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Conserved domains on  [gi|22094135|ref|NP_115871|]
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histone-lysine N-methyltransferase, H3 lysine-79 specific isoform 1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DOT1 pfam08123
Histone methylation protein DOT1; The DOT1 domain regulates gene expression by methylating ...
 115-317 8.04e-107

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


:

Pssm-ID: 149273  Cd Length: 205  Bit Score: 337.74  E-value: 8.04e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135    115 YNHSV-TDPEKLNNYEPFSPEVYGETSFDLVAQMIDEIKMTDDDLFVDLGSGVGQVVLQVAAATNCKHHYGVEKADIPAK 193
Cdd:pfam08123    1 YSRSVsPDANKLNHYKAFSNEVYGELLPEFLSDVLDKCNLGPQDVFVDLGSGVGNCVLQAALEFGCKLSFGCEIMDNASN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135    194 YAETMDREFRKWMKWYGKKHAEYTLERGDFLSEEWRERI-ANTSVIFVNNFAFGPEVDHQLKERFANMKEGGRIVSSKPF 272
Cdd:pfam08123   81 LAELQDEEFKKRCKLFGKKLGKIEFIRGSFLDNERVEEIiPEADVILVNNFAFDPELNLQLKEMLQDLKDGCKIISLKSF 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 22094135    273 APLNFRINSRNLSDIGTIMRVVELSPLKGSVSWTGKPVSYYLHTI 317
Cdd:pfam08123  161 VPLNYRINFRNLSDIFNILKVEELKLPEGSVSWTSRGVEYYISTV 205
CC_DOT1L cd20902
coiled coil domain of disruptor of telomeric-silencing 1-like (DOT1L) and similar proteins; ...
 483-547 2.24e-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: 2.24e-32
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22094135  483 ALQKLLESFKIQYLQFLAYTKTPQYKASLQELLGQEKEKNAQLLGAAQQLLSHCQAQKEEIRRLF 547
Cdd:cd20902    1 ALQKLLESFKIQYLQFLAYMKTPQYKASLQQQIEQEKEKNKQLTGKAQQLEKQIQALQKEGVRLL 65
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
511-661 3.54e-09

Uncharacterized protein, contains DUF3084 domain [Function unknown];


:

Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 60.69  E-value: 3.54e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135  511 LQELLGQEKEKNAQLLGAAQQLlshcQAQKEEIRRLfQQKLDELgvkaltYNDLIQAQKEISAHNQQL---REQSEQLEQ 587
Cdd:COG4372   47 LEQLREELEQAREELEQLEEEL----EQARSELEQL-EEELEEL------NEQLQAAQAELAQAQEELeslQEEAEELQE 115

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22094135  588 DNRALRGQsLQLLKARCEELQLDWATLSLEKLLKEKQ--ALKSQISEKQRHCLELQISIVELEKSQRQQELLQLKS 661
Cdd:COG4372  116 ELEELQKE-RQDLEQQRKQLEAQIAELQSEIAEREEElkELEEQLESLQEELAALEQELQALSEAEAEQALDELLK 190
PHA03307 super family cl33723
transcriptional regulator ICP4; Provisional
 775-1124 2.11e-05

transcriptional regulator ICP4; Provisional


The actual alignment was detected with superfamily member PHA03307:

Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 49.40  E-value: 2.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135   775 SPAKIVLRRHLSQDHTVPGRPAAS----ELHSRAEHTKENGLPYQSPSVPGSmklSPQDPRPLSPGALQLAGEKSSEKGL 850
Cdd:PHA03307   74 GPGTEAPANESRSTPTWSLSTLAPaspaREGSPTPPGPSSPDPPPPTPPPAS---PPPSPAPDLSEMLRPVGSPGPPPAA 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135   851 RERAYGSSGE-----LITSLPISIPLSTVQPNKLPVSIPLASVvlPSRAERARSTPSPvlQPRDPSSTLEkqiGANAHGA 925
Cdd:PHA03307  151 SPPAAGASPAavasdAASSRQAALPLSSPEETARAPSSPPAEP--PPSTPPAAASPRP--PRRSSPISAS---ASSPAPA 223

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135   926 GSRSLALAPAGFSYAGSVAISGALAGSPASLTPGAEPATLDESSSSGSLfATVGSRSSTPQHplllAQPRNSLPASPAHQ 1005
Cdd:PHA03307  224 PGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEA-SGWNGPSSRPGP----ASSSSSPRERSPSP 298

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135  1006 LSSSPRLGGAAQGPLPEASKGDLPSDSGFSDPESEAKRRivftittGAGSakqSPSSKHSPLTASARGDcvPSHGQDSRR 1085
Cdd:PHA03307  299 SPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSR-------GAAV---SPGPSPSRSPSPSRPP--PPADPSSPR 366

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 22094135  1086 RGRRKRASAGTPSLSAGVSPKRRALPSVAGLFTQPSGSP 1124
Cdd:PHA03307  367 KRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATG 405
 
Name Accession Description Interval E-value
DOT1 pfam08123
Histone methylation protein DOT1; The DOT1 domain regulates gene expression by methylating ...
 115-317 8.04e-107

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


Pssm-ID: 149273  Cd Length: 205  Bit Score: 337.74  E-value: 8.04e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135    115 YNHSV-TDPEKLNNYEPFSPEVYGETSFDLVAQMIDEIKMTDDDLFVDLGSGVGQVVLQVAAATNCKHHYGVEKADIPAK 193
Cdd:pfam08123    1 YSRSVsPDANKLNHYKAFSNEVYGELLPEFLSDVLDKCNLGPQDVFVDLGSGVGNCVLQAALEFGCKLSFGCEIMDNASN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135    194 YAETMDREFRKWMKWYGKKHAEYTLERGDFLSEEWRERI-ANTSVIFVNNFAFGPEVDHQLKERFANMKEGGRIVSSKPF 272
Cdd:pfam08123   81 LAELQDEEFKKRCKLFGKKLGKIEFIRGSFLDNERVEEIiPEADVILVNNFAFDPELNLQLKEMLQDLKDGCKIISLKSF 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 22094135    273 APLNFRINSRNLSDIGTIMRVVELSPLKGSVSWTGKPVSYYLHTI 317
Cdd:pfam08123  161 VPLNYRINFRNLSDIFNILKVEELKLPEGSVSWTSRGVEYYISTV 205
CC_DOT1L cd20902
coiled coil domain of disruptor of telomeric-silencing 1-like (DOT1L) and similar proteins; ...
 483-547 2.24e-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: 2.24e-32
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22094135  483 ALQKLLESFKIQYLQFLAYTKTPQYKASLQELLGQEKEKNAQLLGAAQQLLSHCQAQKEEIRRLF 547
Cdd:cd20902    1 ALQKLLESFKIQYLQFLAYMKTPQYKASLQQQIEQEKEKNKQLTGKAQQLEKQIQALQKEGVRLL 65
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
511-661 3.54e-09

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 60.69  E-value: 3.54e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135  511 LQELLGQEKEKNAQLLGAAQQLlshcQAQKEEIRRLfQQKLDELgvkaltYNDLIQAQKEISAHNQQL---REQSEQLEQ 587
Cdd:COG4372   47 LEQLREELEQAREELEQLEEEL----EQARSELEQL-EEELEEL------NEQLQAAQAELAQAQEELeslQEEAEELQE 115

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22094135  588 DNRALRGQsLQLLKARCEELQLDWATLSLEKLLKEKQ--ALKSQISEKQRHCLELQISIVELEKSQRQQELLQLKS 661
Cdd:COG4372  116 ELEELQKE-RQDLEQQRKQLEAQIAELQSEIAEREEElkELEEQLESLQEELAALEQELQALSEAEAEQALDELLK 190
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 506-660 3.45e-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: 55.45  E-value: 3.45e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135    506 QYKASLQELLgQEKEKNAQLLGAAQQLLSHCQAQKEEIRRLFQQKLDELGVKALTYNDLIQAQKEISAHNQQLREQSEQL 585
Cdd:TIGR02168  236 ELREELEELQ-EELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANL 314

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22094135    586 EQDNRALRGQsLQLLKARCEELQLDWATLS--LEKLLKEKQALKSQISEKQRHCLELQISIVELEK--SQRQQELLQLK 660
Cdd:TIGR02168  315 ERQLEELEAQ-LEELESKLDELAEELAELEekLEELKEELESLEAELEELEAELEELESRLEELEEqlETLRSKVAQLE 392
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 506-684 8.25e-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: 50.51  E-value: 8.25e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135    506 QYKASLQELLGQEKEKNAQLLGAAQQLLS--------HCQAQKE--EIRRL------FQQKLDELGVKALTYNDLIQ--- 566
Cdd:pfam05557   80 LKKKYLEALNKKLNEKESQLADAREVISClknelselRRQIQRAelELQSTnseleeLQERLDLLKAKASEAEQLRQnle 159

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135    567 -AQKEISAHNQQLREqseqLEQDNrALRGQSLQLLKARCEELqldwatLSLEKLLKEKQALK---SQISEKQRHCLEL-- 640
Cdd:pfam05557  160 kQQSSLAEAEQRIKE----LEFEI-QSQEQDSEIVKNSKSEL------ARIPELEKELERLRehnKHLNENIENKLLLke 228

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22094135    641 -----------------QISIVELEKSQRQQEllqLKSCVPPDDALSLHLRGKGALGRELE 684
Cdd:pfam05557  229 evedlkrklereekyreEAATLELEKEKLEQE---LQSWVKLAQDTGLNLRSPEDLSRRIE 286
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 775-1124 2.11e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 49.40  E-value: 2.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135   775 SPAKIVLRRHLSQDHTVPGRPAAS----ELHSRAEHTKENGLPYQSPSVPGSmklSPQDPRPLSPGALQLAGEKSSEKGL 850
Cdd:PHA03307   74 GPGTEAPANESRSTPTWSLSTLAPaspaREGSPTPPGPSSPDPPPPTPPPAS---PPPSPAPDLSEMLRPVGSPGPPPAA 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135   851 RERAYGSSGE-----LITSLPISIPLSTVQPNKLPVSIPLASVvlPSRAERARSTPSPvlQPRDPSSTLEkqiGANAHGA 925
Cdd:PHA03307  151 SPPAAGASPAavasdAASSRQAALPLSSPEETARAPSSPPAEP--PPSTPPAAASPRP--PRRSSPISAS---ASSPAPA 223

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135   926 GSRSLALAPAGFSYAGSVAISGALAGSPASLTPGAEPATLDESSSSGSLfATVGSRSSTPQHplllAQPRNSLPASPAHQ 1005
Cdd:PHA03307  224 PGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEA-SGWNGPSSRPGP----ASSSSSPRERSPSP 298

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135  1006 LSSSPRLGGAAQGPLPEASKGDLPSDSGFSDPESEAKRRivftittGAGSakqSPSSKHSPLTASARGDcvPSHGQDSRR 1085
Cdd:PHA03307  299 SPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSR-------GAAV---SPGPSPSRSPSPSRPP--PPADPSSPR 366

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 22094135  1086 RGRRKRASAGTPSLSAGVSPKRRALPSVAGLFTQPSGSP 1124
Cdd:PHA03307  367 KRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATG 405
PRK11281 PRK11281
mechanosensitive channel MscK;
479-656 9.88e-05

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 47.21  E-value: 9.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135   479 PTPPALQKLLESFKIQYLQFLAytKTPQYKASLQELlgqekekNAQLLGAAQQLLshcQAQkEEIRRL-------FQQKL 551
Cdd:PRK11281   52 KLLEAEDKLVQQDLEQTLALLD--KIDRQKEETEQL-------KQQLAQAPAKLR---QAQ-AELEALkddndeeTRETL 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135   552 DELGVKAL------TYNDLIQAQKEISAHNQQLREQSEQLEQDNRALRGQSLQLLKarceelqldwatlsLEKLLKEKQA 625
Cdd:PRK11281  119 STLSLRQLesrlaqTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQ--------------IRNLLKGGKV 184

                         170       180       190
                  ....*....|....*....|....*....|.
gi 22094135   626 LKSQISEKQRHCLELQISIVELEKSQRQQEL 656
Cdd:PRK11281  185 GGKALRPSQRVLLQAEQALLNAQNDLQRKSL 215
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 159-267 2.20e-03

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


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 39.34  E-value: 2.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135  159 FVDLGSGVGQvVLQVAAATNCKHHYGVEKADIPAKYAETmdrefrkwmKWYGKKHAEYTLERGDFlsEEWRERIANT-SV 237
Cdd:cd02440    2 VLDLGCGTGA-LALALASGPGARVTGVDISPVALELARK---------AAAALLADNVEVLKGDA--EELPPEADESfDV 69

                         90       100       110
                 ....*....|....*....|....*....|..
gi 22094135  238 IFVNN-FAFGPEVDHQLKERFAN-MKEGGRIV 267
Cdd:cd02440   70 IISDPpLHHLVEDLARFLEEARRlLKPGGVLV 101
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 500-598 4.55e-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: 4.55e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135     500 AYTKTPQYKASLQELLGQEKEKNAQLlgaaqqllshcQAQKEEIRRLfQQKLDELGVKaLTYNDLIQAQKEISAHNQQLR 579
Cdd:smart00935    9 ILQESPAGKAAQKQLEKEFKKRQAEL-----------EKLEKELQKL-KEKLQKDAAT-LSEAAREKKEKELQKKVQEFQ 75

                            90
                    ....*....|....*....
gi 22094135     580 EQSEQLEQDNRALRGQSLQ 598
Cdd:smart00935   76 RKQQKLQQDLQKRQQEELQ 94
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 506-660 6.09e-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: 40.64  E-value: 6.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135  506 QYKASLQELLGQEKE----KNAQllgAAQQllsHCQAQKEEIR------------------RLFQQKLDEL--------- 554
Cdd:cd16269   90 KFQKKLMEQLEEKKEefckQNEE---ASSK---RCQALLQELSapleekisqgsysvpggyQLYLEDREKLvekyrqvpr 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135  555 -GVKAL------------TYNDLIQAQKEISAHNQQL---REQSEQLEQDNRALRGQ---SLQLLKARcEELQLDWATLS 615
Cdd:cd16269  164 kGVKAEevlqeflqskeaEAEAILQADQALTEKEKEIeaeRAKAEAAEQERKLLEEQqreLEQKLEDQ-ERSYEEHLRQL 242

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 22094135  616 LEKLLKEKQALKSQISEKQRHCLELQISIVE---LEKSQR-QQELLQLK 660
Cdd:cd16269  243 KEKMEEERENLLKEQERALESKLKEQEALLEegfKEQAELlQEEIRSLK 291
 
Name Accession Description Interval E-value
DOT1 pfam08123
Histone methylation protein DOT1; The DOT1 domain regulates gene expression by methylating ...
 115-317 8.04e-107

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


Pssm-ID: 149273  Cd Length: 205  Bit Score: 337.74  E-value: 8.04e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135    115 YNHSV-TDPEKLNNYEPFSPEVYGETSFDLVAQMIDEIKMTDDDLFVDLGSGVGQVVLQVAAATNCKHHYGVEKADIPAK 193
Cdd:pfam08123    1 YSRSVsPDANKLNHYKAFSNEVYGELLPEFLSDVLDKCNLGPQDVFVDLGSGVGNCVLQAALEFGCKLSFGCEIMDNASN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135    194 YAETMDREFRKWMKWYGKKHAEYTLERGDFLSEEWRERI-ANTSVIFVNNFAFGPEVDHQLKERFANMKEGGRIVSSKPF 272
Cdd:pfam08123   81 LAELQDEEFKKRCKLFGKKLGKIEFIRGSFLDNERVEEIiPEADVILVNNFAFDPELNLQLKEMLQDLKDGCKIISLKSF 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 22094135    273 APLNFRINSRNLSDIGTIMRVVELSPLKGSVSWTGKPVSYYLHTI 317
Cdd:pfam08123  161 VPLNYRINFRNLSDIFNILKVEELKLPEGSVSWTSRGVEYYISTV 205
CC_DOT1L cd20902
coiled coil domain of disruptor of telomeric-silencing 1-like (DOT1L) and similar proteins; ...
 483-547 2.24e-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: 2.24e-32
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22094135  483 ALQKLLESFKIQYLQFLAYTKTPQYKASLQELLGQEKEKNAQLLGAAQQLLSHCQAQKEEIRRLF 547
Cdd:cd20902    1 ALQKLLESFKIQYLQFLAYMKTPQYKASLQQQIEQEKEKNKQLTGKAQQLEKQIQALQKEGVRLL 65
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
511-661 3.54e-09

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 60.69  E-value: 3.54e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135  511 LQELLGQEKEKNAQLLGAAQQLlshcQAQKEEIRRLfQQKLDELgvkaltYNDLIQAQKEISAHNQQL---REQSEQLEQ 587
Cdd:COG4372   47 LEQLREELEQAREELEQLEEEL----EQARSELEQL-EEELEEL------NEQLQAAQAELAQAQEELeslQEEAEELQE 115

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22094135  588 DNRALRGQsLQLLKARCEELQLDWATLSLEKLLKEKQ--ALKSQISEKQRHCLELQISIVELEKSQRQQELLQLKS 661
Cdd:COG4372  116 ELEELQKE-RQDLEQQRKQLEAQIAELQSEIAEREEElkELEEQLESLQEELAALEQELQALSEAEAEQALDELLK 190
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 508-695 9.23e-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: 9.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135  508 KASLQELLGQEKEKNAQLLGAAQQLLSHCQAQKEEIRRLFQQKLDELGVKALTYNDLIQAQKEISAHNQQLREQSEQLEQ 587
Cdd:COG1196  304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135  588 DNRALRG--QSLQLLKARCEELQLDWATLS--LEKLLKEKQALKSQISEKQRHCLELQISIVELEKSQRQQELLQLKSCV 663
Cdd:COG1196  384 LAEELLEalRAAAELAAQLEELEEAEEALLerLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 22094135  664 PPDDALSLHLRGK---GALGRELEPDASRLHLELD 695
Cdd:COG1196  464 LLAELLEEAALLEaalAELLEELAEAAARLLLLLE 498
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
495-659 2.47e-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: 2.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135  495 YLQFLAYTKTPQYKASLQELlGQEKEKNAQLLGAAQQLLSHCQAQKEEIRRLFQQKLDELgvkaltynDLIQAQKEISAH 574
Cdd:COG4913  603 VLGFDNRAKLAALEAELAEL-EEELAEAEERLEALEAELDALQERREALQRLAEYSWDEI--------DVASAEREIAEL 673

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135  575 NQQLreqsEQLEQDNRALRGqslqlLKARCEELQLDWATLS--LEKLLKEKQALKSQISEKQRHCLELQISIVELEKSQR 652
Cdd:COG4913  674 EAEL----ERLDASSDDLAA-----LEEQLEELEAELEELEeeLDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLAR 744


                 ....*..
gi 22094135  653 QQELLQL 659
Cdd:COG4913  745 LELRALL 751
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 506-660 3.45e-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: 55.45  E-value: 3.45e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135    506 QYKASLQELLgQEKEKNAQLLGAAQQLLSHCQAQKEEIRRLFQQKLDELGVKALTYNDLIQAQKEISAHNQQLREQSEQL 585
Cdd:TIGR02168  236 ELREELEELQ-EELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANL 314

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22094135    586 EQDNRALRGQsLQLLKARCEELQLDWATLS--LEKLLKEKQALKSQISEKQRHCLELQISIVELEK--SQRQQELLQLK 660
Cdd:TIGR02168  315 ERQLEELEAQ-LEELESKLDELAEELAELEekLEELKEELESLEAELEELEAELEELESRLEELEEqlETLRSKVAQLE 392
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
492-690 1.85e-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: 1.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135  492 KIQYLQFLAyTKTPQYKASLQ-ELLGQEKEKNAQLLGAAQQLLSHCQAQ----KEEIRRLfQQKLDELGVKALTyndliQ 566
Cdd:COG4913  270 RLAELEYLR-AALRLWFAQRRlELLEAELEELRAELARLEAELERLEARldalREELDEL-EAQIRGNGGDRLE-----Q 342

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135  567 AQKEISAHNQQLREQSEQLEQDNRALR--GQSLQLLKARCEELQLDWATLsLEKLLKEKQALksqisEKQRHCLELQISI 644
Cdd:COG4913  343 LEREIERLERELEERERRRARLEALLAalGLPLPASAEEFAALRAEAAAL-LEALEEELEAL-----EEALAEAEAALRD 416

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 22094135  645 VELEKSQRQQELLQL---KSCVPPDdalSLHLRgkGALGRELEPDASRL 690
Cdd:COG4913  417 LRRELRELEAEIASLerrKSNIPAR---LLALR--DALAEALGLDEAEL 460
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
506-659 2.03e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 52.46  E-value: 2.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135  506 QYKASLQELLGQEKEKNA------------QLLGAAQQLLSHCQAQKEEIRRL--FQQKLDELGVKALTYNDLIQAQKEI 571
Cdd:COG4717   89 EYAELQEELEELEEELEEleaeleelreelEKLEKLLQLLPLYQELEALEAELaeLPERLEELEERLEELRELEEELEEL 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135  572 SAHNQQLREQSEQLEQDNRALRGQSLQLLKARCEELQLDWATlsLEKLLKEKQALKSQISEKQRhclELQISIVELEKSQ 651
Cdd:COG4717  169 EAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAE--LEEELEEAQEELEELEEELE---QLENELEAAALEE 243


                 ....*...
gi 22094135  652 RQQELLQL 659
Cdd:COG4717  244 RLKEARLL 251
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 483-661 4.27e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.48  E-value: 4.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135  483 ALQKLLESFKIQyLQFLAYTktpQYKASLQELLGQEKEKNAQLLGAAQQLlSHCQAQKEEIRRLFQQKLDELGVKALTYN 562
Cdd:COG1196  217 ELKEELKELEAE-LLLLKLR---ELEAELEELEAELEELEAELEELEAEL-AELEAELEELRLELEELELELEEAQAEEY 291

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135  563 DLIQAQKEISAHNQQLREQSEQLEQDNRALRGQsLQLLKARCEEL--QLDWATLSLEKLLKEKQALKSQISEKQRHCLEL 640
Cdd:COG1196  292 ELLAELARLEQDIARLEERRRELEERLEELEEE-LAELEEELEELeeELEELEEELEEAEEELEEAEAELAEAEEALLEA 370

                        170       180
                 ....*....|....*....|...
gi 22094135  641 QISIVELEK--SQRQQELLQLKS 661
Cdd:COG1196  371 EAELAEAEEelEELAEELLEALR 393
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
541-663 5.26e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 51.31  E-value: 5.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135  541 EEIRRLfQQKLDELGVKALTYNDLIQAQKEISAHNQQLREQSEQLEQDNRALRGQ-SLQLLKARCEELQLDWATLS--LE 617
Cdd:COG4717   71 KELKEL-EEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLlQLLPLYQELEALEAELAELPerLE 149

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 22094135  618 KLLKEKQALKS---QISEKQRHCLELQISIVELEKSQRQQELLQLKSCV 663
Cdd:COG4717  150 ELEERLEELREleeELEELEAELAELQEELEELLEQLSLATEEELQDLA 198
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 506-656 5.33e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.21  E-value: 5.33e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135    506 QYKASLQELLGQEKEKNAQLLGAAQQL------LSHCQAQKEEIRRLFQQKLDELGVKALTYNDLIQAQKEISAHNQQLR 579
Cdd:TIGR02168  306 ILRERLANLERQLEELEAQLEELESKLdelaeeLAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLR 385

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22094135    580 EQSEQLEQDNRALRGQsLQLLKARCEELQldwatLSLEKLLKEKQALKSQISEKQRHCLELQISIVELEKSQRQQEL 656
Cdd:TIGR02168  386 SKVAQLELQIASLNNE-IERLEARLERLE-----DRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEEL 456
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 506-661 6.57e-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: 6.57e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135    506 QYKASLQELlgqEKEKNAQLLGAAQQLLSHCQAQKEEIRrlfqqkldelgvkaltyNDLIQAQKEISAHNQQ---LREQS 582
Cdd:TIGR04523  292 QLKSEISDL---NNQKEQDWNKELKSELKNQEKKLEEIQ-----------------NQISQNNKIISQLNEQisqLKKEL 351

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135    583 EQLEQDNRALRGQ------SLQLLKARCEELQLdwatlSLEKLLKEKQALKSQIS--EKQRHCLELQISIVELEKSQRQQ 654
Cdd:TIGR04523  352 TNSESENSEKQREleekqnEIEKLKKENQSYKQ-----EIKNLESQINDLESKIQnqEKLNQQKDEQIKKLQQEKELLEK 426


                   ....*..
gi 22094135    655 ELLQLKS 661
Cdd:TIGR04523  427 EIERLKE 433
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 506-684 8.25e-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: 50.51  E-value: 8.25e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135    506 QYKASLQELLGQEKEKNAQLLGAAQQLLS--------HCQAQKE--EIRRL------FQQKLDELGVKALTYNDLIQ--- 566
Cdd:pfam05557   80 LKKKYLEALNKKLNEKESQLADAREVISClknelselRRQIQRAelELQSTnseleeLQERLDLLKAKASEAEQLRQnle 159

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135    567 -AQKEISAHNQQLREqseqLEQDNrALRGQSLQLLKARCEELqldwatLSLEKLLKEKQALK---SQISEKQRHCLEL-- 640
Cdd:pfam05557  160 kQQSSLAEAEQRIKE----LEFEI-QSQEQDSEIVKNSKSEL------ARIPELEKELERLRehnKHLNENIENKLLLke 228

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22094135    641 -----------------QISIVELEKSQRQQEllqLKSCVPPDDALSLHLRGKGALGRELE 684
Cdd:pfam05557  229 evedlkrklereekyreEAATLELEKEKLEQE---LQSWVKLAQDTGLNLRSPEDLSRRIE 286
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 517-660 9.46e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.32  E-value: 9.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135  517 QEKEKNAQLLGAAQQLLSHCQAQKEEIRRLFQQKLDELGVKALTYN-DLIQAQKEISAHNQQLREQSEQLEQDNRALRGQ 595
Cdd:COG1196  277 EELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEeELAELEEELEELEEELEELEEELEEAEEELEEA 356

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22094135  596 SLQLLKARCEELQldwATLSLEKLLKEKQALKSQISEKQRHCLELQISIVELEKSQRQQELLQLK 660
Cdd:COG1196  357 EAELAEAEEALLE---AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER 418
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 512-661 1.08e-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: 1.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135    512 QELLGQEKEKNaQLLGAAQQLLSHCQAQKEEIRRL--------------------FQQKLDELgvkALTYN----DLIQA 567
Cdd:TIGR04523  412 EQIKKLQQEKE-LLEKEIERLKETIIKNNSEIKDLtnqdsvkeliiknldntresLETQLKVL---SRSINkikqNLEQK 487

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135    568 QKEISAHNQQ---LREQSEQLEQDNRALRGQSLQLL----KARCEELQLDWATLSLEKLLKE------KQALKSQISEKQ 634
Cdd:TIGR04523  488 QKELKSKEKElkkLNEEKKELEEKVKDLTKKISSLKekieKLESEKKEKESKISDLEDELNKddfelkKENLEKEIDEKN 567

                          170       180
                   ....*....|....*....|....*...
gi 22094135    635 RHCLELQISIVELEKSQRQ-QELLQLKS 661
Cdd:TIGR04523  568 KEIEELKQTQKSLKKKQEEkQELIDQKE 595
MscS_porin pfam12795
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...
 483-661 1.39e-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: 48.07  E-value: 1.39e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135    483 ALQKLLESF---------KIQYLQFLAYTKTPQY--KASLQELLGQEKEKNAQLLgAAQQLLSHCQAQKEEIR---RLFQ 548
Cdd:pfam12795   41 AYQKALDDApaelrelrqELAALQAKAEAAPKEIlaSLSLEELEQRLLQTSAQLQ-ELQNQLAQLNSQLIELQtrpERAQ 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135    549 QKLDELgvkaltyndlIQAQKEISAHNQQLREQSEQLEQDNRALRGQSLQLLKARCEEL----------------QLDWA 612
Cdd:pfam12795  120 QQLSEA----------RQRLQQIRNRLNGPAPPGEPLSEAQRWALQAELAALKAQIDMLeqellsnnnrqdllkaRRDLL 189

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 22094135    613 TLSLEKLLKEKQALKSQISEKQRhclelqisiVELEKSQRQQELLQLKS 661
Cdd:pfam12795  190 TLRIQRLEQQLQALQELLNEKRL---------QEAEQAVAQTEQLAEEA 229
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 488-661 1.51e-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: 1.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135    488 LESFKIQYLQFLAYTKTPQYKaSLQELLGQEKEKNAQLLGAAQQLLSHCQAQKEEIRRLFQQKLDELGVKALTYNDLIQA 567
Cdd:TIGR04523  194 NKLLKLELLLSNLKKKIQKNK-SLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEK 272

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135    568 QKEISAHNQQLREQSEQLEQdnralrgqslqlLKARceelqldwatlsLEKLLKEKQA-----LKSQISEKQRHCLELQI 642
Cdd:TIGR04523  273 QKELEQNNKKIKELEKQLNQ------------LKSE------------ISDLNNQKEQdwnkeLKSELKNQEKKLEEIQN 328

                          170       180
                   ....*....|....*....|.
gi 22094135    643 SIVELEK--SQRQQELLQLKS 661
Cdd:TIGR04523  329 QISQNNKiiSQLNEQISQLKK 349
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 508-660 1.56e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.67  E-value: 1.56e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135    508 KASLQELLGQEKEKNAQLLGAAQQLlSHCQAQKEEIRRLFQQKLDElgvkaltYNDLIQAQKEISAHNQQLREQSEQLEQ 587
Cdd:TIGR02168  837 ERRLEDLEEQIEELSEDIESLAAEI-EELEELIEELESELEALLNE-------RASLEEALALLRSELEELSEELRELES 908

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22094135    588 DNRALRgQSLQLLKARCEELQLDwatlsLEKLLKEKQALKSQISEKQRHCLELQI---SIVELEKSQRQQELLQLK 660
Cdd:TIGR02168  909 KRSELR-RELEELREKLAQLELR-----LEGLEVRIDNLQERLSEEYSLTLEEAEaleNKIEDDEEEARRRLKRLE 978
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
504-658 1.57e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.77  E-value: 1.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135  504 TPQYKASLQELLGQEKEKNAQLLGAAQQLLshCQAQKEEIRRLFQQK----LDELGVKALTYNDLIQAQKEISAHNQQLR 579
Cdd:COG4717  335 SPEELLELLDRIEELQELLREAEELEEELQ--LEELEQEIAALLAEAgvedEEELRAALEQAEEYQELKEELEELEEQLE 412

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135  580 EQSEQLEQdnrALRGQSLQLLKARCEELQLDWATLS--LEKLLKEKQALKSQISEkqrhclelqisiveLEKSQRQQELL 657
Cdd:COG4717  413 ELLGELEE---LLEALDEEELEEELEELEEELEELEeeLEELREELAELEAELEQ--------------LEEDGELAELL 475


                 .
gi 22094135  658 Q 658
Cdd:COG4717  476 Q 476
Rootletin pfam15035
Ciliary rootlet component, centrosome cohesion;
493-660 1.79e-05

Ciliary rootlet component, centrosome cohesion;


Pssm-ID: 464459 [Multi-domain]  Cd Length: 190  Bit Score: 47.34  E-value: 1.79e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135    493 IQYLQflayTKTPQYKASLQELLGQEKEKNAQLlgAAQQLLSHCQAQKEEIRRLFQQKLDELGVKALTYNDLIQAQKEIS 572
Cdd:pfam15035   18 VQKLQ----AKVLQYKKRCSELEQQLLEKTSEL--EKTELLLRKLTLEPRLQRLEREHSADLEEALIRLEEERQRSESLS 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135    573 AHNQQLREQSEQLEQDNRALRgQSLQLLKArceelqlDWATLSLEKLLK------EKQALKSQISEKQRHCLELQISIVE 646
Cdd:pfam15035   92 QVNSLLREQLEQASRANEALR-EDLQKLTN-------DWERAREELEQKesewrkEEEAFNEYLSSEHSRLLSLWREVVA 163

                          170       180
                   ....*....|....*....|
gi 22094135    647 LE------KSQRQQELLQLK 660
Cdd:pfam15035  164 VRrqftelKTATERDLSELK 183
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 500-661 2.09e-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: 49.30  E-value: 2.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135    500 AYTKTPQYKASLQELlgQEKeknaqlLGAAQQLLSHCQAQKEEIRRLFQQKLDELgvKALTyNDLIQAQKEISAHNQQLR 579
Cdd:TIGR02169  665 GILFSRSEPAELQRL--RER------LEGLKRELSSLQSELRRIENRLDELSQEL--SDAS-RKIGEIEKEIEQLEQEEE 733

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135    580 EQSEQLEQDNRALRG---------QSLQLLKARCEELQLDWATL--SLEKL--------LKEKQALKSQIsEKQRHCLEL 640
Cdd:TIGR02169  734 KLKERLEELEEDLSSleqeienvkSELKELEARIEELEEDLHKLeeALNDLearlshsrIPEIQAELSKL-EEEVSRIEA 812

                          170       180
                   ....*....|....*....|.
gi 22094135    641 QISIVELEKSQRQQELLQLKS 661
Cdd:TIGR02169  813 RLREIEQKLNRLTLEKEYLEK 833
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 775-1124 2.11e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 49.40  E-value: 2.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135   775 SPAKIVLRRHLSQDHTVPGRPAAS----ELHSRAEHTKENGLPYQSPSVPGSmklSPQDPRPLSPGALQLAGEKSSEKGL 850
Cdd:PHA03307   74 GPGTEAPANESRSTPTWSLSTLAPaspaREGSPTPPGPSSPDPPPPTPPPAS---PPPSPAPDLSEMLRPVGSPGPPPAA 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135   851 RERAYGSSGE-----LITSLPISIPLSTVQPNKLPVSIPLASVvlPSRAERARSTPSPvlQPRDPSSTLEkqiGANAHGA 925
Cdd:PHA03307  151 SPPAAGASPAavasdAASSRQAALPLSSPEETARAPSSPPAEP--PPSTPPAAASPRP--PRRSSPISAS---ASSPAPA 223

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135   926 GSRSLALAPAGFSYAGSVAISGALAGSPASLTPGAEPATLDESSSSGSLfATVGSRSSTPQHplllAQPRNSLPASPAHQ 1005
Cdd:PHA03307  224 PGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEA-SGWNGPSSRPGP----ASSSSSPRERSPSP 298

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135  1006 LSSSPRLGGAAQGPLPEASKGDLPSDSGFSDPESEAKRRivftittGAGSakqSPSSKHSPLTASARGDcvPSHGQDSRR 1085
Cdd:PHA03307  299 SPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSR-------GAAV---SPGPSPSRSPSPSRPP--PPADPSSPR 366

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 22094135  1086 RGRRKRASAGTPSLSAGVSPKRRALPSVAGLFTQPSGSP 1124
Cdd:PHA03307  367 KRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATG 405
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 509-655 3.04e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 48.22  E-value: 3.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135  509 ASLQELLGQEKEKNAQLLGAAQQ--------LLSHCQAQKEEIRRL--FQQKLDELGVKAltyNDLIQAQKEISAHNQQL 578
Cdd:COG4942   93 AELRAELEAQKEELAELLRALYRlgrqpplaLLLSPEDFLDAVRRLqyLKYLAPARREQA---EELRADLAELAALRAEL 169

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22094135  579 REQSEQLEQDNRALRGQSLQLLKARCEELQLdwatlsLEKLLKEKQALKSQISEKQRHCLELQISIVELEKSQRQQE 655
Cdd:COG4942  170 EAERAELEALLAELEEERAALEALKAERQKL------LARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 512-655 4.20e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.39  E-value: 4.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135  512 QELLGQEKEKNAQLLGAAQQLLshcQAQKEEIrrlfQQKLDELGvkaltyNDLIQAQKEISAHNQQLREQSEQLEQDNRA 591
Cdd:COG1196  216 RELKEELKELEAELLLLKLREL---EAELEEL----EAELEELE------AELEELEAELAELEAELEELRLELEELELE 282

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22094135  592 L--RGQSLQLLKARCEEL--QLDWATLSLEKLLKEKQALKSQISEKQRHCLELQISIVELEKSQRQQE 655
Cdd:COG1196  283 LeeAQAEEYELLAELARLeqDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE 350
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
545-661 6.32e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.20  E-value: 6.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135  545 RLFQQKLDELGVKALTYNDLIQAQKEISAHNQQLREQSEQLEQDNRALRGQSLQLLKARcEEL-----QLDWATLSLEKL 619
Cdd:COG4372   14 SLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQAR-SELeqleeELEELNEQLQAA 92

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 22094135  620 LKEKQALKSQISEKQRHCLELQISIVELEKSQR--QQELLQLKS 661
Cdd:COG4372   93 QAELAQAQEELESLQEEAEELQEELEELQKERQdlEQQRKQLEA 136
DUF4686 pfam15742
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ...
 496-659 7.36e-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: 46.98  E-value: 7.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135    496 LQFLAYTKTPQYKASLQELLGQEKEKNA----QLLGAAQQLLSHCQAQKEEIRRLFQQKLDElgvkaltynDLIQAQKEI 571
Cdd:pfam15742   97 LEVLKQAQSIKSQNSLQEKLAQEKSRVAdaeeKILELQQKLEHAHKVCLTDTCILEKKQLEE---------RIKEASENE 167

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135    572 SAHNQQLREQSEQ---LEQDNRALRGQ--SLQLLKARCEE--LQLDWATLSLEKLLKEKQALKSQISEKQRHCLEL--QI 642
Cdd:pfam15742  168 AKLKQQYQEEQQKrklLDQNVNELQQQvrSLQDKEAQLEMtnSQQQLRIQQQEAQLKQLENEKRKSDEHLKSNQELseKL 247

                          170
                   ....*....|....*..
gi 22094135    643 SIVELEKSQRQQELLQL 659
Cdd:pfam15742  248 SSLQQEKEALQEELQQV 264
PRK11281 PRK11281
mechanosensitive channel MscK;
479-656 9.88e-05

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 47.21  E-value: 9.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135   479 PTPPALQKLLESFKIQYLQFLAytKTPQYKASLQELlgqekekNAQLLGAAQQLLshcQAQkEEIRRL-------FQQKL 551
Cdd:PRK11281   52 KLLEAEDKLVQQDLEQTLALLD--KIDRQKEETEQL-------KQQLAQAPAKLR---QAQ-AELEALkddndeeTRETL 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135   552 DELGVKAL------TYNDLIQAQKEISAHNQQLREQSEQLEQDNRALRGQSLQLLKarceelqldwatlsLEKLLKEKQA 625
Cdd:PRK11281  119 STLSLRQLesrlaqTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQ--------------IRNLLKGGKV 184

                         170       180       190
                  ....*....|....*....|....*....|.
gi 22094135   626 LKSQISEKQRHCLELQISIVELEKSQRQQEL 656
Cdd:PRK11281  185 GGKALRPSQRVLLQAEQALLNAQNDLQRKSL 215
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 508-660 1.41e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.60  E-value: 1.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135    508 KASLQELLGQEKEKNAQL---LGAA--QQLLSHCQAQKEEIRRLfQQKLDELGVK--ALTYnDLIQAQKEIsahnQQLRE 580
Cdd:TIGR02169  767 IEELEEDLHKLEEALNDLearLSHSriPEIQAELSKLEEEVSRI-EARLREIEQKlnRLTL-EKEYLEKEI----QELQE 840

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135    581 QSEQLEqDNRALRGQSLQLLKARCEEL--QLDWATLSLEKLLKEKQALKSQISEKQRHCLELQISIVELEkSQRQQELLQ 658
Cdd:TIGR02169  841 QRIDLK-EQIKSIEKEIENLNGKKEELeeELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELE-AQIEKKRKR 918


                   ..
gi 22094135    659 LK 660
Cdd:TIGR02169  919 LS 920
Jnk-SapK_ap_N pfam09744
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ...
 530-635 1.54e-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: 1.54e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135    530 QQLLSHCQAQ-------KEEIRRLFQQKLDELGVKALTYNDLIQAQKEISAHNQQLREQSEQLEQDNRALRGQSLQLLKA 602
Cdd:pfam09744   39 ESLASRNQEHnveleelREDNEQLETQYEREKALRKRAEEELEEIEDQWEQETKDLLSQVESLEEENRRLEADHVSRLEE 118

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 22094135    603 RceELQLDWATLSLEKllKEKQALKS--QISEKQR 635
Cdd:pfam09744  119 K--EAELKKEYSKLHE--RETEVLRKlkEVVDRQR 149
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
 508-641 1.78e-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: 43.01  E-value: 1.78e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135    508 KASLQELLGQEKEKNAQLLGAAQQLLSHCQAQKEEIRRLfQQKldelgvkaltYNDLIQAQKEISAHNQQLREQSEQLEQ 587
Cdd:pfam07926    3 LSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREA-QQN----------YERELVLHAEDIKALQALREELNELKA 71

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 22094135    588 DNRALRGQsLQLLKARCEELQLDWAtlslekllKEKQALKSQISEKQRHCLELQ 641
Cdd:pfam07926   72 EIAELKAE-AESAKAELEESEESWE--------EQKKELEKELSELEKRIEDLN 116
PHA03247 PHA03247
large tegument protein UL36; Provisional
 811-1260 2.36e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.08  E-value: 2.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135   811 GLPYQSPSVPGSMKLSPQDPRPlSPGALQLAGEKSSEKGLRERAYGSSGELITSLP-----------ISIPLSTVQPNKL 879
Cdd:PHA03247 2610 GPAPPSPLPPDTHAPDPPPPSP-SPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPrrarrlgraaqASSPPQRPRRRAA 2688

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135   880 PVSI-PLASVVLPSRAERarsTPSPvlQPRDPSSTLEKQIGANAHGAGSRSLALAPAGFSYAGSVAISGALAGSPASLTP 958
Cdd:PHA03247 2689 RPTVgSLTSLADPPPPPP---TPEP--APHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTT 2763

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135   959 GAEPATLDESSSSGSLFATVGSRSSTPQHPLLLAQPRNSLPASPAhqlssSPRLGGAAQGPLPEASKGDLPSdsgfsdpe 1038
Cdd:PHA03247 2764 AGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPP-----AAVLAPAAALPPAASPAGPLPP-------- 2830

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135  1039 seakrrivftiTTGAGSAKQSPSSKHSPLTASARGDCVPshGQDSRRRGRRKRASAgTPSLSAGVSPKRRALPSVaglft 1118
Cdd:PHA03247 2831 -----------PTSAQPTAPPPPPGPPPPSLPLGGSVAP--GGDVRRRPPSRSPAA-KPAAPARPPVRRLARPAV----- 2891

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135  1119 QPSGSPLNLnsmvsninQPLEITAISSPEtslksSPVPYQDHDQPPVLKKERPLSQTNGAHYSPLTSDEEPGSEDEPSSA 1198
Cdd:PHA03247 2892 SRSTESFAL--------PPDQPERPPQPQ-----APPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGA 2958

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22094135  1199 RIERKIATISLESKSPPKTLENGGGLAGRKPAPAGEPVNSSKWKSTFSPISDIGLAKSADSP 1260
Cdd:PHA03247 2959 VPQPWLGALVPGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLSRVSSWASSLALHEETDPP 3020
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 512-660 2.61e-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: 2.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135    512 QELLGQEKEKNAQLLGAAQQLLSHCQAQKEEIR---------RLFQQK-LDELGVKALTYNDLIQAQKEISAHNQQLREQ 581
Cdd:pfam13868  175 REEIEEEKEREIARLRAQQEKAQDEKAERDELRaklyqeeqeRKERQKeREEAEKKARQRQELQQAREEQIELKERRLAE 254

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135    582 SEQLEQD--NRALRGQSLQLLKARCEELQldwatlSLEKLLKEKQALKSQISEKQRHCL-ELQISIVELEKSQRQQELLQ 658
Cdd:pfam13868  255 EAEREEEefERMLRKQAEDEEIEQEEAEK------RRMKRLEHRRELEKQIEEREEQRAaEREEELEEGERLREEEAERR 328


                   ..
gi 22094135    659 LK 660
Cdd:pfam13868  329 ER 330
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
511-634 2.83e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.53  E-value: 2.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135  511 LQELLGQEKEKNAQL---LGAAQQLLSHCQAQ--KEEIRRLfQQKLDELgvkaltYNDLIQAQKEISAHNQQLreqsEQL 585
Cdd:COG4717  397 YQELKEELEELEEQLeelLGELEELLEALDEEelEEELEEL-EEELEEL------EEELEELREELAELEAEL----EQL 465

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 22094135  586 EQDNR--ALRgQSLQLLKARCEELQLDWATLSL-EKLLkeKQALKSQISEKQ 634
Cdd:COG4717  466 EEDGElaELL-QELEELKAELRELAEEWAALKLaLELL--EEAREEYREERL 514
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 485-656 3.10e-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: 3.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135    485 QKLLESFKIQYLQFLAYTKTPQYKASLQELLGQEKEKNAQLLGAAQQLLSHCQAQKEEIRRLfQQKLDELGVKALTYNDL 564
Cdd:TIGR00618  641 LALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQC-QTLLRELETHIEEYDRE 719

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135    565 IQAQKEIS-AHNQQLREQSEQLEQDNRALRGQSLQLLKARCEELQLDW-ATLSLEKLLKEKQALKSQISEKQRHCLELQI 642
Cdd:TIGR00618  720 FNEIENASsSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNeEVTAALQTGAELSHLAAEIQFFNRLREEDTH 799

                          170
                   ....*....|....
gi 22094135    643 SIVELEkSQRQQEL 656
Cdd:TIGR00618  800 LLKTLE-AEIGQEI 812
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 509-661 3.14e-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: 3.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135  509 ASLQELLGQEKEKNAQLLGAAQQLLSHCQAQK---EEIRRLFQQKLDELGVKALTYNDLIQAQKEISAHNQQLREQSEQL 585
Cdd:COG1196  281 LELEEAQAEEYELLAELARLEQDIARLEERRReleERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22094135  586 EQDNRALRGQSLQLlkarcEELQLDWATLSLEKLLKEKQALKSQISEKQrhcLELQISIVELEKSQRQQELLQLKS 661
Cdd:COG1196  361 AEAEEALLEAEAEL-----AEAEEELEELAEELLEALRAAAELAAQLEE---LEEAEEALLERLERLEEELEELEE 428
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 506-658 4.64e-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: 4.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135    506 QYKASLQELLGQEKEKNAQLLGAAQQLlshcQAQKEEIRRLFQQKLDElgvkaltyndLIQAQKEISAHNQQLREQsEQL 585
Cdd:pfam13868   52 ERERALEEEEEKEEERKEERKRYRQEL----EEQIEEREQKRQEEYEE----------KLQEREQMDEIVERIQEE-DQA 116

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22094135    586 EQDNRALRGQSLQLLKARCEELQLDWATLSLEKLLKEKQALKSQISEKQ-----RHCLELQIsivELEKSQRQQELLQ 658
Cdd:pfam13868  117 EAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAereeeREAEREEI---EEEKEREIARLRA 191
fliJ PRK05689
flagella biosynthesis chaperone FliJ;
509-634 5.90e-04

flagella biosynthesis chaperone FliJ;


Pssm-ID: 235563 [Multi-domain]  Cd Length: 147  Bit Score: 41.84  E-value: 5.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135   509 ASLQELLGQEKEKNAQLLGAAQQLLSHCQAQKEEI---RRLFQQKLDELGVKALT------YNDLI-QAQKEISAHNQQL 578
Cdd:PRK05689    8 ATLLDLAEKAEEQAALQLGQARQELQQAEQQLKMLedyRLEYRQQLNDRGSAGMTsswwinYQQFLqQLEKAITQQRQQL 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 22094135   579 REQSEQLEQdnrALrgQSLQLLKARCEELQldwaTLsLEKLLKEKQALKSQISEKQ 634
Cdd:PRK05689   88 TQWTQKVDN---AR--KYWQEKKQRLEALE----TL-QERYQTEARLAENKREQKQ 133
HrpE_YscL_not TIGR02499
type III secretion apparatus protein, HrpE/YscL family; This model is related to pfam06188, ...
 529-688 6.29e-04

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: 42.28  E-value: 6.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135    529 AQQLLSHCQAQKEEIRRLFQQKLDELgvKALTYNDliqaqkeisAHNQQLREQSEQL----EQDNRALRGqslqlLKARC 604
Cdd:TIGR02499   15 AQAILAAARQRAEAILADAEEEAEAS--RQLGYEQ---------GLEQFWQEAAAQLaewqQEAEQLEAS-----LEERL 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135    605 EELQLDwatlSLEKLLKEkqalksqISEKQRHCLELQisivELEKSQRQQELLQLkSCVPPD-DALSLHLRGKGALGR-E 682
Cdd:TIGR02499   79 AELVLQ----ALEQILGE-------YDEPERLVRLLR----QLLRAVANQGRLTL-RVHPEQlDEVREALAERLALEPwE 142


                   ....*.
gi 22094135    683 LEPDAS 688
Cdd:TIGR02499  143 LEPDAS 148
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 534-712 6.47e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 44.66  E-value: 6.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135    534 SHCQAQKEE-IRRLF--QQKLDELgvkaltyNDLIqaqKEISAHNQQLREQSEQLEQdnralrgqsLQLLKARCEELQLD 610
Cdd:TIGR02168  168 SKYKERRKEtERKLErtRENLDRL-------EDIL---NELERQLKSLERQAEKAER---------YKELKAELRELELA 228

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135    611 WATLSLEKLLKEKQALKSQISEKQRHCLELQisiveLEKSQRQQELLQLKSCVPPDDALSLHLRGK-GALGRELepdaSR 689
Cdd:TIGR02168  229 LLVLRLEELREELEELQEELKEAEEELEELT-----AELQELEEKLEELRLEVSELEEEIEELQKElYALANEI----SR 299

                          170       180
                   ....*....|....*....|...
gi 22094135    690 LHLELDCTKFSLPHLSSMSPELS 712
Cdd:TIGR02168  300 LEQQKQILRERLANLERQLEELE 322
PHA03247 PHA03247
large tegument protein UL36; Provisional
 884-1297 6.98e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.54  E-value: 6.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135   884 PLASVVLPSRAERARSTPSPVLQPRDPSSTL-EKQIGANAHGAGSRslalAPAGFSyaGSVAISGALAGSPASLTPGAEP 962
Cdd:PHA03247 2554 PLPPAAPPAAPDRSVPPPRPAPRPSEPAVTSrARRPDAPPQSARPR----APVDDR--GDPRGPAPPSPLPPDTHAPDPP 2627

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135   963 ATlDESSSSGSLFATVGSRSSTPQHPLLLAQPRNSLPASPAHQLSSSPRLGGAAQGPLPEASKGDLPSDSGFSDPESEAK 1042
Cdd:PHA03247 2628 PP-SPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPP 2706

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135  1043 rrivftiTTGAGSAKQSPSSKHSPLTASARGDCVPshgqdsRRRGRRKRASAGTPSLSAGVS-PKRRALPSVAGLFTQPS 1121
Cdd:PHA03247 2707 -------TPEPAPHALVSATPLPPGPAAARQASPA------LPAAPAPPAVPAGPATPGGPArPARPPTTAGPPAPAPPA 2773

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135  1122 GSPlnlnsmvSNINQPLEITAISSPETSLKSSPVPYQDHDQPPVLKkerplsqtngAHYSPLTSDEEPGSEDEPSSARIE 1201
Cdd:PHA03247 2774 APA-------AGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVL----------APAAALPPAASPAGPLPPPTSAQP 2836

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135  1202 rkiATISLESKSPPKTLENGGGLAG----RKPAPAGEPVnSSKWKSTFSPISDigLAKSADSPLQASSALSQNSLFTFR- 1276
Cdd:PHA03247 2837 ---TAPPPPPGPPPPSLPLGGSVAPggdvRRRPPSRSPA-AKPAAPARPPVRR--LARPAVSRSTESFALPPDQPERPPq 2910

                         410       420
                  ....*....|....*....|..
gi 22094135  1277 -PALEEPSADAKLAAHPRKGFP 1297
Cdd:PHA03247 2911 pQAPPPPQPQPQPPPPPQPQPP 2932
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 508-691 7.88e-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: 7.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135    508 KASLQELLGQEKEknaqLLGAAQQLLSHCQAQKEEIRRLFQQKLDELGVKALTYNDLIQAQKEISAHNQQLREQSEQlEQ 587
Cdd:pfam01576   42 KNALQEQLQAETE----LCAEAEEMRARLAARKQELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDE-EE 116

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135    588 DNRalrgQSLQLLK----ARCEELQLDwaTLSLE----KLLKEKQALKSQISEKQRHCLElqisivELEKSQRQQELLQL 659
Cdd:pfam01576  117 AAR----QKLQLEKvtteAKIKKLEED--ILLLEdqnsKLSKERKLLEERISEFTSNLAE------EEEKAKSLSKLKNK 184

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 22094135    660 KSCVPPDDALSLHLRGKG-----ALGRELEPDASRLH 691
Cdd:pfam01576  185 HEAMISDLEERLKKEEKGrqeleKAKRKLEGESTDLQ 221
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
511-661 8.35e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.99  E-value: 8.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135  511 LQELLGQEKEKNAQLLGAAQQLlshcQAQKEEIRRLfQQKLDELGVKALTYNDLIQAQkEISAHNQQLREQ-------SE 583
Cdd:COG4717   76 LEEELKEAEEKEEEYAELQEEL----EELEEELEEL-EAELEELREELEKLEKLLQLL-PLYQELEALEAElaelperLE 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135  584 QLEQDNRALRGQSLQL--LKARCEELQLDWATLSLEKLLKEKQALKSQISEKQRhcLELQISIVELEKSQRQQELLQLKS 661
Cdd:COG4717  150 ELEERLEELRELEEELeeLEAELAELQEELEELLEQLSLATEEELQDLAEELEE--LQQRLAELEEELEEAQEELEELEE 227
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 540-661 8.90e-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: 8.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135    540 KEEIRRLFQQKLDELGVKALTYNDLIQAQKE---ISAHNQQLREQSEQLEQDNRALRGQSLQ----LLKARCEELQLDWA 612
Cdd:TIGR04523  123 EVELNKLEKQKKENKKNIDKFLTEIKKKEKElekLNNKYNDLKKQKEELENELNLLEKEKLNiqknIDKIKNKLLKLELL 202

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 22094135    613 TLSLEKLLKEKQALKSQISE--KQRHCL-----ELQISIVELEK--SQRQQELLQLKS 661
Cdd:TIGR04523  203 LSNLKKKIQKNKSLESQISElkKQNNQLkdnieKKQQEINEKTTeiSNTQTQLNQLKD 260
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 484-661 9.61e-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: 9.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135    484 LQKLLESFKIQYLQFLAYTK-TPQYKASLQELlgqeKEKNAQLLGAAQQLlshcQAQKEEIRRLFQQKLDELGVK--ALT 560
Cdd:TIGR04523  484 LEQKQKELKSKEKELKKLNEeKKELEEKVKDL----TKKISSLKEKIEKL----ESEKKEKESKISDLEDELNKDdfELK 555

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135    561 YNDLiqaQKEISAHNQQLreqsEQLEQDNRALrgqslqllKARCEELQLDwatlsLEKLLKEKQALKSQISEKQRHCLEL 640
Cdd:TIGR04523  556 KENL---EKEIDEKNKEI----EELKQTQKSL--------KKKQEEKQEL-----IDQKEKEKKDLIKEIEEKEKKISSL 615

                          170       180
                   ....*....|....*....|...
gi 22094135    641 --QISIVELEKSQRQQELLQLKS 661
Cdd:TIGR04523  616 ekELEKAKKENEKLSSIIKNIKS 638
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 451-690 9.91e-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: 43.66  E-value: 9.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135    451 DAYRSpHSPFY-----QLPPSVQRHSPNPLlvaptppALQKLLE------SFKIQYLQFL--AYTKTPQYKASLQ---EL 514
Cdd:pfam10174  278 EVYKS-HSKFMknkidQLKQELSKKESELL-------ALQTKLEtltnqnSDCKQHIEVLkeSLTAKEQRAAILQtevDA 349

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135    515 LGQEKEKNAQLLGAAQQLLSHCQAQKE----EIRRLfqqkLDELGVKALTYNDLiqaQKEISAHNQQLREQSEQLEQdnr 590
Cdd:pfam10174  350 LRLRLEEKESFLNKKTKQLQDLTEEKStlagEIRDL----KDMLDVKERKINVL---QKKIENLQEQLRDKDKQLAG--- 419

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135    591 alrgqslqlLKARCEELQ-----LDWATLSLEKLLKEK----QALKSQISEKQRHCLElqisivELEksQRQQELLQLKS 661
Cdd:pfam10174  420 ---------LKERVKSLQtdssnTDTALTTLEEALSEKeriiERLKEQREREDRERLE------ELE--SLKKENKDLKE 482

                          250       260
                   ....*....|....*....|....*....
gi 22094135    662 CVppdDALSLHLRGKGALGRELEPDASRL 690
Cdd:pfam10174  483 KV---SALQPELTEKESSLIDLKEHASSL 508
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 503-657 1.02e-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: 43.79  E-value: 1.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135  503 KTPQYKASLQELLGQEKEKNAQLLGAAQQLlSHCQAQK----EEIRRL------FQQKLDELGVKALTYNDLIQAqkeis 572
Cdd:COG3096  348 KIERYQEDLEELTERLEEQEEVVEEAAEQL-AEAEARLeaaeEEVDSLksqladYQQALDVQQTRAIQYQQAVQA----- 421

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135  573 ahnqqLREQSEQLEQDNRALRGQSLQLLKARCEELQLDWATLSLEKLLKEKQALKSQIsekqRHCLELQISIV-ELEKS- 650
Cdd:COG3096  422 -----LEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQF----EKAYELVCKIAgEVERSq 492


                 ....*....
gi 22094135  651 --QRQQELL 657
Cdd:COG3096  493 awQTARELL 501
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 472-661 1.09e-03

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 43.80  E-value: 1.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135    472 PNPLLVAP-TPPALQKLLESFKIQYLQFLAYTKTpqYKASLQELLGQEKEKNAQLLGAAQ--QLLSHC-QAQKEEIRRLF 547
Cdd:TIGR00618  513 PNPARQDIdNPGPLTRRMQRGEQTYAQLETSEED--VYHQLTSERKQRASLKEQMQEIQQsfSILTQCdNRSKEDIPNLQ 590

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135    548 Q---------QKLDELGVKALTYNDLIQAQKEISAHNQQLREQSEQLEQDNR----ALRGQSLQLLKARCEELQLDWATL 614
Cdd:TIGR00618  591 NitvrlqdltEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELAlkltALHALQLTLTQERVREHALSIRVL 670

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 22094135    615 SLEKL------LKEKQALKSQIS---EKQRHCLELQISIVE-LEKSQRQQELLQLKS 661
Cdd:TIGR00618  671 PKELLasrqlaLQKMQSEKEQLTywkEMLAQCQTLLRELEThIEEYDREFNEIENAS 727
CENP-F_leu_zip pfam10473
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ...
 567-647 1.28e-03

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


Pssm-ID: 463102 [Multi-domain]  Cd Length: 140  Bit Score: 40.74  E-value: 1.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135    567 AQKEISAHNQQLREQSE---QLEQDNRALRG------QSLQLLKARCEELqlDWATLSLEKLLKEKQALKSQISEKQRHC 637
Cdd:pfam10473   50 SKAEVETLKAEIEEMAQnlrDLELDLVTLRSekenltKELQKKQERVSEL--ESLNSSLENLLEEKEQEKVQMKEESKTA 127

                           90
                   ....*....|.
gi 22094135    638 LE-LQISIVEL 647
Cdd:pfam10473  128 VEmLQTQLKEL 138
PRK11281 PRK11281
mechanosensitive channel MscK;
509-655 1.69e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 42.98  E-value: 1.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135   509 ASLQELLGqekEKNAQLLGA------AQQLLSHCQAQKEEIRRLFqqKLDELGVKALTYNDLIQAQKEISAHNQQLrEQS 582
Cdd:PRK11281  138 QNAQNDLA---EYNSQLVSLqtqperAQAALYANSQRLQQIRNLL--KGGKVGGKALRPSQRVLLQAEQALLNAQN-DLQ 211

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22094135   583 EQLEQDNRALrgQSLqllkarcEELQLDWATLSLEKLLKEKQALKSQISEKQrhcleLQISIVELEKSQRQQE 655
Cdd:PRK11281  212 RKSLEGNTQL--QDL-------LQKQRDYLTARIQRLEHQLQLLQEAINSKR-----LTLSEKTVQEAQSQDE 270
IKBKB_SDD pfam18397
IQBAL scaffold dimerization domain; This is the C-terminal scaffold dimerization domain (SDD) ...
 531-657 1.82e-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: 1.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135    531 QLLSHCQAQKEEIRRLFQqkldelGVKA-----LTYN-DLIQAQKEISAHNQQLREQSEQLEqdnralrgQSLQLLKARC 604
Cdd:pfam18397   44 QAWHYIRGLKEDYSRLQQ------GQRAamlslLRYNsNLSKMKNEMFSMSQQLKAKLDFFK--------TSIQIDLEKY 109

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22094135    605 EElQLDWATLSlEKLLK---------EKQALKSQISEKQRHCLELQISIVELEKS---QRQQELL 657
Cdd:pfam18397  110 SE-QMAFGISS-EKMLSawremeqkaELCGQVAEVNKLDEEMMALQTDIVELQRSpfaRRQGEVL 172
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
511-658 1.85e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 1.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135   511 LQELLGQEKEKNAQllGAAQQLLSHCQAQKEEIRRLFQQK--LDELgVKALTyNDLIQAQKEISAHNQQLREQSEQLEQD 588
Cdd:PRK03918  151 VRQILGLDDYENAY--KNLGEVIKEIKRRIERLEKFIKRTenIEEL-IKEKE-KELEEVLREINEISSELPELREELEKL 226

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135   589 NRALrgQSLQLLKARCEELQLDwatlsLEKLLKEKQALKSQISEKQRHCLELQISIVELEKSQRQQELLQ 658
Cdd:PRK03918  227 EKEV--KELEELKEEIEELEKE-----LESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELK 289
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 517-663 1.90e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 42.85  E-value: 1.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135    517 QEKEKNAQLLGA----AQQLLSHCQAQKEEIRRLFQQKLDELgvkaltyndliQAqkeisahnQQLREQSEQLeQDNRAL 592
Cdd:pfam01576  204 QELEKAKRKLEGestdLQEQIAELQAQIAELRAQLAKKEEEL-----------QA--------ALARLEEETA-QKNNAL 263

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135    593 RgqSLQLLKARCEELQLDwatLSLEKLLKEKqalksqiSEKQRHCL--ELQISIVELE------------KSQRQQELLQ 658
Cdd:pfam01576  264 K--KIRELEAQISELQED---LESERAARNK-------AEKQRRDLgeELEALKTELEdtldttaaqqelRSKREQEVTE 331


                   ....*
gi 22094135    659 LKSCV 663
Cdd:pfam01576  332 LKKAL 336
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
483-660 2.06e-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: 2.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135  483 ALQKLLESFKIQYlqflaYTKTPQYKASLQELLGQEKEKnaqllgaAQQLLSHCQAQKEE--IRRLF-QQKLDELGVKAL 559
Cdd:COG4913  159 ALKARLKKQGVEF-----FDSFSAYLARLRRRLGIGSEK-------ALRLLHKTQSFKPIgdLDDFVrEYMLEEPDTFEA 226

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135  560 -------------TYNDLIQAQK------EISAHNQQLREQSEQLEQdNRALR--------GQSLQLLKARCEELQLDwa 612
Cdd:COG4913  227 adalvehfddlerAHEALEDAREqiellePIRELAERYAAARERLAE-LEYLRaalrlwfaQRRLELLEAELEELRAE-- 303

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22094135  613 tlsLEKLLKEKQALKSQISEKQRHCLEL-----------------QISIVELEKSQRQQELLQLK 660
Cdd:COG4913  304 ---LARLEAELERLEARLDALREELDELeaqirgnggdrleqlerEIERLERELEERERRRARLE 365
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 159-267 2.20e-03

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


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 39.34  E-value: 2.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135  159 FVDLGSGVGQvVLQVAAATNCKHHYGVEKADIPAKYAETmdrefrkwmKWYGKKHAEYTLERGDFlsEEWRERIANT-SV 237
Cdd:cd02440    2 VLDLGCGTGA-LALALASGPGARVTGVDISPVALELARK---------AAAALLADNVEVLKGDA--EELPPEADESfDV 69

                         90       100       110
                 ....*....|....*....|....*....|..
gi 22094135  238 IFVNN-FAFGPEVDHQLKERFAN-MKEGGRIV 267
Cdd:cd02440   70 IISDPpLHHLVEDLARFLEEARRlLKPGGVLV 101
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 517-654 2.37e-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: 2.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135    517 QEKEKNAQLLGAAQQLLSHCQAQKEEIRRLFQQKLDELGVKALTYNDLIQA--------QKEISAH---------NQQLR 579
Cdd:pfam13868  116 AEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEreeereaeREEIEEEkereiarlrAQQEK 195

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135    580 EQSEQLEQDN-RALRGQSLQLLKARCEELQLdwatlsLEKLLKEKQALKS----QISEKQRhCLELQIsivELEKSQRQQ 654
Cdd:pfam13868  196 AQDEKAERDElRAKLYQEEQERKERQKEREE------AEKKARQRQELQQareeQIELKER-RLAEEA---EREEEEFER 265
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 539-671 3.14e-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: 3.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135    539 QKEEIRRLFQQKLDELGVKALTYNDLI----QAQKEisahNQQLREQSEQLEQDNralrgQSLQLLKARCEELQ-----L 609
Cdd:pfam13851   34 EIAELKKKEERNEKLMSEIQQENKRLTeplqKAQEE----VEELRKQLENYEKDK-----QSLKNLKARLKVLEkelkdL 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135    610 DWATLSL----EKLLKEKQALKSQ----ISEKQRHClELQISIVE---------LEKSQRQ-QELLQlkSCVPPDDALSL 671
Cdd:pfam13851  105 KWEHEVLeqrfEKVERERDELYDKfeaaIQDVQQKT-GLKNLLLEkklqalgetLEKKEAQlNEVLA--AANLDPDALQA 181
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 519-658 4.20e-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: 4.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135    519 KEKNAQLLGAAQQLLSHCQAQKEEIRRLFQQKLDELGVKALTYN-DLIQAQKEISAHNQQLREQSEQLEQDNRALRGQS- 596
Cdd:pfam08614   20 EAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQLReELAELYRSRGELAQRLVDLNEELQELEKKLREDEr 99

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22094135    597 -LQLLKARCEELQLdwATLSLEKLLKEK----QALKSQISEkqrhcLELQISIVElEKSQRQQ----ELLQ 658
Cdd:pfam08614  100 rLAALEAERAQLEE--KLKDREEELREKrklnQDLQDELVA-----LQLQLNMAE-EKLRKLEkenrELVE 162
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 500-598 4.55e-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: 4.55e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135     500 AYTKTPQYKASLQELLGQEKEKNAQLlgaaqqllshcQAQKEEIRRLfQQKLDELGVKaLTYNDLIQAQKEISAHNQQLR 579
Cdd:smart00935    9 ILQESPAGKAAQKQLEKEFKKRQAEL-----------EKLEKELQKL-KEKLQKDAAT-LSEAAREKKEKELQKKVQEFQ 75

                            90
                    ....*....|....*....
gi 22094135     580 EQSEQLEQDNRALRGQSLQ 598
Cdd:smart00935   76 RKQQKLQQDLQKRQQEELQ 94
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
 336-683 4.84e-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: 41.28  E-value: 4.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135    336 EEQEAARRRQQRESKSNAATPTKGPEGKVAGPADAPMDSGAEEEKAGAATVKKPSPSKARKKKLNKKGRKMAGR---KRG 412
Cdd:pfam09731   83 KEEKKQVKIPRQSGVSSEVAEEEKEATKDAAEAKAQLPKSEQEKEKALEEVLKEAISKAESATAVAKEAKDDAIqavKAH 162

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135    413 RPKKMNTANPERKP--KKNQTALDALHA-----------QTVSQTAASSPQD--AYRSPHS---PFYQLPPSVQRHSPNP 474
Cdd:pfam09731  163 TDSLKEASDTAEISreKATDSALQKAEAlaeklkevinlAKQSEEEAAPPLLdaAPETPPKlpeHLDNVEEKVEKAQSLA 242

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135    475 LLVAPtppaLQKLLESFKIQYLQFLAyTKTPQYKASLQELLGQEKEKNAQLLGAAQ-------QLLSHCQAQKE------ 541
Cdd:pfam09731  243 KLVDQ----YKELVASERIVFQQELV-SIFPDIIPVLKEDNLLSNDDLNSLIAHAHreidqlsKKLAELKKREEkhiera 317

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135    542 -EIRRLFQQKLDELGVKALTY---NDLIQAQKEISAHNQQLREQSE-----QLEQDNRALRGQSLQLLKARCEELQLDWA 612
Cdd:pfam09731  318 lEKQKEELDKLAEELSARLEEvraADEAQLRLEFEREREEIRESYEeklrtELERQAEAHEEHLKDVLVEQEIELQREFL 397

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22094135    613 TLSLEKLLKEKQALKSQISE-----KQRHCLELQISIVELEKSQRQQelLQLkSCVPPDDAL--SLHLRGKGALGREL 683
Cdd:pfam09731  398 QDIKEKVEEERAGRLLKLNEllanlKGLEKATSSHSEVEDENRKAQQ--LWL-AVEALRSTLedGSADSRPRPLVREL 472
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 519-646 5.72e-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: 41.21  E-value: 5.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135    519 KEKNAQLLGAAQQLLSHCQAQKE---EIR--RLFQQKL---DELGVKALTYNDLIQAqkEIsaHNQQLREQSEQLEQDNR 590
Cdd:pfam05622  217 EEKLEALQKEKERLIIERDTLREtneELRcaQLQQAELsqaDALLSPSSDPGDNLAA--EI--MPAEIREKLIRLQHENK 292

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 22094135    591 ALRGQSLQLLKARCEELQ--LDWATLSLEKLLKEKQALKSQISEKQRHCLELQISIVE 646
Cdd:pfam05622  293 MLRLGQEGSYRERLTELQqlLEDANRRKNELETQNRLANQRILELQQQVEELQKALQE 350
BBC smart00502
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains
 508-640 5.79e-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: 5.79e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135     508 KASLQELLGQEKEKNAQLLGAAQQLlshcqaqkEEIRRLFQQKLDElgvkaltyndliqAQKEISAHNQQLREQSEQLEQ 587
Cdd:smart00502    2 REALEELLTKLRKKAAELEDALKQL--------ISIIQEVEENAAD-------------VEAQIKAAFDELRNALNKRKK 60

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|...
gi 22094135     588 dnralrgQSLQLLKARCEELQLDwatlsLEKLLKEKQALKSQISEKQRHCLEL 640
Cdd:smart00502   61 -------QLLEDLEEQKENKLKV-----LEQQLESLTQKQEKLSHAINFTEEA 101
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 506-660 6.09e-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: 40.64  E-value: 6.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135  506 QYKASLQELLGQEKE----KNAQllgAAQQllsHCQAQKEEIR------------------RLFQQKLDEL--------- 554
Cdd:cd16269   90 KFQKKLMEQLEEKKEefckQNEE---ASSK---RCQALLQELSapleekisqgsysvpggyQLYLEDREKLvekyrqvpr 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135  555 -GVKAL------------TYNDLIQAQKEISAHNQQL---REQSEQLEQDNRALRGQ---SLQLLKARcEELQLDWATLS 615
Cdd:cd16269  164 kGVKAEevlqeflqskeaEAEAILQADQALTEKEKEIeaeRAKAEAAEQERKLLEEQqreLEQKLEDQ-ERSYEEHLRQL 242

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 22094135  616 LEKLLKEKQALKSQISEKQRHCLELQISIVE---LEKSQR-QQELLQLK 660
Cdd:cd16269  243 KEKMEEERENLLKEQERALESKLKEQEALLEegfKEQAELlQEEIRSLK 291
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
 500-598 6.18e-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: 6.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135  500 AYTKTPQYKASLQELLGQEKEKNAQLlgaaqqllshcQAQKEEIRRLfQQKLDELGVKaLTYNDLIQAQKEISAHNQQLR 579
Cdd:COG2825   34 ILQESPEGKAAQKKLEKEFKKRQAEL-----------QKLEKELQAL-QEKLQKEAAT-LSEEERQKKERELQKKQQELQ 100

                         90
                 ....*....|....*....
gi 22094135  580 EQSEQLEQDNRALRGQSLQ 598
Cdd:COG2825  101 RKQQEAQQDLQKRQQELLQ 119
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 506-660 6.86e-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: 39.74  E-value: 6.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135  506 QYKASLQELLG--QEKEKNAQ------LLGAAQQLLSHCQAQKEEIRRLfQQKLDELGVKAltyNDLIQAQ----KEISA 573
Cdd:cd00176    4 QFLRDADELEAwlSEKEELLSstdygdDLESVEALLKKHEALEAELAAH-EERVEALNELG---EQLIEEGhpdaEEIQE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135  574 HNQQLREQSEQLEQ--DNRALR-GQSLQLLK--ARCEELqLDWAT---------------LSLEKLLKEKQALKSQISEK 633
Cdd:cd00176   80 RLEELNQRWEELRElaEERRQRlEEALDLQQffRDADDL-EQWLEekeaalasedlgkdlESVEELLKKHKELEEELEAH 158

                        170       180
                 ....*....|....*....|....*..
gi 22094135  634 QRHCLELQISIVELEKSQRQQELLQLK 660
Cdd:cd00176  159 EPRLKSLNELAEELLEEGHPDADEEIE 185
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 500-658 7.30e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.58  E-value: 7.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135  500 AYTKTPQYKASLQELLGQEKEKNAQLLGAAQQLlshcQAQKEEIRRLfQQKLDELGvkaltyNDLIQAQKEISAHNQQLR 579
Cdd:COG3883   14 ADPQIQAKQKELSELQAELEAAQAELDALQAEL----EELNEEYNEL-QAELEALQ------AEIDKLQAEIAEAEAEIE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135  580 EQSEQLEQDNRAL--RGQSLQLLKA------------RCEelQLDWATLSLEKLLKEKQALKSQISEKQRhclELQISIV 645
Cdd:COG3883   83 ERREELGERARALyrSGGSVSYLDVllgsesfsdfldRLS--ALSKIADADADLLEELKADKAELEAKKA---ELEAKLA 157

                        170
                 ....*....|...
gi 22094135  646 ELEKSQRQQELLQ 658
Cdd:COG3883  158 ELEALKAELEAAK 170
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
483-658 7.90e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.77  E-value: 7.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135  483 ALQKLLESFKIQYLQFLAYTKTPQYKASLQELLGQEKEKNAQLLGAaqqllshcQAQKEEIRRLFQQKLDELGvkALTYN 562
Cdd:COG3206  193 EAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEA--------EARLAALRAQLGSGPDALP--ELLQS 262

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094135  563 DLIQA-QKEISAHNQQLREQSEQLEQDN---RALRGQSLQLLKARCEELQLDWATLS--LEKLLKEKQALKSQISEKQRH 636
Cdd:COG3206  263 PVIQQlRAQLAELEAELAELSARYTPNHpdvIALRAQIAALRAQLQQEAQRILASLEaeLEALQAREASLQAQLAQLEAR 342

                        170       180
                 ....*....|....*....|..
gi 22094135  637 CLELQISIVELEKSQRQQELLQ 658
Cdd:COG3206  343 LAELPELEAELRRLEREVEVAR 364
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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