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Conserved domains on  [gi|1935850156|gb|KAF9413631|]
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hypothetical protein HW555_008209 [Spodoptera exigua]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DUF1759 super family cl04160
Protein of unknown function (DUF1759); This is a family of proteins of unknown function. Most ...
 1233-1373 9.46e-32

Protein of unknown function (DUF1759); This is a family of proteins of unknown function. Most of the members are gag-polyproteins.


The actual alignment was detected with superfamily member pfam03564:

Pssm-ID: 281552  Cd Length: 148  Bit Score: 121.78  E-value: 9.46e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156 1233 FFGNYHKWISFKDLFQEAVHNNKSIPNAQKMQLLKTKLKGEAERIIQHLNISSENYQVCWDILNHRYNNDRLIFTSHMNI 1312
Cdd:pfam03564    1 FSGDYKEWPAFWDLFESTIHSKPHLPKVQKFNYLKSLLKGEAANVVAHLAITASNYESAWEALKKRYDNPRVIKRSLLNE 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1935850156 1313 LLSIPTMQNQVDTQIKNMFDTINECMNSLKNLGVDVTAMGPMVVHLLTLKLDTQTLSEYTQ 1373
Cdd:pfam03564   81 FMKLPSTNEDSVSQLRRFVDAANEIIRGLEALGENADQYDCILVHLLLQKLDEESRRKWIS 141
TMF_DNA_bd pfam12329
TATA element modulatory factor 1 DNA binding; This is the middle region of a family of TATA ...
 660-731 9.82e-19

TATA element modulatory factor 1 DNA binding; This is the middle region of a family of TATA element modulatory factor 1 proteins conserved in eukaryotes that contains at its N-terminal section a number of leucine zippers that could potentially form coiled coil structures.. The whole proteins bind to the TATA element of some RNA polymerase II promoters and repress their activity. by competing with the binding of TATA binding protein. TMFs are evolutionarily conserved golgins that bind Rab6, a ubiquitous ras-like GTP-binding Golgi protein, and contribute to Golgi organization in animal and plant cells.


:

Pssm-ID: 372049 [Multi-domain]  Cd Length: 74  Bit Score: 81.97  E-value: 9.82e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1935850156  660 LENTLKEKDEVIAQLQEEGEKLARQQLQHSNIIKKLRAKEKDNEQVIKGLRDKIAEQSAELDRMKRSIAAKE 731
Cdd:pfam12329    3 LEKLLKEKDEQIAQLMEEGEKLSKKELKLNNTIKKLRAKNKELEKEIAELKKKLEKLEKELENLEERLKRAE 74
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 550-850 5.93e-14

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 77.67  E-value: 5.93e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  550 SDESQGSENERLMRRLCEMAELLEARENRLLEMSRNNADLAENNADLKSQVESLISKHEggdintiteDYTQRMSALEKK 629
Cdd:COG1196    219 KEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELE---------ELELELEEAQAE 289

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  630 FQQAIREKDQLRKQLDqvksesssrknssELENTLKEKDEVIAQLQEEGEKLARQQLQHSNIIKKLRAKEKDNEQVIKGL 709
Cdd:COG1196    290 EYELLAELARLEQDIA-------------RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  710 RDKIAEQSAELDRMKRSIAAKEELEVSQIEAVYRLTTANKKLETELMETRSQLDDTQQKLEGSRASLEGARRELAELQRg 789
Cdd:COG1196    357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE- 435

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1935850156  790 sadlarRAAAAQHAHETAQRADHDLRALRAELAQLREDRRTEEKKWVAREEALRRELQEAR 850
Cdd:COG1196    436 ------EEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490
TMF_TATA_bd super family cl26375
TATA element modulatory factor 1 TATA binding; This is the C-terminal conserved coiled coil ...
 1701-1783 2.32e-13

TATA element modulatory factor 1 TATA binding; This is the C-terminal conserved coiled coil region of a family of TATA element modulatory factor 1 proteins conserved in eukaryotes. The proteins bind to the TATA element of some RNA polymerase II promoters and repress their activity. by competing with the binding of TATA binding protein. TMF1_TATA_bd is the most conserved part of the TMFs. TMFs are evolutionarily conserved golgins that bind Rab6, a ubiquitous ras-like GTP-binding Golgi protein, and contribute to Golgi organization in animal and plant cells. The Rab6-binding domain appears to be the same region as this C-terminal family.


The actual alignment was detected with superfamily member pfam12325:

Pssm-ID: 432481 [Multi-domain]  Cd Length: 115  Bit Score: 67.96  E-value: 2.32e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156 1701 SALRRRDGEVRALVAHRDSLRGQRDQLAAELARCQAALDDM--------------QSVQEQYDALLQMYGEKEEQMAELR 1766
Cdd:pfam12325   19 STIRRLEGELASLKEELARLEAQRDEARQEIVKLMKENEELkelkkeleelekelKELEQRYETTLELLGEKSEEVEELK 98

                           90
                   ....*....|....*..
gi 1935850156 1767 LDLQDVTQLYKAQLDEL 1783
Cdd:pfam12325   99 ADVEDLKEMYREQVQQL 115
pepsin_retropepsin_like super family cl11403
Cellular and retroviral pepsin-like aspartate proteases; This family includes both cellular ...
 1573-1653 7.81e-03

Cellular and retroviral pepsin-like aspartate proteases; This family includes both cellular and retroviral pepsin-like aspartate proteases. The cellular pepsin and pepsin-like enzymes are twice as long as their retroviral counterparts. The cellular pepsin-like aspartic proteases are found in mammals, plants, fungi and bacteria. These well known and extensively characterized enzymes include pepsins, chymosin, rennin, cathepsins, and fungal aspartic proteases. Several have long been known to be medically (rennin, cathepsin D and E, pepsin) or commercially (chymosin) important. The eukaryotic pepsin-like proteases contain two domains possessing similar topological features. The N- and C-terminal domains, although structurally related by a 2-fold axis, have only limited sequence homology except in the vicinity of the active site. This suggests that the enzymes evolved by an ancient duplication event. The eukaryotic pepsin-like proteases have two active site ASP residues with each N- and C-terminal lobe contributing one residue. While the fungal and mammalian pepsins are bilobal proteins, retropepsins function as dimers and the monomer resembles structure of the N- or C-terminal domains of eukaryotic enzyme. The active site motif (Asp-Thr/Ser-Gly-Ser) is conserved between the retroviral and eukaryotic proteases and between the N-and C-terminal of eukaryotic pepsin-like proteases. The retropepsin-like family includes pepsin-like aspartate proteases from retroviruses, retrotransposons and retroelements; as well as eukaryotic DNA-damage-inducible proteins (DDIs), and bacterial aspartate peptidases. Retropepsin is synthesized as part of the POL polyprotein that contains an aspartyl-protease, a reverse transcriptase, RNase H, and an integrase. The POL polyprotein undergoes specific enzymatic cleavage to yield the mature proteins. This family of aspartate proteases is classified by MEROPS as the peptidase family A1 (pepsin A) and A2 (retropepsin family).


The actual alignment was detected with superfamily member pfam05585:

Pssm-ID: 472175  Cd Length: 164  Bit Score: 39.14  E-value: 7.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156 1573 VRIQGINGEYHTMRALIDQGSQASLITENAAQILKLPRRACKGVIVGVSANQTN-CKGVLSLVASSLYSNYTFQTEVEQS 1651
Cdd:pfam05585    1 VVVSNAQGARTKCRLLFDSGSELSYISERCINRLGLARTPSRILVIGISGDKAPqTRGSNRTVISSRLSNGTLAVRAHVL 80


                   ..
gi 1935850156 1652 SR 1653
Cdd:pfam05585   81 KK 82
 
Name Accession Description Interval E-value
DUF1759 pfam03564
Protein of unknown function (DUF1759); This is a family of proteins of unknown function. Most ...
 1233-1373 9.46e-32

Protein of unknown function (DUF1759); This is a family of proteins of unknown function. Most of the members are gag-polyproteins.


Pssm-ID: 281552  Cd Length: 148  Bit Score: 121.78  E-value: 9.46e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156 1233 FFGNYHKWISFKDLFQEAVHNNKSIPNAQKMQLLKTKLKGEAERIIQHLNISSENYQVCWDILNHRYNNDRLIFTSHMNI 1312
Cdd:pfam03564    1 FSGDYKEWPAFWDLFESTIHSKPHLPKVQKFNYLKSLLKGEAANVVAHLAITASNYESAWEALKKRYDNPRVIKRSLLNE 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1935850156 1313 LLSIPTMQNQVDTQIKNMFDTINECMNSLKNLGVDVTAMGPMVVHLLTLKLDTQTLSEYTQ 1373
Cdd:pfam03564   81 FMKLPSTNEDSVSQLRRFVDAANEIIRGLEALGENADQYDCILVHLLLQKLDEESRRKWIS 141
TMF_DNA_bd pfam12329
TATA element modulatory factor 1 DNA binding; This is the middle region of a family of TATA ...
 660-731 9.82e-19

TATA element modulatory factor 1 DNA binding; This is the middle region of a family of TATA element modulatory factor 1 proteins conserved in eukaryotes that contains at its N-terminal section a number of leucine zippers that could potentially form coiled coil structures.. The whole proteins bind to the TATA element of some RNA polymerase II promoters and repress their activity. by competing with the binding of TATA binding protein. TMFs are evolutionarily conserved golgins that bind Rab6, a ubiquitous ras-like GTP-binding Golgi protein, and contribute to Golgi organization in animal and plant cells.


Pssm-ID: 372049 [Multi-domain]  Cd Length: 74  Bit Score: 81.97  E-value: 9.82e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1935850156  660 LENTLKEKDEVIAQLQEEGEKLARQQLQHSNIIKKLRAKEKDNEQVIKGLRDKIAEQSAELDRMKRSIAAKE 731
Cdd:pfam12329    3 LEKLLKEKDEQIAQLMEEGEKLSKKELKLNNTIKKLRAKNKELEKEIAELKKKLEKLEKELENLEERLKRAE 74
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 550-850 5.93e-14

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 77.67  E-value: 5.93e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  550 SDESQGSENERLMRRLCEMAELLEARENRLLEMSRNNADLAENNADLKSQVESLISKHEggdintiteDYTQRMSALEKK 629
Cdd:COG1196    219 KEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELE---------ELELELEEAQAE 289

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  630 FQQAIREKDQLRKQLDqvksesssrknssELENTLKEKDEVIAQLQEEGEKLARQQLQHSNIIKKLRAKEKDNEQVIKGL 709
Cdd:COG1196    290 EYELLAELARLEQDIA-------------RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  710 RDKIAEQSAELDRMKRSIAAKEELEVSQIEAVYRLTTANKKLETELMETRSQLDDTQQKLEGSRASLEGARRELAELQRg 789
Cdd:COG1196    357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE- 435

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1935850156  790 sadlarRAAAAQHAHETAQRADHDLRALRAELAQLREDRRTEEKKWVAREEALRRELQEAR 850
Cdd:COG1196    436 ------EEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490
TMF_TATA_bd pfam12325
TATA element modulatory factor 1 TATA binding; This is the C-terminal conserved coiled coil ...
 1701-1783 2.32e-13

TATA element modulatory factor 1 TATA binding; This is the C-terminal conserved coiled coil region of a family of TATA element modulatory factor 1 proteins conserved in eukaryotes. The proteins bind to the TATA element of some RNA polymerase II promoters and repress their activity. by competing with the binding of TATA binding protein. TMF1_TATA_bd is the most conserved part of the TMFs. TMFs are evolutionarily conserved golgins that bind Rab6, a ubiquitous ras-like GTP-binding Golgi protein, and contribute to Golgi organization in animal and plant cells. The Rab6-binding domain appears to be the same region as this C-terminal family.


Pssm-ID: 432481 [Multi-domain]  Cd Length: 115  Bit Score: 67.96  E-value: 2.32e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156 1701 SALRRRDGEVRALVAHRDSLRGQRDQLAAELARCQAALDDM--------------QSVQEQYDALLQMYGEKEEQMAELR 1766
Cdd:pfam12325   19 STIRRLEGELASLKEELARLEAQRDEARQEIVKLMKENEELkelkkeleelekelKELEQRYETTLELLGEKSEEVEELK 98

                           90
                   ....*....|....*..
gi 1935850156 1767 LDLQDVTQLYKAQLDEL 1783
Cdd:pfam12325   99 ADVEDLKEMYREQVQQL 115
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 555-857 3.09e-12

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: 72.01  E-value: 3.09e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  555 GSENERLMRRLCEMAELLEAREnRLLEMSRNNADLAENNADLKSQVESLisKHEGGDINTITEDYTQRMSALEKKFQQAI 634
Cdd:TIGR02168  663 GGSAKTNSSILERRREIEELEE-KIEELEEKIAELEKALAELRKELEEL--EEELEQLRKELEELSRQISALRKDLARLE 739

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  635 REKDQLRKQLDQvksesssrknsseLENTLKEKDEVIAQLQEEGEKLARQQLQHSNIIKKLRAKEKDNEQVIKGLRDKIA 714
Cdd:TIGR02168  740 AEVEQLEERIAQ-------------LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALD 806

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  715 EQSAELDRMKRSIAakeelevsqieavyRLTTANKKLETELMETRSQLDDTQQKLEGSRASLEGARRELAELQRGSADLA 794
Cdd:TIGR02168  807 ELRAELTLLNEEAA--------------NLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELE 872

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1935850156  795 RRAAAAQHAHETAQRAdhdLRALRAELAQLREDRRTEEKKwvAREeaLRRELQEAREACTALE 857
Cdd:TIGR02168  873 SELEALLNERASLEEA---LALLRSELEELSEELRELESK--RSE--LRRELEELREKLAQLE 928
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 551-849 1.54e-08

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 59.14  E-value: 1.54e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  551 DESQGSENERLMRRLCEMAELLEareNRLLEMSRNNADLAENNADLKSQVESliskhEGGDINTITEDYTQRMSALEKKF 630
Cdd:pfam07888   11 EESHGEEGGTDMLLVVPRAELLQ---NRLEECLQERAELLQAQEAANRQREK-----EKERYKRDREQWERQRRELESRV 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  631 QQAIREKDQLRKQLDQvksesssrknsseLENTLKEKDEVIAQLQEEGEKLARQQLQHSNIIKKLrakekdnEQVIKGLR 710
Cdd:pfam07888   83 AELKEELRQSREKHEE-------------LEEKYKELSASSEELSEEKDALLAQRAAHEARIREL-------EEDIKTLT 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  711 DKIAEQSAELDRMKrsiaakeelevsqiEAVYRLTTANKKLETELMETRSQLDDTQQKLEGSRASLEGARRELAELQRGS 790
Cdd:pfam07888  143 QRVLERETELERMK--------------ERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQV 208

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1935850156  791 ADLARRAAAAQHAHETAQRADHDLRALRAELAQLREDRRTEEKKwvarEEALRRELQEA 849
Cdd:pfam07888  209 LQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERK----VEGLGEELSSM 263
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
555-859 2.83e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 52.37  E-value: 2.83e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  555 GSENERLMRRLCEMAELLEARENRLLEMSRNNADLAENNADLKSQVESL-------------ISKHEGGDIntiTEDYTQ 621
Cdd:PRK03918   383 GLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELkkakgkcpvcgreLTEEHRKEL---LEEYTA 459

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  622 RMSALEKKFQQAIREKDQLRKQLDQVKSESSSRKNSSELENTLKEkdevIAQLQEEGEKLArqqlqhsniIKKLRAKEKD 701
Cdd:PRK03918   460 ELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQ----LKELEEKLKKYN---------LEELEKKAEE 526

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  702 NEqvikGLRDKIAEQSAELDRMKRSIAAKEELEVSQIEAVYRLTTANKKLETELMETRSQLDDTQQKLEGSRASLEGARR 781
Cdd:PRK03918   527 YE----KLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYN 602

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  782 EL-------AELQRGSADLARRAAAAQHAHETAQRADHDLRALRAELAQLREDRRTEEKKWVARE-EALRRELQEAREAC 853
Cdd:PRK03918   603 EYlelkdaeKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEyLELSRELAGLRAEL 682


                   ....*.
gi 1935850156  854 TALESS 859
Cdd:PRK03918   683 EELEKR 688
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
600-725 2.33e-04

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 46.00  E-value: 2.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  600 VESLISKHEGGDINTITEDYTQRMSALEKKFQQAIREKDQLRKQLDQVKSESSSrknsseLENTLKEKDEVIAQLQEEGE 679
Cdd:COG2433    378 IEEALEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEE------LEAELEEKDERIERLERELS 451

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1935850156  680 KLARQQLQHSNIIKKLRAKEKDNEQV---IKGLRDKIAEQSAELDRMKR 725
Cdd:COG2433    452 EARSEERREIRKDREISRLDREIERLereLEEERERIEELKRKLERLKE 500
PRK11281 PRK11281
mechanosensitive channel MscK;
674-780 2.05e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 42.98  E-value: 2.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  674 LQEEGEKLARQQLQHS-NIIKKLRAKEKDNEQvikgLRDKIAEQSAELDRMKRSIAAKEELEVSQIEAVYRlTTANKKLE 752
Cdd:PRK11281    53 LLEAEDKLVQQDLEQTlALLDKIDRQKEETEQ----LKQQLAQAPAKLRQAQAELEALKDDNDEETRETLS-TLSLRQLE 127

                           90       100
                   ....*....|....*....|....*...
gi 1935850156  753 TELMETRSQLDDTQQKLEGSRASLEGAR 780
Cdd:PRK11281   128 SRLAQTLDQLQNAQNDLAEYNSQLVSLQ 155
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1697-1783 2.18e-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: 2.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156 1697 EDALSALRRR----DGEVRALVAHRDSLRGQR-DQLAAELARCQAALDDMQSVQEQYDALLQMYGEK----EEQMAELRL 1767
Cdd:COG4913    308 EAELERLEARldalREELDELEAQIRGNGGDRlEQLEREIERLERELEERERRRARLEALLAALGLPlpasAEEFAALRA 387

                           90
                   ....*....|....*.
gi 1935850156 1768 DLQDVTQLYKAQLDEL 1783
Cdd:COG4913    388 EAAALLEALEEELEAL 403
DUF1758 pfam05585
Putative peptidase (DUF1758); This is a family of nematode proteins of unknown function. ...
 1573-1653 7.81e-03

Putative peptidase (DUF1758); This is a family of nematode proteins of unknown function. However, it seems likely that these proteins act as aspartic peptidases.


Pssm-ID: 147642  Cd Length: 164  Bit Score: 39.14  E-value: 7.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156 1573 VRIQGINGEYHTMRALIDQGSQASLITENAAQILKLPRRACKGVIVGVSANQTN-CKGVLSLVASSLYSNYTFQTEVEQS 1651
Cdd:pfam05585    1 VVVSNAQGARTKCRLLFDSGSELSYISERCINRLGLARTPSRILVIGISGDKAPqTRGSNRTVISSRLSNGTLAVRAHVL 80


                   ..
gi 1935850156 1652 SR 1653
Cdd:pfam05585   81 KK 82
 
Name Accession Description Interval E-value
DUF1759 pfam03564
Protein of unknown function (DUF1759); This is a family of proteins of unknown function. Most ...
 1233-1373 9.46e-32

Protein of unknown function (DUF1759); This is a family of proteins of unknown function. Most of the members are gag-polyproteins.


Pssm-ID: 281552  Cd Length: 148  Bit Score: 121.78  E-value: 9.46e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156 1233 FFGNYHKWISFKDLFQEAVHNNKSIPNAQKMQLLKTKLKGEAERIIQHLNISSENYQVCWDILNHRYNNDRLIFTSHMNI 1312
Cdd:pfam03564    1 FSGDYKEWPAFWDLFESTIHSKPHLPKVQKFNYLKSLLKGEAANVVAHLAITASNYESAWEALKKRYDNPRVIKRSLLNE 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1935850156 1313 LLSIPTMQNQVDTQIKNMFDTINECMNSLKNLGVDVTAMGPMVVHLLTLKLDTQTLSEYTQ 1373
Cdd:pfam03564   81 FMKLPSTNEDSVSQLRRFVDAANEIIRGLEALGENADQYDCILVHLLLQKLDEESRRKWIS 141
TMF_DNA_bd pfam12329
TATA element modulatory factor 1 DNA binding; This is the middle region of a family of TATA ...
 660-731 9.82e-19

TATA element modulatory factor 1 DNA binding; This is the middle region of a family of TATA element modulatory factor 1 proteins conserved in eukaryotes that contains at its N-terminal section a number of leucine zippers that could potentially form coiled coil structures.. The whole proteins bind to the TATA element of some RNA polymerase II promoters and repress their activity. by competing with the binding of TATA binding protein. TMFs are evolutionarily conserved golgins that bind Rab6, a ubiquitous ras-like GTP-binding Golgi protein, and contribute to Golgi organization in animal and plant cells.


Pssm-ID: 372049 [Multi-domain]  Cd Length: 74  Bit Score: 81.97  E-value: 9.82e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1935850156  660 LENTLKEKDEVIAQLQEEGEKLARQQLQHSNIIKKLRAKEKDNEQVIKGLRDKIAEQSAELDRMKRSIAAKE 731
Cdd:pfam12329    3 LEKLLKEKDEQIAQLMEEGEKLSKKELKLNNTIKKLRAKNKELEKEIAELKKKLEKLEKELENLEERLKRAE 74
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 550-850 5.93e-14

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 77.67  E-value: 5.93e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  550 SDESQGSENERLMRRLCEMAELLEARENRLLEMSRNNADLAENNADLKSQVESLISKHEggdintiteDYTQRMSALEKK 629
Cdd:COG1196    219 KEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELE---------ELELELEEAQAE 289

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  630 FQQAIREKDQLRKQLDqvksesssrknssELENTLKEKDEVIAQLQEEGEKLARQQLQHSNIIKKLRAKEKDNEQVIKGL 709
Cdd:COG1196    290 EYELLAELARLEQDIA-------------RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  710 RDKIAEQSAELDRMKRSIAAKEELEVSQIEAVYRLTTANKKLETELMETRSQLDDTQQKLEGSRASLEGARRELAELQRg 789
Cdd:COG1196    357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE- 435

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1935850156  790 sadlarRAAAAQHAHETAQRADHDLRALRAELAQLREDRRTEEKKWVAREEALRRELQEAR 850
Cdd:COG1196    436 ------EEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490
TMF_TATA_bd pfam12325
TATA element modulatory factor 1 TATA binding; This is the C-terminal conserved coiled coil ...
 1701-1783 2.32e-13

TATA element modulatory factor 1 TATA binding; This is the C-terminal conserved coiled coil region of a family of TATA element modulatory factor 1 proteins conserved in eukaryotes. The proteins bind to the TATA element of some RNA polymerase II promoters and repress their activity. by competing with the binding of TATA binding protein. TMF1_TATA_bd is the most conserved part of the TMFs. TMFs are evolutionarily conserved golgins that bind Rab6, a ubiquitous ras-like GTP-binding Golgi protein, and contribute to Golgi organization in animal and plant cells. The Rab6-binding domain appears to be the same region as this C-terminal family.


Pssm-ID: 432481 [Multi-domain]  Cd Length: 115  Bit Score: 67.96  E-value: 2.32e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156 1701 SALRRRDGEVRALVAHRDSLRGQRDQLAAELARCQAALDDM--------------QSVQEQYDALLQMYGEKEEQMAELR 1766
Cdd:pfam12325   19 STIRRLEGELASLKEELARLEAQRDEARQEIVKLMKENEELkelkkeleelekelKELEQRYETTLELLGEKSEEVEELK 98

                           90
                   ....*....|....*..
gi 1935850156 1767 LDLQDVTQLYKAQLDEL 1783
Cdd:pfam12325   99 ADVEDLKEMYREQVQQL 115
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 555-857 3.09e-12

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: 72.01  E-value: 3.09e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  555 GSENERLMRRLCEMAELLEAREnRLLEMSRNNADLAENNADLKSQVESLisKHEGGDINTITEDYTQRMSALEKKFQQAI 634
Cdd:TIGR02168  663 GGSAKTNSSILERRREIEELEE-KIEELEEKIAELEKALAELRKELEEL--EEELEQLRKELEELSRQISALRKDLARLE 739

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  635 REKDQLRKQLDQvksesssrknsseLENTLKEKDEVIAQLQEEGEKLARQQLQHSNIIKKLRAKEKDNEQVIKGLRDKIA 714
Cdd:TIGR02168  740 AEVEQLEERIAQ-------------LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALD 806

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  715 EQSAELDRMKRSIAakeelevsqieavyRLTTANKKLETELMETRSQLDDTQQKLEGSRASLEGARRELAELQRGSADLA 794
Cdd:TIGR02168  807 ELRAELTLLNEEAA--------------NLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELE 872

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1935850156  795 RRAAAAQHAHETAQRAdhdLRALRAELAQLREDRRTEEKKwvAREeaLRRELQEAREACTALE 857
Cdd:TIGR02168  873 SELEALLNERASLEEA---LALLRSELEELSEELRELESK--RSE--LRRELEELREKLAQLE 928
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 620-858 3.76e-12

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: 70.18  E-value: 3.76e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  620 TQRMSALEKKFQQAIREKDQLRKQLDQvksessSRKNSSELENTLKEKDEVIAQLQEEGEKLARQQLQHSNIIKKLRAKE 699
Cdd:COG4942     19 ADAAAEAEAELEQLQQEIAELEKELAA------LKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  700 KDNEQVIKGLRDKIAEQSAELDRMKRSIAAKEELEVSQIEAVYRLTTANKKLETELMETRSQLDDTQQKLEGSRASLEGA 779
Cdd:COG4942     93 AELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1935850156  780 RRELAELQRgsadlarraaaaqhahetaqradhDLRALRAELAQLREDRRTEEKKWVAREEALRRELQEAREACTALES 858
Cdd:COG4942    173 RAELEALLA------------------------ELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 588-858 5.44e-10

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: 64.69  E-value: 5.44e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  588 DLAENNADLKSQVESLISKHEggdintiteDYTQRMSALEKKFQQAIREKDQLRKQLDQVKSE-SSSRKNSSELENTLKE 666
Cdd:TIGR02168  236 ELREELEELQEELKEAEEELE---------ELTAELQELEEKLEELRLEVSELEEEIEELQKElYALANEISRLEQQKQI 306

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  667 KDEVIAQLQEEGEKLARQQLQHSNIIKKLRAKEKDNEQVIKGLRDKIAEQSAELDRMKrsiAAKEELEvsqieavyrltT 746
Cdd:TIGR02168  307 LRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELE---AELEELE-----------S 372

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  747 ANKKLETELMETRSQLDDTQQKLEGSRASLEGARRELAELQRGSADLARRAAAAQHAHETAQRADHDLRAlrAELAQLRE 826
Cdd:TIGR02168  373 RLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAEL--EELEEELE 450

                          250       260       270
                   ....*....|....*....|....*....|..
gi 1935850156  827 DRRTEEKKWVAREEALRRELQEAREACTALES 858
Cdd:TIGR02168  451 ELQEELERLEEALEELREELEEAEQALDAAER 482
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 543-827 6.35e-09

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: 61.23  E-value: 6.35e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  543 ASVQSNTSDESQGSENERLMRRLCEMAELLEARENRLLEMSRNNADLAENNADLKSQVESLISKHEGGDINTIT-----E 617
Cdd:TIGR02168  664 GSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARleaevE 743

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  618 DYTQRMSALEKKFQQAIREKDQLRKQLDQvksessSRKNSSELENTLKEKDEVIAQLQEEGEKLARQQLQHSNIIKKLRA 697
Cdd:TIGR02168  744 QLEERIAQLSKELTELEAEIEELEERLEE------AEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNE 817

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  698 KEKDNEQVIKGLRDKIAEQSAELDRMKRSIAAKEElevsQIEavyRLTTANKKLETELMETRSQLDDTQQKLEGSRASLE 777
Cdd:TIGR02168  818 EAANLRERLESLERRIAATERRLEDLEEQIEELSE----DIE---SLAAEIEELEELIEELESELEALLNERASLEEALA 890

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1935850156  778 GARRELAELQRGsadlarraaaAQHAHETAQRADHDLRALRAELAQLRED 827
Cdd:TIGR02168  891 LLRSELEELSEE----------LRELESKRSELRRELEELREKLAQLELR 930
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
631-852 6.46e-09

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 61.08  E-value: 6.46e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  631 QQAIREKDQLRKQLDQvksesssrknsseLENTLKEKDEVIAQLQEEGEKLARQQLQHSNiIKKLRAKEKDneqvIKGLR 710
Cdd:COG4913    606 FDNRAKLAALEAELAE-------------LEEELAEAEERLEALEAELDALQERREALQR-LAEYSWDEID----VASAE 667

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  711 DKIAEQSAELDRMKRSIAAKEELEvSQIEAvyrlttankkLETELMETRSQLDDTQQKLEGSRASLEGARRELAELQRGS 790
Cdd:COG4913    668 REIAELEAELERLDASSDDLAALE-EQLEE----------LEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1935850156  791 ADLARRAAAAQHAHETAQRADHDLRALRAEL-AQLREDRRTEEKKWVAREEALRRELQEAREA 852
Cdd:COG4913    737 EAAEDLARLELRALLEERFAAALGDAVERELrENLEERIDALRARLNRAEEELERAMRAFNRE 799
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 529-848 1.53e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.95  E-value: 1.53e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  529 LATKIRGHNRELSEASVQSNTSDESQGSENERLMRRLCEMAELLEARENrllemsrnnadLAENNADLKsqvesliskhe 608
Cdd:COG1196    279 LELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAE-----------LEEELEELE----------- 336

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  609 ggdintitedytQRMSALEKKFQQAIREKDQLRKQLDQvksesssrknsseLENTLKEKDEVIAQLQEEGEKLARQQLQH 688
Cdd:COG1196    337 ------------EELEELEEELEEAEEELEEAEAELAE-------------AEEALLEAEAELAEAEEELEELAEELLEA 391

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  689 SNIIKKLRAKEKDNEQVIKGLRDKIAEQSAELDRMKRSIAAKEELEVSQIEAVYRLTTANKKLETELMETRSQLDDTQQK 768
Cdd:COG1196    392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  769 LEGSRASLEGARRELAELqRGSADLARRAAAAQHAHETAQRADHDLRALRAELAQLREDRRTEEKKWVAREEALRRELQE 848
Cdd:COG1196    472 AALLEAALAELLEELAEA-AARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQN 550
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 551-849 1.54e-08

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 59.14  E-value: 1.54e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  551 DESQGSENERLMRRLCEMAELLEareNRLLEMSRNNADLAENNADLKSQVESliskhEGGDINTITEDYTQRMSALEKKF 630
Cdd:pfam07888   11 EESHGEEGGTDMLLVVPRAELLQ---NRLEECLQERAELLQAQEAANRQREK-----EKERYKRDREQWERQRRELESRV 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  631 QQAIREKDQLRKQLDQvksesssrknsseLENTLKEKDEVIAQLQEEGEKLARQQLQHSNIIKKLrakekdnEQVIKGLR 710
Cdd:pfam07888   83 AELKEELRQSREKHEE-------------LEEKYKELSASSEELSEEKDALLAQRAAHEARIREL-------EEDIKTLT 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  711 DKIAEQSAELDRMKrsiaakeelevsqiEAVYRLTTANKKLETELMETRSQLDDTQQKLEGSRASLEGARRELAELQRGS 790
Cdd:pfam07888  143 QRVLERETELERMK--------------ERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQV 208

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1935850156  791 ADLARRAAAAQHAHETAQRADHDLRALRAELAQLREDRRTEEKKwvarEEALRRELQEA 849
Cdd:pfam07888  209 LQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERK----VEGLGEELSSM 263
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 532-902 2.10e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.57  E-value: 2.10e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  532 KIRGHNRELSEASVQSNTSDESQGSENERLMRRLCEMAELLEARENRLLEMSRNNADLAENNADLKSQVESLISKheggd 611
Cdd:COG1196    289 EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA----- 363

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  612 intitedyTQRMSALEKKFQQAIREKDQLRKQLDQvksessSRKNSSELENTLKEKDEVIAQLQEEGEKLARQQLQHSNI 691
Cdd:COG1196    364 --------EEALLEAEAELAEAEEELEELAEELLE------ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  692 IKKLRAKEKDNEQVIKGLRDKIAEQSAELDRMKRSIAAKEELEVSQIEAVYRLTTANKKLETELMETRSQLDDTQQKLEG 771
Cdd:COG1196    430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEG 509

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  772 SRASLE-----GARRELAELQRGSADLARRAAAAQHAHETAQRADHDLRALRA--ELAQLREDRRTEEKKWVAREEALRR 844
Cdd:COG1196    510 VKAALLlaglrGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAieYLKAAKAGRATFLPLDKIRARAALA 589

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1935850156  845 ELQEAREACTALESSCSGGGGEGGAGAVLSQLAQLQAAALDRERAHAHALRQRALQLG 902
Cdd:COG1196    590 AALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLR 647
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 527-737 1.30e-07

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: 55.93  E-value: 1.30e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  527 KSLATKIRGHNRELSEASVQSNTSD------ESQGSENERLMRRLCEMAELLEARENRL-LEMSRNNADLAENNADLKSQ 599
Cdd:COG4942     30 EQLQQEIAELEKELAALKKEEKALLkqlaalERRIAALARRIRALEQELAALEAELAELeKEIAELRAELEAQKEELAEL 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  600 VESLISKHEGGDINTI--TEDYTQ--RMSALEKKFQQAIREK-DQLRKQLDQVKSESSSrknsseLENTLKEKDEVIAQL 674
Cdd:COG4942    110 LRALYRLGRQPPLALLlsPEDFLDavRRLQYLKYLAPARREQaEELRADLAELAALRAE------LEAERAELEALLAEL 183

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1935850156  675 QEEGEKLARQQLQHSNIIKKLRAKEKDNEQVIKGLRDKIAEQSAELDRMKRSIAAKEELEVSQ 737
Cdd:COG4942    184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 622-858 1.36e-07

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: 57.00  E-value: 1.36e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  622 RMSALEKKFQQAIREKDQLRKQLDQvksesssrknsseLENTLKEKDEVIAQLQEEGEKLARQQLQHSNIIKKLRAKEKD 701
Cdd:TIGR02169  682 RLEGLKRELSSLQSELRRIENRLDE-------------LSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSS 748

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  702 NEQVIKGLRDKIAEQSAELDRMKRSIAaKEELEVSQIEAVYR------LTTANKKLETELMETRSQLDDTQQKLEGSRAS 775
Cdd:TIGR02169  749 LEQEIENVKSELKELEARIEELEEDLH-KLEEALNDLEARLShsripeIQAELSKLEEEVSRIEARLREIEQKLNRLTLE 827

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  776 LEGARRELAELQRgsadlarRAAAAQHAHETAQRADHDLRALRAELAQLREDRRTEEKKWVAREEALRRELQEAREACTA 855
Cdd:TIGR02169  828 KEYLEKEIQELQE-------QRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRE 900


                   ...
gi 1935850156  856 LES 858
Cdd:TIGR02169  901 LER 903
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 625-851 2.65e-07

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: 55.84  E-value: 2.65e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  625 ALEKKFQQAIREKDQLRKQLDQVKSE-SSSRKNSSELENTLKEKDEVIAQLQEEGEKLARQQLQHSNI-IKKLRAKEKDN 702
Cdd:TIGR02169  234 ALERQKEAIERQLASLEEELEKLTEEiSELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAeIASLERSIAEK 313

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  703 EQVIKGLRDKIAEQSAELDRMKRSIAA-KEELEVSQIEaVYRLTTANKKLETELMETRSQLDD-------TQQKLEGSRA 774
Cdd:TIGR02169  314 ERELEDAEERLAKLEAEIDKLLAEIEElEREIEEERKR-RDKLTEEYAELKEELEDLRAELEEvdkefaeTRDELKDYRE 392

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  775 SLEGARRELAELQRgsadlarraaAAQHAHETAQRADHDLRALRAELAQLRED-RRTEEKKWVAREE--ALRRELQEARE 851
Cdd:TIGR02169  393 KLEKLKREINELKR----------ELDRLQEELQRLSEELADLNAAIAGIEAKiNELEEEKEDKALEikKQEWKLEQLAA 462
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 660-859 4.57e-07

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 54.07  E-value: 4.57e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  660 LENTLKEKDEVIAQLQEEGEKLARQQLQHSNIIKKLRAKEKDNEQVIKGLRDKIAEQSAELDR----MKRSIAAKEELEV 735
Cdd:COG3883     28 LQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEraraLYRSGGSVSYLDV 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  736 -----------SQIEAVYRLTTANKKLETELMETRSQLDDTQQKLEGSRASLEGARRELAELQRgsadlarraaaaqhah 804
Cdd:COG3883    108 llgsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA---------------- 171

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1935850156  805 etaqradhDLRALRAELAQLREDRRTEEKKWVAREEALRRELQEAREACTALESS 859
Cdd:COG3883    172 --------ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
571-788 1.46e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 53.23  E-value: 1.46e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  571 LLEARENRLLEMSRNNADLAENNADlksQVESLISK-HEGGDINTITEDYTQRMSALEKKFQQAIREKDQLRKQLDQVks 649
Cdd:COG4717     47 LLERLEKEADELFKPQGRKPELNLK---ELKELEEElKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL-- 121

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  650 esSSRKNSSELENTLKEKDEVIAQLQEEGEKLARQQLQHSNIIKKLRAkekdneqvikgLRDKIAEQSAELDRMKRSIAA 729
Cdd:COG4717    122 --EKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEE-----------LEAELAELQEELEELLEQLSL 188

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1935850156  730 KEELEVSQ-IEAVYRLTTANKKLETELMETRSQLDDTQQKLEGSRASLEGA--RRELAELQR 788
Cdd:COG4717    189 ATEEELQDlAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAalEERLKEARL 250
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 526-787 1.51e-06

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: 53.53  E-value: 1.51e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  526 GKSLATKIRGHNRELSEASVQSNTSDESQgsenERLMRRLCEMAELLEARENRLLEMSRNNADLAENNA-DLKSQVESLI 604
Cdd:TIGR02169  225 GYELLKEKEALERQKEAIERQLASLEEEL----EKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQlRVKEKIGELE 300

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  605 SKHEggDINTITEDYTQRMSALEKKFQQAIREKDQLRKQLDQVKSE-SSSRKNSSELENTLKEKDEV----IAQLQEEGE 679
Cdd:TIGR02169  301 AEIA--SLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREiEEERKRRDKLTEEYAELKEEledlRAELEEVDK 378

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  680 KLARQQLQHSNIIKKL-RAKEKDNE--QVIKGLRDKIAEQSAELDRMKRSIAAKEE-------------LEVSQIEavYR 743
Cdd:TIGR02169  379 EFAETRDELKDYREKLeKLKREINElkRELDRLQEELQRLSEELADLNAAIAGIEAkineleeekedkaLEIKKQE--WK 456

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1935850156  744 LTTANKKLETElmetRSQLDDTQQKLEGSRASLEGARRELAELQ 787
Cdd:TIGR02169  457 LEQLAADLSKY----EQELYDLKEEYDRVEKELSKLQRELAEAE 496
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 673-859 2.17e-06

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 50.69  E-value: 2.17e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  673 QLQEEGEKLARqqLQHsnIIKKLRAKEKDNEQVIKGLRDKIAEQSAELDRMKRSIAAKEElEVSQIEAvyRLttanKKLE 752
Cdd:COG1579     11 DLQELDSELDR--LEH--RLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLEL-EIEEVEA--RI----KKYE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  753 TELMETRS--QLDDTQQKLEGSRASLEGARRELAELQrgsadlarraaaaqhahETAQRADHDLRALRAELAQLREDRRT 830
Cdd:COG1579     80 EQLGNVRNnkEYEALQKEIESLKRRISDLEDEILELM-----------------ERIEELEEELAELEAELAELEAELEE 142

                          170       180
                   ....*....|....*....|....*....
gi 1935850156  831 EEKKWVAREEALRRELQEAREACTALESS 859
Cdd:COG1579    143 KKAELDEELAELEAELEELEAEREELAAK 171
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
555-859 2.83e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 52.37  E-value: 2.83e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  555 GSENERLMRRLCEMAELLEARENRLLEMSRNNADLAENNADLKSQVESL-------------ISKHEGGDIntiTEDYTQ 621
Cdd:PRK03918   383 GLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELkkakgkcpvcgreLTEEHRKEL---LEEYTA 459

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  622 RMSALEKKFQQAIREKDQLRKQLDQVKSESSSRKNSSELENTLKEkdevIAQLQEEGEKLArqqlqhsniIKKLRAKEKD 701
Cdd:PRK03918   460 ELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQ----LKELEEKLKKYN---------LEELEKKAEE 526

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  702 NEqvikGLRDKIAEQSAELDRMKRSIAAKEELEVSQIEAVYRLTTANKKLETELMETRSQLDDTQQKLEGSRASLEGARR 781
Cdd:PRK03918   527 YE----KLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYN 602

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  782 EL-------AELQRGSADLARRAAAAQHAHETAQRADHDLRALRAELAQLREDRRTEEKKWVARE-EALRRELQEAREAC 853
Cdd:PRK03918   603 EYlelkdaeKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEyLELSRELAGLRAEL 682


                   ....*.
gi 1935850156  854 TALESS 859
Cdd:PRK03918   683 EELEKR 688
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 527-783 4.80e-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: 51.60  E-value: 4.80e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  527 KSLATKIRGHNRELSeasvQSNTSDESQGSENERLMRRLCEMAELLEARENRLLEMSRNNADLAENNADLKSQVESLISK 606
Cdd:TIGR02168  785 EELEAQIEQLKEELK----ALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAE 860

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  607 HEggDINTITEDYTQRMSALEKKFQQAIREKDQLRKQLDQVKSE-SSSRKNSSELENTLKEKDEVIAQLQEEGEKLaRQQ 685
Cdd:TIGR02168  861 IE--ELEELIEELESELEALLNERASLEEALALLRSELEELSEElRELESKRSELRRELEELREKLAQLELRLEGL-EVR 937

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  686 LQhsNIIKKLRAKEKDNEQVIKGLRDKIAEQSA----ELDRMKRSIAAKEELEVSQIEAVyrlttanKKLETELMETRSQ 761
Cdd:TIGR02168  938 ID--NLQERLSEEYSLTLEEAEALENKIEDDEEearrRLKRLENKIKELGPVNLAAIEEY-------EELKERYDFLTAQ 1008

                          250       260
                   ....*....|....*....|..
gi 1935850156  762 LDDtqqkLEGSRASLEGARREL 783
Cdd:TIGR02168 1009 KED----LTEAKETLEEAIEEI 1026
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
557-788 8.58e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 50.83  E-value: 8.58e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  557 ENERLMRRLCEMAELLEARENRLlemSRNNADLAENNADLKSQVESLISKHEGgDINTITEDyTQRMSALEKKFQQAIRE 636
Cdd:PRK03918   490 KKESELIKLKELAEQLKELEEKL---KKYNLEELEKKAEEYEKLKEKLIKLKG-EIKSLKKE-LEKLEELKKKLAELEKK 564

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  637 KDQLRKQLdqvksesssrknsSELENTLKEK-----DEVIAQLQEEgEKLARQQLQHSNIIKKLRAKE---KDNEQVIKG 708
Cdd:PRK03918   565 LDELEEEL-------------AELLKELEELgfesvEELEERLKEL-EPFYNEYLELKDAEKELEREEkelKKLEEELDK 630

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  709 LRDKIAEQSAELDRMKRSIaakEELEVSQIEAVYR-LTTANKKLETELMETRSQLDDTQQKLEGSRASLEGARRELAELQ 787
Cdd:PRK03918   631 AFEELAETEKRLEELRKEL---EELEKKYSEEEYEeLREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEERE 707


                   .
gi 1935850156  788 R 788
Cdd:PRK03918   708 K 708
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 660-858 8.60e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.83  E-value: 8.60e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  660 LENTLKEKDEVIAQLQEEGEKLARQQLQHSNIIKKLRAKEKDNEQVIKGLRDKIAEQSAE-------LDRMKRSIAAKEE 732
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEveqleerIAQLSKELTELEA 761

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  733 LEVSQIEAVYRLTTANKKLETELMETRSQLDDTQQKLEGSRASLEGARRELAELQRGSADLARRAAAAQHAHETAQR--- 809
Cdd:TIGR02168  762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERrle 841

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  810 --------ADHDLRALRAELAQLREDRRTEEKK---WVAREEALRRELQEAREACTALES 858
Cdd:TIGR02168  842 dleeqieeLSEDIESLAAEIEELEELIEELESEleaLLNERASLEEALALLRSELEELSE 901
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
590-857 1.36e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 50.06  E-value: 1.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  590 AENNADLKSQVESLISKHEggDINTITEDYTQRMSALEKKFQQAIREKDQLRKQLDQVKSEsssrknsseLENTLKEKDE 669
Cdd:PRK03918   164 YKNLGEVIKEIKRRIERLE--KFIKRTENIEELIKEKEKELEEVLREINEISSELPELREE---------LEKLEKEVKE 232

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  670 ViAQLQEEGEKLARQQLQHSNIIKKLRAKEKDNEQVIKGLRDKIAEQSAELDRMKrSIAAKEELEVSQIEAVYRLTTANK 749
Cdd:PRK03918   233 L-EELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELR 310

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  750 KLETELMETRSQLDDTQ---QKLEGSRASLEGARRELAELQRgsadlarraaaAQHAHETAQRADHDLRALRAELAQLRE 826
Cdd:PRK03918   311 EIEKRLSRLEEEINGIEeriKELEEKEERLEELKKKLKELEK-----------RLEELEERHELYEEAKAKKEELERLKK 379

                          250       260       270
                   ....*....|....*....|....*....|.
gi 1935850156  827 DRRTEEKkwvareEALRRELQEAREACTALE 857
Cdd:PRK03918   380 RLTGLTP------EKLEKELEELEKAKEEIE 404
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
620-851 1.76e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.91  E-value: 1.76e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  620 TQRMSALEKKFQQAIREKDQLRKQLD---QVKSESSSRKNSSELENTLKEKDEVIAQLQEEGEKLARQQLQhsniIKKLR 696
Cdd:COG4913    623 EEELAEAEERLEALEAELDALQERREalqRLAEYSWDEIDVASAEREIAELEAELERLDASSDDLAALEEQ----LEELE 698

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  697 AKEKDNEQVIKGLRDKIAEQSAELDRMKRSIAAKEEL--EVSQIEAVYRLTTANKKLETELmetrsqLDDTQQKLegsRA 774
Cdd:COG4913    699 AELEELEEELDELKGEIGRLEKELEQAEEELDELQDRleAAEDLARLELRALLEERFAAAL------GDAVEREL---RE 769

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  775 SLEGARRELAELQRGSADLARRAAAAQHAHETAQRADHD-----LRALRAELAQLREDR--RTEEK------KWVARE-- 839
Cdd:COG4913    770 NLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDadlesLPEYLALLDRLEEDGlpEYEERfkellnENSIEFva 849

                          250
                   ....*....|....*
gi 1935850156  840 ---EALRRELQEARE 851
Cdd:COG4913    850 dllSKLRRAIREIKE 864
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
539-790 1.83e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 49.63  E-value: 1.83e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  539 ELSEASVQSNTSDESQGSEN--ERLMRRLCEMAELLEARENRLLEMSRNN--ADLAENNADLKSQVESLiskheggdint 614
Cdd:COG3206    156 ALAEAYLEQNLELRREEARKalEFLEEQLPELRKELEEAEAALEEFRQKNglVDLSEEAKLLLQQLSEL----------- 224

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  615 itedyTQRMSALEKKFQQAIREKDQLRKQLDQVKSESSSRKNSSELENTLKEKDEVIAQLQEegeklarqqlqhsniikk 694
Cdd:COG3206    225 -----ESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAE------------------ 281

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  695 LRAKEKDNEQVIKGLRDKIAEQSAELDRMKRSIAAKEELEVSQIEAvyRLTTANKKLET------ELMETRSQLDDTQQK 768
Cdd:COG3206    282 LSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQA--REASLQAQLAQlearlaELPELEAELRRLERE 359

                          250       260
                   ....*....|....*....|....
gi 1935850156  769 LEGSRASLEG--ARRELAELQRGS 790
Cdd:COG3206    360 VEVARELYESllQRLEEARLAEAL 383
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 527-786 3.23e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 48.91  E-value: 3.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  527 KSLATKIRGHNRELSEASVQSNTSDESQGSENERLMRRLCEMAELLEARENRLLEMSRNNADLAENNADL---------- 596
Cdd:TIGR02169  705 DELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLhkleealndl 784

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  597 ---------------KSQVESLISKHEG--GDINTITEDYTQRMSALEKKFQQAIREKDQLRKQLDQVKSE-SSSRKNSS 658
Cdd:TIGR02169  785 earlshsripeiqaeLSKLEEEVSRIEArlREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEiENLNGKKE 864

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  659 ELENTLKEKDEVIAQLQEEGEKLARQQLQHSNIIKKLRAKEKDNEQVIKGLRDKIAEQSAELDRMKRSIAA-----KEEL 733
Cdd:TIGR02169  865 ELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEiedpkGEDE 944

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1935850156  734 EVSQIEAVYRLTTAN-KKLETELM--------------ETRSQLDDtqqkLEGSRASLEGARRELAEL 786
Cdd:TIGR02169  945 EIPEEELSLEDVQAElQRVEEEIRalepvnmlaiqeyeEVLKRLDE----LKEKRAKLEEERKAILER 1008
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
621-835 4.34e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 48.76  E-value: 4.34e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  621 QRMSALEKKFQQAIREKDQLRkQLDQVKSESSSRKNSSELENTLKEKDEVIAQLQEEGEKLARQQLQHSNIIKKLRAKEK 700
Cdd:COG4913    255 EPIRELAERYAAARERLAELE-YLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIR 333

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  701 DN--------EQVIKGLRDKIAEQSAELDRMKRSIAA--------KEELEVSQIEAVYRLTTankkLETELMETRSQLDD 764
Cdd:COG4913    334 GNggdrleqlEREIERLERELEERERRRARLEALLAAlglplpasAEEFAALRAEAAALLEA----LEEELEALEEALAE 409

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  765 TQQKLEGSRASLEGARRELAELQRGSADLarraaaaqhahetaqraDHDLRALRAELAQ---LREDR----------RTE 831
Cdd:COG4913    410 AEAALRDLRRELRELEAEIASLERRKSNI-----------------PARLLALRDALAEalgLDEAElpfvgelievRPE 472


                   ....
gi 1935850156  832 EKKW 835
Cdd:COG4913    473 EERW 476
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
620-851 5.12e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.23  E-value: 5.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  620 TQRMSALEKKFQQAIREKDQLRKQLDQVK-SESSSRKNSSELENTLKEKDEVIAQLQEEGEKLARQQLQHSNIIKKLRAK 698
Cdd:COG4717    301 GKEAEELQALPALEELEEEELEELLAALGlPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAG 380

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  699 EKDNEQVIKGLR--DKIAEQSAELDRMKRSIAAKEELEVSQIEAVYRlttanKKLETELMETRSQLDDTQQKLEGSRASL 776
Cdd:COG4717    381 VEDEEELRAALEqaEEYQELKEELEELEEQLEELLGELEELLEALDE-----EELEEELEELEEELEELEEELEELREEL 455

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1935850156  777 EGARRELAELQRgsadlarraaaaqhahetaqraDHDLRALRAELAQLREDRRTEEKKWVAR---EEALRRELQEARE 851
Cdd:COG4717    456 AELEAELEQLEE----------------------DGELAELLQELEELKAELRELAEEWAALklaLELLEEAREEYRE 511
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 617-859 7.23e-05

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 47.86  E-value: 7.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  617 EDYTQRMSALEKKFQQAIREkdqLRKQLDQVKSESSS-RKNSSELENTLKEKDEVIAQLQEEGEKLARQQLQHSNIIKKL 695
Cdd:pfam01576   88 EERSQQLQNEKKKMQQHIQD---LEEQLDEEEAARQKlQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEF 164

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  696 RAKEKDNEQVIKGL---RDKIAEQSAEL-DRMKRSIAAKEELEvsqieavyrltTANKKLETELMETRSQLDDTQQKLEG 771
Cdd:pfam01576  165 TSNLAEEEEKAKSLsklKNKHEAMISDLeERLKKEEKGRQELE-----------KAKRKLEGESTDLQEQIAELQAQIAE 233

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  772 SRASLEGARRELAELQrgsadlarraAAAQHAHETAQRADHDLRALRAELAQLREDRRTeEKKWVAREEALRRELQEARE 851
Cdd:pfam01576  234 LRAQLAKKEEELQAAL----------ARLEEETAQKNNALKKIRELEAQISELQEDLES-ERAARNKAEKQRRDLGEELE 302


                   ....*....
gi 1935850156  852 AC-TALESS 859
Cdd:pfam01576  303 ALkTELEDT 311
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
587-861 9.91e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 47.34  E-value: 9.91e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  587 ADLAENNADLKSQVESLISKHEggdintitedytqRMSALEKkfqqAIREKDQLRKQLDQVKSESSSRknsselENTLKE 666
Cdd:PRK02224   478 EELEAELEDLEEEVEEVEERLE-------------RAEDLVE----AEDRIERLEERREDLEELIAER------RETIEE 534

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  667 KDEVIAQLQEEGEKLARQQLQHSNIIKKLRAKEKDNEQVIKGLRDKIAEQSAELDRMKR---SIAAKEELEvsqiEAVYR 743
Cdd:PRK02224   535 KRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERirtLLAAIADAE----DEIER 610

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  744 LTTANKKLETELMETRSQLDDTQQKLEGSRASLEGARRELAELQRgsadlarraaaaqhahetaQRADHDLRALRAELAQ 823
Cdd:PRK02224   611 LREKREALAELNDERRERLAEKRERKRELEAEFDEARIEEAREDK-------------------ERAEEYLEQVEEKLDE 671

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1935850156  824 LREDRRTEEKKWVAREEALrRELQEAREACTALESSCS 861
Cdd:PRK02224   672 LREERDDLQAEIGAVENEL-EELEELRERREALENRVE 708
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 560-852 1.13e-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: 46.45  E-value: 1.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  560 RLMRRLCEMAELLEARENRLLEMSRNNADLAENNADLKSQVESLISKHEGgdintitedytQRMSALEKKFQQAIREKDQ 639
Cdd:pfam13868    9 RELNSKLLAAKCNKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALE-----------EEEEKEEERKEERKRYRQE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  640 LRKQLDQvksesSSRKNSSELENTLKEK---DEVIAQLQEEGEKLARQqlqhsniikKLRAKEKdneqvikgLRDKIAEQ 716
Cdd:pfam13868   78 LEEQIEE-----REQKRQEEYEEKLQEReqmDEIVERIQEEDQAEAEE---------KLEKQRQ--------LREEIDEF 135

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  717 SAELDRMKRSIAAKEELEVSQIEAVYRLTTAN-KKLETELMETRSQLDDTQQKLegsRASLEGARRELAELQRgsadlar 795
Cdd:pfam13868  136 NEEQAEWKELEKEEEREEDERILEYLKEKAEReEEREAEREEIEEEKEREIARL---RAQQEKAQDEKAERDE------- 205

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1935850156  796 raaaaqhahetaqradhdLRALRAELAQLREDRRtEEKKWVAREEALRRELQEAREA 852
Cdd:pfam13868  206 ------------------LRAKLYQEEQERKERQ-KEREEAEKKARQRQELQQAREE 243
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 572-786 1.23e-04

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 46.94  E-value: 1.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  572 LEARENRLLEMSRNNADLAENNADLKSQVESLISKheggdintitedytqrmsalEKKFQQAIREKDQLRKQLDQVKSES 651
Cdd:TIGR04523  491 LKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEK--------------------IEKLESEKKEKESKISDLEDELNKD 550

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  652 SSRKNSSELENTLKEKDEVIAQLQEEGEKLARQQLQHSNIIKKlraKEKDNEQVIKGLRDKIAEQSaELDRmkrsiaake 731
Cdd:TIGR04523  551 DFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQ---KEKEKKDLIKEIEEKEKKIS-SLEK--------- 617

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1935850156  732 ELEVSQIEavyrlttaNKKLETELMETRSQLDDTQQKLEGSRASLEGARRELAEL 786
Cdd:TIGR04523  618 ELEKAKKE--------NEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEI 664
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
671-857 1.74e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 46.30  E-value: 1.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  671 IAQLQEEGEKLARQQLQ-HSNIIKKLRAKEKDneqvIKGLRDKIAEQSAELDRMKRSIAAKEELEVSQIEAVYRLTTANK 749
Cdd:COG4717     48 LERLEKEADELFKPQGRkPELNLKELKELEEE----LKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEK 123

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  750 KLEteLMETRSQLDDTQQKLEGSRASLEGARRELAELQRgsadlarraaaaqhahetaqrADHDLRALRAELAQLREDRR 829
Cdd:COG4717    124 LLQ--LLPLYQELEALEAELAELPERLEELEERLEELRE---------------------LEEELEELEAELAELQEELE 180

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1935850156  830 TEEKKWVAREEA----LRRELQEAREACTALE 857
Cdd:COG4717    181 ELLEQLSLATEEelqdLAEELEELQQRLAELE 212
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
698-858 1.75e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 46.57  E-value: 1.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  698 KEKDNEQVIKGLRDKIAEQSAELDRmkrsiaakeeLEVSQIEAVYRLTTANKKLEtELMETRSQLDDTQQKLEGSRASLE 777
Cdd:PRK02224   200 EEKDLHERLNGLESELAELDEEIER----------YEEQREQARETRDEADEVLE-EHEERREELETLEAEIEDLRETIA 268

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  778 GARRELAELqRGSADLARRAAAAQHAHETAQRADHDLRALRAELAQLREDRRTEekkwvaREEALRRELQEAREACTALE 857
Cdd:PRK02224   269 ETEREREEL-AEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELED------RDEELRDRLEECRVAAQAHN 341


                   .
gi 1935850156  858 S 858
Cdd:PRK02224   342 E 342
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
663-858 1.89e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.45  E-value: 1.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  663 TLKEKDEVIAQLQEEGEKLARqqlqhsniikkLRAKEKDNEQVIKGLRDKIAEQSAELDRmKRSIAAKEELEVSQiEAVY 742
Cdd:COG4913    246 DAREQIELLEPIRELAERYAA-----------ARERLAELEYLRAALRLWFAQRRLELLE-AELEELRAELARLE-AELE 312

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  743 RLTTANKKLETELMETRSQLDDTQ-QKLEGSRASLEGARRELAELQRGSADLARRAAAAQHAHETAQRadhDLRALRAEL 821
Cdd:COG4913    313 RLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAE---EFAALRAEA 389

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1935850156  822 AQLREDRRTEEK-------KWVAREEALRRELQEAREACTALES 858
Cdd:COG4913    390 AALLEALEEELEaleealaEAEAALRDLRRELRELEAEIASLER 433
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
600-725 2.33e-04

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 46.00  E-value: 2.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  600 VESLISKHEGGDINTITEDYTQRMSALEKKFQQAIREKDQLRKQLDQVKSESSSrknsseLENTLKEKDEVIAQLQEEGE 679
Cdd:COG2433    378 IEEALEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEE------LEAELEEKDERIERLERELS 451

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1935850156  680 KLARQQLQHSNIIKKLRAKEKDNEQV---IKGLRDKIAEQSAELDRMKR 725
Cdd:COG2433    452 EARSEERREIRKDREISRLDREIERLereLEEERERIEELKRKLERLKE 500
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
710-857 4.77e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.29  E-value: 4.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  710 RDKIAEQSAELDRMKRSIAAKEElEVSQIEAVYRLTTANKkletELMETRSQLDDTQQKLEGSRASLEGARRELAELQRG 789
Cdd:COG4913    609 RAKLAALEAELAELEEELAEAEE-RLEALEAELDALQERR----EALQRLAEYSWDEIDVASAEREIAELEAELERLDAS 683

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1935850156  790 SAdlarraaaaqhahetaqradhDLRALRAELAQLREDRRTEEKKWVA---REEALRRELQEAREACTALE 857
Cdd:COG4913    684 SD---------------------DLAALEEQLEELEAELEELEEELDElkgEIGRLEKELEQAEEELDELQ 733
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
559-851 9.03e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.28  E-value: 9.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  559 ERLMRRLCEMAELLEARENRLLEMSRNNADLAENNADLKSQVESLIS-KHEGGDINTITEDYTQRMSALEKKFQQAIREK 637
Cdd:PRK03918   189 ENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEElKEEIEELEKELESLEGSKRKLEEKIRELEERI 268

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  638 DQLRKQL----DQVKSESSSRKNSSELENTLKEKDEVIAQLQEEGEKLARQQLQHSNIIKKLRAKEKDNEQV------IK 707
Cdd:PRK03918   269 EELKKEIeeleEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLeelkkkLK 348

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  708 GLRDKIA--EQSAELDRMKRSIAA-----KEELEVSQIEAVYRLTTANKKLETELMETRSQLDDTQQKLEGSRASLEGA- 779
Cdd:PRK03918   349 ELEKRLEelEERHELYEEAKAKKEelerlKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAi 428

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  780 -------------RRELAELQRGsADLARRAAAAQHAHETAQRADHDLRALRAELAQLREDRRTEEKkwVAREEALRREL 846
Cdd:PRK03918   429 eelkkakgkcpvcGRELTEEHRK-ELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESE--LIKLKELAEQL 505


                   ....*
gi 1935850156  847 QEARE 851
Cdd:PRK03918   506 KELEE 510
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 552-782 1.04e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 43.96  E-value: 1.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  552 ESQGSENERLMRRLCEMaELLEARENRLLEMSRNnadlaENNADLKSQVESLISKheggdinTITEDYTQRmsalekKFQ 631
Cdd:pfam17380  356 EERKRELERIRQEEIAM-EISRMRELERLQMERQ-----QKNERVRQELEAARKV-------KILEEERQR------KIQ 416

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  632 QAIREKDQLRKQLD---QVKSESSSRKNSSELENTLKEKDEviaqLQEEGEKLaRQQLQHSNIIKKLRAKEKDNEQVIKG 708
Cdd:pfam17380  417 QQKVEMEQIRAEQEearQREVRRLEEERAREMERVRLEEQE----RQQQVERL-RQQEEERKRKKLELEKEKRDRKRAEE 491

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  709 LRDKIAEQsaELDRMKRSIAAKE--------ELEVSQiEAVY-----RLTTANKKLETElMETRSQLDDTQQKLEGSRAS 775
Cdd:pfam17380  492 QRRKILEK--ELEERKQAMIEEErkrkllekEMEERQ-KAIYeeerrREAEEERRKQQE-MEERRRIQEQMRKATEERSR 567


                   ....*..
gi 1935850156  776 LEGARRE 782
Cdd:pfam17380  568 LEAMERE 574
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 556-857 1.06e-03

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 43.95  E-value: 1.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  556 SENERLMRRLCEMAELLEARENRLL-------EMSRN-NADLAENNADLKSQVESLISkheggDINTITEDYTQRMSALE 627
Cdd:pfam15921  274 SEHEVEITGLTEKASSARSQANSIQsqleiiqEQARNqNSMYMRQLSDLESTVSQLRS-----ELREAKRMYEDKIEELE 348

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  628 KKFQQAIREKDQLRKQLDQVksesssRKNSSELENTLKekdEVIAQLQEEGEKLARQQLQHsniiKKLRAKEKDNEQVIK 707
Cdd:pfam15921  349 KQLVLANSELTEARTERDQF------SQESGNLDDQLQ---KLLADLHKREKELSLEKEQN----KRLWDRDTGNSITID 415

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  708 GLRDKIAEQSAELDR-------MKRSIAAKEELEVSQIEAVYRLTTANKKLETELMETRSQLDDTQQKLEGSRASLEGAR 780
Cdd:pfam15921  416 HLRRELDDRNMEVQRleallkaMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSE 495

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1935850156  781 RELAELqrgsadlarraaaaqhaHETAQRADHDLRALRAELAQLRE--DRRTEEKKWVAREEalrRELQEAREACTALE 857
Cdd:pfam15921  496 RTVSDL-----------------TASLQEKERAIEATNAEITKLRSrvDLKLQELQHLKNEG---DHLRNVQTECEALK 554
DUF4201 pfam13870
Domain of unknown function (DUF4201); This is a family of coiled-coil proteins from eukaryotes. ...
 660-788 1.15e-03

Domain of unknown function (DUF4201); This is a family of coiled-coil proteins from eukaryotes. The function is not known.


Pssm-ID: 464008 [Multi-domain]  Cd Length: 177  Bit Score: 41.82  E-value: 1.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  660 LENTLKEKDEVIAQLQEEGEKLAR---QQLQHSNI------------IKKLRAKEKDNEQVIKGLRDKIAEQSAELDRMK 724
Cdd:pfam13870   18 LKHTLAKIQEKLEQKEELGEGLTMidfLQLQIENQalnekieernkeLKRLKLKVTNTVHALTHLKEKLHFLSAELSRLK 97

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1935850156  725 RSIAAKEELEVSQIEAVYRLTTANKKLETELMETRSQL------------DDTQQKLEGSRASLEGARRELAELQR 788
Cdd:pfam13870   98 KELRERQELLAKLRKELYRVKLERDKLRKQNKKLRQQGgllhvpallhdyDKTKAEVEEKRKSVKKLRRKVKILEM 173
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
527-777 1.49e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 42.59  E-value: 1.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  527 KSLATKIRGHNRELSEASVQSNTSDESQGSENERLMRRLCEMAELLEARENRLLEMSRNNADLAENNA---DLKSQVESL 603
Cdd:COG1340     18 EELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEklnELREELDEL 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  604 ISKHEGGDINTITEDY-TQRMSALEKKFQ----------QAIREKDQLRKQLDQVKSESSSRKNSSELENTLKEKDEVIA 672
Cdd:COG1340     98 RKELAELNKAGGSIDKlRKEIERLEWRQQtevlspeeekELVEKIKELEKELEKAKKALEKNEKLKELRAELKELRKEAE 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  673 QLQEEGEKLARQQLQHSNII-------KKLRAKEKDNEQVIKGLRDKIAEQSAELDRMKRSIAakeelEVSQIEAVYRLT 745
Cdd:COG1340    178 EIHKKIKELAEEAQELHEEMielykeaDELRKEADELHKEIVEAQEKADELHEEIIELQKELR-----ELRKELKKLRKK 252

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1935850156  746 TANKKLETELMETRSQLDDTQQKLE-GSRASLE 777
Cdd:COG1340    253 QRALKREKEKEELEEKAEEIFEKLKkGEKLTTE 285
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
621-788 1.68e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.97  E-value: 1.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  621 QRMSALEKKFQQAIREKDQLRKQLDQVksesssrknSSELENTLKEKDEVIAQLQEEGEKLARQQLQHSNIIKKLRAKEK 700
Cdd:COG4372     38 FELDKLQEELEQLREELEQAREELEQL---------EEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  701 DNEQvikgLRDKIAEQSAELDRMKRSIAAKEELEVSQIEAVYRLTTANKKLETELMETRSQLDDTQQKLEgsRASLEGAR 780
Cdd:COG4372    109 EAEE----LQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQ--ALSEAEAE 182


                   ....*...
gi 1935850156  781 RELAELQR 788
Cdd:COG4372    183 QALDELLK 190
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
616-786 1.72e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 42.59  E-value: 1.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  616 TEDYTQRMSALEKKFQQAIREKDQLRKQLDQVksesssrknSSELENTLKEKDEVIAQLQEEGEKLARQQLQHSNIIKKL 695
Cdd:COG1340      3 TDELSSSLEELEEKIEELREEIEELKEKRDEL---------NEELKELAEKRDELNAQVKELREEAQELREKRDELNEKV 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  696 R-AKEKDNE--QVIKGLRDKIAE---QSAELDRMKRSIAAKEElEVSQIEavYRLTTAN-------------KKLETEL- 755
Cdd:COG1340     74 KeLKEERDElnEKLNELREELDElrkELAELNKAGGSIDKLRK-EIERLE--WRQQTEVlspeeekelvekiKELEKELe 150

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1935850156  756 -----METRSQLDDTQQKLEGSRASLEGARRELAEL 786
Cdd:COG1340    151 kakkaLEKNEKLKELRAELKELRKEAEEIHKKIKEL 186
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
624-788 1.76e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.58  E-value: 1.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  624 SALEKKFQQAIREKDQLRKQLDQVKSEsssrknsseLENTLKEKDEVIAQLQEEGEKLARQQLQHSNIIKKLRAKEKDNE 703
Cdd:COG4372     27 AALSEQLRKALFELDKLQEELEQLREE---------LEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELA 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  704 QvikgLRDKIAEQSAELDRMKRSIAA-KEELEvsqieavyRLTTANKKLETELMETRSQLDDTQQKLEGSRASLEGARRE 782
Cdd:COG4372     98 Q----AQEELESLQEEAEELQEELEElQKERQ--------DLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165


                   ....*.
gi 1935850156  783 LAELQR 788
Cdd:COG4372    166 LAALEQ 171
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
695-851 1.91e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.08  E-value: 1.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  695 LRAKEKDNEQVIKGLRDKIAEQSAELDRMKRSIAA-KEELEVSQIEAVYRLTTAN-KKLETELMETRSQLDDTQQKLEGS 772
Cdd:COG3206    166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEfRQKNGLVDLSEEAKLLLQQlSELESQLAEARAELAEAEARLAAL 245

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  773 RASLEGARRELAELQRGSADLARRAAAAQHAHETA-------------QRADHDLRALRAELAQ----LREDRRTEEKKW 835
Cdd:COG3206    246 RAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAelsarytpnhpdvIALRAQIAALRAQLQQeaqrILASLEAELEAL 325

                          170
                   ....*....|....*.
gi 1935850156  836 VAREEALRRELQEARE 851
Cdd:COG3206    326 QAREASLQAQLAQLEA 341
PRK11281 PRK11281
mechanosensitive channel MscK;
674-780 2.05e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 42.98  E-value: 2.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  674 LQEEGEKLARQQLQHS-NIIKKLRAKEKDNEQvikgLRDKIAEQSAELDRMKRSIAAKEELEVSQIEAVYRlTTANKKLE 752
Cdd:PRK11281    53 LLEAEDKLVQQDLEQTlALLDKIDRQKEETEQ----LKQQLAQAPAKLRQAQAELEALKDDNDEETRETLS-TLSLRQLE 127

                           90       100
                   ....*....|....*....|....*...
gi 1935850156  753 TELMETRSQLDDTQQKLEGSRASLEGAR 780
Cdd:PRK11281   128 SRLAQTLDQLQNAQNDLAEYNSQLVSLQ 155
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1697-1783 2.18e-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: 2.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156 1697 EDALSALRRR----DGEVRALVAHRDSLRGQR-DQLAAELARCQAALDDMQSVQEQYDALLQMYGEK----EEQMAELRL 1767
Cdd:COG4913    308 EAELERLEARldalREELDELEAQIRGNGGDRlEQLEREIERLERELEERERRRARLEALLAALGLPlpasAEEFAALRA 387

                           90
                   ....*....|....*.
gi 1935850156 1768 DLQDVTQLYKAQLDEL 1783
Cdd:COG4913    388 EAAALLEALEEELEAL 403
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
689-852 2.32e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 42.92  E-value: 2.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  689 SNIIKKLrAKEKDNEQVIKGLrdkIAEQSAE--LDRMKRSIAAKEELEVSQIEAVYRLTTA-----NKKLETELMETRSQ 761
Cdd:COG2433    353 ERVEKKV-PPDVDRDEVKARV---IRGLSIEeaLEELIEKELPEEEPEAEREKEHEERELTeeeeeIRRLEEQVERLEAE 428

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  762 LDDTQQKLEGSRASLEGARRELAELQRgsadlarraaaaqhAHETAQRADHDLRALRAELAQLREDRRTEEKkwvaREEA 841
Cdd:COG2433    429 VEELEAELEEKDERIERLERELSEARS--------------EERREIRKDREISRLDREIERLERELEEERE----RIEE 490

                          170
                   ....*....|.
gi 1935850156  842 LRRELQEAREA 852
Cdd:COG2433    491 LKRKLERLKEL 501
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 621-755 3.44e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 42.12  E-value: 3.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  621 QRMSALEKKFQQAIREKDQLRKQLDQvksesssrknsseLENTLKEKdevIAQLQEEGEKL-ARQQLQHSNIIKKlrAKe 699
Cdd:PRK00409   523 ASLEELERELEQKAEEAEALLKEAEK-------------LKEELEEK---KEKLQEEEDKLlEEAEKEAQQAIKE--AK- 583

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1935850156  700 KDNEQVIKGLRDKIAEQSAeldrmkrSIAAKEelevsQIEAVYRLTTANKKLETEL 755
Cdd:PRK00409   584 KEADEIIKELRQLQKGGYA-------SVKAHE-----LIEARKRLNKANEKKEKKK 627
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 529-782 5.12e-03

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 41.48  E-value: 5.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  529 LATKIRGHNRELSEASVQSntSDESQGSENERLMRRLCEMAELLEARENRLLEMSRNNADLAENNADLKSQVESLISKHE 608
Cdd:COG5185    287 LIKQFENTKEKIAEYTKSI--DIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIE 364

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  609 GGDINTITEDYTQRMSALEKKFQQAIREKDQLRKQLDQVKSESSSRknsseLENTLKEKDEVIAQLQEEGEKLARQQLQH 688
Cdd:COG5185    365 NIVGEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILAT-----LEDTLKAADRQIEELQRQIEQATSSNEEV 439

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  689 SNIIKKLRAKEKDNEQVIKGLRDKIAEQSA-ELDRMKRSIAAKEELEVSQIEAvyRLTTANKKLETELMETRSQLDDTQQ 767
Cdd:COG5185    440 SKLLNELISELNKVMREADEESQSRLEEAYdEINRSVRSKKEDLNEELTQIES--RVSTLKATLEKLRAKLERQLEGVRS 517

                          250
                   ....*....|....*
gi 1935850156  768 KLEGSRASLEGARRE 782
Cdd:COG5185    518 KLDQVAESLKDFMRA 532
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 663-777 5.54e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 41.45  E-value: 5.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  663 TLKE-KDEVIAQLQEEG----------------EKLARQQLQHSNIIKKLRaKEKDNEQVIKGLRDKIAEQSAEldrmkr 725
Cdd:PRK05771    13 TLKSyKDEVLEALHELGvvhiedlkeelsnerlRKLRSLLTKLSEALDKLR-SYLPKLNPLREEKKKVSVKSLE------ 85

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1935850156  726 SIAAKEELEVSQIEAVYRlttankkletELMETRSQLDDTQQKLEGSRASLE 777
Cdd:PRK05771    86 ELIKDVEEELEKIEKEIK----------ELEEEISELENEIKELEQEIERLE 127
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 567-770 5.65e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 41.54  E-value: 5.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  567 EMAELLEARENRLLEMsrnNADLAENN---ADLKSQVESLisKHEGGDINTITEDYTQRMSALEKKFQQAIREKDQLRKQ 643
Cdd:TIGR04523  311 ELKSELKNQEKKLEEI---QNQISQNNkiiSQLNEQISQL--KKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQE 385

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  644 LDQVKSESSSrknsseLENTLKEKDEVIAQLQEEGEKLARQQLQHSNIIKKLRAKEKDNEQVIKGLRDKIAEQSAELDRM 723
Cdd:TIGR04523  386 IKNLESQIND------LESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNL 459

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1935850156  724 KRSIAAKEElevsQIEAvyrLTTANKKLETELMETRSQLDDTQQKLE 770
Cdd:TIGR04523  460 DNTRESLET----QLKV---LSRSINKIKQNLEQKQKELKSKEKELK 499
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 553-855 5.91e-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: 41.49  E-value: 5.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  553 SQGSENERLMRRLCEMAELLEARENrlLEMSRNNADLA-ENNADLKSQVESLISKHEG--GDINTITEDYTQRMSALEKK 629
Cdd:TIGR00618  150 PQGEFAQFLKAKSKEKKELLMNLFP--LDQYTQLALMEfAKKKSLHGKAELLTLRSQLltLCTPCMPDTYHERKQVLEKE 227

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  630 FQQAIREKDQLRKQLDQVKSESSSRKNSSELENTLKE----------KDEVIAQLQEEGEkLARQQLQHSNIIKKLRAKE 699
Cdd:TIGR00618  228 LKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQlrarieelraQEAVLEETQERIN-RARKAAPLAAHIKAVTQIE 306

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  700 KDNEQVIKGLRDKIAEQSAELdrMKRSIAAKEELEVSQieavyrlttaNKKLETELMETRSQLDDTQQKLEGSRASLEga 779
Cdd:TIGR00618  307 QQAQRIHTELQSKMRSRAKLL--MKRAAHVKQQSSIEE----------QRRLLQTLHSQEIHIRDAHEVATSIREISC-- 372

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1935850156  780 rRELAELQRgsadlarraaaAQHAHETAQRADHDLRALRAELAQLREDRRTEEKKwVAREEALRRELQEAREACTA 855
Cdd:TIGR00618  373 -QQHTLTQH-----------IHTLQQQKTTLTQKLQSLCKELDILQREQATIDTR-TSAFRDLQGQLAHAKKQQEL 435
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
532-770 6.76e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.18  E-value: 6.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  532 KIRGHNRELSEASVQSNTSDE---------SQGSENERLMRRLCEMAELLEARENRLLEMSRNNADLAENNADLKSQVES 602
Cdd:PRK02224   476 RVEELEAELEDLEEEVEEVEErleraedlvEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEE 555

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  603 lisKHEGGDINTI-TEDYTQRMSALEKKFQQAIREKDQLRKQLDQVKSESSSRKNSSelenTLKEKDEVIAQLQEEG-EK 680
Cdd:PRK02224   556 ---KREAAAEAEEeAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIE----RLREKREALAELNDERrER 628

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  681 LA-----RQQLQHS---NIIKKLRAKEKDNEQVIKGLRDKIAEQSAELDRMKRSI-AAKEELEvsqieavyrlttankKL 751
Cdd:PRK02224   629 LAekrerKRELEAEfdeARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIgAVENELE---------------EL 693

                          250
                   ....*....|....*....
gi 1935850156  752 EtELMETRSQLDDTQQKLE 770
Cdd:PRK02224   694 E-ELRERREALENRVEALE 711
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 574-857 7.68e-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: 41.48  E-value: 7.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  574 ARENRLLEMSRNNADLAENNAD----------LKSQVESLISKHE----GGDINTITEDYTQRMSALEKKFQQAIREKDQ 639
Cdd:COG3096    782 AREKRLEELRAERDELAEQYAKasfdvqklqrLHQAFSQFVGGHLavafAPDPEAELAALRQRRSELERELAQHRAQEQQ 861

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  640 LRKQLDQVKSESSSRKNSSELENTLKEKD--EVIAQLQEEGEKL--ARQQL-QHSNIIKK-------LRAKEKDNEQvik 707
Cdd:COG3096    862 LRQQLDQLKEQLQLLNKLLPQANLLADETlaDRLEELREELDAAqeAQAFIqQHGKALAQleplvavLQSDPEQFEQ--- 938

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  708 gLRDKIAEQSAELDRMKRSIAAKEEL-----EVSQIEAVYRLTTA---NKKLETELMETRSQLDDTQQKLEGSRASLEGA 779
Cdd:COG3096    939 -LQADYLQAKEQQRRLKQQIFALSEVvqrrpHFSYEDAVGLLGENsdlNEKLRARLEQAEEARREAREQLRQAQAQYSQY 1017

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  780 RRELAELqRGSadlarraaaaqhahetAQRADHDLRALRAELAQL--REDRRTEEKkwvAREEalRRELQEA----REAC 853
Cdd:COG3096   1018 NQVLASL-KSS----------------RDAKQQTLQELEQELEELgvQADAEAEER---ARIR--RDELHEElsqnRSRR 1075


                   ....
gi 1935850156  854 TALE 857
Cdd:COG3096   1076 SQLE 1079
DUF1758 pfam05585
Putative peptidase (DUF1758); This is a family of nematode proteins of unknown function. ...
 1573-1653 7.81e-03

Putative peptidase (DUF1758); This is a family of nematode proteins of unknown function. However, it seems likely that these proteins act as aspartic peptidases.


Pssm-ID: 147642  Cd Length: 164  Bit Score: 39.14  E-value: 7.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156 1573 VRIQGINGEYHTMRALIDQGSQASLITENAAQILKLPRRACKGVIVGVSANQTN-CKGVLSLVASSLYSNYTFQTEVEQS 1651
Cdd:pfam05585    1 VVVSNAQGARTKCRLLFDSGSELSYISERCINRLGLARTPSRILVIGISGDKAPqTRGSNRTVISSRLSNGTLAVRAHVL 80


                   ..
gi 1935850156 1652 SR 1653
Cdd:pfam05585   81 KK 82
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
527-858 8.14e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.18  E-value: 8.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  527 KSLATKIRGHNRELSEASVQSNTSDEsqgsENERLMRRLCEMAELLEARENRLLEMsrnnadlaennADLKSQVESLISk 606
Cdd:PRK02224   202 KDLHERLNGLESELAELDEEIERYEE----QREQARETRDEADEVLEEHEERREEL-----------ETLEAEIEDLRE- 265

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  607 heggdinTITEDYTQRmsaleKKFQQAIREKDQLRKQL-----DQVKSESSSRKNSSELENTLKEKDEVIAQLQEEGEKL 681
Cdd:PRK02224   266 -------TIAETERER-----EELAEEVRDLRERLEELeeerdDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEEC 333

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  682 ARQQLQHSNIIKKLRAKEKDNEQVIKGLRDKIAEQSAELDRMKRSIA----AKEELEvSQIE----AVYRLTTANKKLET 753
Cdd:PRK02224   334 RVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEdrreEIEELE-EEIEelreRFGDAPVDLGNAED 412

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  754 ELMETRSQLDDTQQKLEGSRASLEGARRELAELQR-----------------------GSADLARRAAAAQHAHETAQRA 810
Cdd:PRK02224   413 FLEELREERDELREREAELEATLRTARERVEEAEAlleagkcpecgqpvegsphvetiEEDRERVEELEAELEDLEEEVE 492

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  811 DHDLRALRAE------------------LAQLREDRRT-------------------EEKKWVAREEA--LRRELQEARE 851
Cdd:PRK02224   493 EVEERLERAEdlveaedrierleerredLEELIAERREtieekreraeelreraaelEAEAEEKREAAaeAEEEAEEARE 572


                   ....*..
gi 1935850156  852 ACTALES 858
Cdd:PRK02224   573 EVAELNS 579
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
666-832 8.36e-03

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 40.42  E-value: 8.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  666 EKDEVIAQLQEEGEKLARQQLQHSniIKKLRAKEkDNEQVIKGLRDKIAEQSAELDrmkrsiAAKEELEVSQIEAvyrlt 745
Cdd:COG1566     68 KKGQVLARLDPTDLQAALAQAEAQ--LAAAEAQL-ARLEAELGAEAEIAAAEAQLA------AAQAQLDLAQREL----- 133

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935850156  746 TANKKLETELMETRSQLDDTQQKLEGSRASLEGARRElaelqrgsadlarraaaaqhaHETAQ---RADHDLRALRAELA 822
Cdd:COG1566    134 ERYQALYKKGAVSQQELDEARAALDAAQAQLEAAQAQ---------------------LAQAQaglREEEELAAAQAQVA 192

                          170
                   ....*....|
gi 1935850156  823 QLREDRRTEE 832
Cdd:COG1566    193 QAEAALAQAE 202
 
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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