NCBI Conserved Domain Search

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

516-664

9.33e-09

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.79 E-value: 9.33e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422 516 RTYLKQQEKL-----NLILQKKQQLQMEVKMLSssKSMKELTEEQQNLQKELESLQNEHAQRMEEFYVEQKDLEKKLEQI 590
Cdd:COG1196  213 ERYRELKEELkeleaELLLLKLRELEAELEELE--AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE 290

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 223029422 591 mkqkctcdsNLEKDKEAEYAGQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQILKSSKTAKE 664
Cdd:COG1196  291 ---------YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE 355

Mplasa_alph_rch

TIGR04523

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...

530-664

8.94e-08

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

Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 55.41 E-value: 8.94e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422  530 QKKQQLQMEVKMLSSSKSMKELTEEQQNLQKELESLQNEHAQRMEEfyVEQKdlEKKLEQIMKQKctcDSNLEKDKEAEy 609
Cdd:TIGR04523 319 QEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRE--LEEK--QNEIEKLKKEN---QSYKQEIKNLE- 390

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 223029422  610 aGQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQILKSSKTAKE 664
Cdd:TIGR04523 391 -SQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKD 444

PRK12704

phosphodiesterase; Provisional

519-664

4.58e-07

phosphodiesterase; Provisional

Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 52.86 E-value: 4.58e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422 519 LKQQEKlnlILQKKQQLQMEVKmlsssKSMKELTE-EQQNLQKElESLQNehaqRMEEFYVEQKDLEKKLEQIMKQKctc 597
Cdd:PRK12704  60 LEAKEE---IHKLRNEFEKELR-----ERRNELQKlEKRLLQKE-ENLDR----KLELLEKREEELEKKEKELEQKQ--- 123

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 223029422 598 dSNLEKdKEAEYAGQLAELRQRLDH-----AEADRQELQDELrqEREARQKLEMMIKELKLQI-LKSSKTAKE 664
Cdd:PRK12704 124 -QELEK-KEEELEELIEEQLQELERisgltAEEAKEILLEKV--EEEARHEAAVLIKEIEEEAkEEADKKAKE 192

TPH

pfam13868

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...

504-655

3.38e-06

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: 49.53 E-value: 3.38e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422  504 EDDKGKIMEEVMRTYLKQQEKLNLILQKKQQLQMEV-KMLSSSKSMKELTEEQQNLQKE-LESLQNEHAQRMEEFYVEQK 581
Cdd:pfam13868  97 LQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIdEFNEEQAEWKELEKEEEREEDErILEYLKEKAEREEEREAERE 176

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 223029422  582 DLEKKLEQIMkQKCTCDSNLEKDKEAEyagqLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 655
Cdd:pfam13868 177 EIEEEKEREI-ARLRAQQEKAQDEKAE----RDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQI 245

GBP_C

cd16269

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...

504-652

2.76e-05

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

Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 46.42 E-value: 2.76e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422 504 EDDKGKIMEEVMRTYLKQQEKL-NLILQKKQQL-QMEVKMlsssKSMKELTEEQQNLQKELESLQNEHAQRMEEfyvEQK 581
Cdd:cd16269  161 VPRKGVKAEEVLQEFLQSKEAEaEAILQADQALtEKEKEI----EAERAKAEAAEQERKLLEEQQRELEQKLED---QER 233

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 223029422 582 DLEKKLEQimkqkctcdsnLEKDKEAEYAGQLAELRQRLDHAEADRQELQDElrQEREARQKLEMMIKELK 652
Cdd:cd16269  234 SYEEHLRQ-----------LKEKMEEERENLLKEQERALESKLKEQEALLEE--GFKEQAELLQEEIRSLK 291

OmpH

smart00935

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...

548-650

3.71e-05

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

Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 44.11 E-value: 3.71e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422   548 MKELTEEQQNLQKELESLQNEHAQRMEEFYVEQKDLEKKLEQIMKQKCTCDSNLEKDKEAEYAGQLAELRQrldhaeaDR 627
Cdd:smart00935   6 VQKILQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLSEAAREKKEKELQKKVQEFQR-------KQ 78

                           90       100
                   ....*....|....*....|....
gi 223029422   628 QELQDELRQER-EARQKLEMMIKE 650
Cdd:smart00935  79 QKLQQDLQKRQqEELQKILDKINK 102

SCP-1

pfam05483

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...

335-664

6.78e-04

Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 42.79 E-value: 6.78e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422  335 FSMRSGKRNQSKTDAPSGMELQSWYPVIKQEGDHV---------------SQTHSFLHPSYYlYMCDKVVAPNVSLTSAV 399
Cdd:pfam05483  23 FAKSNLSKNGENIDSDPAFQKLNFLPMLEQVANSGdchyqeglkdsdfenSEGLSRLYSKLY-KEAEKIKKWKVSIEAEL 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422  400 SQsKELTKTEASKSISRQSEKAHssgKLQKTVSYPDVSLEE--QEKMDL----KTSRELCSRLDASISNNSTSKRKSE-- 471
Cdd:pfam05483 102 KQ-KENKLQENRKIIEAQRKAIQ---ELQFENEKVSLKLEEeiQENKDLikenNATRHLCNLLKETCARSAEKTKKYEye 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422  472 -----SATCNLVRDINKVGIGL----VAAASSPLLVKDVICED-DKGKIMEEVMRTYLKQQEK-LNLIL----QKKQQL- 535
Cdd:pfam05483 178 reetrQVYMDLNNNIEKMILAFeelrVQAENARLEMHFKLKEDhEKIQHLEEEYKKEINDKEKqVSLLLiqitEKENKMk 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422  536 --------------QMEVKMLSSSKSMKELTEEQQNLQKELESLQnehaQRMEEFYVEQKDLEKKLEQIMKQKCtcdsNL 601
Cdd:pfam05483 258 dltflleesrdkanQLEEKTKLQDENLKELIEKKDHLTKELEDIK----MSLQRSMSTQKALEEDLQIATKTIC----QL 329

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422  602 EKDKEAeyagQLAEL-RQRLDHA------EADRQELQDELRQEREARQKLEMMIKELKLQILKSSKTAKE 664
Cdd:pfam05483 330 TEEKEA----QMEELnKAKAAHSfvvtefEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEE 395

Name

Accession

Description

Interval

E-value

DHD_Sno

cd21084

Dachshund-homology domain found in Ski-like protein (Sno) and similar proteins; Ski-like ...

117-216

4.04e-66

Pssm-ID: 410787 Cd Length: 100 Bit Score: 212.13 E-value: 4.04e-66

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422 117 PSDSSTELTQTVLEGESISCFQVGGEKRLCLPQVLNSVLREFTLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAP 196
Cdd:cd21084    1 PSDSSTELTQTVLEGESISCFMVGGEKRLCLPQVLNSVLRDFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAP 80

                         90       100
                 ....*....|....*....|
gi 223029422 197 SCGLITLTDAQRLCNALLRP 216
Cdd:cd21084   81 SCGLITLTDAQRLCNALLRP 100

c-SKI_SMAD_bind

smart01046

c-SKI Smad4 binding domain; c-SKI is an oncoprotein that inhibits TGF-beta signaling through ...

241-336

2.57e-57

c-SKI Smad4 binding domain; c-SKI is an oncoprotein that inhibits TGF-beta signaling through interaction with Smad proteins. This domain binds to Smad4.

Pssm-ID: 198114 Cd Length: 95 Bit Score: 188.73 E-value: 2.57e-57

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422   241 AFEVEHECLGKCQGLFAPQFYVQPDAPCIQCLECCGMFAPQTFVMHSHRSPDKRTCHWGFESAKWHCYLHVNQKYlGTPE 320
Cdd:smart01046   1 SFRVYHECFGKCQGLFVPELYSSPDAPCIQCLECRGMFSPQKFVMHSHRSPEKRTCHWGFDSANWRSYLHVAKDY-GTEE 79

                           90
                   ....*....|....*.
gi 223029422   321 EKKLKIILEEMKEKFS 336
Cdd:smart01046  80 REKLEQLLEEMKEKFN 95

c-SKI_SMAD_bind

pfam08782

c-SKI Smad4 binding domain; c-SKI is an oncoprotein that inhibits TGF-beta signaling through ...

241-335

2.94e-55

c-SKI Smad4 binding domain; c-SKI is an oncoprotein that inhibits TGF-beta signaling through interaction with Smad proteins. This domain binds to Smad4

Pssm-ID: 462602 Cd Length: 94 Bit Score: 182.85 E-value: 2.94e-55

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422  241 AFEVEHECLGKCQGLFAPQFYVQPDAPCIQCLECCGMFAPQTFVMHSHRSPDKRTCHWGFESAKWHCYLHVNQkYLGTPE 320
Cdd:pfam08782   1 SFEVYHECFGKCRGLFVPELYTSPRAACIQCLECRLMFSPQKFVFHSHRSPENRTCHWGFDSANWRAYLHLAR-YLDTPD 79

                          90
                  ....*....|....*
gi 223029422  321 EKKLKIILEEMKEKF 335
Cdd:pfam08782  80 REKLEQLLEDLKAKF 94

DHD_Ski_Sno

cd21079

Dachshund-homology domain found in Ski, Ski-like protein (Sno), and similar proteins; Ski may ...

124-214

4.77e-52

Dachshund-homology domain found in Ski, Ski-like protein (Sno), and similar proteins; Ski may play a role in terminal differentiation of skeletal muscle cells but not in the determination of cells to the myogenic lineage. It functions as a repressor of transforming growth factor-beta (TGF-beta) signaling. Ski-like protein, also known as SKIL or Sno, is the ski proto-oncogene homolog. It may have regulatory roles in cell division or differentiation in response to extracellular signals. The Dachshund-homology domain (DHD), also known as the N-terminal Ski/Sno/Dac domain, adopts a mixed alpha/beta structure containing a helix-turn-helix motif, similar to features found in the forkhead/winged-helix family of DNA binding proteins. It contains a conserved CLPQ motif and can bind co-factors. Its structure suggests that it may also bind DNA.

Pssm-ID: 410782 Cd Length: 91 Bit Score: 174.29 E-value: 4.77e-52

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422 124 LTQTVLEGESISCFQVGGEKRLCLPQVLNSVLREFTLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAPSCGLITL 203
Cdd:cd21079    1 LKETLLEGETIACFVVGGEKRLCLPQILNTVLRDFSLQQINRVCDDLHIYCSRCTPEQLETLKLAGILPPSAPSCGLITK 80

                         90
                 ....*....|.
gi 223029422 204 TDAQRLCNALL 214
Cdd:cd21079   81 TDAERLCSALL 91

DHD_Ski

cd21083

Dachshund-homology domain found in Ski and similar proteins; Ski may play a role in terminal ...

117-214

1.72e-48

Dachshund-homology domain found in Ski and similar proteins; Ski may play a role in terminal differentiation of skeletal muscle cells but not in the determination of cells to the myogenic lineage. It functions as a repressor of transforming growth factor-beta (TGF-beta) signaling. The Dachshund-homology domain (DHD), also known as the N-terminal Ski/Sno/Dac domain, adopts a mixed alpha/beta structure containing a helix-turn-helix motif, similar to features found in the forkhead/winged-helix family of DNA binding proteins. It contains a conserved CLPQ motif and can bind co-factors. Its structure suggests that it may also bind DNA.

Pssm-ID: 410786 Cd Length: 102 Bit Score: 165.24 E-value: 1.72e-48

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422 117 PSDSSTELTQTVLEGESISCFQVGGEKRLCLPQVLNSVLREFTLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAP 196
Cdd:cd21083    3 PSDRSTERCETILEGETISCFVVGGEKRLCLPQILNSVLRDFSLQQINSVCDELHIYCSRCTADQLEILKVMGILPFSAP 82

                         90
                 ....*....|....*...
gi 223029422 197 SCGLITLTDAQRLCNALL 214
Cdd:cd21083   83 SCGLITKTDAERLCNALL 100

Ski_Sno

pfam02437

SKI/SNO/DAC family; This family contains a presumed domain that is about 100 amino acids long. ...

116-215

6.55e-48

Pssm-ID: 460558 Cd Length: 100 Bit Score: 163.22 E-value: 6.55e-48

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422  116 IPSDSSTELTQTVLEGESISCFQVGGEKRLCLPQVLNSVLREFTLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNA 195
Cdd:pfam02437   1 TNTDTNNERMETMLEGEVISCFMVGGEERLCLPQILNTLLKDFSLTQINTVCDELIITCVRCTPEQLEILKLLGILPPSV 80

                          90       100
                  ....*....|....*....|
gi 223029422  196 PSCGLITLTDAQRLCNALLR 215
Cdd:pfam02437  81 RRCGLITKTDAERLCDALLH 100

DHD_Ski_Sno_Dac

cd21074

Dachshund-homology domain found in the Ski/Sno/Dac family of transcriptional regulators; The ...

124-211

1.03e-33

Dachshund-homology domain found in the Ski/Sno/Dac family of transcriptional regulators; The Dachshund-homology domain (DHD), also known as the N-terminal Ski/Sno/Dac domain, adopts a mixed alpha/beta structure containing a helix-turn-helix motif, similar to features found in the forkhead/winged-helix family of DNA binding proteins. It contains a conserved CLPQ motif and can bind co-factors. Its structure suggests that it may also bind DNA. Members of this family include the Ski protein, Ski-like protein (Sno), and Dachshund proteins. Ski may play a role in terminal differentiation of skeletal muscle cells but not in the determination of cells to the myogenic lineage. It functions as a repressor of transforming growth factor-beta (TGF-beta) signaling. Ski-like protein, also known as SKIL or Sno, is the ski proto-oncogene homolog. It may have regulatory roles in cell division or differentiation in response to extracellular signals. Dachshund proteins are essential components of a regulatory network controlling cell fate determination. They have been implicated in eye, limb, brain, and muscle development.

Pssm-ID: 410781 Cd Length: 88 Bit Score: 123.94 E-value: 1.03e-33

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422 124 LTQTVLEGESISCFQVGGEKRLCLPQVLNSVLREFTLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAPSCGLITL 203
Cdd:cd21074    1 LVTSTLEGKRIAGFEIDGEERLCLPQILNLVLKDFVQTQIHNRCTKLKIICTRCDQEQLKILKRLGILPPKAKSCGLISK 80


                 ....*...
gi 223029422 204 TDAQRLCN 211
Cdd:cd21074   81 SDAERLLN 88

DHD_Skor

cd21080

Dachshund-homology domain found in SKI family transcriptional corepressors, Skor1, Skor2 and ...

124-214

5.18e-16

Dachshund-homology domain found in SKI family transcriptional corepressors, Skor1, Skor2 and similar proteins; Skor1, also known as functional Smad-suppressing element on chromosome 15 (Fussel-15), LBX1 corepressor 1, or ladybird homeobox corepressor 1, acts as a transcriptional corepressor of LBX1 and inhibits BMP signaling. Skor2, also known as functional Smad-suppressing element on chromosome 18 (Fussel-18), LBX1 corepressor 1-like protein, or ladybird homeobox corepressor 1-like protein, exhibits transcriptional repressor activity. It acts as a transforming growth factor-beta (TGF-beta) antagonist in the nervous system. The Dachshund-homology domain (DHD), also known as the N-terminal Ski/Sno/Dac domain, adopts a mixed alpha/beta structure containing a helix-turn-helix motif, similar to features found in the forkhead/winged-helix family of DNA binding proteins. It contains a conserved CLPQ motif and can bind co-factors. Its structure suggests that it may also bind DNA.

Pssm-ID: 410783 Cd Length: 91 Bit Score: 73.63 E-value: 5.18e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422 124 LTQTVLEGESISCFQVGGEKRLCLPQVLNSVLREFTLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAPSCGLITL 203
Cdd:cd21080    1 VGTVILYGVPIVSLVIDGQERLCLAQISNTLLKDYSYNEIHNRRVALGITCVQCTPVQLEILRRAGAMPISSRRCGMITK 80

                         90
                 ....*....|.
gi 223029422 204 TDAQRLCNALL 214
Cdd:cd21080   81 REAERLCKSFL 91

Smc

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

516-664

9.33e-09

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.79 E-value: 9.33e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422 516 RTYLKQQEKL-----NLILQKKQQLQMEVKMLSssKSMKELTEEQQNLQKELESLQNEHAQRMEEFYVEQKDLEKKLEQI 590
Cdd:COG1196  213 ERYRELKEELkeleaELLLLKLRELEAELEELE--AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE 290

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 223029422 591 mkqkctcdsNLEKDKEAEYAGQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQILKSSKTAKE 664
Cdd:COG1196  291 ---------YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE 355

COG4913

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

522-655

1.85e-08

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

Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.00 E-value: 1.85e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422  522 QEKLNLILQKKQQLQMEVKmlsssksmkELTEEQQNLQKELESLQN--EHAQRMEEFYVEQKD---LEKKLEQIMKQKct 596
Cdd:COG4913   609 RAKLAALEAELAELEEELA---------EAEERLEALEAELDALQErrEALQRLAEYSWDEIDvasAEREIAELEAEL-- 677

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 223029422  597 cdSNLEKDKeaeyaGQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 655
Cdd:COG4913   678 --ERLDASS-----DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEEL 729

Mplasa_alph_rch

TIGR04523

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...

530-664

8.94e-08

Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 55.41 E-value: 8.94e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422  530 QKKQQLQMEVKMLSSSKSMKELTEEQQNLQKELESLQNEHAQRMEEfyVEQKdlEKKLEQIMKQKctcDSNLEKDKEAEy 609
Cdd:TIGR04523 319 QEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRE--LEEK--QNEIEKLKKEN---QSYKQEIKNLE- 390

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 223029422  610 aGQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQILKSSKTAKE 664
Cdd:TIGR04523 391 -SQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKD 444

SMC_prok_B

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...

396-655

1.38e-07

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

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.06 E-value: 1.38e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422   396 TSAVSQSKELTktEASKSISRQSEKAHSsgkLQKTVSYPDVSLEEQEKMdLKTSRELCSRLDASISNNSTSKRKSESATC 475
Cdd:TIGR02168  670 SSILERRREIE--ELEEKIEELEEKIAE---LEKALAELRKELEELEEE-LEQLRKELEELSRQISALRKDLARLEAEVE 743

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422   476 NLVRDINKVGIGLVAAASSPLLVKDVICEDDKGKIMEEVMRTYLKQQeklnlILQKKQQLQMEVKMLSS-SKSMKELTEE 554
Cdd:TIGR02168  744 QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ-----IEQLKEELKALREALDElRAELTLLNEE 818

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422   555 QQNLQKELESLQNEHA------------------------QRMEEFYVEQKDLEKKLEQIMKQKCTCDSNLEKDKEAEY- 609
Cdd:TIGR02168  819 AANLRERLESLERRIAaterrledleeqieelsedieslaAEIEELEELIEELESELEALLNERASLEEALALLRSELEe 898

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 223029422   610 -AGQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 655
Cdd:TIGR02168  899 lSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945

COG4913

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

528-645

4.23e-07

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

Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.38 E-value: 4.23e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422  528 ILQKKQQLQmevKMLSSSKSMKELTEEQQNLQKELESLQNEHAQRMEEfyveQKDLEKKLEQIMKQKCTCDSNLEKDKEA 607
Cdd:COG4913   670 IAELEAELE---RLDASSDDLAALEEQLEELEAELEELEEELDELKGE----IGRLEKELEQAEEELDELQDRLEAAEDL 742

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 223029422  608 EYAGQLAELRQRLDHAEAD------RQELQDELRQEREARQKLE 645
Cdd:COG4913   743 ARLELRALLEERFAAALGDaverelRENLEERIDALRARLNRAE 786

PRK12704

phosphodiesterase; Provisional

519-664

4.58e-07

phosphodiesterase; Provisional

Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 52.86 E-value: 4.58e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422 519 LKQQEKlnlILQKKQQLQMEVKmlsssKSMKELTE-EQQNLQKElESLQNehaqRMEEFYVEQKDLEKKLEQIMKQKctc 597
Cdd:PRK12704  60 LEAKEE---IHKLRNEFEKELR-----ERRNELQKlEKRLLQKE-ENLDR----KLELLEKREEELEKKEKELEQKQ--- 123

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 223029422 598 dSNLEKdKEAEYAGQLAELRQRLDH-----AEADRQELQDELrqEREARQKLEMMIKELKLQI-LKSSKTAKE 664
Cdd:PRK12704 124 -QELEK-KEEELEELIEEQLQELERisgltAEEAKEILLEKV--EEEARHEAAVLIKEIEEEAkEEADKKAKE 192

YhaN

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

522-654

5.10e-07

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 5.10e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422 522 QEKLNLILQKKQQLQMEVKMLSSSKSMKELTEEQQNLQKELESLQNEHAQRmEEFYVEQKDLEKKLEQI---MKQKCTCD 598
Cdd:COG4717  108 EAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEEL-RELEEELEELEAELAELqeeLEELLEQL 186

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 223029422 599 SNLEKDKEAEYAGQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQ 654
Cdd:COG4717  187 SLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242

DR0291

COG1579

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...

529-657

7.73e-07

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: 7.73e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422 529 LQKKQQLQMEVKmlssskSMKELteeqQNLQKELESLQNEhaqrmeefyveQKDLEKKLEQIMKQKCTCDSNLEKDKEae 608
Cdd:COG1579   75 IKKYEEQLGNVR------NNKEY----EALQKEIESLKRR-----------ISDLEDEILELMERIEELEEELAELEA-- 131

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 223029422 609 yagQLAELRQRLDHAEADRQELQDELRQEREA-RQKLEMMIKELKLQILK 657
Cdd:COG1579  132 ---ELAELEAELEEKKAELDEELAELEAELEElEAEREELAAKIPPELLA 178

PRK00409

recombination and DNA strand exchange inhibitor protein; Reviewed

510-652

1.33e-06

recombination and DNA strand exchange inhibitor protein; Reviewed

Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 51.75 E-value: 1.33e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422 510 IMEEVMRTYLKQQEKLNLILQKKQQLQMEvkmlsssksMKELTEEQQNLQKELESLQNEHAQRMEEFYVEQKDLEKKLEQ 589
Cdd:PRK00409 503 IIEEAKKLIGEDKEKLNELIASLEELERE---------LEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEK 573

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 223029422 590 IMKQKctcdsnLEKDKEaEYAGQLAELR--QRLDHAEADRQELQDELRQEREARQKLEMMIKELK 652
Cdd:PRK00409 574 EAQQA------IKEAKK-EADEIIKELRqlQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQK 631

SMC_prok_A

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...

439-658

1.63e-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: 51.61 E-value: 1.63e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422   439 EEQEKMDLKTSRELCSRLDASISNNSTSKRKSESATCNLVRDINKVGIGLVAAASSPLLVKDVICEDDKGKIMEEVMRty 518
Cdd:TIGR02169  732 EEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSR-- 809

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422   519 lkQQEKLNLILQKKQQLQMEVKMLSSSKsmkeltEEQQNLQKELESLQNEHAQRMEEFYVEQKDLEKKLEQImkqkctcd 598
Cdd:TIGR02169  810 --IEARLREIEQKLNRLTLEKEYLEKEI------QELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEEL-------- 873

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 223029422   599 snleKDKEAEYAGQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKEL--KLQILKS 658
Cdd:TIGR02169  874 ----EAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELkaKLEALEE 931

SMC_prok_B

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...

530-664

2.15e-06

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.21 E-value: 2.15e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422   530 QKKQQLQMEVKMLSSSksMKELTEEQQNLQKELE-------SLQNEHAQRMEEFYV---EQKDLEKKLEQIMKQKctcdS 599
Cdd:TIGR02168  239 EELEELQEELKEAEEE--LEELTAELQELEEKLEelrlevsELEEEIEELQKELYAlanEISRLEQQKQILRERL----A 312

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 223029422   600 NLEKDKEaEYAGQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKEL--KLQILKSSKTAKE 664
Cdd:TIGR02168  313 NLERQLE-ELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELeaELEELESRLEELE 378

TPH

pfam13868

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...

504-655

3.38e-06

Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 49.53 E-value: 3.38e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422  504 EDDKGKIMEEVMRTYLKQQEKLNLILQKKQQLQMEV-KMLSSSKSMKELTEEQQNLQKE-LESLQNEHAQRMEEFYVEQK 581
Cdd:pfam13868  97 LQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIdEFNEEQAEWKELEKEEEREEDErILEYLKEKAEREEEREAERE 176

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 223029422  582 DLEKKLEQIMkQKCTCDSNLEKDKEAEyagqLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 655
Cdd:pfam13868 177 EIEEEKEREI-ARLRAQQEKAQDEKAE----RDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQI 245

YhaN

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

520-655

3.78e-06

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 3.78e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422 520 KQQEKLNLILQKKQQLQMEVKMLSSSKSMKELTEEQQNLQKELESLQnEHAQRMEEFYVEQKDLEKKLEQIMKQKctcdS 599
Cdd:COG4717   99 ELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELP-ERLEELEERLEELRELEEELEELEAEL----A 173

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 223029422 600 NLEKDKEAEYAGQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 655
Cdd:COG4717  174 ELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229

ClpA

COG0542

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...

539-650

3.92e-06

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];

Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 50.08 E-value: 3.92e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422 539 VKMLSSSK--SMKELTEEQQNLQKELESLQNE----HAQRMEEFYVEQKDLEKKLEQIMKQKctcdsnlekDKEAEYAGQ 612
Cdd:COG0542  402 VRMEIDSKpeELDELERRLEQLEIEKEALKKEqdeaSFERLAELRDELAELEEELEALKARW---------EAEKELIEE 472

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 223029422 613 LAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKE 650
Cdd:COG0542  473 IQELKEELEQRYGKIPELEKELAELEEELAELAPLLRE 510

PRK03918

DNA double-strand break repair ATPase Rad50;

502-652

4.61e-06

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.06 E-value: 4.61e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422 502 ICEDDKGKIMEE-------VMRTYLKQQEKLNLILQKKQQLQMEVKMLSSSKSMKELTEEQQNLQKELESLQNEHAQRME 574
Cdd:PRK03918 445 LTEEHRKELLEEytaelkrIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKA 524

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 223029422 575 EFYVEqkdLEKKLEQIMKQKCTCDSNLEKDKEAEyaGQLAELRQRLDHAEADRQELQDELRQER-EARQKLEMMIKELK 652
Cdd:PRK03918 525 EEYEK---LKEKLIKLKGEIKSLKKELEKLEELK--KKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELE 598

SMC_prok_B

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...

520-661

4.96e-06

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.06 E-value: 4.96e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422   520 KQQEKLNLILQKKQQ----LQMEVKMLSSS-----KSMKELTEEQQNLQKELESLQNEHA---QRMEEFYVEQKDLEKKL 587
Cdd:TIGR02168  239 EELEELQEELKEAEEeleeLTAELQELEEKleelrLEVSELEEEIEELQKELYALANEISrleQQKQILRERLANLERQL 318

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422   588 EQIMKQKCTCDSNLEKDKE---------AEYAGQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQILKS 658
Cdd:TIGR02168  319 EELEAQLEELESKLDELAEelaeleeklEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL 398


                   ...
gi 223029422   659 SKT 661
Cdd:TIGR02168  399 NNE 401

Smc

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

520-656

5.00e-06

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.94 E-value: 5.00e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422 520 KQQEKLNLILQKKQQLQMEVKMLSssKSMKELTEEQQNLQKELESLQNEHAQRMEEfyveQKDLEKKLEQIMKQKctcdS 599
Cdd:COG1196  257 ELEAELAELEAELEELRLELEELE--LELEEAQAEEYELLAELARLEQDIARLEER----RRELEERLEELEEEL----A 326

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 223029422 600 NLEKDKEAEYAgQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQIL 656
Cdd:COG1196  327 ELEEELEELEE-ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382

EnvC

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...

520-664

6.73e-06

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

Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.99 E-value: 6.73e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422 520 KQQEKLNLILQKKQQLQMEVKMLSssKSMKELTEEQQNLQKELESLQNEHAQRMEEFY-----------VEQKDLEKK-- 586
Cdd:COG4942   59 ALERRIAALARRIRALEQELAALE--AELAELEKEIAELRAELEAQKEELAELLRALYrlgrqpplallLSPEDFLDAvr 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422 587 ----LEQIMKQKctcdsnleKDKEAEYAGQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQILKSSKTA 662
Cdd:COG4942  137 rlqyLKYLAPAR--------REQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKEL 208


                 ..
gi 223029422 663 KE 664
Cdd:COG4942  209 AE 210

EzrA

pfam06160

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...

546-658

6.89e-06

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.

Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 49.08 E-value: 6.89e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422  546 KSMKELTEEQQNLQKELESLQneHAQRMEEFYVE-QKDLEKKLEQIMKQKCTCDSNLEKDKEA--EYAGQLAELRQRLDH 622
Cdd:pfam06160 298 DYLEHAEEQNKELKEELERVQ--QSYTLNENELErVRGLEKQLEELEKRYDEIVERLEEKEVAysELQEELEEILEQLEE 375

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 223029422  623 AEADRQELQDELR----QEREARQKLEMMIKEL---KLQILKS 658
Cdd:pfam06160 376 IEEEQEEFKESLQslrkDELEAREKLDEFKLELreiKRLVEKS 418

PRK11637

AmiB activator; Provisional

518-642

8.02e-06

AmiB activator; Provisional

Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 48.92 E-value: 8.02e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422 518 YLKQ--QEKLNLILQKKQQLQMEVKMLsssksmkeltEEQQNLQKELESLQNEHAQRMEEFYVEQKDLEKKLEqimkqkc 595
Cdd:PRK11637 163 YLNQarQETIAELKQTREELAAQKAEL----------EEKQSQQKTLLYEQQAQQQKLEQARNERKKTLTGLE------- 225

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 223029422 596 tcdSNLEKDKEaeyagQLAELRQ---RLDHAEAdRQELQDELRQEREARQ 642
Cdd:PRK11637 226 ---SSLQKDQQ-----QLSELRAnesRLRDSIA-RAEREAKARAEREARE 266

COG4913

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

515-660

8.03e-06

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

Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 8.03e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422  515 MRTYLKQQEKLNLILQKKQQLQMEVKMLSSSKSmkELTEEQQNLQKELESLQNEHAQ----RMEEFYVEQKDLEKKLEQI 590
Cdd:COG4913   280 ALRLWFAQRRLELLEAELEELRAELARLEAELE--RLEARLDALREELDELEAQIRGnggdRLEQLEREIERLERELEER 357

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 223029422  591 ------MKQKC-TCDSNLEKDkEAEYAGQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELK--LQILKSSK 660
Cdd:COG4913   358 errrarLEALLaALGLPLPAS-AEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEaeIASLERRK 435

DHD_SKIDA1

cd21082

Dachshund-homology domain found in SKI/DACH domain-containing protein 1 (SKIDA1) and similar ...

127-211

8.35e-06

Dachshund-homology domain found in SKI/DACH domain-containing protein 1 (SKIDA1) and similar proteins; SKIDA1 is also known as protein DLN-1. Its biological function remains unclear. The Dachshund-homology domain (DHD), also known as the N-terminal Ski/Sno/Dac domain, adopts a mixed alpha/beta structure containing a helix-turn-helix motif, similar to features found in the forkhead/winged-helix family of DNA binding proteins. It contains a conserved CLPQ motif and can bind co-factors. Its structure suggests that it may also bind DNA.

Pssm-ID: 410785 Cd Length: 91 Bit Score: 44.64 E-value: 8.35e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422 127 TVLEGESISCFQVGGEKRLCLPQVLNSVLREFTLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAPSCGLITLTDA 206
Cdd:cd21082    4 EEVHGVELGYLYINGKQMFALSQVFTDLLPNTPRTTVHKRMDRLKVKKHHCDLEELRKLKALNGIAFHAAKCTLISREDV 83


                 ....*
gi 223029422 207 QRLCN 211
Cdd:cd21082   84 ERLYS 88

YhaN

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

509-652

9.01e-06

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 9.01e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422 509 KIMEEVMRTYLKQQEKLNLILQKKQQLQMEvkmlsssksMKELTEEQQNLQKELESLqnEHAQRMEEFYVEQKDLEKKLE 588
Cdd:COG4717   74 KELEEELKEAEEKEEEYAELQEELEELEEE---------LEELEAELEELREELEKL--EKLLQLLPLYQELEALEAELA 142

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 223029422 589 QIMKQkctcdsnLEKDKEAEyaGQLAELRQRLDHAEADRQELQDELRQERE-----ARQKLEMMIKELK 652
Cdd:COG4717  143 ELPER-------LEELEERL--EELRELEEELEELEAELAELQEELEELLEqlslaTEEELQDLAEELE 202

YhaN

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

518-664

1.01e-05

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 1.01e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422 518 YLKQQEKLNLILQKKQQLQMEVKMLSSS-KSMKELTEEQQNLQKELESLQNEHAQRMEEfyVEQKDLEKKLEQIMKQKCT 596
Cdd:COG4717   59 FKPQGRKPELNLKELKELEEELKEAEEKeEEYAELQEELEELEEELEELEAELEELREE--LEKLEKLLQLLPLYQELEA 136

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 223029422 597 CDSNLekdkeAEYAGQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQILKSSKTAKE 664
Cdd:COG4717  137 LEAEL-----AELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAE 199

SMC_prok_B

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...

511-664

1.02e-05

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.90 E-value: 1.02e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422   511 MEEVMRTYLKQQEKLNLILQKKQQLQMEVKMLSSSKsmKELTEEQQNLQKELESLQNEHAQRMEEFYVEQKDLEKKLEQI 590
Cdd:TIGR02168  686 IEELEEKIAELEKALAELRKELEELEEELEQLRKEL--EELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEI 763

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422   591 MKQKCTCDSNLEKDKEAE------------YAGQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQILKS 658
Cdd:TIGR02168  764 EELEERLEEAEEELAEAEaeieeleaqieqLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDL 843


                   ....*.
gi 223029422   659 SKTAKE 664
Cdd:TIGR02168  844 EEQIEE 849

AAA_13

pfam13166

AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...

476-664

1.03e-05

AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.

Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 48.90 E-value: 1.03e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422  476 NLVRDINKVgigLVAAASSPLLVKDVICEDDKGKIMEEVMRTYLKQQEKLNLILQKKQQ-LQMEVKMLSSSKSMKELTEE 554
Cdd:pfam13166 287 RLQKLIEKV---ESAISSLLAQLPAVSDLASLLSAFELDVEDIESEAEVLNSQLDGLRRaLEAKRKDPFKSIELDSVDAK 363

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422  555 QQN---LQKELESLQNEHAQRMEEFYVEQKDLEKKLEQIMKQKctCDSNLEKDKEAeYAGqlaelrqrldhAEADRQELQ 631
Cdd:pfam13166 364 IESindLVASINELIAKHNEITDNFEEEKNKAKKKLRLHLVEE--FKSEIDEYKDK-YAG-----------LEKAINSLE 429

                         170       180       190
                  ....*....|....*....|....*....|...
gi 223029422  632 DELRQEREARQKLEMMIKELKLQILKSSKTAKE 664
Cdd:pfam13166 430 KEIKNLEAEIKKLREEIKELEAQLRDHKPGADE 462

CwlO1

COG3883

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...

545-645

1.04e-05

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

Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 1.04e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422 545 SKSMKELTEEQQNLQKELESLQNEHAQRMEEFYVEQKDLEKKLEQIMKQKctcdsnlekdkeAEYAGQLAELRQRLDHAE 624
Cdd:COG3883  128 ADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQ------------AEQEALLAQLSAEEAAAE 195

                         90       100
                 ....*....|....*....|.
gi 223029422 625 ADRQELQDELRQEREARQKLE 645
Cdd:COG3883  196 AQLAELEAELAAAEAAAAAAA 216

YhaN

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

516-656

1.62e-05

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 1.62e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422 516 RTYLKQQEKLNLILQKKQQLQMEVKMLSSSKSMKELTEEQQNLQKELESLQNEHAQRMEEfyveQKDLEKKLEQimkqkc 595
Cdd:COG4717  395 EEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREE----LAELEAELEQ------ 464

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 223029422 596 tcdsnLEKDkeaeyaGQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQIL 656
Cdd:COG4717  465 -----LEED------GELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERL 514

GBP_C

pfam02841

Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...

497-652

1.72e-05

Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.

Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 47.28 E-value: 1.72e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422  497 LVKDVICEDDKGKIMEEVMRTYLKQQEKL-NLILQKKQQLQMEVKMLSSSKSMKELTEEQQnlqKELESLQNEHAQRMEE 575
Cdd:pfam02841 160 LEAKYNQVPRKGVKAEEVLQEFLQSKEAVeEAILQTDQALTAKEKAIEAERAKAEAAEAEQ---ELLREKQKEEEQMMEA 236

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 223029422  576 FYVEQKDLEKKLEQIMkqkctcdsnlekdkEAEYAGQLAELRQRLDHaeaDRQELQDELRQEREAR-QKLEMMIKELK 652
Cdd:pfam02841 237 QERSYQEHVKQLIEKM--------------EAEREQLLAEQERMLEH---KLQEQEELLKEGFKTEaESLQKEIQDLK 297

GBP_C

cd16269

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...

504-652

2.76e-05

Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 46.42 E-value: 2.76e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422 504 EDDKGKIMEEVMRTYLKQQEKL-NLILQKKQQL-QMEVKMlsssKSMKELTEEQQNLQKELESLQNEHAQRMEEfyvEQK 581
Cdd:cd16269  161 VPRKGVKAEEVLQEFLQSKEAEaEAILQADQALtEKEKEI----EAERAKAEAAEQERKLLEEQQRELEQKLED---QER 233

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 223029422 582 DLEKKLEQimkqkctcdsnLEKDKEAEYAGQLAELRQRLDHAEADRQELQDElrQEREARQKLEMMIKELK 652
Cdd:cd16269  234 SYEEHLRQ-----------LKEKMEEERENLLKEQERALESKLKEQEALLEE--GFKEQAELLQEEIRSLK 291

mukB

PRK04863

chromosome partition protein MukB;

553-664

3.11e-05

chromosome partition protein MukB;

Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.26 E-value: 3.11e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422  553 EEQQNLQKELESLQNEHAqRMEEFYVEQKDLEKKLEQIMKQkctcdSNLEKDKEAEYAGQLAELRQRLDHaeadrqeLQD 632
Cdd:PRK04863  506 REQRHLAEQLQQLRMRLS-ELEQRLRQQQRAERLLAEFCKR-----LGKNLDDEDELEQLQEELEARLES-------LSE 572

                          90       100       110
                  ....*....|....*....|....*....|..
gi 223029422  633 ELRQEREARQKLEMMIKELKLQILKSSKTAKE 664
Cdd:PRK04863  573 SVSEARERRMALRQQLEQLQARIQRLAARAPA 604

PRK03918

DNA double-strand break repair ATPase Rad50;

511-660

3.29e-05

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 3.29e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422 511 MEEVMRTYLKQQEKLNLILQKKQQLQMEVKMLSSS-KSMKELTEEQQNLQKELESLQNEhAQRMEEFYVEQKDLEKKLEQ 589
Cdd:PRK03918 288 LKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEiNGIEERIKELEEKEERLEELKKK-LKELEKRLEELEERHELYEE 366

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 223029422 590 IMKQKctcdSNLEKDKEAEYAGQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI--LKSSK 660
Cdd:PRK03918 367 AKAKK----EELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIeeLKKAK 435

OmpH

smart00935

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...

548-650

3.71e-05

Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 44.11 E-value: 3.71e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422   548 MKELTEEQQNLQKELESLQNEHAQRMEEFYVEQKDLEKKLEQIMKQKCTCDSNLEKDKEAEYAGQLAELRQrldhaeaDR 627
Cdd:smart00935   6 VQKILQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLSEAAREKKEKELQKKVQEFQR-------KQ 78

                           90       100
                   ....*....|....*....|....
gi 223029422   628 QELQDELRQER-EARQKLEMMIKE 650
Cdd:smart00935  79 QKLQQDLQKRQqEELQKILDKINK 102

Myosin_tail_1

pfam01576

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...

505-655

4.41e-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: 46.71 E-value: 4.41e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422   505 DDKGKIMEEVMRTYLKQQEKLNlilqkKQQLQMEVKMLSSSKSMKELTEEQQNLQKelesLQNEHAQRMEEFYVEQKDLE 584
Cdd:pfam01576  130 EAKIKKLEEDILLLEDQNSKLS-----KERKLLEERISEFTSNLAEEEEKAKSLSK----LKNKHEAMISDLEERLKKEE 200

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 223029422   585 K---KLEQImKQKCTCDSNLEKDKEAEYAGQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 655
Cdd:pfam01576  201 KgrqELEKA-KRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQI 273

PRK04778

septation ring formation regulator EzrA; Provisional

513-658

4.68e-05

septation ring formation regulator EzrA; Provisional

Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 46.37 E-value: 4.68e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422 513 EVMRTYLKQQEKLNlilqkkQQLQMEVKMLSSSK--SMKELtEEQQNLQKELESLQN---EHAQRME-------EFYVEQ 580
Cdd:PRK04778 313 DTLPDFLEHAKEQN------KELKEEIDRVKQSYtlNESEL-ESVRQLEKQLESLEKqydEITERIAeqeiaysELQEEL 385

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422 581 KDLEKKLEQIMKQkctcdsnlekdkEAEYAGQLAELRQrldhaeadrqelqdelrQEREARQKLEMMIKEL---KLQILK 657
Cdd:PRK04778 386 EEILKQLEEIEKE------------QEKLSEMLQGLRK-----------------DELEAREKLERYRNKLheiKRYLEK 436


                 .
gi 223029422 658 S 658
Cdd:PRK04778 437 S 437

GumC

COG3206

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

522-662

5.80e-05

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

Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.16 E-value: 5.80e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422 522 QEKLNLILQKKQQLQMEVKMLSSSKSMKELTEEQQNLQKELESLQ----NEH--AQRMEEfyvEQKDLEKKLEQIMKQ-K 594
Cdd:COG3206  239 EARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSarytPNHpdVIALRA---QIAALRAQLQQEAQRiL 315

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 223029422 595 CTCDSNLE--KDKEAEYAGQLAELRQRLDHAEADRQELQdELRQERE-ARQKLEMMIKELK-LQILKSSKTA 662
Cdd:COG3206  316 ASLEAELEalQAREASLQAQLAQLEARLAELPELEAELR-RLEREVEvARELYESLLQRLEeARLAEALTVG 386

SMC_prok_A

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...

520-664

6.07e-05

Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.60 E-value: 6.07e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422   520 KQQEKLNLILQKKQQ--LQMEVKMLSSSKSMKELTEEQQN-LQKELESLQNEHAQ--RMEEFYV-EQKDLEKKL----EQ 589
Cdd:TIGR02169  251 EELEKLTEEISELEKrlEEIEQLLEELNKKIKDLGEEEQLrVKEKIGELEAEIASleRSIAEKErELEDAEERLakleAE 330

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422   590 IMKQKCTCDS--------NLEKDK-EAEYAG---QLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQILK 657
Cdd:TIGR02169  331 IDKLLAEIEElereieeeRKRRDKlTEEYAElkeELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDR 410


                   ....*..
gi 223029422   658 SSKTAKE 664
Cdd:TIGR02169  411 LQEELQR 417

COG2433

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

480-652

6.78e-05

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: 6.78e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422 480 DINKVGIGLVAAASspllVKDVI---CEDDKGKIMEEVMRTYLKQQEKLNLILQKKQQLQMEVKmlsssksmkelteeqq 556
Cdd:COG2433  364 DRDEVKARVIRGLS----IEEALeelIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVE---------------- 423

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422 557 NLQKELESLQNEHAQRMEEFyveqKDLEKKLEQIMKQKctcDSNLEKDKEAeyagqlaelrQRLDhAEADRqeLQDELRQ 636
Cdd:COG2433  424 RLEAEVEELEAELEEKDERI----ERLERELSEARSEE---RREIRKDREI----------SRLD-REIER--LERELEE 483

                        170
                 ....*....|....*.
gi 223029422 637 EREARQKLEMMIKELK 652
Cdd:COG2433  484 ERERIEELKRKLERLK 499

F-BAR_PSTPIP

cd07647

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine ...

508-640

9.12e-05

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine Phosphatase-Interacting Proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Vetebrates contain two Proline-Serine-Threonine Phosphatase-Interacting Proteins (PSTPIPs), PSTPIP1 and PSTPIP2. PSTPIPs are mainly expressed in hematopoietic cells and are involved in the regulation of cell adhesion and motility. Mutations in PSTPIPs have been shown to cause autoinflammatory disorders. PSTPIP1 contains an N-terminal F-BAR domain, PEST motifs, and a C-terminal SH3 domain, while PSTPIP2 contains only the N-terminal F-BAR domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.

Pssm-ID: 153331 [Multi-domain] Cd Length: 239 Bit Score: 44.39 E-value: 9.12e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422 508 GKIMEEVMRTYLKQQEKL------NLI-LQKKQQLQMEVKMLSSS-KSMKELTEEQQNLQKELESLQNEHAQRMEEFYVE 579
Cdd:cd07647   17 GKKMCKELEDFLKQRAKAeedygkALLkLSKSAGPGDEIGTLKSSwDSLRKETENVANAHIQLAQSLREEAEKLEEFREK 96

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 223029422 580 QKDLEKKLEQIM----KQKCTCDSNL--------EKDKEAEYAGQLAElRQRLDHAEADRQELQDELRQEREA 640
Cdd:cd07647   97 QKEERKKTEDIMkrsqKNKKELYKKTmkakksyeQKCREKDKAEQAYE-KSSSGAQPKEAEKLKKKAAQCKTS 168

SMC_N

pfam02463

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...

504-664

9.57e-05

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.

Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 45.73 E-value: 9.57e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422   504 EDDKGKIMEEVMRTYLKQQEKLNLILQKKQQLQMEVKMLSSSKSMKELTEEQQNLQKELESLQNEHAQRMEEFYVEQKDL 583
Cdd:pfam02463  239 IDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKE 318

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422   584 EK----KLEQIMKQKCTCDSNLEK------DKEAEYAGQLAELRQRLDHAEADRQELQDELRQERE---ARQKLEMMIKE 650
Cdd:pfam02463  319 SEkekkKAEKELKKEKEEIEELEKelkeleIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESErlsSAAKLKEEELE 398

                          170
                   ....*....|....
gi 223029422   651 LKLQILKSSKTAKE 664
Cdd:pfam02463  399 LKSEEEKEAQLLLE 412

MukB

COG3096

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...

513-645

1.03e-04

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: 45.71 E-value: 1.03e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422  513 EVMRTYLKQQeklnLILQKKQQLQMEvkmlsssksmkeLTEEQQNL--QKELESLQNEHAQRMEEFYVEQKDLEKKLEQI 590
Cdd:COG3096   499 ELLRRYRSQQ----ALAQRLQQLRAQ------------LAELEQRLrqQQNAERLLEEFCQRIGQQLDAAEELEELLAEL 562

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 223029422  591 MKQKCTCDSNLEKDKEaeyagQLAELRQRLDHAEADRQELQDELRQEREARQKLE 645
Cdd:COG3096   563 EAQLEELEEQAAEAVE-----QRSELRQQLEQLRARIKELAARAPAWLAAQDALE 612

GAS

pfam13851

Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...

531-656

1.05e-04

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

Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 43.74 E-value: 1.05e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422  531 KKQQLQMEVKMLSSSKSMKELTEEQQNLQKELESLQNE------HAQRMEEFYVEQKDLEKKLeqimkqkctcdSNLEKD 604
Cdd:pfam13851  39 KKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQlenyekDKQSLKNLKARLKVLEKEL-----------KDLKWE 107

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 223029422  605 KEaeyagqlaELRQRLDHAEADRQELQDELRQE-REARQK--LEMMIKELKLQIL 656
Cdd:pfam13851 108 HE--------VLEQRFEKVERERDELYDKFEAAiQDVQQKtgLKNLLLEKKLQAL 154

EnvC

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...

511-664

1.29e-04

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: 44.75 E-value: 1.29e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422 511 MEEVMRTYLKQQEKLNLILQKKQQLQMEVKMLSssKSMKELTEEQQNLQKELESLQnehaQRMEEFYVEQKDLEKKLEQ- 589
Cdd:COG4942   29 LEQLQQEIAELEKELAALKKEEKALLKQLAALE--RRIAALARRIRALEQELAALE----AELAELEKEIAELRAELEAq 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422 590 ----------------------IMKQkctcDSNLEKDKEAEYAGQLAE-LRQRLDHAEADRQELQDELRQEREARQKLEM 646
Cdd:COG4942  103 keelaellralyrlgrqpplalLLSP----EDFLDAVRRLQYLKYLAPaRREQAEELRADLAELAALRAELEAERAELEA 178

                        170       180
                 ....*....|....*....|
gi 223029422 647 MIKELK--LQILKSSKTAKE 664
Cdd:COG4942  179 LLAELEeeRAALEALKAERQ 198

PRK12704

phosphodiesterase; Provisional

510-655

1.31e-04

phosphodiesterase; Provisional

Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.15 E-value: 1.31e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422 510 IMEEVMRTYLKQ-QEKLNLILQKKQqlqMEVKMLSSSKsMKELTEEQQNLQKELEslqNEHAQRMEEFyveqKDLEKKL- 587
Cdd:PRK12704  24 VRKKIAEAKIKEaEEEAKRILEEAK---KEAEAIKKEA-LLEAKEEIHKLRNEFE---KELRERRNEL----QKLEKRLl 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422 588 --EQIMKQKctcDSNLEKdKEAEYAGQLAELRQRLDHAEADRQELQDELRQER------------EARQK-LEMMIKELK 652
Cdd:PRK12704  93 qkEENLDRK---LELLEK-REEELEKKEKELEQKQQELEKKEEELEELIEEQLqelerisgltaeEAKEIlLEKVEEEAR 168


                 ...
gi 223029422 653 LQI 655
Cdd:PRK12704 169 HEA 171

DUF4201

pfam13870

Domain of unknown function (DUF4201); This is a family of coiled-coil proteins from eukaryotes. ...

525-654

1.53e-04

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: 42.98 E-value: 1.53e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422  525 LNLILQKKQQLQMEVKmlssSKSMKELTEeqqNLQK-ELESLQNEHAQRMEEfyVEQKDLEkkLEQiMKQKCTCDS---N 600
Cdd:pfam13870  13 LELITLKHTLAKIQEK----LEQKEELGE---GLTMiDFLQLQIENQALNEK--IEERNKE--LKR-LKLKVTNTVhalT 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 223029422  601 LEKDKEAEYAGQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQ 654
Cdd:pfam13870  81 HLKEKLHFLSAELSRLKKELRERQELLAKLRKELYRVKLERDKLRKQNKKLRQQ 134

SMC_prok_A

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...

509-664

1.85e-04

Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.67 E-value: 1.85e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422   509 KIMEEVMRTYLKQQEKLNLIlqKKQQLQMEVKMLSSSKSMKELTEEQQNLQKELESLQNEHAQRMEEFYVEQKDLEKKLE 588
Cdd:TIGR02169  280 KIKDLGEEEQLRVKEKIGEL--EAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTE 357

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422   589 QIMKQKCTCDSNL----EKDKE-AEYAGQLAELRQRLDHAEADRQE-------LQDELRQEREARQKLEMMIKELKLQIL 656
Cdd:TIGR02169  358 EYAELKEELEDLRaeleEVDKEfAETRDELKDYREKLEKLKREINElkreldrLQEELQRLSEELADLNAAIAGIEAKIN 437


                   ....*...
gi 223029422   657 KSSKTAKE 664
Cdd:TIGR02169  438 ELEEEKED 445

HEC1

COG5185

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...

512-652

2.40e-04

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: 44.18 E-value: 2.40e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422 512 EEVMRTYLKQQEKLNLILQKKQQLQ-------MEVKMLSSSKSMKELTEEQQNLQKELESLQNEHAQRMEEFY--VEQKD 582
Cdd:COG5185  295 KEKIAEYTKSIDIKKATESLEEQLAaaeaeqeLEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVgeVELSK 374

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 223029422 583 LEKKLEQIMKQ-KCTCDSNLEKDKEAEYAGQ--LAELRQRLDHAEADRQELQDELRQereARQKLEMMIKELK 652
Cdd:COG5185  375 SSEELDSFKDTiESTKESLDEIPQNQRGYAQeiLATLEDTLKAADRQIEELQRQIEQ---ATSSNEEVSKLLN 444

HlpA

COG2825

Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...

546-650

2.80e-04

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

Pssm-ID: 442073 [Multi-domain] Cd Length: 171 Bit Score: 42.13 E-value: 2.80e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422 546 KSMKELTEEQQNLQKELESLQNEhAQRMeefyveQKDLEKKLEQIMKQKCTCDSNLEKDKEAEYAGQLAELRQRldhaea 625
Cdd:COG2825   36 QESPEGKAAQKKLEKEFKKRQAE-LQKL------EKELQALQEKLQKEAATLSEEERQKKERELQKKQQELQRK------ 102

                         90       100
                 ....*....|....*....|....*.
gi 223029422 626 dRQELQDELRQER-EARQKLEMMIKE 650
Cdd:COG2825  103 -QQEAQQDLQKRQqELLQPILEKIQK 127

PRK03918

DNA double-strand break repair ATPase Rad50;

504-652

3.19e-04

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 3.19e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422 504 EDDKGKIMEEVMRTYLKQQEKLNLILQKKQQLQMEVKMLSSSKSmkelteEQQNLQKELESLQNEHAQRMEEFYVEQKDL 583
Cdd:PRK03918 569 EEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEK------ELEREEKELKKLEEELDKAFEELAETEKRL 642

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 223029422 584 EKKLEQI--MKQKCTCD-----SNLEKDKEAEYAG---QLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELK 652
Cdd:PRK03918 643 EELRKELeeLEKKYSEEeyeelREEYLELSRELAGlraELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE 721

EnvC

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...

542-664

3.23e-04

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: 43.60 E-value: 3.23e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422 542 LSSSKSMKELTEEQQNLQKELESLQnehaQRMEEFYVEQKDLEKKLEQIMKQkctcdSNLEKDKEAEYAGQLAELRQRLD 621
Cdd:COG4942   16 AAQADAAAEAEAELEQLQQEIAELE----KELAALKKEEKALLKQLAALERR-----IAALARRIRALEQELAALEAELA 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 223029422 622 HAEADRQELQDELRQERE--ARQ--KLEMMIKELKLQILKSSKTAKE 664
Cdd:COG4942   87 ELEKEIAELRAELEAQKEelAELlrALYRLGRQPPLALLLSPEDFLD 133

PRK04778

septation ring formation regulator EzrA; Provisional

533-664

3.27e-04

septation ring formation regulator EzrA; Provisional

Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 43.67 E-value: 3.27e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422 533 QQLQMEVKMLSssKSMKE----LTEEQQNLQKELESLQNEHAQ-RMEEFYVEQKDLEKKLEQIMKQkctCDSNLEkdkea 607
Cdd:PRK04778 201 DQLEEELAALE--QIMEEipelLKELQTELPDQLQELKAGYRElVEEGYHLDHLDIEKEIQDLKEQ---IDENLA----- 270

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 223029422 608 eyagQLAELrqRLDHAEADRQELQDE-------LRQEREARQKLEMMIKELKLQILKSSKTAKE 664
Cdd:PRK04778 271 ----LLEEL--DLDEAEEKNEEIQERidqlydiLEREVKARKYVEKNSDTLPDFLEHAKEQNKE 328

PRK03918

DNA double-strand break repair ATPase Rad50;

498-652

3.28e-04

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 3.28e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422 498 VKDVICEddKGKIMEEVMRtylkqqeKLNLILQKKQQLQMEVKMLSSS-KSMKELTEEQQNLQKELESLQNEHA------ 570
Cdd:PRK03918 191 IEELIKE--KEKELEEVLR-------EINEISSELPELREELEKLEKEvKELEELKEEIEELEKELESLEGSKRkleeki 261

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422 571 ----QRMEEFYVEQKDLEKKLEQI--MKQKCTCDSNLEKDKEaEYAGQLAELRQRLDHAEADRQELQDELRQEREARQKL 644
Cdd:PRK03918 262 releERIEELKKEIEELEEKVKELkeLKEKAEEYIKLSEFYE-EYLDELREIEKRLSRLEEEINGIEERIKELEEKEERL 340


                 ....*...
gi 223029422 645 EMMIKELK 652
Cdd:PRK03918 341 EELKKKLK 348

DUF4175

pfam13779

Domain of unknown function (DUF4175);

548-650

3.94e-04

Domain of unknown function (DUF4175);

Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 43.82 E-value: 3.94e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422  548 MKELTEEQQNLQKELESLQNEHAQRMeefyvEQKDLEKKLEQImkqkctcdsnlekdKEAEYAGQLAELRQRLDHAE--- 624
Cdd:pfam13779 526 MQALAEQAQQNPQDLQQPDDPNAQEM-----TQQDLQRMLDRI--------------EELARSGRRAEAQQMLSQLQqml 586

                          90       100       110
                  ....*....|....*....|....*....|..
gi 223029422  625 -----ADRQELQDELRQE-REARQKLEMMIKE 650
Cdd:pfam13779 587 enlqaGQPQQQQQQGQSEmQQAMDELGDLLRE 618

YhaN

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

484-652

4.33e-04

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 4.33e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422 484 VGIGLVAAASSPLLVKDVICEDDKGKIMEEVMRTYLKQQEKLNLI----LQKKQQLQMEVKMLSSSKSMKELTEEQQNLQ 559
Cdd:COG4717  281 LVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLaalgLPPDLSPEELLELLDRIEELQELLREAEELE 360

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422 560 KELESLQNEHAQR----------MEEFYV------EQKDLEKKLEQIMKQkctCDSNLEKDKEAEYAGQLAELRQRLDHA 623
Cdd:COG4717  361 EELQLEELEQEIAallaeagvedEEELRAaleqaeEYQELKEELEELEEQ---LEELLGELEELLEALDEEELEEELEEL 437

                        170       180
                 ....*....|....*....|....*....
gi 223029422 624 EADRQELQDELRQEREARQKLEMMIKELK 652
Cdd:COG4717  438 EEELEELEEELEELREELAELEAELEQLE 466

FAM184

pfam15665

Family with sequence similarity 184, A and B; The function of FAM184 is not known.

504-652

5.68e-04

Family with sequence similarity 184, A and B; The function of FAM184 is not known.

Pssm-ID: 464788 [Multi-domain] Cd Length: 211 Bit Score: 41.57 E-value: 5.68e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422  504 EDDKGKIMEEVMRTYLKQQEKLNLILQKKQQLQMEVKMLSSSKSMKE--LTEEQQNLQKELES---LQNEHAQRMEEFYV 578
Cdd:pfam15665  24 EEEIQQILAETREKILQYKSKIGEELDLKRRIQTLEESLEQHERMKRqaLTEFEQYKRRVEERelkAEAEHRQRVVELSR 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422  579 E----QKDLEKKLEQIMKQKctcdSNLEKDKE-------AEYAGQLAELRQRLD--HAE--ADRQELQDELRQEREA-RQ 642
Cdd:pfam15665 104 EveeaKRAFEEKLESFEQLQ----AQFEQEKRkaleelrAKHRQEIQELLTTQRaqSASslAEQEKLEELHKAELESlRK 179

                         170
                  ....*....|
gi 223029422  643 KLEMMIKELK 652
Cdd:pfam15665 180 EVEDLRKEKK 189

mukB

PRK04863

chromosome partition protein MukB;

513-659

5.95e-04

chromosome partition protein MukB;

Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.41 E-value: 5.95e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422  513 EVMRTYLKQQEKLNLILQKKQQLQMEVKMLsssksmKELTEEQQNLQK-----------------ELESLQNEHAQRMEE 575
Cdd:PRK04863  496 DVARELLRRLREQRHLAEQLQQLRMRLSEL------EQRLRQQQRAERllaefckrlgknlddedELEQLQEELEARLES 569

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422  576 FYVEQKDLEKK---LEQIMKQKCTCDSNLEKDKEAEYAGQ--LAELRQRLDHAEADRQEL----QDELRQEREARQ---K 643
Cdd:PRK04863  570 LSESVSEARERrmaLRQQLEQLQARIQRLAARAPAWLAAQdaLARLREQSGEEFEDSQDVteymQQLLERERELTVerdE 649

                         170
                  ....*....|....*.
gi 223029422  644 LEMMIKELKLQILKSS 659
Cdd:PRK04863  650 LAARKQALDEEIERLS 665

ATAD3_N

pfam12037

ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ...

540-647

6.21e-04

ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal domain of ATPase family AAA domain-containing protein 3 (ATAD3) which is involved in dimerization and interacts with the inner surface of the outer mitochondrial membrane. This domain is found associated with the AAA ATPase domain (pfam00004). ATAD3 is essential for mitochondrial network organization, mitochondrial metabolism and cell growth at organizm and cellular level. It may also play an important role in mitochondrial protein synthesis.

Pssm-ID: 463442 [Multi-domain] Cd Length: 264 Bit Score: 42.28 E-value: 6.21e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422  540 KMLSSSKSMK---ELTEEQ-QNLQKELESLQNEHAQRMEEFYVEQKDLE----KKLEQIMKQkctcdsnlEKDKEAEYAG 611
Cdd:pfam12037  36 RELESSPHAKkalELMKKQeQTRQAELQAKIKEYEAAQEQLKIERQRVEyeerRKTLQEETK--------QKQQRAQYQD 107

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 223029422  612 QLAelRQRL-DHAEADRQELQDELRQEREARQKLEMM 647
Cdd:pfam12037 108 ELA--RKRYqDQLEAQRRRNEELLRKQEESVAKQEAM 142

YhaN

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

556-654

6.26e-04

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 6.26e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422 556 QNLQKELESLQNEHAQRMEEFYVEQKDLEKKLEQimkqkctcdsnlEKDKEAEYA---GQLAELRQRLDHAEADRQELQD 632
Cdd:COG4717   49 ERLEKEADELFKPQGRKPELNLKELKELEEELKE------------AEEKEEEYAelqEELEELEEELEELEAELEELRE 116

                         90       100
                 ....*....|....*....|..
gi 223029422 633 ELRQEREARQKLEMMIKELKLQ 654
Cdd:COG4717  117 ELEKLEKLLQLLPLYQELEALE 138

DR0291

COG1579

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...

511-655

6.49e-04

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: 41.83 E-value: 6.49e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422 511 MEEVMRTYLKQQEKLNLILQKKQQLqmevkmlsssksmKELTEEQQNLQKELESLQnehaQRMEEFYVEQKDLEKKLEQI 590
Cdd:COG1579    2 MPEDLRALLDLQELDSELDRLEHRL-------------KELPAELAELEDELAALE----ARLEAAKTELEDLEKEIKRL 64

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 223029422 591 MKQKCTCDSNLEKDKEA--------EYAGQLAElrqrLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 655
Cdd:COG1579   65 ELEIEEVEARIKKYEEQlgnvrnnkEYEALQKE----IESLKRRISDLEDEILELMERIEELEEELAELEAEL 133

SCP-1

pfam05483

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...

335-664

6.78e-04

Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 42.79 E-value: 6.78e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422  335 FSMRSGKRNQSKTDAPSGMELQSWYPVIKQEGDHV---------------SQTHSFLHPSYYlYMCDKVVAPNVSLTSAV 399
Cdd:pfam05483  23 FAKSNLSKNGENIDSDPAFQKLNFLPMLEQVANSGdchyqeglkdsdfenSEGLSRLYSKLY-KEAEKIKKWKVSIEAEL 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422  400 SQsKELTKTEASKSISRQSEKAHssgKLQKTVSYPDVSLEE--QEKMDL----KTSRELCSRLDASISNNSTSKRKSE-- 471
Cdd:pfam05483 102 KQ-KENKLQENRKIIEAQRKAIQ---ELQFENEKVSLKLEEeiQENKDLikenNATRHLCNLLKETCARSAEKTKKYEye 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422  472 -----SATCNLVRDINKVGIGL----VAAASSPLLVKDVICED-DKGKIMEEVMRTYLKQQEK-LNLIL----QKKQQL- 535
Cdd:pfam05483 178 reetrQVYMDLNNNIEKMILAFeelrVQAENARLEMHFKLKEDhEKIQHLEEEYKKEINDKEKqVSLLLiqitEKENKMk 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422  536 --------------QMEVKMLSSSKSMKELTEEQQNLQKELESLQnehaQRMEEFYVEQKDLEKKLEQIMKQKCtcdsNL 601
Cdd:pfam05483 258 dltflleesrdkanQLEEKTKLQDENLKELIEKKDHLTKELEDIK----MSLQRSMSTQKALEEDLQIATKTIC----QL 329

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422  602 EKDKEAeyagQLAEL-RQRLDHA------EADRQELQDELRQEREARQKLEMMIKELKLQILKSSKTAKE 664
Cdd:pfam05483 330 TEEKEA----QMEELnKAKAAHSfvvtefEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEE 395

DHD_Dac

cd21081

Dachshund-homology domain found in the retinal determination protein Dachshund and similar ...

131-209

7.69e-04

Dachshund-homology domain found in the retinal determination protein Dachshund and similar proteins; Dachshund proteins act as transcription factors involved in the regulation of organogenesis. They may be a regulator of SIX1, SIX6 and probably SIX5. The Dachshund-homology domain (DHD), also known as the N-terminal Ski/Sno/Dac domain, adopts a mixed alpha/beta structure containing a helix-turn-helix motif, similar to features found in the forkhead/winged-helix family of DNA binding proteins. It contains a conserved CLPQ motif and can bind co-factors. Its structure suggests that it may also bind DNA. It has been postulated that Dachshund proteins may bind to chromatin DNA via their DHD domains.

Pssm-ID: 410784 Cd Length: 95 Bit Score: 39.27 E-value: 7.69e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422 131 GESISCFQVGGEKRLCLPQVLNSVLREFT--LQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAPSCGLITLTDAQR 208
Cdd:cd21081   10 GAKVAAFTVDGEELICLPQAFELFLKHLVggLHTVYTKLKRLDITPVVCNVEQVRILRGLGAIQPGVNRCKLISRKDFDT 89


                 .
gi 223029422 209 L 209
Cdd:cd21081   90 L 90

FCH_F-BAR

cd07610

The Extended FES-CIP4 Homology (FCH) or F-BAR (FCH and Bin/Amphiphysin/Rvs) domain, a ...

506-655

9.19e-04

The Extended FES-CIP4 Homology (FCH) or F-BAR (FCH and Bin/Amphiphysin/Rvs) domain, a dimerization module that binds and bends membranes; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. F-BAR domain containing proteins, also known as Pombe Cdc15 homology (PCH) family proteins, include Fes and Fer tyrosine kinases, PACSINs/Syndapins, FCHO, PSTPIP, CIP4-like proteins and srGAPs. Many members also contain an SH3 domain and play roles in endocytosis. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules. These tubules have diameters larger than those observed with N-BARs. The F-BAR domains of some members such as NOSTRIN and Rgd1 are important for the subcellular localization of the protein.

Pssm-ID: 153294 [Multi-domain] Cd Length: 191 Bit Score: 40.79 E-value: 9.19e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422 506 DKGKIMEEVMRTYLKQQEKL---------NLILQKKQQLQMEVKMLSSS-KSMKELTEE--------QQNLQKELESLQN 567
Cdd:cd07610   10 ELGLDLLKDLREFLKKRAAIeeeyaknlqKLAKKFSKKPESGKTSLGTSwNSLREETESaatvheelSEKLSQLIREPLE 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422 568 EHAQRMEEfyvEQKDLEKKLEQIMKQKCTCDSNLEKDKEAEYAGQLAEL-RQRLDHAEADRQELQDELRQEREARQKLEM 646
Cdd:cd07610   90 KVKEDKEQ---ARKKELAEGEKLKKKLQELWAKLAKKADEEYREQVEKLnPAQSEYEEEKLNKIQAEQEREEERLEILKD 166


                 ....*....
gi 223029422 647 MIKELKLQI 655
Cdd:cd07610  167 NLKNYINAI 175

EnvC

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...

520-664

9.53e-04

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: 42.06 E-value: 9.53e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422 520 KQQEKLNLILQK--KQQLQMEVKMLSSSKSMKELTEEQQNLQkeleSLQNEHAQRMEEFYVEQKDLEKKLEQIMKQKctc 597
Cdd:COG4942  101 AQKEELAELLRAlyRLGRQPPLALLLSPEDFLDAVRRLQYLK----YLAPARREQAEELRADLAELAALRAELEAER--- 173

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 223029422 598 dsnleKDKEAEYAgQLAELRQRLDHAEADRQELQDELRQEREARQK----LEMMIKELKLQILKSSKTAKE 664
Cdd:COG4942  174 -----AELEALLA-ELEEERAALEALKAERQKLLARLEKELAELAAelaeLQQEAEELEALIARLEAEAAA 238

DUF4670

pfam15709

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...

506-646

9.89e-04

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.

Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 42.25 E-value: 9.89e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422  506 DKGKIMEEVMRtyLKQQEKLNLILQKKQQLQMEvkmlsssKSMKELTEEQQNLQKELEslQNEHAQRMEEFYVEQKDLEK 585
Cdd:pfam15709 369 ERAEKMREELE--LEQQRRFEEIRLRKQRLEEE-------RQRQEEEERKQRLQLQAA--QERARQQQEEFRRKLQELQR 437

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 223029422  586 KLEQIMKQKctcdSNLEKDKEAEYAGQLAELRQRL-DHAEADRQELQDElRQEREARQKLEM 646
Cdd:pfam15709 438 KKQQEEAER----AEAEKQRQKELEMQLAEEQKRLmEMAEEERLEYQRQ-KQEAEEKARLEA 494

DUF5401

pfam17380

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

519-655

9.97e-04

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: 42.42 E-value: 9.97e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422  519 LKQQEKLNLILQKKQQLQMEVKMLSSSKSMKELTEEQQNLQKELESLQNEHAQRMEEFYVEQKDL----EKKLEQIMKQK 594
Cdd:pfam17380 278 VQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMamerERELERIRQEE 357

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 223029422  595 CTcdSNLEKDKEAEYAGQLAELRQrLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 655
Cdd:pfam17380 358 RK--RELERIRQEEIAMEISRMRE-LERLQMERQQKNERVRQELEAARKVKILEEERQRKI 415

DUF4200

pfam13863

Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...

554-664

1.04e-03

Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.

Pssm-ID: 464003 [Multi-domain] Cd Length: 119 Bit Score: 39.47 E-value: 1.04e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422  554 EQQNLQKELESLQNEHAQRMEEFYVEQKDLEKKLEQIMKqkctcdsnlekdkeaeyagQLAELRQRLDHAEADRQELQDE 633
Cdd:pfam13863   7 EMFLVQLALDAKREEIERLEELLKQREEELEKKEQELKE-------------------DLIKFDKFLKENDAKRRRALKK 67

                          90       100       110
                  ....*....|....*....|....*....|...
gi 223029422  634 LRQEREARQKLEMMIKELKLQI--LKSSKTAKE 664
Cdd:pfam13863  68 AEEETKLKKEKEKEIKKLTAQIeeLKSEISKLE 100

GAS

pfam13851

Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...

504-630

1.31e-03

Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 40.66 E-value: 1.31e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422  504 EDDKGKIMEEV------MRTYLKQQEKLNLILQKKQQLQMEVKMlssskSMKELTEEQQNLQKELESLQNEHA---QRME 574
Cdd:pfam13851  42 EERNEKLMSEIqqenkrLTEPLQKAQEEVEELRKQLENYEKDKQ-----SLKNLKARLKVLEKELKDLKWEHEvleQRFE 116

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422  575 EFYVEQKDLEKKLEQIM---KQKCTCDSN-LEKdkeaeyagQLAELRQRLDHAEADRQEL 630
Cdd:pfam13851 117 KVERERDELYDKFEAAIqdvQQKTGLKNLlLEK--------KLQALGETLEKKEAQLNEV 168

COG4372

Uncharacterized protein, contains DUF3084 domain [Function unknown];

544-664

1.46e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];

Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 1.46e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422 544 SSKSMKELTEEQQNLQKELESLQNEHAQRMEEFyveqKDLEKKLEQIMKQkctcdsnLEKDKEaeyagQLAELRQRLDHA 623
Cdd:COG4372   29 LSEQLRKALFELDKLQEELEQLREELEQAREEL----EQLEEELEQARSE-------LEQLEE-----ELEELNEQLQAA 92

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 223029422 624 EADRQELQDELRQEREARQKLEMMIKELKLQILKSSKTAKE 664
Cdd:COG4372   93 QAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQ 133

MAP65_ASE1

pfam03999

Microtubule associated protein (MAP65/ASE1 family);

512-660

1.61e-03

Microtubule associated protein (MAP65/ASE1 family);

Pssm-ID: 427641 [Multi-domain] Cd Length: 477 Bit Score: 41.53 E-value: 1.61e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422  512 EEVMRTYLKQQEKLNLILQKKQQLQMEVKMLSSSKSMKEL--TEEQQNLQKELESLQNEHAQRMEEFyveqKDLEKKLEQ 589
Cdd:pfam03999 100 EHLRKEKAPRLAEIKELLEQLQQLCEELGEEPLPLLIDPLpsLEELESFRKHLENLRNEKERRLEEV----NELKKQIKL 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422  590 IMKQ--------------------KCTCDSNLEKDKEA--EYAGQLAELRQRLDHAEADRQELQDELR-----QEREARQ 642
Cdd:pfam03999 176 LMEEldlvpgtdfeedllcesednFCLSRENIDKLRKLikQLEEQKAEREEKIDDLREKILELWNRLQvpqeeQESFVRE 255

                         170       180
                  ....*....|....*....|....*.
gi 223029422  643 ----KLEMMI---KEL-KLQILKSSK 660
Cdd:pfam03999 256 nnslSQDTIDalrEELqRLEELKKKN 281

OmpH

pfam03938

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...

546-650

1.76e-03

Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 39.10 E-value: 1.76e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422  546 KSMKELTEEQQNLQKELESLQNEHAQRMEEFYVEQKDLEKKLEQIMKQKctcdsnleKDKEAEYAGQLAELRQRldhaea 625
Cdd:pfam03938  12 EESPEGKAAQAQLEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEER--------EEKEQELQKKEQELQQL------ 77

                          90       100
                  ....*....|....*....|....*.
gi 223029422  626 dRQELQDELRQER-EARQKLEMMIKE 650
Cdd:pfam03938  78 -QQKAQQELQKKQqELLQPIQDKINK 102

CwlO1

COG3883

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...

543-636

1.78e-03

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

Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 1.78e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422 543 SSSKSMKELTEEQQNLQKELESLQNEhAQRMEEfyvEQKDLEKKLEQIMKqkctcdsnlekdkeaeyagQLAELRQRLDH 622
Cdd:COG3883   20 AKQKELSELQAELEAAQAELDALQAE-LEELNE---EYNELQAELEALQA-------------------EIDKLQAEIAE 76

                         90
                 ....*....|....
gi 223029422 623 AEADRQELQDELRQ 636
Cdd:COG3883   77 AEAEIEERREELGE 90

COG4913

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

544-658

2.00e-03

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

Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 2.00e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422  544 SSKSMKELTE-------EQQNLQKELESLQnEHAQRMEEFYVEQKDLEKK---LEQIMKQKCTCDSNLEKDKEAEYAG-- 611
Cdd:COG4913   202 SFKPIGDLDDfvreymlEEPDTFEAADALV-EHFDDLERAHEALEDAREQielLEPIRELAERYAAARERLAELEYLRaa 280

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 223029422  612 --------QLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQILKS 658
Cdd:COG4913   281 lrlwfaqrRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGN 335

Mitofilin

pfam09731

Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...

437-631

2.11e-03

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

Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 41.28 E-value: 2.11e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422  437 SLEEQEKMDLKtsRELCSRLDASISN----NSTSKRKSESATCNLVRDINKVGIGLVAaassplLVKDVicEDDKGKIME 512
Cdd:pfam09731 250 ELVASERIVFQ--QELVSIFPDIIPVlkedNLLSNDDLNSLIAHAHREIDQLSKKLAE------LKKRE--EKHIERALE 319

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422  513 EVMRTYLKQQEKLNLILQKKQQLQMEVKMLSSSKSMKELTEE-QQNLQKELESLQNEHAQRMEEFYVEQK-DLEKKLEQI 590
Cdd:pfam09731 320 KQKEELDKLAEELSARLEEVRAADEAQLRLEFEREREEIRESyEEKLRTELERQAEAHEEHLKDVLVEQEiELQREFLQD 399

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 223029422  591 MKQKCTCDSNLEKDKEAEYAGQLAEL-RQRLDHAEADRQELQ 631
Cdd:pfam09731 400 IKEKVEEERAGRLLKLNELLANLKGLeKATSSHSEVEDENRK 441

Myosin_tail_1

pfam01576

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...

523-664

2.15e-03

Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 41.31 E-value: 2.15e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422   523 EKLNLILQKK-QQLQMEVKMLSSSKS-----MKELTEEQQNLQ---KELESLQNEHAQRMEEFYVEQK-------DLEKK 586
Cdd:pfam01576  376 EKAKQALESEnAELQAELRTLQQAKQdsehkRKKLEGQLQELQarlSESERQRAELAEKLSKLQSELEsvssllnEAEGK 455

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422   587 LEQIMKQKCTCDSNLEKDKE--AEYAGQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQILKSSKTAKE 664
Cdd:pfam01576  456 NIKLSKDVSSLESQLQDTQEllQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEE 535

Smc

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

477-651

2.18e-03

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.46 E-value: 2.18e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422 477 LVRDINKVGIGLVAAASSPLLVKDVICEDDKGKIMEEVMRTYLKQQEKLNLILQKKQQLQMEVKMLSSSKSMKELTEEQQ 556
Cdd:COG1196  623 LGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAE 702

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422 557 NLQKELESLQNEHAQRMEEFYVEQKDLEKKLEQIMKQKCTCDSNLEKDKEAEYAG---QLAELRQRLDHAEADRQEL--- 630
Cdd:COG1196  703 EEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPeppDLEELERELERLEREIEALgpv 782

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 223029422 631 --------------QDELRQER----EARQKLEMMIKEL 651
Cdd:COG1196  783 nllaieeyeeleerYDFLSEQRedleEARETLEEAIEEI 821

Mplasa_alph_rch

TIGR04523

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...

505-664

2.34e-03

Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.16 E-value: 2.34e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422  505 DDKGKIMEEVMRTYLKQQEKLNLIL-QKKQQLQMEVKMLSSSKS-MKELTEEQQNLQKELESLQNehaqRMEEFYVEQKD 582
Cdd:TIGR04523 460 DNTRESLETQLKVLSRSINKIKQNLeQKQKELKSKEKELKKLNEeKKELEEKVKDLTKKISSLKE----KIEKLESEKKE 535

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422  583 LEKKLEQIMKQKCTCDSNLEKDKeaeYAGQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQILKSSKTA 662
Cdd:TIGR04523 536 KESKISDLEDELNKDDFELKKEN---LEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKI 612


                  ..
gi 223029422  663 KE 664
Cdd:TIGR04523 613 SS 614

COG4372

Uncharacterized protein, contains DUF3084 domain [Function unknown];

521-664

2.71e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];

Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 2.71e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422 521 QQEKLNLILQKKQQLQMEVKMLSSSKSMKELTEEQQNLQKELESLQNEHAQRMEEfyveqkdlEKKLEQIMKQKctcdsn 600
Cdd:COG4372   83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQ--------IAELQSEIAER------ 148

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 223029422 601 lekdkeaeyAGQLAELRQRLDHAEADRQELQDELRQ--EREARQKLEMMIKELKLQILKSSKTAKE 664
Cdd:COG4372  149 ---------EEELKELEEQLESLQEELAALEQELQAlsEAEAEQALDELLKEANRNAEKEEELAEA 205

GumC

COG3206

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

522-651

3.09e-03

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

Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.77 E-value: 3.09e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422 522 QEKLNLILQKKQQLQMEVKMLSSSKSMKELTEEQQNLQKELEslqnehaqrmeefyveqkDLEKKLEQIMKQKCTCDSNL 601
Cdd:COG3206  151 AAVANALAEAYLEQNLELRREEARKALEFLEEQLPELRKELE------------------EAEAALEEFRQKNGLVDLSE 212

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 223029422 602 EKDKEAEyagQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKEL 651
Cdd:COG3206  213 EAKLLLQ---QLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL 259

PTZ00121

MAEBL; Provisional

504-650

3.41e-03

MAEBL; Provisional

Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 3.41e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422  504 EDDKGKIMEEVMRT-YLKQQEKLNLIlqKKQQLQMevKMLSSSKSMKELTEEQQNLQKELESL--QNEHAQRMEEFYVEQ 580
Cdd:PTZ00121 1636 EQLKKKEAEEKKKAeELKKAEEENKI--KAAEEAK--KAEEDKKKAEEAKKAEEDEKKAAEALkkEAEEAKKAEELKKKE 1711

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 223029422  581 KDLEKKLEQIMKQKCTCDSNLE--KDKEAEYAGQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKE 650
Cdd:PTZ00121 1712 AEEKKKAEELKKAEEENKIKAEeaKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE 1783

PRK03918

DNA double-strand break repair ATPase Rad50;

513-653

3.43e-03

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 3.43e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422 513 EVMRTYLKQQEKLNLILQKKQQLQMEVKMLSSSKSMKELtEEQQNLQKELESLQNEHAQRMEEFYVEQKDLEKKLEQIMK 592
Cdd:PRK03918 355 EELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKEL-EELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKK 433

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 223029422 593 QKCTC-------DSNLEKDKEAEYAGQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKL 653
Cdd:PRK03918 434 AKGKCpvcgrelTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKEL 501

YhaN

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

519-650

3.57e-03

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 3.57e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422 519 LKQQEKLNLILQKKQQLQMEVKM---------LSSSKSMKELTEEQQNLQKELESLQNEHAQRMEEFYVEQkdLEKKLEQ 589
Cdd:COG4717  359 LEEELQLEELEQEIAALLAEAGVedeeelraaLEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEE--LEEELEE 436

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 223029422 590 IMKQKctcdSNLEKDKEAEYAgQLAELRQRLDHAEADRqELQDELRQEREARQKLEMMIKE 650
Cdd:COG4717  437 LEEEL----EELEEELEELRE-ELAELEAELEQLEEDG-ELAELLQELEELKAELRELAEE 491

DUF4659

pfam15558

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...

519-650

4.16e-03

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.

Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 40.02 E-value: 4.16e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422  519 LKQQEKLNLILQKKQ----QLQMEVKMLSSSKSMKELT----------EEQQNLQKELES----LQNEHAQRMEEFYVEQ 580
Cdd:pfam15558 145 LQLQERLEEACHKRQlkerEEQKKVQENNLSELLNHQArkvlvdcqakAEELLRRLSLEQslqrSQENYEQLVEERHREL 224

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 223029422  581 KDLEKKLE-QIMKQKCTCDSNLEKDKE-AEYAGQLAE--LRQRLDHAEADRQELQDELRQEREARQKLEMMIKE 650
Cdd:pfam15558 225 REKAQKEEeQFQRAKWRAEEKEEERQEhKEALAELADrkIQQARQVAHKTVQDKAQRARELNLEREKNHHILKL 298

mukB

PRK04863

chromosome partition protein MukB;

616-664

4.32e-03

chromosome partition protein MukB;

Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.33 E-value: 4.32e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 223029422  616 LRQRLDHAEADRQELQDELRQ-EREARQKLEMMIKelklqiLKSSKTAKE 664
Cdd:PRK04863  990 LRQRLEQAEQERTRAREQLRQaQAQLAQYNQVLAS------LKSSYDAKR 1033

MukB

COG3096

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...

554-652

4.36e-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: 40.32 E-value: 4.36e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422  554 EQQNLQKELESLQNEHAQrMEEFYVEQKDLEKKLEQIMKQkctcdSNLEKDKEAEYAGQLAELRQRLDHAEADRQELQDE 633
Cdd:COG3096   506 SQQALAQRLQQLRAQLAE-LEQRLRQQQNAERLLEEFCQR-----IGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQ 579

                          90
                  ....*....|....*....
gi 223029422  634 LRQEREARQKLEMMIKELK 652
Cdd:COG3096   580 RSELRQQLEQLRARIKELA 598

Nup88

pfam10168

Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ...

513-658

4.91e-03

Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.

Pssm-ID: 462975 [Multi-domain] Cd Length: 713 Bit Score: 40.03 E-value: 4.91e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422  513 EVMRT-YLKQQE--------KLNLI-LQKKQQLQmevkmlssskSMKELTEEQQNLQKELESLqnehAQRMEEFYVEQKD 582
Cdd:pfam10168 542 QVFREeYLKKHDlareeiqkRVKLLkLQKEQQLQ----------ELQSLEEERKSLSERAEKL----AEKYEEIKDKQEK 607

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422  583 LEKKLEQIMKQKCTCDSNL---EKD--KEAE-YAGQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQIL 656
Cdd:pfam10168 608 LMRRCKKVLQRLNSQLPVLsdaEREmkKELEtINEQLKHLANAIKQAKKKMNYQRYQIAKSQSIRKKSSLSLSEKQRKTI 687


                  ..
gi 223029422  657 KS 658
Cdd:pfam10168 688 KE 689

COG4913

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

520-664

4.93e-03

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

Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 4.93e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422  520 KQQEKLNLILQKKQQLQMEVKMLSSSKSMKELTEEQQNLQKELESLQNEHA------QRMEEFYVEQKDLEKKLEQIMKQ 593
Cdd:COG4913   635 ALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDdlaaleEQLEELEAELEELEEELDELKGE 714

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 223029422  594 KCTCDSNLEKDKEaeyagQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQILKSSKTAKE 664
Cdd:COG4913   715 IGRLEKELEQAEE-----ELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRA 780

PRK11281

mechanosensitive channel MscK;

542-634

4.96e-03

mechanosensitive channel MscK;

Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 40.28 E-value: 4.96e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422  542 LSSSKSMKELTEE----QQNLQKELESLQNehAQRMEEfyvEQKDLEKKLEQIMKQKCTCDSNLE--KDKEAEYAGQ--- 612
Cdd:PRK11281   45 LDALNKQKLLEAEdklvQQDLEQTLALLDK--IDRQKE---ETEQLKQQLAQAPAKLRQAQAELEalKDDNDEETREtls 119

                          90       100
                  ....*....|....*....|....*
gi 223029422  613 ---LAELRQRLDHAEADRQELQDEL 634
Cdd:PRK11281  120 tlsLRQLESRLAQTLDQLQNAQNDL 144

COG4372

Uncharacterized protein, contains DUF3084 domain [Function unknown];

520-664

5.68e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];

Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.50 E-value: 5.68e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422 520 KQQEKLNLILQKKQQLQMEVKMLSssKSMKELTEEQQNLQKELESLQNEHAQRMEEfyveQKDLEKKLEQIMKQKCTCDS 599
Cdd:COG4372   98 QAQEELESLQEEAEELQEELEELQ--KERQDLEQQRKQLEAQIAELQSEIAEREEE----LKELEEQLESLQEELAALEQ 171

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 223029422 600 NLEKDKEAEYAGQLAELRQrldhaEADRQELQDELRQEREARQKLEMMIKELKLQILKSSKTAKE 664
Cdd:COG4372  172 ELQALSEAEAEQALDELLK-----EANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKL 231

DUF5401

pfam17380

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

505-646

5.76e-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: 39.72 E-value: 5.76e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422  505 DDKGKIMEEVMRTYLKQQEKLNLILQKKQQLQMEvkmlssSKSMKELTEEQQNLqKELESLQNEHAQRMEEFYVE----- 579
Cdd:pfam17380 330 DRQAAIYAEQERMAMERERELERIRQEERKRELE------RIRQEEIAMEISRM-RELERLQMERQQKNERVRQEleaar 402

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 223029422  580 -QKDLEKKLEQIMKQKCTCDSNLEKDKEAEYAGQLAELRQ-------RLDHAEADRQELQDELRQERE--ARQKLEM 646
Cdd:pfam17380 403 kVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEeraremeRVRLEEQERQQQVERLRQQEEerKRKKLEL 479

PRK03918

DNA double-strand break repair ATPase Rad50;

549-652

5.77e-03

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 5.77e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422 549 KELTEEQQNLQKELESLQN------EHAQRMEEFYVEQKDLEKKLEQIMKQKctcdSNLEKDKEA--EYAGQLAELRQRL 620
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTENieelikEKEKELEEVLREINEISSELPELREEL----EKLEKEVKEleELKEEIEELEKEL 247

                         90       100       110
                 ....*....|....*....|....*....|..
gi 223029422 621 DHAEADRQELQDELRQEREARQKLEMMIKELK 652
Cdd:PRK03918 248 ESLEGSKRKLEEKIRELEERIEELKKEIEELE 279

SMC_N

pfam02463

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...

518-657

5.86e-03

Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 39.95 E-value: 5.86e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422   518 YLKQQEKLNLILQKKQQLQMEVKMLSSSKSMKELTEEQQNLQKELESLQnehaqrmeefyvEQKDLEKKLEQIMKQKCTC 597
Cdd:pfam02463  231 YLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEK------------EKKLQEEELKLLAKEEEEL 298

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422   598 DSNLEKDKEaeyagQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQILK 657
Cdd:pfam02463  299 KSELLKLER-----RKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREA 353

sbcc

TIGR00618

exonuclease SbcC; All proteins in this family for which functions are known are part of an ...

530-654

6.73e-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: 39.95 E-value: 6.73e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422   530 QKKQQLQMEVKMLSSSKSMKELTEEQQNLQKELESLQNEHAQ---RMEEFYVEQKDL---------EKKLEQIMKQKCTC 597
Cdd:TIGR00618  370 ISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATidtRTSAFRDLQGQLahakkqqelQQRYAELCAAAITC 449

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 223029422   598 DSNLEKDKEAEyagqLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQ 654
Cdd:TIGR00618  450 TAQCEKLEKIH----LQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEE 502

F-BAR_PSTPIP1

cd07671

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine ...

509-650

6.75e-03

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine Phosphatase-Interacting Protein 1; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Proline-Serine-Threonine Phosphatase-Interacting Protein 1 (PSTPIP1), also known as CD2 Binding Protein 1 (CD2BP1), is mainly expressed in hematopoietic cells. It is a binding partner of the cell surface receptor CD2 and PTP-PEST, a tyrosine phosphatase which functions in cell motility and Rac1 regulation. It also plays a role in the activation of the Wiskott-Aldrich syndrome protein (WASP), which couples actin rearrangement and T cell activation. Mutations in the gene encoding PSTPIP1 cause the autoinflammatory disorder known as PAPA (pyogenic sterile arthritis, pyoderma gangrenosum, and acne) syndrome. PSTPIP1 contains an N-terminal F-BAR domain, PEST motifs, and a C-terminal SH3 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.

Pssm-ID: 153355 [Multi-domain] Cd Length: 242 Bit Score: 38.79 E-value: 6.75e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422 509 KIMEEVMRTYLKQQEKLN---LILQKKQQLQMEVKMLSSS-KSMKELTEEQQNLQKELESLQNEHAQRMEEFYVEQKDLE 584
Cdd:cd07671   22 KDVEELLKQRAQAEERYGkelVQIARKAGGQTEINTLKASfDQLKQQIENIGNSHIQLAGMLREELKSLEEFRERQKEQR 101

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 223029422 585 KKLEQIMKQ---------KCTCDSNL---EKDKEAEYAGQLAELRQRLDHaEADRQELQDELRQEREARQKLEMMIKE 650
Cdd:cd07671  102 KKYEAVMERvqkskvslyKKTMESKKtyeQRCREADEAEQTFERSSSTGN-PKQSEKSQNKAKQCRDAATEAERVYKQ 178

SMC_prok_A

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...

509-660

6.80e-03

Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 39.67 E-value: 6.80e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422   509 KIMEEVMRTYLKQQEKLN---------LILQKKQQlQMEVKMLSSSK-----SMKELTEEQQNLQKELESLQ---NEHAQ 571
Cdd:TIGR02169  187 ERLDLIIDEKRQQLERLRrerekaeryQALLKEKR-EYEGYELLKEKealerQKEAIERQLASLEEELEKLTeeiSELEK 265

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422   572 RMEEfyveqkdLEKKLEQIMKQkctcdsnLEKDKEAEYAG---QLAELRQRLDHAEADRQELQDELRQEREARQKLEMMI 648
Cdd:TIGR02169  266 RLEE-------IEQLLEELNKK-------IKDLGEEEQLRvkeKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEI 331

                          170
                   ....*....|..
gi 223029422   649 KELKLQILKSSK 660
Cdd:TIGR02169  332 DKLLAEIEELER 343

MukB

COG3096

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...

515-655

6.85e-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: 39.94 E-value: 6.85e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422  515 MRTYLKQQEKLNLILQKKQQLQMEVKMLSSSKS-----MKELtEEQQNLQKELES-LQ--NEHAQRMEEFYVEQKDLEKk 586
Cdd:COG3096   274 MRHANERRELSERALELRRELFGARRQLAEEQYrlvemAREL-EELSARESDLEQdYQaaSDHLNLVQTALRQQEKIER- 351

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 223029422  587 leqimkqkctcdsnlekdkeaeYAGQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 655
Cdd:COG3096   352 ----------------------YQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQL 398

PspA_IM30

pfam04012

PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...

549-663

6.89e-03

PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.

Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 38.51 E-value: 6.89e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422  549 KELTEEQQNLQKELESLQNEHAQRMEEFYVEQKDLEKKLEQIMKQKCTCDSNLEKDKEaEYAGQLAELRQRLDHAEADRQ 628
Cdd:pfam04012  25 KMLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGNE-ELAREALAEKKSLEKQAEALE 103

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 223029422  629 ELQDELR----QEREARQKLEMMIKEL--KLQILKS-SKTAK 663
Cdd:pfam04012 104 TQLAQQRsaveQLRKQLAALETKIQQLkaKKNLLKArLKAAK 145

HEC1

COG5185

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...

462-655

7.03e-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: 39.56 E-value: 7.03e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422 462 NNSTSKRKSESATCNLVRDINKVGIGLVAAASSpllvKDVICEDDKgKIMEEVMRTYLKQQEKLNLILQKKQQLQMEVKM 541
Cdd:COG5185  173 NQNLKKLEIFGLTLGLLKGISELKKAEPSGTVN----SIKESETGN-LGSESTLLEKAKEIINIEEALKGFQDPESELED 247

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422 542 LSS-SKSMKELTEEQQNLQKELESLQNEHAQRMEEFYVEQK----DLEKKLEQIMKQKCTCDSNLEKDKEAEYAGQLAEL 616
Cdd:COG5185  248 LAQtSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIkqfeNTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQEL 327

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 223029422 617 RQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 655
Cdd:COG5185  328 EESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENI 366

tolA

PRK09510

cell envelope integrity inner membrane protein TolA; Provisional

506-645

7.65e-03

cell envelope integrity inner membrane protein TolA; Provisional

Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 39.02 E-value: 7.65e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422 506 DKGKIMEEvmrtYLKQQEKLNLILQKKQQLQMEVKMLSSSKSMKELTEEQQNLQKELESLQNEHAQRMEEFYVEQKDLEK 585
Cdd:PRK09510  56 DPGAVVEQ----YNRQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQ 131

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 223029422 586 KLEQIMKQKCTCDSNLEKDKE----AEYAGQLAELRQRLDHAEADRQelqdelrQEREARQKLE 645
Cdd:PRK09510 132 KQAEEAAAKAAAAAKAKAEAEakraAAAAKKAAAEAKKKAEAEAAKK-------AAAEAKKKAE 188

DUF4472

pfam14739

Domain of unknown function (DUF4472); This family is specific to the Chordates. Some members ...

554-652

8.12e-03

Domain of unknown function (DUF4472); This family is specific to the Chordates. Some members also carry Kinesin-motor domains at their N-terminus, Kinesin, pfam00225.

Pssm-ID: 464291 [Multi-domain] Cd Length: 107 Bit Score: 36.51 E-value: 8.12e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422  554 EQQNLQ--KELESLQNEHAQRMEEFYVEQKDLEKKLeqimkqkctcdSNLEkdkeaeyaGQLAELRQRLDHAEADRQELQ 631
Cdd:pfam14739   2 EEEKLQisKALVDLQIENNKLREQYEAEKFELKNKL-----------LNLE--------NRVLELELRLEKAAEEIQDLR 62

                          90       100
                  ....*....|....*....|.
gi 223029422  632 DELRQEREARQKLEMMIKELK 652
Cdd:pfam14739  63 ERLRELEDDRRELAEEFVALK 83

PHA02562

endonuclease subunit; Provisional

535-634

8.37e-03

endonuclease subunit; Provisional

Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 39.23 E-value: 8.37e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422 535 LQMEVKMLSSSK-SMKELTEEQQNLQKELESLQNEHAQRMEEFYVEQKDLEKKLEQIMKQKCTCDSNLEKDKEaEYAGQL 613
Cdd:PHA02562 179 LNQQIQTLDMKIdHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIE-DPSAAL 257

                         90       100
                 ....*....|....*....|.
gi 223029422 614 AELRQRLDHAEADRQELQDEL 634
Cdd:PHA02562 258 NKLNTAAAKIKSKIEQFQKVI 278

PRK02224

DNA double-strand break repair Rad50 ATPase;

549-645

8.47e-03

DNA double-strand break repair Rad50 ATPase;

Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.25 E-value: 8.47e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422 549 KELTEEQQNLQKELESLQNEHAQRMEEfyveQKDLEKKLEQIMKQKCTCDSNLEK--DKEAEYAGQLAELRQRLDHAEAD 626
Cdd:PRK02224 359 EELREEAAELESELEEAREAVEDRREE----IEELEEEIEELRERFGDAPVDLGNaeDFLEELREERDELREREAELEAT 434

                         90
                 ....*....|....*....
gi 223029422 627 RQELQDELrqeREARQKLE 645
Cdd:PRK02224 435 LRTARERV---EEAEALLE 450

HEC1

COG5185

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...

395-645

8.78e-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: 39.17 E-value: 8.78e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422 395 LTSAVSQSKELTKTEASKSISRQSEKAHSSGKLQKTVS--YPDVSLEEQEKMDLKTSRELCSRLDASISNNS--TSKRKS 470
Cdd:COG5185  255 LEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFEntKEKIAEYTKSIDIKKATESLEEQLAAAEAEQEleESKRET 334

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422 471 ESATCNLVRDINKVGIGLVAAASSPLLVKDVICEDDKGKIMEEVMRTYLKQQEKLNL-ILQKKQQLQMEVKMLSS--SKS 547
Cdd:COG5185  335 ETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEELDSFKDTIESTKEsLDEIPQNQRGYAQEILAtlEDT 414

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422 548 MKELTEEQQNLQKELESLQNEhaqrMEEFYVEQKDLEKKLEQIMKQKctcDSNLEKDKEAEYAGQLAELRQRLDHAEADR 627
Cdd:COG5185  415 LKAADRQIEELQRQIEQATSS----NEEVSKLLNELISELNKVMREA---DEESQSRLEEAYDEINRSVRSKKEDLNEEL 487

                        250
                 ....*....|....*...
gi 223029422 628 QELQDELRQEREARQKLE 645
Cdd:COG5185  488 TQIESRVSTLKATLEKLR 505

EnvC

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...

509-593

8.92e-03

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

Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 38.98 E-value: 8.92e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029422 509 KIMEEVMRTYLKQQEKLNLILQKKQQLQ-MEVKMLSSSKSMKELTEEQQNLQKELESLQNEHAQRMEEFYVEQKDLEKKL 587
Cdd:COG4942  150 EQAEELRADLAELAALRAELEAERAELEaLLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229


                 ....*.
gi 223029422 588 EQIMKQ 593
Cdd:COG4942  230 ARLEAE 235

EnvC