAQN------LRDLELDLVT----LRSEKENL 85

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462568124  296 EQDnralrgqsLQLLKARCEELqlDWATLSLEKLLKEKQALKSQISEKQRHCLE-LQISIVEL 357
Cdd:pfam10473   86 TKE--------LQKKQERVSEL--ESLNSSLENLLEEKEQEKVQMKEESKTAVEmLQTQLKEL 138
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 219-371 2.38e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.70  E-value: 2.38e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  219 ASLQELLGQEKEKNAQLLGAAQQLLSHCQAQK---EEIRRLFQQKLDELGVKALTYNDLIQAQKEISAHNQQLREQSEQL 295
Cdd:COG1196    281 LELEEAQAEEYELLAELARLEQDIARLEERRReleERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462568124  296 EQDNRALRGQSLQLlkarcEELQLDWATLSLEKLLKEKQALKSQISEKQrhcLELQISIVELEKSQRQQELLQLKS 371
Cdd:COG1196    361 AEAEEALLEAEAEL-----AEAEEELEELAEELLEALRAAAELAAQLEE---LEEAEEALLERLERLEEELEELEE 428
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 222-370 2.44e-04

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: 44.91  E-value: 2.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  222 QELLGQEKEKNAQLLGAAQQLLSHCQAQKEEIR---------RLFQQK-LDELGVKALTYNDLIQAQKEISAHNQQLREQ 291
Cdd:pfam13868  175 REEIEEEKEREIARLRAQQEKAQDEKAERDELRaklyqeeqeRKERQKeREEAEKKARQRQELQQAREEQIELKERRLAE 254

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  292 SEQLEQD--NRALRGQSLQLLKARCEELQldwatlSLEKLLKEKQALKSQISEKQRHCL-ELQISIVELEKSQRQQELLQ 368
Cdd:pfam13868  255 EAEREEEefERMLRKQAEDEEIEQEEAEK------RRMKRLEHRRELEKQIEEREEQRAaEREEELEEGERLREEEAERR 328


                   ..
gi 2462568124  369 LK 370
Cdd:pfam13868  329 ER 330
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 195-366 2.62e-04

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 45.73  E-value: 2.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  195 QKLLESFKIQYLQFLAYTKTPQYKASLQELLGQEKEKNAQLLGAAQQLLSHCQAQKEEIRRLfQQKLDELGVKALTYNDL 274
Cdd:TIGR00618  641 LALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQC-QTLLRELETHIEEYDRE 719

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  275 IQAQKEIS-AHNQQLREQSEQLEQDNRALRGQSLQLLKARCEELQLDW-ATLSLEKLLKEKQALKSQISEKQRHCLELQI 352
Cdd:TIGR00618  720 FNEIENASsSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNeEVTAALQTGAELSHLAAEIQFFNRLREEDTH 799

                          170
                   ....*....|....
gi 2462568124  353 SIVELEkSQRQQEL 366
Cdd:TIGR00618  800 LLKTLE-AEIGQEI 812
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 161-400 2.73e-04

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 45.58  E-value: 2.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  161 DAYRSpHSPFY-----QLPPSVQRHSPNPLlvaptppALQKLLE------SFKIQYLQFL--AYTKTPQYKASLQ---EL 224
Cdd:pfam10174  278 EVYKS-HSKFMknkidQLKQELSKKESELL-------ALQTKLEtltnqnSDCKQHIEVLkeSLTAKEQRAAILQtevDA 349

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  225 LGQEKEKNAQLLGAAQQLLSHCQAQKE----EIRRLfqqkLDELGVKALTYNDLiqaQKEISAHNQQLREQSEQLEQdnr 300
Cdd:pfam10174  350 LRLRLEEKESFLNKKTKQLQDLTEEKStlagEIRDL----KDMLDVKERKINVL---QKKIENLQEQLRDKDKQLAG--- 419

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  301 alrgqslqlLKARCEELQ-----LDWATLSLEKLLKEK----QALKSQISEKQRHCLElqisivELEksQRQQELLQLKS 371
Cdd:pfam10174  420 ---------LKERVKSLQtdssnTDTALTTLEEALSEKeriiERLKEQREREDRERLE------ELE--SLKKENKDLKE 482

                          250       260
                   ....*....|....*....|....*....
gi 2462568124  372 CVppdDALSLHLRGKGALGRELEPDASRL 400
Cdd:pfam10174  483 KV---SALQPELTEKESSLIDLKEHASSL 508
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 213-401 2.76e-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: 45.55  E-value: 2.76e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  213 KTPQYKASLQELLGQEKEKNAQLLGAAQQLLSHCQAQKE------EIR-RLF--QQKLDE--------LGVKALTYNDLI 275
Cdd:pfam01576   16 KVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETElcaeaeEMRaRLAarKQELEEilhelesrLEEEEERSQQLQ 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  276 QAQKEISAHNQQLREQSEQlEQDNRalrgQSLQLLK----ARCEELQLDwaTLSLE----KLLKEKQALKSQISEKQRHC 347
Cdd:pfam01576   96 NEKKKMQQHIQDLEEQLDE-EEAAR----QKLQLEKvtteAKIKKLEED--ILLLEdqnsKLSKERKLLEERISEFTSNL 168

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462568124  348 LElqisivELEKSQRQQELLQLKSCVPPDDALSLHLRGKG-----ALGRELEPDASRLH 401
Cdd:pfam01576  169 AE------EEEKAKSLSKLKNKHEAMISDLEERLKKEEKGrqeleKAKRKLEGESTDLQ 221
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 244-422 2.87e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.43  E-value: 2.87e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  244 SHCQAQKEE-IRRLF--QQKLDELgvkaltyNDLIqaqKEISAHNQQLREQSEQLEQdnralrgqsLQLLKARCEELQLD 320
Cdd:TIGR02168  168 SKYKERRKEtERKLErtRENLDRL-------EDIL---NELERQLKSLERQAEKAER---------YKELKAELRELELA 228

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  321 WATLSLEKLLKEKQALKSQISEKQRHCLELQisiveLEKSQRQQELLQLKSCVPPDDALSLHLRGK-GALGRELepdaSR 399
Cdd:TIGR02168  229 LLVLRLEELREELEELQEELKEAEEELEELT-----AELQELEEKLEELRLEVSELEEEIEELQKElYALANEI----SR 299

                          170       180
                   ....*....|....*....|...
gi 2462568124  400 LHLELDCTKFSLPHLSSMSPELS 422
Cdd:TIGR02168  300 LEQQKQILRERLANLERQLEELE 322
fliJ PRK05689
flagella biosynthesis chaperone FliJ;
219-344 3.75e-04

flagella biosynthesis chaperone FliJ;


Pssm-ID: 235563 [Multi-domain]  Cd Length: 147  Bit Score: 42.22  E-value: 3.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  219 ASLQELLGQEKEKNAQLLGAAQQLLSHCQAQKEEI---RRLFQQKLDELGVKALT------YNDLI-QAQKEISAHNQQL 288
Cdd:PRK05689     8 ATLLDLAEKAEEQAALQLGQARQELQQAEQQLKMLedyRLEYRQQLNDRGSAGMTsswwinYQQFLqQLEKAITQQRQQL 87

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462568124  289 REQSEQLEQdnrALrgQSLQLLKARCEELQldwaTLsLEKLLKEKQALKSQISEKQ 344
Cdd:PRK05689    88 TQWTQKVDN---AR--KYWQEKKQRLEALE----TL-QERYQTEARLAENKREQKQ 133
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 216-368 4.34e-04

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: 44.14  E-value: 4.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  216 QYKASLQELLGQEKEKNAQLLGAAQQLlshcQAQKEEIRRLFQQKLDElgvkaltyndLIQAQKEISAHNQQLREQsEQL 295
Cdd:pfam13868   52 ERERALEEEEEKEEERKEERKRYRQEL----EEQIEEREQKRQEEYEE----------KLQEREQMDEIVERIQEE-DQA 116

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462568124  296 EQDNRALRGQSLQLLKARCEELQLDWATLSLEKLLKEKQALKSQISEKQ-----RHCLELQIsivELEKSQRQQELLQ 368
Cdd:pfam13868  117 EAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAereeeREAEREEI---EEEKEREIARLRA 191
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
221-371 4.49e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.76  E-value: 4.49e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  221 LQELLGQEKEKNAQLLGAAQQLlshcQAQKEEIRRLfQQKLDELGVKALTYNDLIQAQkEISAHNQQLREQ-------SE 293
Cdd:COG4717     76 LEEELKEAEEKEEEYAELQEEL----EELEEELEEL-EAELEELREELEKLEKLLQLL-PLYQELEALEAElaelperLE 149

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  294 QLEQDNRALRGQSLQL--LKARCEELQLDWATLSLEKLLKEKQALKSQISEKQRhcLELQISIVELEKSQRQQELLQLKS 371
Cdd:COG4717    150 ELEERLEELRELEEELeeLEAELAELQEELEELLEQLSLATEEELQDLAEELEE--LQQRLAELEEELEEAQEELEELEE 227
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 227-373 6.38e-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: 44.40  E-value: 6.38e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  227 QEKEKNAQLLGA----AQQLLSHCQAQKEEIRRLFQQKLDELgvkaltyndliQAqkeisahnQQLREQSEQLeQDNRAL 302
Cdd:pfam01576  204 QELEKAKRKLEGestdLQEQIAELQAQIAELRAQLAKKEEEL-----------QA--------ALARLEEETA-QKNNAL 263

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  303 RgqSLQLLKARCEELQLDwatLSLEKLLKEKqalksqiSEKQRHCL--ELQISIVELE------------KSQRQQELLQ 368
Cdd:pfam01576  264 K--KIRELEAQISELQED---LESERAARNK-------AEKQRRDLgeELEALKTELEdtldttaaqqelRSKREQEVTE 331


                   ....*
gi 2462568124  369 LKSCV 373
Cdd:pfam01576  332 LKKAL 336
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 182-371 8.26e-04

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 44.19  E-value: 8.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  182 PNPLLVAP-TPPALQKLLESFKIQYLQFLAYTKTpqYKASLQELLGQEKEKNAQLLGAAQ--QLLSHC-QAQKEEIRRLF 257
Cdd:TIGR00618  513 PNPARQDIdNPGPLTRRMQRGEQTYAQLETSEED--VYHQLTSERKQRASLKEQMQEIQQsfSILTQCdNRSKEDIPNLQ 590

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  258 Q---------QKLDELGVKALTYNDLIQAQKEISAHNQQLREQSEQLEQDNR----ALRGQSLQLLKARCEELQLDWATL 324
Cdd:TIGR00618  591 NitvrlqdltEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELAlkltALHALQLTLTQERVREHALSIRVL 670

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462568124  325 SLEKL------LKEKQALKSQIS---EKQRHCLELQISIVE-LEKSQRQQELLQLKS 371
Cdd:TIGR00618  671 PKELLasrqlaLQKMQSEKEQLTywkEMLAQCQTLLRELEThIEEYDREFNEIENAS 727
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 250-371 8.32e-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: 43.86  E-value: 8.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  250 KEEIRRLFQQKLDELGVKALTYNDLIQAQKE---ISAHNQQLREQSEQLEQDNRALRGQSLQ----LLKARCEELQLDWA 322
Cdd:TIGR04523  123 EVELNKLEKQKKENKKNIDKFLTEIKKKEKElekLNNKYNDLKKQKEELENELNLLEKEKLNiqknIDKIKNKLLKLELL 202

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462568124  323 TLSLEKLLKEKQALKSQISE--KQRHCL-----ELQISIVELEK--SQRQQELLQLKS 371
Cdd:TIGR04523  203 LSNLKKKIQKNKSLESQISElkKQNNQLkdnieKKQQEINEKTTeiSNTQTQLNQLKD 260
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 194-371 8.99e-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: 43.86  E-value: 8.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  194 LQKLLESFKIQYLQFLAYTK-TPQYKASLQELlgqeKEKNAQLLGAAQQLlshcQAQKEEIRRLFQQKLDELGVK--ALT 270
Cdd:TIGR04523  484 LEQKQKELKSKEKELKKLNEeKKELEEKVKDL----TKKISSLKEKIEKL----ESEKKEKESKISDLEDELNKDdfELK 555

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  271 YNDLiqaQKEISAHNQQLreqsEQLEQDNRALrgqslqllKARCEELQLDwatlsLEKLLKEKQALKSQISEKQRHCLEL 350
Cdd:TIGR04523  556 KENL---EKEIDEKNKEI----EELKQTQKSL--------KKKQEEKQEL-----IDQKEKEKKDLIKEIEEKEKKISSL 615

                          170       180
                   ....*....|....*....|...
gi 2462568124  351 --QISIVELEKSQRQQELLQLKS 371
Cdd:TIGR04523  616 ekELEKAKKENEKLSSIIKNIKS 638
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 213-367 1.25e-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: 43.40  E-value: 1.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  213 KTPQYKASLQELLGQEKEKNAQLLGAAQQLlSHCQAQK----EEIRRL------FQQKLDELGVKALTYNDLIQAqkeis 282
Cdd:COG3096    348 KIERYQEDLEELTERLEEQEEVVEEAAEQL-AEAEARLeaaeEEVDSLksqladYQQALDVQQTRAIQYQQAVQA----- 421

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  283 ahnqqLREQSEQLEQDNRALRGQSLQLLKARCEELQLDWATLSLEKLLKEKQALKSQIsekqRHCLELQISIV-ELEKS- 360
Cdd:COG3096    422 -----LEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQF----EKAYELVCKIAgEVERSq 492


                   ....*....
gi 2462568124  361 --QRQQELL 367
Cdd:COG3096    493 awQTARELL 501
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 216-370 1.55e-03

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 41.66  E-value: 1.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  216 QYKASLQELLG--QEKEKNAQ------LLGAAQQLLSHCQAQKEEIRRLfQQKLDELGVKAltyNDLIQAQ----KEISA 283
Cdd:cd00176      4 QFLRDADELEAwlSEKEELLSstdygdDLESVEALLKKHEALEAELAAH-EERVEALNELG---EQLIEEGhpdaEEIQE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  284 HNQQLREQSEQLEQ--DNRALR-GQSLQLLK--ARCEELqLDW-----ATL----------SLEKLLKEKQALKSQISEK 343
Cdd:cd00176     80 RLEELNQRWEELRElaEERRQRlEEALDLQQffRDADDL-EQWleekeAALasedlgkdleSVEELLKKHKELEEELEAH 158

                          170       180
                   ....*....|....*....|....*..
gi 2462568124  344 QRHCLELQISIVELEKSQRQQELLQLK 370
Cdd:cd00176    159 EPRLKSLNELAEELLEEGHPDADEEIE 185
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
221-368 1.55e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 1.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  221 LQELLGQEKEKNAQllGAAQQLLSHCQAQKEEIRRLFQQK--LDELgVKALTyNDLIQAQKEISAHNQQLREQSEQLEQD 298
Cdd:PRK03918   151 VRQILGLDDYENAY--KNLGEVIKEIKRRIERLEKFIKRTenIEEL-IKEKE-KELEEVLREINEISSELPELREELEKL 226

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  299 NRALrgQSLQLLKARCEELQLDwatlsLEKLLKEKQALKSQISEKQRHCLELQISIVELEKSQRQQELLQ 368
Cdd:PRK03918   227 EKEV--KELEELKEEIEELEKE-----LESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELK 289
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
193-370 1.69e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.98  E-value: 1.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  193 ALQKLLESFKIQYlqflaYTKTPQYKASLQELLGQEKEKnaqllgaAQQLLSHCQAQKEE--IRRLF-QQKLDELGVKAL 269
Cdd:COG4913    159 ALKARLKKQGVEF-----FDSFSAYLARLRRRLGIGSEK-------ALRLLHKTQSFKPIgdLDDFVrEYMLEEPDTFEA 226

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  270 -------------TYNDLIQAQK------EISAHNQQLREQSEQLEQdNRALR--------GQSLQLLKARCEELQLDwa 322
Cdd:COG4913    227 adalvehfddlerAHEALEDAREqiellePIRELAERYAAARERLAE-LEYLRaalrlwfaQRRLELLEAELEELRAE-- 303

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462568124  323 tlsLEKLLKEKQALKSQISEKQRHCLEL-----------------QISIVELEKSQRQQELLQLK 370
Cdd:COG4913    304 ---LARLEAELERLEARLDALREELDELeaqirgnggdrleqlerEIERLERELEERERRRARLE 365
IKBKB_SDD pfam18397
IQBAL scaffold dimerization domain; This is the C-terminal scaffold dimerization domain (SDD) ...
 241-367 1.70e-03

IQBAL scaffold dimerization domain; This is the C-terminal scaffold dimerization domain (SDD) found in inhibitor of nuclear factor kappa-B kinase subunit beta IKBKB (EC:2.7.11.10). IKK2 also known as IKBKB is one of the core component of IKB kinases (IKK). IKB kinase (IKK) is an enzyme that quickly becomes active in response to diverse stresses on a cell. The SDD consists primarily of two long alpha-helices.


Pssm-ID: 465745  Cd Length: 275  Bit Score: 42.01  E-value: 1.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  241 QLLSHCQAQKEEIRRLFQqkldelGVKA-----LTYN-DLIQAQKEISAHNQQLREQSEQLEqdnralrgQSLQLLKARC 314
Cdd:pfam18397   44 QAWHYIRGLKEDYSRLQQ------GQRAamlslLRYNsNLSKMKNEMFSMSQQLKAKLDFFK--------TSIQIDLEKY 109

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462568124  315 EElQLDWATLSlEKLLK---------EKQALKSQISEKQRHCLELQISIVELEKS---QRQQELL 367
Cdd:pfam18397  110 SE-QMAFGISS-EKMLSawremeqkaELCGQVAEVNKLDEEMMALQTDIVELQRSpfaRRQGEVL 172
PRK11281 PRK11281
mechanosensitive channel MscK;
219-365 1.84e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 42.98  E-value: 1.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  219 ASLQELLGqekEKNAQLLGA------AQQLLSHCQAQKEEIRRLFqqKLDELGVKALTYNDLIQAQKEISAHNQQLrEQS 292
Cdd:PRK11281   138 QNAQNDLA---EYNSQLVSLqtqperAQAALYANSQRLQQIRNLL--KGGKVGGKALRPSQRVLLQAEQALLNAQN-DLQ 211

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462568124  293 EQLEQDNRALrgQSLqllkarcEELQLDWATLSLEKLLKEKQALKSQISEKQrhcleLQISIVELEKSQRQQE 365
Cdd:PRK11281   212 RKSLEGNTQL--QDL-------LQKQRDYLTARIQRLEHQLQLLQEAINSKR-----LTLSEKTVQEAQSQDE 270
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 216-370 1.86e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 42.18  E-value: 1.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  216 QYKASLQELLGQEKE----KNAQllgAAQQllsHCQAQKEEIR------------------RLFQQKLDEL--------- 264
Cdd:cd16269     90 KFQKKLMEQLEEKKEefckQNEE---ASSK---RCQALLQELSapleekisqgsysvpggyQLYLEDREKLvekyrqvpr 163

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  265 -GVKAL------------TYNDLIQAQKEISAHNQQL---REQSEQLEQDNRALRGQ---SLQLLKARcEELQLDWATLS 325
Cdd:cd16269    164 kGVKAEevlqeflqskeaEAEAILQADQALTEKEKEIeaeRAKAEAAEQERKLLEEQqreLEQKLEDQ-ERSYEEHLRQL 242

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 2462568124  326 LEKLLKEKQALKSQISEKQRHCLELQISIVE---LEKSQR-QQELLQLK 370
Cdd:cd16269    243 KEKMEEERENLLKEQERALESKLKEQEALLEegfKEQAELlQEEIRSLK 291
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 227-364 2.22e-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: 41.83  E-value: 2.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  227 QEKEKNAQLLGAAQQLLSHCQAQKEEIRRLFQQKLDELGVKALTYNDLIQA--------QKEISAH---------NQQLR 289
Cdd:pfam13868  116 AEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEreeereaeREEIEEEkereiarlrAQQEK 195

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  290 EQSEQLEQDN-RALRGQSLQLLKARCEELQLdwatlsLEKLLKEKQALKS----QISEKQRhCLELQIsivELEKSQRQQ 364
Cdd:pfam13868  196 AQDEKAERDElRAKLYQEEQERKERQKEREE------AEKKARQRQELQQareeQIELKER-RLAEEA---EREEEEFER 265
HrpE_YscL_not TIGR02499
type III secretion apparatus protein, HrpE/YscL family; This model is related to pfam06188, ...
 239-398 2.37e-03

type III secretion apparatus protein, HrpE/YscL family; This model is related to pfam06188, but is broader. pfam06188 describes HrpE-like proteins, components of bacterial type III secretion systems primarily in bacteria that infect plants. This model includes also the homologous proteins of animal pathogens, such as YscL of Yersinia pestis. This model excludes the related protein FliH of the bacterial flagellar apparatus (see pfam02108) [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]


Pssm-ID: 274165 [Multi-domain]  Cd Length: 166  Bit Score: 40.36  E-value: 2.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  239 AQQLLSHCQAQKEEIRRLFQQKLDELgvKALTYNDliqaqkeisAHNQQLREQSEQL----EQDNRALRGqslqlLKARC 314
Cdd:TIGR02499   15 AQAILAAARQRAEAILADAEEEAEAS--RQLGYEQ---------GLEQFWQEAAAQLaewqQEAEQLEAS-----LEERL 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  315 EELQLDwatlSLEKLLKEkqalksqISEKQRHCLELQisivELEKSQRQQELLQLkSCVPPD-DALSLHLRGKGALGR-E 392
Cdd:TIGR02499   79 AELVLQ----ALEQILGE-------YDEPERLVRLLR----QLLRAVANQGRLTL-RVHPEQlDEVREALAERLALEPwE 142


                   ....*.
gi 2462568124  393 LEPDAS 398
Cdd:TIGR02499  143 LEPDAS 148
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 502-834 2.86e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.47  E-value: 2.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  502 PGRPAASELHSRAEHTKENGLPYQSPSVPGSMKLSPQDPRPLSPGALQLAGEKSSEKGLRERAYGSSGElitSLPISIPL 581
Cdd:PHA03307    81 ANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPA---ASPPAAGA 157

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  582 STVQPNKLPVSIPLASVVLPSRAERARSTPSPvlQPRDPsstlekqiganahgaGSRSLALAPAGFSYAGSVAISGALAG 661
Cdd:PHA03307   158 SPAAVASDAASSRQAALPLSSPEETARAPSSP--PAEPP---------------PSTPPAAASPRPPRRSSPISASASSP 220

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  662 SPASLTPGAEPA--TLDESSSSGSLFATVGSRSSTPQ-HPLLLAQPRNSLPASPAHQ-----LSSSPRLGGAAQGPLPEA 733
Cdd:PHA03307   221 APAPGRSAADDAgaSSSDSSSSESSGCGWGPENECPLpRPAPITLPTRIWEASGWNGpssrpGPASSSSSPRERSPSPSP 300

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  734 SKGDLP--------SDSGFSDPESEAKRrivfTITTGAGSAKQSPSSKHSPLTASARGDCVPSHGQDSRRRGRRKRASAG 805
Cdd:PHA03307   301 SSPGSGpapsspraSSSSSSSRESSSSS----TSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPS 376

                          330       340
                   ....*....|....*....|....*....
gi 2462568124  806 TPSLSAGVSPKRRALPSVAGLFTQPSGSP 834
Cdd:PHA03307   377 SPAASAGRPTRRRARAAVAGRARRRDATG 405
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 249-381 2.95e-03

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 40.66  E-value: 2.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  249 QKEEIRRLFQQKLDELGVKALTYNDLI----QAQKEisahNQQLREQSEQLEQDNralrgQSLQLLKARCEELQ-----L 319
Cdd:pfam13851   34 EIAELKKKEERNEKLMSEIQQENKRLTeplqKAQEE----VEELRKQLENYEKDK-----QSLKNLKARLKVLEkelkdL 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  320 DWATLSL----EKLLKEKQALKSQ----ISEKQRHClELQISIVE---------LEKSQRQ-QELLQlkSCVPPDDALSL 381
Cdd:pfam13851  105 KWEHEVLeqrfEKVERERDELYDKfeaaIQDVQQKT-GLKNLLLEkklqalgetLEKKEAQlNEVLA--AANLDPDALQA 181
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 229-356 2.97e-03

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


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 41.98  E-value: 2.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  229 KEKNAQLLGAAQQLLSHCQAQKE---EIR--RLFQQKL---DELGVKALTYNDLIQAqkEIsaHNQQLREQSEQLEQDNR 300
Cdd:pfam05622  217 EEKLEALQKEKERLIIERDTLREtneELRcaQLQQAELsqaDALLSPSSDPGDNLAA--EI--MPAEIREKLIRLQHENK 292

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462568124  301 ALRGQSLQLLKARCEELQ--LDWATLSLEKLLKEKQALKSQISEKQRHCLELQISIVE 356
Cdd:pfam05622  293 MLRLGQEGSYRERLTELQqlLEDANRRKNELETQNRLANQRILELQQQVEELQKALQE 350
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 210-308 4.27e-03

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


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 39.10  E-value: 4.27e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124   210 AYTKTPQYKASLQELLGQEKEKNAQLlgaaqqllshcQAQKEEIRRLfQQKLDELGVKaLTYNDLIQAQKEISAHNQQLR 289
Cdd:smart00935    9 ILQESPAGKAAQKQLEKEFKKRQAEL-----------EKLEKELQKL-KEKLQKDAAT-LSEAAREKKEKELQKKVQEFQ 75

                            90
                    ....*....|....*....
gi 2462568124   290 EQSEQLEQDNRALRGQSLQ 308
Cdd:smart00935   76 RKQQKLQQDLQKRQQEELQ 94
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 229-368 4.40e-03

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


Pssm-ID: 462536 [Multi-domain]  Cd Length: 176  Bit Score: 39.92  E-value: 4.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  229 KEKNAQLLGAAQQLLSHCQAQKEEIRRLFQQKLDELGVKALTYN-DLIQAQKEISAHNQQLREQSEQLEQDNRALRGQS- 306
Cdd:pfam08614   20 EAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQLReELAELYRSRGELAQRLVDLNEELQELEKKLREDEr 99

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462568124  307 -LQLLKARCEELQLdwATLSLEKLLKEK----QALKSQISEkqrhcLELQISIVElEKSQRQQ----ELLQ 368
Cdd:pfam08614  100 rLAALEAERAQLEE--KLKDREEELREKrklnQDLQDELVA-----LQLQLNMAE-EKLRKLEkenrELVE 162
BBC smart00502
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains
 218-350 5.44e-03

B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains


Pssm-ID: 128778  Cd Length: 127  Bit Score: 38.40  E-value: 5.44e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124   218 KASLQELLGQEKEKNAQLLGAAQQLlshcqaqkEEIRRLFQQKLDElgvkaltyndliqAQKEISAHNQQLREQSEQLEQ 297
Cdd:smart00502    2 REALEELLTKLRKKAAELEDALKQL--------ISIIQEVEENAAD-------------VEAQIKAAFDELRNALNKRKK 60

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|...
gi 2462568124   298 dnralrgQSLQLLKARCEELQLDwatlsLEKLLKEKQALKSQISEKQRHCLEL 350
Cdd:smart00502   61 -------QLLEDLEEQKENKLKV-----LEQQLESLTQKQEKLSHAINFTEEA 101
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 216-367 5.69e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.90  E-value: 5.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  216 QYKASLQELLGQEKEKNAQLLGAAQQ---LLSHCQAQKEEIRRLfQQKLDELGVK-ALTYNDLIQAQKEISAHNQQLREQ 291
Cdd:COG4942     24 EAEAELEQLQQEIAELEKELAALKKEekaLLKQLAALERRIAAL-ARRIRALEQElAALEAELAELEKEIAELRAELEAQ 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  292 SEQLEQDNRAL--RGQ------------------SLQLLKARCEELQLDWATL--SLEKLLKEKQALKSQISEKQRHCLE 349
Cdd:COG4942    103 KEELAELLRALyrLGRqpplalllspedfldavrRLQYLKYLAPARREQAEELraDLAELAALRAELEAERAELEALLAE 182

                          170
                   ....*....|....*...
gi 2462568124  350 LQISIVELEKSQRQQELL 367
Cdd:COG4942    183 LEEERAALEALKAERQKL 200
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
 210-308 5.80e-03

Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442073 [Multi-domain]  Cd Length: 171  Bit Score: 39.43  E-value: 5.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  210 AYTKTPQYKASLQELLGQEKEKNAQLlgaaqqllshcQAQKEEIRRLfQQKLDELGVKaLTYNDLIQAQKEISAHNQQLR 289
Cdd:COG2825     34 ILQESPEGKAAQKKLEKEFKKRQAEL-----------QKLEKELQAL-QEKLQKEAAT-LSEEERQKKERELQKKQQELQ 100

                           90
                   ....*....|....*....
gi 2462568124  290 EQSEQLEQDNRALRGQSLQ 308
Cdd:COG2825    101 RKQQEAQQDLQKRQQELLQ 119
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 274-370 6.24e-03

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: 40.88  E-value: 6.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  274 LIQAQKEISAHNQQLREQSEQ---LEQDNRALRGQ---SLQLLKARCEELQLDWATL-SLEKLLKEKQ-----------A 335
Cdd:pfam05557   29 RIELEKKASALKRQLDRESDRnqeLQKRIRLLEKReaeAEEALREQAELNRLKKKYLeALNKKLNEKEsqladarevisC 108

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2462568124  336 LKSQISEKQRHC----LELQISIVELEKSQRQQELLQLK 370
Cdd:pfam05557  109 LKNELSELRRQIqraeLELQSTNSELEELQERLDLLKAK 147
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
 46-393 6.87e-03

Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.


Pssm-ID: 430783 [Multi-domain]  Cd Length: 618  Bit Score: 40.90  E-value: 6.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124   46 EEQEAARRRQQRESKSNAATPTKGPEGKVAGPADAPMDSGAEEEKAGAATVKKPSPSKARKKKLNKKGRKMAGR---KRG 122
Cdd:pfam09731   83 KEEKKQVKIPRQSGVSSEVAEEEKEATKDAAEAKAQLPKSEQEKEKALEEVLKEAISKAESATAVAKEAKDDAIqavKAH 162

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  123 RPKKMNTANPERKP--KKNQTALDALHA-----------QTVSQTAASSPQD--AYRSPHS---PFYQLPPSVQRHSPNP 184
Cdd:pfam09731  163 TDSLKEASDTAEISreKATDSALQKAEAlaeklkevinlAKQSEEEAAPPLLdaAPETPPKlpeHLDNVEEKVEKAQSLA 242

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  185 LLVAPtppaLQKLLESFKIQYLQFLAyTKTPQYKASLQELLGQEKEKNAQLLGAAQ-------QLLSHCQAQKE------ 251
Cdd:pfam09731  243 KLVDQ----YKELVASERIVFQQELV-SIFPDIIPVLKEDNLLSNDDLNSLIAHAHreidqlsKKLAELKKREEkhiera 317

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  252 -EIRRLFQQKLDELGVKALTY---NDLIQAQKEISAHNQQLREQSE-----QLEQDNRALRGQSLQLLKARCEELQLDWA 322
Cdd:pfam09731  318 lEKQKEELDKLAEELSARLEEvraADEAQLRLEFEREREEIRESYEeklrtELERQAEAHEEHLKDVLVEQEIELQREFL 397

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462568124  323 TLSLEKLLKEKQALKSQISE-----KQRHCLELQISIVELEKSQRQQelLQLkSCVPPDDAL--SLHLRGKGALGREL 393
Cdd:pfam09731  398 QDIKEKVEEERAGRLLKLNEllanlKGLEKATSSHSEVEDENRKAQQ--LWL-AVEALRSTLedGSADSRPRPLVREL 472
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 221-368 8.07e-03

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 39.35  E-value: 8.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  221 LQELLGQEKEKNAQLLGAAQQLLSHCQAQKEEIR-RL--FQQKLDELGVKALTYNDLIQAQKEISAHNQQ-------LRE 290
Cdd:cd00176     45 LEAELAAHEERVEALNELGEQLIEEGHPDAEEIQeRLeeLNQRWEELRELAEERRQRLEEALDLQQFFRDaddleqwLEE 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568124  291 QSEQLEQDNRALRGQSLQLLKARCEELQ---------LDWATLSLEKLLKEKQALKSQISEKQRHCLELQISIVELEKSQ 361
Cdd:cd00176    125 KEAALASEDLGKDLESVEELLKKHKELEeeleaheprLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEE 204


                   ....*..
gi 2462568124  362 RQQELLQ 368
Cdd:cd00176    205 RQKKLEE 211
 
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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