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Conserved domains on  [gi|67476728|sp|P42566|]
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RecName: Full=Epidermal growth factor receptor substrate 15; Short=Protein Eps15; AltName: Full=Protein AF-1p

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
 121-215 3.11e-43

Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe (NPF) sequences.


:

Pssm-ID: 197477 [Multi-domain]  Cd Length: 96  Bit Score: 151.66  E-value: 3.11e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    121 PWAVKPEDKAKYDAIFDSLSP-VNGFLSGDKVKPVLLNSKLPVDILGRVWELSDIDHDGMLDRDEFAVAMFLVYCALEKE 199
Cdd:smart00027   1 PWAISPEDKAKYEQIFRSLDKnQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGY 80

                           90
                   ....*....|....*.
gi 67476728    200 PVPMSLPPALVPPSKR 215
Cdd:smart00027  81 PIPASLPPSLIPPSKR 96
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
 218-313 2.07e-41

Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe (NPF) sequences.


:

Pssm-ID: 197477 [Multi-domain]  Cd Length: 96  Bit Score: 146.65  E-value: 2.07e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    218 WVVSPAEKAKYDEIFLKTDKDMDGFVSGLEVREIFLKTGLPSTLLAHIWSLCDTKDCGKLSKDQFALAFHLISQKLIkGI 297
Cdd:smart00027   2 WAISPEDKAKYEQIFRSLDKNQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLN-GY 80

                           90
                   ....*....|....*.
gi 67476728    298 DPPHVLTPEMIPPSDR 313
Cdd:smart00027  81 PIPASLPPSLIPPSKR 96
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
 13-103 3.46e-28

Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe (NPF) sequences.


:

Pssm-ID: 197477 [Multi-domain]  Cd Length: 96  Bit Score: 108.90  E-value: 3.46e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728     13 SSGNPVYEKYYRQVDTGNTGRVLASDAAAFLKKSGLPDLILGKIWDLADTDGKGILNKQEFFVALRLVACAQNGLEVSLS 92
Cdd:smart00027   6 PEDKAKYEQIFRSLDKNQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGYPIPAS 85

                           90
                   ....*....|.
gi 67476728     93 SLNLAVPPPRF 103
Cdd:smart00027  86 LPPSLIPPSKR 96
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
330-493 9.30e-17

Uncharacterized protein, contains DUF3084 domain [Function unknown];


:

Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 83.03  E-value: 9.30e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 330 SAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLE 409
Cdd:COG4372  35 KALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQ 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 410 EQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQL--EPLQQHLQDSQQ 487
Cdd:COG4372 115 EELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEaeQALDELLKEANR 194


                ....*.
gi 67476728 488 EISSMQ 493
Cdd:COG4372 195 NAEKEE 200
 
Name Accession Description Interval E-value
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
 121-215 3.11e-43

Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe (NPF) sequences.


Pssm-ID: 197477 [Multi-domain]  Cd Length: 96  Bit Score: 151.66  E-value: 3.11e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    121 PWAVKPEDKAKYDAIFDSLSP-VNGFLSGDKVKPVLLNSKLPVDILGRVWELSDIDHDGMLDRDEFAVAMFLVYCALEKE 199
Cdd:smart00027   1 PWAISPEDKAKYEQIFRSLDKnQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGY 80

                           90
                   ....*....|....*.
gi 67476728    200 PVPMSLPPALVPPSKR 215
Cdd:smart00027  81 PIPASLPPSLIPPSKR 96
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
 218-313 2.07e-41

Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe (NPF) sequences.


Pssm-ID: 197477 [Multi-domain]  Cd Length: 96  Bit Score: 146.65  E-value: 2.07e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    218 WVVSPAEKAKYDEIFLKTDKDMDGFVSGLEVREIFLKTGLPSTLLAHIWSLCDTKDCGKLSKDQFALAFHLISQKLIkGI 297
Cdd:smart00027   2 WAISPEDKAKYEQIFRSLDKNQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLN-GY 80

                           90
                   ....*....|....*.
gi 67476728    298 DPPHVLTPEMIPPSDR 313
Cdd:smart00027  81 PIPASLPPSLIPPSKR 96
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
 13-103 3.46e-28

Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe (NPF) sequences.


Pssm-ID: 197477 [Multi-domain]  Cd Length: 96  Bit Score: 108.90  E-value: 3.46e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728     13 SSGNPVYEKYYRQVDTGNTGRVLASDAAAFLKKSGLPDLILGKIWDLADTDGKGILNKQEFFVALRLVACAQNGLEVSLS 92
Cdd:smart00027   6 PEDKAKYEQIFRSLDKNQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGYPIPAS 85

                           90
                   ....*....|.
gi 67476728     93 SLNLAVPPPRF 103
Cdd:smart00027  86 LPPSLIPPSKR 96
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
 228-293 1.56e-26

Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and signal transduction. The alignment contains a pair of EF-hand motifs, typically one of them is canonical and binds to Ca2+, while the other may not bind to Ca2+. A hydrophobic binding pocket is formed by residues from both EF-hand motifs. The EH domain binds to proteins containing NPF (class I), [WF]W or SWG (class II), or H[TS]F (class III) sequence motifs.


Pssm-ID: 238009 [Multi-domain]  Cd Length: 67  Bit Score: 103.07  E-value: 1.56e-26
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 67476728 228 YDEIFLKTDKDMDGFVSGLEVREIFLKTGLPSTLLAHIWSLCDTKDCGKLSKDQFALAFHLISQKL 293
Cdd:cd00052   1 YDQIFRSLDPDGDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALAL 66
EF-hand_4 pfam12763
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ...
 121-215 2.45e-26

Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin cytoskeleton-regulatory complex END3 and similar proteins from fungi and closely related species.


Pssm-ID: 289529  Cd Length: 104  Bit Score: 103.99  E-value: 2.45e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   121 PWAVKpedkaKYDAIFDSLSPVNGFLSGDKVKPVLLNSKLPVDILGRVWELSDIDHDGMLDRDEFAVAMFLVYCALEKE- 199
Cdd:pfam12763   6 EWEIK-----KYWEIFSGLKPENNKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLIFDLVNGNi 80

                          90
                  ....*....|....*..
gi 67476728   200 -PVPMSLPPALVPPSKR 215
Cdd:pfam12763  81 aDVPDELPDWLVPGSKA 97
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
 132-197 5.76e-25

Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and signal transduction. The alignment contains a pair of EF-hand motifs, typically one of them is canonical and binds to Ca2+, while the other may not bind to Ca2+. A hydrophobic binding pocket is formed by residues from both EF-hand motifs. The EH domain binds to proteins containing NPF (class I), [WF]W or SWG (class II), or H[TS]F (class III) sequence motifs.


Pssm-ID: 238009 [Multi-domain]  Cd Length: 67  Bit Score: 98.45  E-value: 5.76e-25
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 67476728 132 YDAIFDSLSPVN-GFLSGDKVKPVLLNSKLPVDILGRVWELSDIDHDGMLDRDEFAVAMFLVYCALE 197
Cdd:cd00052   1 YDQIFRSLDPDGdGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
 19-85 2.48e-24

Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and signal transduction. The alignment contains a pair of EF-hand motifs, typically one of them is canonical and binds to Ca2+, while the other may not bind to Ca2+. A hydrophobic binding pocket is formed by residues from both EF-hand motifs. The EH domain binds to proteins containing NPF (class I), [WF]W or SWG (class II), or H[TS]F (class III) sequence motifs.


Pssm-ID: 238009 [Multi-domain]  Cd Length: 67  Bit Score: 96.91  E-value: 2.48e-24
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 67476728  19 YEKYYRQVDTGNTGRVLASDAAAFLKKSGLPDLILGKIWDLADTDGKGILNKQEFFVALRLVACAQN 85
Cdd:cd00052   1 YDQIFRSLDPDGDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
330-493 9.30e-17

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 83.03  E-value: 9.30e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 330 SAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLE 409
Cdd:COG4372  35 KALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQ 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 410 EQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQL--EPLQQHLQDSQQ 487
Cdd:COG4372 115 EELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEaeQALDELLKEANR 194


                ....*.
gi 67476728 488 EISSMQ 493
Cdd:COG4372 195 NAEKEE 200
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 333-510 1.91e-14

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: 77.75  E-value: 1.91e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   333 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQL 412
Cdd:TIGR04523 335 KIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQI 414

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   413 KEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSm 492
Cdd:TIGR04523 415 KKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKS- 493

                         170
                  ....*....|....*...
gi 67476728   493 qmKLMEMKDLENHNSQLN 510
Cdd:TIGR04523 494 --KEKELKKLNEEKKELE 509
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 355-509 5.67e-12

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


Pssm-ID: 462536 [Multi-domain]  Cd Length: 176  Bit Score: 64.95  E-value: 5.67e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   355 DLKEKEDTIKQRTsevQDLQDEVQRE-NTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAEL 433
Cdd:pfam08614  11 RLLDRTALLEAEN---AKLQSEPESVlPSTSSSKLSKASPQSASIQSLEQLLAQLREELAELYRSRGELAQRLVDLNEEL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   434 TSQESQISTYEEELAKAREELSRLQQETAELEESVEsGKAQLeplqqhLQDSQQEISSMQMKL--ME--MKDLENHNSQL 509
Cdd:pfam08614  88 QELEKKLREDERRLAALEAERAQLEEKLKDREEELR-EKRKL------NQDLQDELVALQLQLnmAEekLRKLEKENREL 160
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
330-503 5.10e-11

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 66.63  E-value: 5.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728  330 SAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRT-SEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKaQL 408
Cdd:PRK03918 546 KELEKLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEPFYNEYLELKDAEKELEREEKELK-KL 624

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728  409 EEQLKEVRKKCAEEAQLISSLKAELTSQESQIStyEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQE 488
Cdd:PRK03918 625 EEELDKAFEELAETEKRLEELRKELEELEKKYS--EEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEE 702

                        170
                 ....*....|....*
gi 67476728  489 ISSMQMKLMEMKDLE 503
Cdd:PRK03918 703 LEEREKAKKELEKLE 717
EF-hand_4 pfam12763
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ...
 32-80 2.89e-07

Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin cytoskeleton-regulatory complex END3 and similar proteins from fungi and closely related species.


Pssm-ID: 289529  Cd Length: 104  Bit Score: 49.68  E-value: 2.89e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 67476728    32 GRVLASDAAAFLKKSGLPDLILGKIWDLADTDGKGILNKQEFFVALRLV 80
Cdd:pfam12763  24 NKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLI 72
EF-hand_4 pfam12763
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ...
 222-319 6.96e-06

Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin cytoskeleton-regulatory complex END3 and similar proteins from fungi and closely related species.


Pssm-ID: 289529  Cd Length: 104  Bit Score: 45.44  E-value: 6.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   222 PAEKAKYDEIFlKTDKDMDGFVSGLEVREIFLKTGLPSTLLAHIWSLCDTKDCGKLSKDQFALAFHLISQkLIKGI--DP 299
Cdd:pfam12763   6 EWEIKKYWEIF-SGLKPENNKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLIFD-LVNGNiaDV 83

                          90       100
                  ....*....|....*....|
gi 67476728   300 PHVLTPEMIPPSDRASLQKN 319
Cdd:pfam12763  84 PDELPDWLVPGSKAHLIQAN 103
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
165-287 1.39e-04

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 42.86  E-value: 1.39e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 165 LGRVWELSDIDHDGMLDRDEFAvAMFLVYCALEKEPVPmSLPPALVPPSKRKTWVVSPAEK---AKYDEIFLKTDKDMDG 241
Cdd:COG5126   7 LDRRFDLLDADGDGVLERDDFE-ALFRRLWATLFSEAD-TDGDGRISREEFVAGMESLFEAtvePFARAAFDLLDTDGDG 84

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 67476728 242 FVSGLEVREIFLKTGLPSTLLAHIWSLCDTKDCGKLSKDQFALAFH 287
Cdd:COG5126  85 KISADEFRRLLTALGVSEEEADELFARLDTDGDGKISFEEFVAAVR 130
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 340-499 1.48e-04

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 43.97  E-value: 1.48e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 340 NEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQV-QELLDELDEQKAQLEEQLKEVRK- 417
Cdd:cd00176  33 ESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLEELNQRwEELRELAEERRQRLEEALDLQQFf 112

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 418 -KCAEEAQLISSLKAELTSQE------------SQISTYEEELAKAREELSRLQQETAELEESVESG-----KAQLEPLQ 479
Cdd:cd00176 113 rDADDLEQWLEEKEAALASEDlgkdlesveellKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDadeeiEEKLEELN 192

                       170       180
                ....*....|....*....|
gi 67476728 480 QHLQDSQQEISSMQMKLMEM 499
Cdd:cd00176 193 ERWEELLELAEERQKKLEEA 212
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 396-505 3.32e-04

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 43.85  E-value: 3.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    396 ELLDELDEQKAQL---EEQLKEVRKKCAEEAQLISSLKAELTSQESQISTY-EEELAKAREELSRLQQE-------TAEL 464
Cdd:smart00787 151 ENLEGLKEDYKLLmkeLELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCdPTELDRAKEKLKKLLQEimikvkkLEEL 230

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 67476728    465 EESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKDLENH 505
Cdd:smart00787 231 EEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGFTFK 271
growth_prot_Scy NF041483
polarized growth protein Scy;
356-493 1.12e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 42.89  E-value: 1.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   356 LKEKEDTIKQR-TSEVQDLQDEVQRENTNLQKLQAqkqqvqELLDEL----DEQKAQLEEQLKEVRKKCAEEAqliSSLK 430
Cdd:NF041483 1119 IRERAEELRDRiTGEIEELHERARRESAEQMKSAG------ERCDALvkaaEEQLAEAEAKAKELVSDANSEA---SKVR 1189

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 67476728   431 -AELTSQESQISTYEEELAKAREELSRLQQET-AELEESVESGKAQLEPLQQHLQDSQQEISSMQ 493
Cdd:NF041483 1190 iAAVKKAEGLLKEAEQKKAELVREAEKIKAEAeAEAKRTVEEGKRELDVLVRRREDINAEISRVQ 1254
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
53-189 1.35e-03

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 39.78  E-value: 1.35e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728  53 LGKIWDLADTDGKGILNKQEFfVALRLVACAQNGLEvslsslnlavppprfHDTSSPLLISGTSAAELPWAVKPED-KAK 131
Cdd:COG5126   7 LDRRFDLLDADGDGVLERDDF-EALFRRLWATLFSE---------------ADTDGDGRISREEFVAGMESLFEATvEPF 70

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 67476728 132 YDAIFDSLSP-VNGFLSGDKVKPVLLNSKLPVDILGRVWELSDIDHDGMLDRDEFAVAM 189
Cdd:COG5126  71 ARAAFDLLDTdGDGKISADEFRRLLTALGVSEEEADELFARLDTDGDGKISFEEFVAAV 129
growth_prot_Scy NF041483
polarized growth protein Scy;
357-480 4.96e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 40.58  E-value: 4.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   357 KEKEDTIKQRTSEVQDLQDEVQREntnlqklqaqkqqVQELLDELDEQKAQL-EEQLKEVRKKCAEEAQLISSLKAElts 435
Cdd:NF041483  520 RQAEETLERTRAEAERLRAEAEEQ-------------AEEVRAAAERAARELrEETERAIAARQAEAAEELTRLHTE--- 583

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 67476728   436 QESQISTYEEELAKAREELSRLQQETAELEESVESGKAQ-LEPLQQ 480
Cdd:NF041483  584 AEERLTAAEEALADARAEAERIRREAAEETERLRTEAAErIRTLQA 629
 
Name Accession Description Interval E-value
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
 121-215 3.11e-43

Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe (NPF) sequences.


Pssm-ID: 197477 [Multi-domain]  Cd Length: 96  Bit Score: 151.66  E-value: 3.11e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    121 PWAVKPEDKAKYDAIFDSLSP-VNGFLSGDKVKPVLLNSKLPVDILGRVWELSDIDHDGMLDRDEFAVAMFLVYCALEKE 199
Cdd:smart00027   1 PWAISPEDKAKYEQIFRSLDKnQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGY 80

                           90
                   ....*....|....*.
gi 67476728    200 PVPMSLPPALVPPSKR 215
Cdd:smart00027  81 PIPASLPPSLIPPSKR 96
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
 218-313 2.07e-41

Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe (NPF) sequences.


Pssm-ID: 197477 [Multi-domain]  Cd Length: 96  Bit Score: 146.65  E-value: 2.07e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    218 WVVSPAEKAKYDEIFLKTDKDMDGFVSGLEVREIFLKTGLPSTLLAHIWSLCDTKDCGKLSKDQFALAFHLISQKLIkGI 297
Cdd:smart00027   2 WAISPEDKAKYEQIFRSLDKNQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLN-GY 80

                           90
                   ....*....|....*.
gi 67476728    298 DPPHVLTPEMIPPSDR 313
Cdd:smart00027  81 PIPASLPPSLIPPSKR 96
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
 13-103 3.46e-28

Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe (NPF) sequences.


Pssm-ID: 197477 [Multi-domain]  Cd Length: 96  Bit Score: 108.90  E-value: 3.46e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728     13 SSGNPVYEKYYRQVDTGNTGRVLASDAAAFLKKSGLPDLILGKIWDLADTDGKGILNKQEFFVALRLVACAQNGLEVSLS 92
Cdd:smart00027   6 PEDKAKYEQIFRSLDKNQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGYPIPAS 85

                           90
                   ....*....|.
gi 67476728     93 SLNLAVPPPRF 103
Cdd:smart00027  86 LPPSLIPPSKR 96
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
 228-293 1.56e-26

Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and signal transduction. The alignment contains a pair of EF-hand motifs, typically one of them is canonical and binds to Ca2+, while the other may not bind to Ca2+. A hydrophobic binding pocket is formed by residues from both EF-hand motifs. The EH domain binds to proteins containing NPF (class I), [WF]W or SWG (class II), or H[TS]F (class III) sequence motifs.


Pssm-ID: 238009 [Multi-domain]  Cd Length: 67  Bit Score: 103.07  E-value: 1.56e-26
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 67476728 228 YDEIFLKTDKDMDGFVSGLEVREIFLKTGLPSTLLAHIWSLCDTKDCGKLSKDQFALAFHLISQKL 293
Cdd:cd00052   1 YDQIFRSLDPDGDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALAL 66
EF-hand_4 pfam12763
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ...
 121-215 2.45e-26

Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin cytoskeleton-regulatory complex END3 and similar proteins from fungi and closely related species.


Pssm-ID: 289529  Cd Length: 104  Bit Score: 103.99  E-value: 2.45e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   121 PWAVKpedkaKYDAIFDSLSPVNGFLSGDKVKPVLLNSKLPVDILGRVWELSDIDHDGMLDRDEFAVAMFLVYCALEKE- 199
Cdd:pfam12763   6 EWEIK-----KYWEIFSGLKPENNKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLIFDLVNGNi 80

                          90
                  ....*....|....*..
gi 67476728   200 -PVPMSLPPALVPPSKR 215
Cdd:pfam12763  81 aDVPDELPDWLVPGSKA 97
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
 132-197 5.76e-25

Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and signal transduction. The alignment contains a pair of EF-hand motifs, typically one of them is canonical and binds to Ca2+, while the other may not bind to Ca2+. A hydrophobic binding pocket is formed by residues from both EF-hand motifs. The EH domain binds to proteins containing NPF (class I), [WF]W or SWG (class II), or H[TS]F (class III) sequence motifs.


Pssm-ID: 238009 [Multi-domain]  Cd Length: 67  Bit Score: 98.45  E-value: 5.76e-25
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 67476728 132 YDAIFDSLSPVN-GFLSGDKVKPVLLNSKLPVDILGRVWELSDIDHDGMLDRDEFAVAMFLVYCALE 197
Cdd:cd00052   1 YDQIFRSLDPDGdGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
 19-85 2.48e-24

Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and signal transduction. The alignment contains a pair of EF-hand motifs, typically one of them is canonical and binds to Ca2+, while the other may not bind to Ca2+. A hydrophobic binding pocket is formed by residues from both EF-hand motifs. The EH domain binds to proteins containing NPF (class I), [WF]W or SWG (class II), or H[TS]F (class III) sequence motifs.


Pssm-ID: 238009 [Multi-domain]  Cd Length: 67  Bit Score: 96.91  E-value: 2.48e-24
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 67476728  19 YEKYYRQVDTGNTGRVLASDAAAFLKKSGLPDLILGKIWDLADTDGKGILNKQEFFVALRLVACAQN 85
Cdd:cd00052   1 YDQIFRSLDPDGDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
330-493 9.30e-17

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 83.03  E-value: 9.30e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 330 SAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLE 409
Cdd:COG4372  35 KALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQ 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 410 EQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQL--EPLQQHLQDSQQ 487
Cdd:COG4372 115 EELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEaeQALDELLKEANR 194


                ....*.
gi 67476728 488 EISSMQ 493
Cdd:COG4372 195 NAEKEE 200
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 333-489 6.43e-16

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: 78.04  E-value: 6.43e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 333 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNlqklqaqkqqvqelLDELDEQKAQLEEQL 412
Cdd:COG1579  17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELE--------------IEEVEARIKKYEEQL 82

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 67476728 413 KEVRKkcAEEAQlisSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEI 489
Cdd:COG1579  83 GNVRN--NKEYE---ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAEL 154
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 333-509 5.27e-15

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 79.60  E-value: 5.27e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 333 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQL 412
Cdd:COG1196 246 AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEEL 325

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 413 KEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGK-AQLEPLQQHLQDSQQEISS 491
Cdd:COG1196 326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAeELLEALRAAAELAAQLEEL 405

                       170
                ....*....|....*...
gi 67476728 492 MQMKLMEMKDLENHNSQL 509
Cdd:COG1196 406 EEAEEALLERLERLEEEL 423
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 333-510 1.91e-14

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: 77.75  E-value: 1.91e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   333 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQL 412
Cdd:TIGR04523 335 KIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQI 414

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   413 KEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSm 492
Cdd:TIGR04523 415 KKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKS- 493

                         170
                  ....*....|....*...
gi 67476728   493 qmKLMEMKDLENHNSQLN 510
Cdd:TIGR04523 494 --KEKELKKLNEEKKELE 509
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 334-498 4.54e-14

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: 76.63  E-value: 4.54e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    334 ELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLK 413
Cdd:TIGR02168  268 KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLE 347

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    414 EVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQ 493
Cdd:TIGR02168  348 ELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELL 427


                   ....*
gi 67476728    494 MKLME 498
Cdd:TIGR02168  428 KKLEE 432
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
324-493 1.42e-13

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 74.95  E-value: 1.42e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728  324 SPVADFSAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLqklqaqkqqvqelLDELDE 403
Cdd:COG4913  279 AALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDR-------------LEQLER 345

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728  404 QKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQistYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQ 483
Cdd:COG4913  346 EIERLERELEERERRRARLEALLAALGLPLPASAEE---FAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELR 422

                        170
                 ....*....|
gi 67476728  484 DSQQEISSMQ 493
Cdd:COG4913  423 ELEAEIASLE 432
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 334-501 2.14e-13

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: 74.71  E-value: 2.14e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    334 ELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLK 413
Cdd:TIGR02168  776 ELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIE 855

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    414 EVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQ 493
Cdd:TIGR02168  856 SLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLE 935


                   ....*...
gi 67476728    494 MKLMEMKD 501
Cdd:TIGR02168  936 VRIDNLQE 943
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 329-508 5.40e-13

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: 73.17  E-value: 5.40e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    329 FSAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQL 408
Cdd:TIGR02168  291 YALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL 370

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    409 EEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGK-----AQLEPLQQHLQ 483
Cdd:TIGR02168  371 ESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAElkelqAELEELEEELE 450

                          170       180
                   ....*....|....*....|....*
gi 67476728    484 DSQQEISSMQMKLMEMKDLENHNSQ 508
Cdd:TIGR02168  451 ELQEELERLEEALEELREELEEAEQ 475
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 333-510 8.23e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 72.66  E-value: 8.23e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 333 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENtnlqklqaqkqqvqELLDELDEQKAQLEEQL 412
Cdd:COG1196 239 AELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQ--------------AEEYELLAELARLEQDI 304

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 413 KEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSM 492
Cdd:COG1196 305 ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384

                       170
                ....*....|....*....
gi 67476728 493 QMKLME-MKDLENHNSQLN 510
Cdd:COG1196 385 AEELLEaLRAAAELAAQLE 403
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 333-501 8.77e-13

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 72.40  E-value: 8.77e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    333 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENtnlqklqAQKQQVQELLDELDEQKAQLEEQL 412
Cdd:TIGR02168  705 KELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS-------KELTELEAEIEELEERLEEAEEEL 777

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    413 KEVRKKCAEEAQLISSLKAELTSQESQISTYEEEL-------AKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDS 485
Cdd:TIGR02168  778 AEAEAEIEELEAQIEQLKEELKALREALDELRAELtllneeaANLRERLESLERRIAATERRLEDLEEQIEELSEDIESL 857

                          170
                   ....*....|....*.
gi 67476728    486 QQEISSMQMKLMEMKD 501
Cdd:TIGR02168  858 AAEIEELEELIEELES 873
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 332-510 1.76e-12

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: 71.20  E-value: 1.76e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   332 IKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQ-------DLQDEVQRENTNLQKLQAQKQQVQELLDELDEQ 404
Cdd:TIGR04523 210 IQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISntqtqlnQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQ 289

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   405 KAQLEEQLKEVRKKcaEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQD 484
Cdd:TIGR04523 290 LNQLKSEISDLNNQ--KEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEE 367

                         170       180       190
                  ....*....|....*....|....*....|
gi 67476728   485 SQQEISSM----QMKLMEMKDLENHNSQLN 510
Cdd:TIGR04523 368 KQNEIEKLkkenQSYKQEIKNLESQINDLE 397
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 330-510 3.42e-12

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 70.47  E-value: 3.42e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    330 SAIKELDTLNNEIVDLQREKNNVEQDLKEKE---DTIKQRTSEVQDLQDEVQRENTNLQklqaqkqqvqELLDELDEQKA 406
Cdd:TIGR02168  236 ELREELEELQEELKEAEEELEELTAELQELEeklEELRLEVSELEEEIEELQKELYALA----------NEISRLEQQKQ 305

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    407 QLEEQLKEVRKKcaeeaqlISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQ 486
Cdd:TIGR02168  306 ILRERLANLERQ-------LEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELE 378

                          170       180
                   ....*....|....*....|....*
gi 67476728    487 QEISSMQMKLMEMK-DLENHNSQLN 510
Cdd:TIGR02168  379 EQLETLRSKVAQLElQIASLNNEIE 403
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 355-509 5.67e-12

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


Pssm-ID: 462536 [Multi-domain]  Cd Length: 176  Bit Score: 64.95  E-value: 5.67e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   355 DLKEKEDTIKQRTsevQDLQDEVQRE-NTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAEL 433
Cdd:pfam08614  11 RLLDRTALLEAEN---AKLQSEPESVlPSTSSSKLSKASPQSASIQSLEQLLAQLREELAELYRSRGELAQRLVDLNEEL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   434 TSQESQISTYEEELAKAREELSRLQQETAELEESVEsGKAQLeplqqhLQDSQQEISSMQMKL--ME--MKDLENHNSQL 509
Cdd:pfam08614  88 QELEKKLREDERRLAALEAERAQLEEKLKDREEELR-EKRKL------NQDLQDELVALQLQLnmAEekLRKLEKENREL 160
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 310-469 6.85e-12

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: 66.10  E-value: 6.85e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 310 PSDRASLQKNIIGsspvadfsAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTS---------EVQDLQDEvqre 380
Cdd:COG1579  30 PAELAELEDELAA--------LEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlgnvrnnkEYEALQKE---- 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 381 ntnlqklqaqkqqvqelLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQIST----YEEELAKAREELSR 456
Cdd:COG1579  98 -----------------IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEkkaeLDEELAELEAELEE 160

                       170
                ....*....|...
gi 67476728 457 LQQETAELEESVE 469
Cdd:COG1579 161 LEAEREELAAKIP 173
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
331-474 7.40e-12

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 69.03  E-value: 7.40e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 331 AIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRT--SEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQL 408
Cdd:COG4717  93 LQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEERLEELRELEEELEELEAEL 172

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 409 EE---QLKEVRKKCAEEA-QLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQ 474
Cdd:COG4717 173 AElqeELEELLEQLSLATeEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
342-501 9.66e-12

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 67.62  E-value: 9.66e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 342 IVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNlqklqaqkqqvqelLDELDEQKAQLEEQLKEVRKKcae 421
Cdd:COG4372  26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEE--------------LEQARSELEQLEEELEELNEQ--- 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 422 eaqlISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKD 501
Cdd:COG4372  89 ----LQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQE 164
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 331-508 1.00e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 69.20  E-value: 1.00e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 331 AIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEE 410
Cdd:COG1196 230 LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE 309

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 411 QLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEIS 490
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389

                       170
                ....*....|....*...
gi 67476728 491 SMQMKLMEMKDLENHNSQ 508
Cdd:COG1196 390 EALRAAAELAAQLEELEE 407
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 327-489 1.17e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 68.81  E-value: 1.17e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 327 ADFSAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKA 406
Cdd:COG1196 289 EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 407 QLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQ 486
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448


                ...
gi 67476728 487 QEI 489
Cdd:COG1196 449 EEE 451
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 329-510 1.90e-11

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: 68.17  E-value: 1.90e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    329 FSAIKELDTLNNEIVDLQREKnnveQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLqaqkqqvqelLDELDEQKAQL 408
Cdd:TIGR02169  705 DELSQELSDASRKIGEIEKEI----EQLEQEEEKLKERLEELEEDLSSLEQEIENVKSE----------LKELEARIEEL 770

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    409 EEQLKEVRKKCAE-EAQL----ISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQ 483
Cdd:TIGR02169  771 EEDLHKLEEALNDlEARLshsrIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIK 850

                          170       180
                   ....*....|....*....|....*...
gi 67476728    484 DSQQEISSMQMKLMEMK-DLENHNSQLN 510
Cdd:TIGR02169  851 SIEKEIENLNGKKEELEeELEELEAALR 878
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 334-504 2.04e-11

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: 68.17  E-value: 2.04e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    334 ELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQ---DEVQREntnlqklqaqkqqvqelLDELDEQKAQLEE 410
Cdd:TIGR02169  675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASrkiGEIEKE-----------------IEQLEQEEEKLKE 737

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    411 QLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRL------------QQETAELEESVESGKAQLEPL 478
Cdd:TIGR02169  738 RLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLearlshsripeiQAELSKLEEEVSRIEARLREI 817

                          170       180       190
                   ....*....|....*....|....*....|
gi 67476728    479 QQHLQDSQQEI----SSMQMKLMEMKDLEN 504
Cdd:TIGR02169  818 EQKLNRLTLEKeyleKEIQELQEQRIDLKE 847
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 333-493 2.78e-11

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: 66.33  E-value: 2.78e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 333 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNlqklqaqkqqvqelLDELDEQKAQLEEQL 412
Cdd:COG4942  34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAE--------------LAELEKEIAELRAEL 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 413 KEVRKKCAE---EAQLISS-------LKAELTSQESQISTYEEELAKAR----EELSRLQQETAELEESVESGKAQLEPL 478
Cdd:COG4942 100 EAQKEELAEllrALYRLGRqpplallLSPEDFLDAVRRLQYLKYLAPARreqaEELRADLAELAALRAELEAERAELEAL 179

                       170
                ....*....|....*
gi 67476728 479 QQHLQDSQQEISSMQ 493
Cdd:COG4942 180 LAELEEERAALEALK 194
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 333-491 2.88e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 67.65  E-value: 2.88e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 333 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENtnlqklqaqkqqvqELLDELDEQKAQLEEQL 412
Cdd:COG1196 281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELE--------------EELEELEEELEELEEEL 346

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 67476728 413 KEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISS 491
Cdd:COG1196 347 EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 333-491 4.33e-11

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: 65.56  E-value: 4.33e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 333 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDL-----------QDEVQRENTNLQKLQAQKQQVQELLDEL 401
Cdd:COG4942  76 QELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLgrqpplalllsPEDFLDAVRRLQYLKYLAPARREQAEEL 155

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 402 DEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQH 481
Cdd:COG4942 156 RADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235

                       170
                ....*....|
gi 67476728 482 LQDSQQEISS 491
Cdd:COG4942 236 AAAAAERTPA 245
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
330-503 5.10e-11

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 66.63  E-value: 5.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728  330 SAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRT-SEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKaQL 408
Cdd:PRK03918 546 KELEKLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEPFYNEYLELKDAEKELEREEKELK-KL 624

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728  409 EEQLKEVRKKCAEEAQLISSLKAELTSQESQIStyEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQE 488
Cdd:PRK03918 625 EEELDKAFEELAETEKRLEELRKELEELEKKYS--EEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEE 702

                        170
                 ....*....|....*
gi 67476728  489 ISSMQMKLMEMKDLE 503
Cdd:PRK03918 703 LEEREKAKKELEKLE 717
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 333-505 1.96e-10

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 65.08  E-value: 1.96e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    333 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQL 412
Cdd:TIGR02168  754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    413 KEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSM 492
Cdd:TIGR02168  834 AATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSEL 913

                          170
                   ....*....|...
gi 67476728    493 QMKLMEMKDLENH 505
Cdd:TIGR02168  914 RRELEELREKLAQ 926
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 331-493 2.92e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 64.19  E-value: 2.92e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 331 AIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEE 410
Cdd:COG1196 349 AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE 428

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 411 QLKEVRKKCAEEAQLISSLKAELTSQEsqistyeEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEIS 490
Cdd:COG1196 429 ALAELEEEEEEEEEALEEAAEEEAELE-------EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501


                ...
gi 67476728 491 SMQ 493
Cdd:COG1196 502 DYE 504
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 335-598 3.24e-10

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


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 64.07  E-value: 3.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   335 LDTLNNEIVD---------------------LQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEvqrentnlqkLQAQKQQ 393
Cdd:pfam10174 312 LETLTNQNSDckqhievlkesltakeqraaiLQTEVDALRLRLEEKESFLNKKTKQLQDLTEE----------KSTLAGE 381

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   394 VQELLDELD--EQKA--------QLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETaE 463
Cdd:pfam10174 382 IRDLKDMLDvkERKInvlqkkieNLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQR-E 460

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   464 LEESVEsgKAQLEPLQQHLQDSQQEISSMQMKLME----MKDLENHNSQLNwcSSPHSIlvngatdycsLSTSSSETANL 539
Cdd:pfam10174 461 REDRER--LEELESLKKENKDLKEKVSALQPELTEkessLIDLKEHASSLA--SSGLKK----------DSKLKSLEIAV 526

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 67476728   540 NEHVEGQSNLESE--PIHQ-ESPARSSPELLPSGVTDENEVTTAVTE--KVCSELD----------NNRHSKEE 598
Cdd:pfam10174 527 EQKKEECSKLENQlkKAHNaEEAVRTNPEINDRIRLLEQEVARYKEEsgKAQAEVErllgilreveNEKNDKDK 600
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
396-510 4.13e-10

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 62.61  E-value: 4.13e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 396 ELLDELDEQKAQLEEQLKEVRKKcaeeaqlISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQL 475
Cdd:COG4372  24 ILIAALSEQLRKALFELDKLQEE-------LEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAEL 96

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 67476728 476 EPLQQHLQDSQQEISSMQMKLM----EMKDLENHNSQLN 510
Cdd:COG4372  97 AQAQEELESLQEEAEELQEELEelqkERQDLEQQRKQLE 135
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 338-490 5.93e-10

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: 63.12  E-value: 5.93e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   338 LNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRK 417
Cdd:TIGR04523 438 NNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTK 517

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   418 KCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSR---------LQQETAELEESVESGKAQLEPLQQHLQDSQQE 488
Cdd:TIGR04523 518 KISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKenlekeideKNKEIEELKQTQKSLKKKQEEKQELIDQKEKE 597


                  ..
gi 67476728   489 IS 490
Cdd:TIGR04523 598 KK 599
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 333-483 8.80e-10

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: 62.78  E-value: 8.80e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    333 KELDTLNNEIVDLQREKNNVEQDLKEKE-------DTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELD--- 402
Cdd:TIGR02169  350 KRRDKLTEEYAELKEELEDLRAELEEVDkefaetrDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNaai 429

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    403 ----EQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELE-------ESVESG 471
Cdd:TIGR02169  430 agieAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEaqaraseERVRGG 509

                          170
                   ....*....|..
gi 67476728    472 KAQLEPLQQHLQ 483
Cdd:TIGR02169  510 RAVEEVLKASIQ 521
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 403-492 9.17e-10

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: 61.70  E-value: 9.17e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 403 EQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHL 482
Cdd:COG4942  20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99

                        90
                ....*....|
gi 67476728 483 QDSQQEISSM 492
Cdd:COG4942 100 EAQKEELAEL 109
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 332-510 2.43e-09

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: 61.19  E-value: 2.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   332 IKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKlqaqkqqvqELLDELDEQKAQLEEQ 411
Cdd:TIGR04523 259 KDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELK---------SELKNQEKKLEEIQNQ 329

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   412 LKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDS------ 485
Cdd:TIGR04523 330 ISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQeklnqq 409

                         170       180       190
                  ....*....|....*....|....*....|
gi 67476728   486 -QQEISSMQ----MKLMEMKDLENHNSQLN 510
Cdd:TIGR04523 410 kDEQIKKLQqekeLLEKEIERLKETIIKNN 439
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 318-510 2.86e-09

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: 60.80  E-value: 2.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   318 KNIIGSSPVADFSAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQ----RENTNLQKLQAQKQQ 393
Cdd:TIGR04523  25 KNIANKQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKdlndKLKKNKDKINKLNSD 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   394 VQELLDELDEQKAQ----------LEEQLKEVRKKCA--------EEAQL-------------ISSLKAELTSQESQIST 442
Cdd:TIGR04523 105 LSKINSEIKNDKEQknklevelnkLEKQKKENKKNIDkflteikkKEKELeklnnkyndlkkqKEELENELNLLEKEKLN 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   443 YEEELAKAREELSR-----------------LQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKDLENH 505
Cdd:TIGR04523 185 IQKNIDKIKNKLLKlelllsnlkkkiqknksLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNK 264


                  ....*.
gi 67476728   506 N-SQLN 510
Cdd:TIGR04523 265 IkKQLS 270
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 332-511 3.06e-09

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: 60.80  E-value: 3.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   332 IKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQ 411
Cdd:TIGR04523 376 KKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELI 455

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   412 LKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISS 491
Cdd:TIGR04523 456 IKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKE 535

                         170       180
                  ....*....|....*....|.
gi 67476728   492 MQMKLMEMKD-LENHNSQLNW 511
Cdd:TIGR04523 536 KESKISDLEDeLNKDDFELKK 556
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
 403-509 3.12e-09

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


Pssm-ID: 462316 [Multi-domain]  Cd Length: 129  Bit Score: 55.72  E-value: 3.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   403 EQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQeSQIST-----YEEELAK----------AREELSRLQQETAELEES 467
Cdd:pfam07926   1 AELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQ-AEIAReaqqnYERELVLhaedikalqaLREELNELKAEIAELKAE 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 67476728   468 VESGKAQLEPLQQHLQDS----QQEISSMQMKLmemKDLENHNSQL 509
Cdd:pfam07926  80 AESAKAELEESEESWEEQkkelEKELSELEKRI---EDLNEQNKLL 122
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
330-498 4.99e-09

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 60.31  E-value: 4.99e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728  330 SAIKELDTLNN--EIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRenTNLQKLQAQKQQVQELLDELDEQKAQ 407
Cdd:COG4913  229 ALVEHFDDLERahEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAA--LRLWFAQRRLELLEAELEELRAELAR 306

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728  408 LEEQLKEVRKKCAEEAQLISSLKAELTSQ--------ESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQ 479
Cdd:COG4913  307 LEAELERLEARLDALREELDELEAQIRGNggdrleqlEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALR 386

                        170
                 ....*....|....*....
gi 67476728  480 QHLQDSQQEISSMQMKLME 498
Cdd:COG4913  387 AEAAALLEALEEELEALEE 405
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 333-493 5.04e-09

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 60.46  E-value: 5.04e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    333 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTnlqklqaQKQQVQELLDELDEQKAQLEEQL 412
Cdd:TIGR02168  677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSR-------QISALRKDLARLEAEVEQLEERI 749

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    413 KEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSM 492
Cdd:TIGR02168  750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESL 829


                   .
gi 67476728    493 Q 493
Cdd:TIGR02168  830 E 830
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 398-487 5.71e-09

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: 59.01  E-value: 5.71e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 398 LDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEP 477
Cdd:COG4942  29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE 108

                        90
                ....*....|
gi 67476728 478 LQQHLQDSQQ 487
Cdd:COG4942 109 LLRALYRLGR 118
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 345-509 6.42e-09

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: 59.80  E-value: 6.42e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    345 LQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQ 424
Cdd:pfam01576   94 LQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEE 173

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    425 LISSLKAELTSQESQISTYEEEL---AKAREELS----RLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLM 497
Cdd:pfam01576  174 KAKSLSKLKNKHEAMISDLEERLkkeEKGRQELEkakrKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLE 253

                          170       180
                   ....*....|....*....|...
gi 67476728    498 E-----------MKDLENHNSQL 509
Cdd:pfam01576  254 EetaqknnalkkIRELEAQISEL 276
HAP1_N pfam04849
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ...
 334-501 8.48e-09

HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.


Pssm-ID: 461455 [Multi-domain]  Cd Length: 309  Bit Score: 58.11  E-value: 8.48e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   334 ELDTLNNEIVDLQREknnveqdLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLK 413
Cdd:pfam04849 109 QLGSAREEILQLRHE-------LSKKDDLLQIYSNDAEESETESSCSTPLRRNESFSSLHGCVQLDALQEKLRGLEEENL 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   414 EVRKKC-----------AEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETA-------ELEESVESGKAQL 475
Cdd:pfam04849 182 KLRSEAshlktetdtyeEKEQQLMSDCVEQLSEANQQMAELSEELARKMEENLRQQEEITsllaqivDLQHKCKELGIEN 261

                         170       180
                  ....*....|....*....|....*.
gi 67476728   476 EPLQQHLQDSQQEISSMQMKLMEMKD 501
Cdd:pfam04849 262 EELQQHLQASKEAQRQLTSELQELQD 287
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
332-503 1.19e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 58.92  E-value: 1.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728  332 IKELDTLNNEIVDLQREKNNVEQDLKEKED---TIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQL 408
Cdd:PRK03918 171 IKEIKRRIERLEKFIKRTENIEELIKEKEKeleEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESL 250

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728  409 EEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEE--ELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQ 486
Cdd:PRK03918 251 EGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERI 330

                        170
                 ....*....|....*..
gi 67476728  487 QEISSMQMKLMEMKDLE 503
Cdd:PRK03918 331 KELEEKEERLEELKKKL 347
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 330-509 1.60e-08

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: 58.54  E-value: 1.60e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    330 SAIKELDTLN--------NEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRentnlqklqaqkqqVQELLDEL 401
Cdd:TIGR02169  269 EIEQLLEELNkkikdlgeEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAK--------------LEAEIDKL 334

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    402 DEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELS-------------------------- 455
Cdd:TIGR02169  335 LAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKdyrekleklkreinelkreldrlqee 414

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 67476728    456 --RLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMK-DLENHNSQL 509
Cdd:TIGR02169  415 lqRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAaDLSKYEQEL 471
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 330-491 1.68e-08

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 57.53  E-value: 1.68e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 330 SAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQ-------------------DL--------------QDE 376
Cdd:COG3883  55 ELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYrsggsvsyldvllgsesfsDFldrlsalskiadadADL 134

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 377 VQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSR 456
Cdd:COG3883 135 LEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214

                       170       180       190
                ....*....|....*....|....*....|....*
gi 67476728 457 LQQETAELEESVESGKAQLEPLQQHLQDSQQEISS 491
Cdd:COG3883 215 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGA 249
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
396-500 1.84e-08

Phage shock protein A [Transcription, Signal transduction mechanisms];


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 55.60  E-value: 1.84e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 396 ELLDE-------LDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEE--ELA--KAREELSR--LQQEtA 462
Cdd:COG1842  16 ALLDKaedpekmLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEkaRLAleKGREDLAReaLERK-A 94

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 67476728 463 ELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMK 500
Cdd:COG1842  95 ELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELK 132
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
333-503 1.93e-08

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 58.10  E-value: 1.93e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 333 KELDTLNNEIVDLQREKNNVeqDLKEKEDTIKQRTSEVQDLQDEVQREntnlqklqaqkqqvqelLDELDEQKAQLEEQL 412
Cdd:COG3206 189 KELEEAEAALEEFRQKNGLV--DLSEEAKLLLQQLSELESQLAEARAE-----------------LAEAEARLAALRAQL 249

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 413 KEVRKKCAEEAQ--LISSLKAELTSQESQI----STY----------EEELAKAREEL-SRLQQETAELEESVESGKAQL 475
Cdd:COG3206 250 GSGPDALPELLQspVIQQLRAQLAELEAELaelsARYtpnhpdvialRAQIAALRAQLqQEAQRILASLEAELEALQARE 329

                       170       180
                ....*....|....*....|....*...
gi 67476728 476 EPLQQHLQDSQQEISSMQMKLMEMKDLE 503
Cdd:COG3206 330 ASLQAQLAQLEARLAELPELEAELRRLE 357
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
335-503 2.69e-08

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 57.47  E-value: 2.69e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 335 LDTLNNEIVDLQRE-----KNNVEQ--DLKEKEDTIKQRTSEVQDLQDEVQRENT----------------NLQKLQAQK 391
Cdd:COG4717  48 LERLEKEADELFKPqgrkpELNLKElkELEEELKEAEEKEEEYAELQEELEELEEeleeleaeleelreelEKLEKLLQL 127

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 392 QQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQL---ISSLKAELTSQESQISTYEEEL-AKAREELSRLQQETAELEES 467
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEERLEELRELeeeLEELEAELAELQEELEELLEQLsLATEEELQDLAEELEELQQR 207

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 67476728 468 VESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKDLE 503
Cdd:COG4717 208 LAELEEELEEAQEELEELEEELEQLENELEAAALEE 243
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
317-499 2.91e-08

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 57.72  E-value: 2.91e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 317 QKNIIGSSPVADfSAIKELDtLNNEIVDLQREKNNVEQDLKEK----------------EDTIKQRTSEV--------QD 372
Cdd:COG3206  86 QIEILKSRPVLE-RVVDKLN-LDEDPLGEEASREAAIERLRKNltvepvkgsnvieisyTSPDPELAAAVanalaeayLE 163

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 373 LQDEVQRENTNlqklqaqkqqvqELLDELDEQKAQLEEQLKEVRKKCAE--EAQLISSLKAELTSQESQISTYEEELAKA 450
Cdd:COG3206 164 QNLELRREEAR------------KALEFLEEQLPELRKELEEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESQLAEA 231

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 67476728 451 REELSRLQQETAELEESVESGKAQLEPLQQH--LQDSQQEISSMQMKLMEM 499
Cdd:COG3206 232 RAELAEAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAEL 282
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
 356-508 3.39e-08

Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.


Pssm-ID: 464776 [Multi-domain]  Cd Length: 193  Bit Score: 54.52  E-value: 3.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   356 LKEKEDTIKQRTSEVQDLQ---DEVQRENtnlqklqaqkqqvqELLDELdeQKAQlEEQLKEVRKKCAEEAQLISSLKAE 432
Cdd:pfam15619   6 LSARLHKIKELQNELAELQsklEELRKEN--------------RLLKRL--QKRQ-EKALGKYEGTESELPQLIARHNEE 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   433 L--------------TSQESQISTYEEELAKAREELSRLQQ--------ETAELEEsvesgkaQLEPLQQHLQDSQQEIS 490
Cdd:pfam15619  69 VrvlrerlrrlqekeRDLERKLKEKEAELLRLRDQLKRLEKlsedknlaEREELQK-------KLEQLEAKLEDKDEKIQ 141

                         170
                  ....*....|....*...
gi 67476728   491 SMQMKLmemkDLENHNSQ 508
Cdd:pfam15619 142 DLERKL----ELENKSFR 155
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
333-481 4.02e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 57.38  E-value: 4.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728  333 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVqRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQL 412
Cdd:PRK03918 231 KELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEI-EELEEKVKELKELKEKAEEYIKLSEFYEEYLDEL 309

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 67476728  413 KEVRKKCAEEAQLISSLKAELTSQESQistyEEELAKAREELSRLQQETAELEESV---ESGKAQLEPLQQH 481
Cdd:PRK03918 310 REIEKRLSRLEEEINGIEERIKELEEK----EERLEELKKKLKELEKRLEELEERHelyEEAKAKKEELERL 377
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
334-504 4.41e-08

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 56.97  E-value: 4.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728  334 ELDTLNNEIVDLQ-------REKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENtnlqklqAQKQQVQELLDELDEQKA 406
Cdd:PRK02224 252 ELETLEAEIEDLRetiaeteREREELAEEVRDLRERLEELEEERDDLLAEAGLDD-------ADAEAVEARREELEDRDE 324

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728  407 QLEEQLKEVRKKCAEEAQLISSLKAELTSQES-------QISTYEEELAKAREELSRLQQETAELEESVESGKA------ 473
Cdd:PRK02224 325 ELRDRLEECRVAAQAHNEEAESLREDADDLEEraeelreEAAELESELEEAREAVEDRREEIEELEEEIEELRErfgdap 404

                        170       180       190
                 ....*....|....*....|....*....|...
gi 67476728  474 -QLEPLQQHLQDSQQEISSMQMKLMEMK-DLEN 504
Cdd:PRK02224 405 vDLGNAEDFLEELREERDELREREAELEaTLRT 437
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
313-493 5.58e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 56.85  E-value: 5.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728  313 RASLQKNIIGsspvadFSAIKELDTLNNEIVDLQREKNNVE---QDLKEKEDTIKQR--------------------TSE 369
Cdd:COG4913  596 RRIRSRYVLG------FDNRAKLAALEAELAELEEELAEAEerlEALEAELDALQERrealqrlaeyswdeidvasaERE 669

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728  370 VQDLQDEVQR-ENTNLQklqaqkqqvqelLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELA 448
Cdd:COG4913  670 IAELEAELERlDASSDD------------LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE 737

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 67476728  449 KAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQ 493
Cdd:COG4913  738 AAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARL 782
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 334-492 6.48e-08

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: 56.61  E-value: 6.48e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    334 ELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLK 413
Cdd:TIGR02169  792 RIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELE 871

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    414 EVRKKCAE-EAQL------ISSLKAELTSQESQISTYEEELAKAREELSRLQ-------QETAELEESVESGK------A 473
Cdd:TIGR02169  872 ELEAALRDlESRLgdlkkeRDELEAQLRELERKIEELEAQIEKKRKRLSELKaklealeEELSEIEDPKGEDEeipeeeL 951

                          170
                   ....*....|....*....
gi 67476728    474 QLEPLQQHLQDSQQEISSM 492
Cdd:TIGR02169  952 SLEDVQAELQRVEEEIRAL 970
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
333-489 1.11e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 54.91  E-value: 1.11e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 333 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQL 412
Cdd:COG4372  87 EQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEEL 166

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 413 KEVRKKCA--EEAQLISSLKaELTSQESQISTYEEELAKA---REELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQ 487
Cdd:COG4372 167 AALEQELQalSEAEAEQALD-ELLKEANRNAEKEEELAEAeklIESLPRELAEELLEAKDSLEAKLGLALSALLDALELE 245


                ..
gi 67476728 488 EI 489
Cdd:COG4372 246 ED 247
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
333-464 1.23e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 55.69  E-value: 1.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728  333 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRentNLQKLQAQKQQVQELLDELDEQKAQLEEQL 412
Cdd:COG4913  338 DRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAA---LRAEAAALLEALEEELEALEEALAEAEAAL 414

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 67476728  413 KEVRKKcaeeaqlISSLKAELTSQESQISTYEEELAKAREELSR-LQQETAEL 464
Cdd:COG4913  415 RDLRRE-------LRELEAEIASLERRKSNIPARLLALRDALAEaLGLDEAEL 460
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 333-510 1.35e-07

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: 1.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   333 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEqkaqLEEQL 412
Cdd:TIGR04523 152 KELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISE----LKKQN 227

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   413 KEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQET-------AELEESVESGKAQLEPL-QQHLQD 484
Cdd:TIGR04523 228 NQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELeqnnkkiKELEKQLNQLKSEISDLnNQKEQD 307

                         170       180
                  ....*....|....*....|....*.
gi 67476728   485 SQQEISSmQMKLMEmKDLENHNSQLN 510
Cdd:TIGR04523 308 WNKELKS-ELKNQE-KKLEEIQNQIS 331
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
330-495 1.40e-07

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 55.43  E-value: 1.40e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728  330 SAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDE------------VQRENtnlqkLQAQKQQVQEL 397
Cdd:PRK02224 346 SLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEieelrerfgdapVDLGN-----AEDFLEELREE 420

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728  398 LDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEP 477
Cdd:PRK02224 421 RDELREREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLER 500

                        170
                 ....*....|....*...
gi 67476728  478 LQQhLQDSQQEISSMQMK 495
Cdd:PRK02224 501 AED-LVEAEDRIERLEER 517
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
329-492 1.56e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 55.16  E-value: 1.56e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 329 FSAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTnlqklqaqkqqVQELLDELDEQKAQL 408
Cdd:COG4717 343 LDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEE-----------YQELKEELEELEEQL 411

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 409 EEQLKEVRKkcAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVEsgkaqLEPLQQHLQDSQQE 488
Cdd:COG4717 412 EELLGELEE--LLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGE-----LAELLQELEELKAE 484


                ....
gi 67476728 489 ISSM 492
Cdd:COG4717 485 LREL 488
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 329-510 1.61e-07

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 54.84  E-value: 1.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728  329 FSAIKELDTLNneIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLqDEVQRENtnlqklqaqkqqvqelldelDEQKAQL 408
Cdd:PRK04778  89 FEAEELNDKFR--FRKAKHEINEIESLLDLIEEDIEQILEELQEL-LESEEKN--------------------REEVEQL 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728  409 EEQLKEVRKKCAEEA----QLISSLKAELTSQESQISTYEEELA-----KAREELSRLQQETAELEESVESGKAQLEPLQ 479
Cdd:PRK04778 146 KDLYRELRKSLLANRfsfgPALDELEKQLENLEEEFSQFVELTEsgdyvEAREILDQLEEELAALEQIMEEIPELLKELQ 225

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 67476728  480 QHLQDSQQEISS----MQMK---------LMEMKDLENHNSQLN 510
Cdd:PRK04778 226 TELPDQLQELKAgyreLVEEgyhldhldiEKEIQDLKEQIDENL 269
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
317-491 1.85e-07

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 55.02  E-value: 1.85e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 317 QKNIIGSSPVADFSAIKELDTLNNEIVDLQREK-------NNVEQDLKEKEDTIKQ--RTSEVQDLQDEVQRENTNLQKL 387
Cdd:COG3206 203 QKNGLVDLSEEAKLLLQQLSELESQLAEARAELaeaearlAALRAQLGSGPDALPEllQSPVIQQLRAQLAELEAELAEL 282

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 388 QAQKQQV----QELLDELDEQKAQLEEqlkevrkkcaEEAQLISSLKAELTSQESQISTYEEELAKAREELSRL---QQE 460
Cdd:COG3206 283 SARYTPNhpdvIALRAQIAALRAQLQQ----------EAQRILASLEAELEALQAREASLQAQLAQLEARLAELpelEAE 352

                       170       180       190
                ....*....|....*....|....*....|.
gi 67476728 461 TAELEESVESGKAQLEPLQQHLQDSQQEISS 491
Cdd:COG3206 353 LRRLEREVEVARELYESLLQRLEEARLAEAL 383
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 331-485 1.90e-07

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 54.84  E-value: 1.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728  331 AIKELDTLNNEIVDL----QRE---KNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDe 403
Cdd:PRK04778 280 AEEKNEEIQERIDQLydilEREvkaRKYVEKNSDTLPDFLEHAKEQNKELKEEIDRVKQSYTLNESELESVRQLEKQLE- 358

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728  404 qkaQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQ 483
Cdd:PRK04778 359 ---SLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKLHEIKRYLE 435


                 ..
gi 67476728  484 DS 485
Cdd:PRK04778 436 KS 437
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 330-501 2.03e-07

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 54.07  E-value: 2.03e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 330 SAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEvqrentnlqklqaqkqqvqelldeLDEQKAQLE 409
Cdd:COG3883  34 AAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAE------------------------IEERREELG 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 410 EQLKEVRKKCAEE------------AQLISSLKA-------------ELTSQESQISTYEEELAKAREELSRLQQETAEL 464
Cdd:COG3883  90 ERARALYRSGGSVsyldvllgsesfSDFLDRLSAlskiadadadlleELKADKAELEAKKAELEAKLAELEALKAELEAA 169

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 67476728 465 EESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKD 501
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELA 206
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
309-473 2.14e-07

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 54.86  E-value: 2.14e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 309 PPSDRASLQKNIIGSSPVADfsAIKEL--DTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQR-ENTnlq 385
Cdd:COG2433 361 PDVDRDEVKARVIRGLSIEE--ALEELieKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEElEAE--- 435

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 386 klqaqkqqvqelLDELDEQKAQLEEQLKEVRKKCAEEAQL---ISSLKAELTSQESQISTYEEELAKAREELSRLQqeta 462
Cdd:COG2433 436 ------------LEEKDERIERLERELSEARSEERREIRKdreISRLDREIERLERELEEERERIEELKRKLERLK---- 499

                       170
                ....*....|.
gi 67476728 463 ELEESVESGKA 473
Cdd:COG2433 500 ELWKLEHSGEL 510
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
331-501 2.23e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 54.68  E-value: 2.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728  331 AIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQ-------------RENTNLQKLQAQKQQVQEL 397
Cdd:PRK03918 382 TGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEelkkakgkcpvcgRELTEEHRKELLEEYTAEL 461

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728  398 ------LDELDEQKAQLEEQLKEVRKKCAEEAQLIS--SLKAELTSQESQISTYE-EELAKAREELSRLQQETAELE--- 465
Cdd:PRK03918 462 kriekeLKEIEEKERKLRKELRELEKVLKKESELIKlkELAEQLKELEEKLKKYNlEELEKKAEEYEKLKEKLIKLKgei 541

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 67476728  466 ESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKD 501
Cdd:PRK03918 542 KSLKKELEKLEELKKKLAELEKKLDELEEELAELLK 577
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 361-464 2.32e-07

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 54.00  E-value: 2.32e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 361 DTIKQRTSEVQDLQDEVQRENtnlqklqaqkqqvqELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQI 440
Cdd:COG4942  20 DAAAEAEAELEQLQQEIAELE--------------KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL 85

                        90       100
                ....*....|....*....|....
gi 67476728 441 STYEEELAKAREELSRLQQETAEL 464
Cdd:COG4942  86 AELEKEIAELRAELEAQKEELAEL 109
EF-hand_4 pfam12763
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ...
 32-80 2.89e-07

Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin cytoskeleton-regulatory complex END3 and similar proteins from fungi and closely related species.


Pssm-ID: 289529  Cd Length: 104  Bit Score: 49.68  E-value: 2.89e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 67476728    32 GRVLASDAAAFLKKSGLPDLILGKIWDLADTDGKGILNKQEFFVALRLV 80
Cdd:pfam12763  24 NKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLI 72
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 330-496 3.66e-07

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 53.30  E-value: 3.66e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 330 SAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENtnlqklqaqkqqvqELLDELDEQKAQLE 409
Cdd:COG3883  13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQ--------------AEIDKLQAEIAEAE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 410 EQLKEVRKKCAEEAQ-------LISSLKAELTSQE-----------SQISTYE----EELAKAREELSRLQQETAELEES 467
Cdd:COG3883  79 AEIEERREELGERARalyrsggSVSYLDVLLGSESfsdfldrlsalSKIADADadllEELKADKAELEAKKAELEAKLAE 158

                       170       180
                ....*....|....*....|....*....
gi 67476728 468 VESGKAQLEPLQQHLQDSQQEISSMQMKL 496
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEQEALLAQL 187
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 352-471 3.79e-07

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 53.23  E-value: 3.79e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 352 VEQDLKEKEDTIKQRTSEVQDLQDEVQREntnlqklqaqkqqvqelLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKA 431
Cdd:COG4942 144 LAPARREQAEELRADLAELAALRAELEAE-----------------RAELEALLAELEEERAALEALKAERQKLLARLEK 206

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 67476728 432 ELTSQESQISTYEEELAKAREELSRLQQETAELEESVESG 471
Cdd:COG4942 207 ELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 397-509 3.98e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.17  E-value: 3.98e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 397 LLDELDEQKAQLEEQlkevRKKcAEEAQLISS----LKAELT-----SQESQISTYEEELAKAREELSRLQQETAELEES 467
Cdd:COG1196 194 ILGELERQLEPLERQ----AEK-AERYRELKEelkeLEAELLllklrELEAELEELEAELEELEAELEELEAELAELEAE 268

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 67476728 468 VESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKDLENHNSQL 509
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER 310
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
402-501 4.80e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 52.98  E-value: 4.80e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 402 DEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQH 481
Cdd:COG4372   2 DRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEE 81

                        90       100
                ....*....|....*....|
gi 67476728 482 LQDSQQEISSMQMKLMEMKD 501
Cdd:COG4372  82 LEELNEQLQAAQAELAQAQE 101
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
332-500 5.14e-07

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 52.22  E-value: 5.14e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 332 IKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDEL---------- 401
Cdd:COG1340  52 VKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLewrqqtevls 131

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 402 -DEQK------AQLEEQLKEvRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAEL---------- 464
Cdd:COG1340 132 pEEEKelvekiKELEKELEK-AKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELykeadelrke 210

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 67476728 465 -----EESVESGKA------QLEPLQQHLQDSQQEISSMQMKLMEMK 500
Cdd:COG1340 211 adelhKEIVEAQEKadelheEIIELQKELRELRKELKKLRKKQRALK 257
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
321-504 5.44e-07

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 53.51  E-value: 5.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728  321 IGSSPVADfsAIKE----LDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRtSEVQDLQDevQRENTNlqklqaqkqqvqE 396
Cdd:PRK02224 461 VEGSPHVE--TIEEdrerVEELEAELEDLEEEVEEVEERLERAEDLVEAE-DRIERLEE--RREDLE------------E 523

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728  397 LLDELDEQKAQLEEQLKEVRKKCAEeaqlissLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESgKAQLE 476
Cdd:PRK02224 524 LIAERRETIEEKRERAEELRERAAE-------LEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIES-LERIR 595

                        170       180
                 ....*....|....*....|....*...
gi 67476728  477 PLQQHLQDSQQEISSMQMKLMEMKDLEN 504
Cdd:PRK02224 596 TLLAAIADAEDEIERLREKREALAELND 623
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 341-510 5.49e-07

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


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 53.59  E-value: 5.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   341 EIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQD-EVQRENTNLQK--LQAQKQQVQELLDELDEQKAQLEEQLKEV-- 415
Cdd:pfam05557  28 ARIELEKKASALKRQLDRESDRNQELQKRIRLLEKrEAEAEEALREQaeLNRLKKKYLEALNKKLNEKESQLADAREVis 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   416 --RKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKA---QLEPLQQHLQ---DSQQ 487
Cdd:pfam05557 108 clKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEaeqRIKELEFEIQsqeQDSE 187

                         170       180       190
                  ....*....|....*....|....*....|
gi 67476728   488 EISSMQMKLMEMKDLEN-------HNSQLN 510
Cdd:pfam05557 188 IVKNSKSELARIPELEKelerlreHNKHLN 217
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
327-486 5.98e-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: 5.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728  327 ADFSAIKE-LDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRentnlqklqAQKQQVQELLDELDEQK 405
Cdd:COG4913  685 DDLAALEEqLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA---------AEDLARLELRALLEERF 755

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728  406 AQL--EEQLKEVRKKCAEEAQLISSLKAELTSQ-ESQISTY-----------------------------EEELAKAREE 453
Cdd:COG4913  756 AAAlgDAVERELRENLEERIDALRARLNRAEEElERAMRAFnrewpaetadldadleslpeylalldrleEDGLPEYEER 835

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 67476728  454 LSRLQQET---------AELEESVESGKAQLEPLQQHLQDSQ 486
Cdd:COG4913  836 FKELLNENsiefvadllSKLRRAIREIKERIDPLNDSLKRIP 877
UPF0242 pfam06785
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ...
 354-492 6.30e-07

Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal transmembrane region and a C-terminal coiled-coil.


Pssm-ID: 429117 [Multi-domain]  Cd Length: 194  Bit Score: 50.59  E-value: 6.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   354 QDLKEKEDTIKQRTSEVQDLQDEVQRENtnlqklqaqkqqvqELLDELDEQKAQLEEQLKEVRKKCAEEaqlisslkael 433
Cdd:pfam06785  83 EGFKILEETLEELQSEEERLEEELSQKE--------------EELRRLTEENQQLQIQLQQISQDFAEF----------- 137

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 67476728   434 tSQESqistyEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSM 492
Cdd:pfam06785 138 -RLES-----EEQLAEKQLLINEYQQTIEEQRSVLEKRQDQIENLESKVRDLNYEIKTL 190
CCDC22 pfam05667
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
 333-480 6.59e-07

Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.


Pssm-ID: 461708 [Multi-domain]  Cd Length: 600  Bit Score: 53.11  E-value: 6.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   333 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQdlqdEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQL 412
Cdd:pfam05667 335 EELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELE----ELKEQNEELEKQYKVKKKTLDLLPDAEENIAKLQALV 410

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 67476728   413 KEVRKKCAEEAQL-----------ISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQ 480
Cdd:pfam05667 411 DASAQRLVELAGQwekhrvplieeYRALKEAKSNKEDESQRKLEEIKELREKIKEVAEEAKQKEELYKQLVAEYERLPK 489
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 333-510 7.76e-07

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: 53.10  E-value: 7.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   333 KELDTLNNEIVDLQREKnnvEQDL-KEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQ 411
Cdd:TIGR04523 288 KQLNQLKSEISDLNNQK---EQDWnKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRE 364

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   412 LKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAreelsrlQQETAELEESVESGKAQLEPLQQHLQDSQQEISS 491
Cdd:TIGR04523 365 LEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQ-------EKLNQQKDEQIKKLQQEKELLEKEIERLKETIIK 437

                         170
                  ....*....|....*....
gi 67476728   492 MQmklMEMKDLENHNSQLN 510
Cdd:TIGR04523 438 NN---SEIKDLTNQDSVKE 453
TMF_DNA_bd pfam12329
TATA element modulatory factor 1 DNA binding; This is the middle region of a family of TATA ...
 396-465 9.20e-07

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


Pssm-ID: 372049 [Multi-domain]  Cd Length: 74  Bit Score: 47.30  E-value: 9.20e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   396 ELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELE 465
Cdd:pfam12329   5 KLLKEKDEQIAQLMEEGEKLSKKELKLNNTIKKLRAKNKELEKEIAELKKKLEKLEKELENLEERLKRAE 74
MscS_porin pfam12795
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...
 330-490 9.89e-07

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


Pssm-ID: 432790 [Multi-domain]  Cd Length: 238  Bit Score: 50.76  E-value: 9.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   330 SAIKELDTLNNEIVDLQREKNNV------EQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDE 403
Cdd:pfam12795  48 DAPAELRELRQELAALQAKAEAApkeilaSLSLEELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQ 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   404 QKAQLEEQLK--EVRKKCAEEAQLIsSLKAELTSQESQISTYEEELAKA--REELSRLQQETAeleesvesgKAQLEPLQ 479
Cdd:pfam12795 128 RLQQIRNRLNgpAPPGEPLSEAQRW-ALQAELAALKAQIDMLEQELLSNnnRQDLLKARRDLL---------TLRIQRLE 197

                         170
                  ....*....|.
gi 67476728   480 QHLQDSQQEIS 490
Cdd:pfam12795 198 QQLQALQELLN 208
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 332-501 1.45e-06

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 51.94  E-value: 1.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   332 IKELDT----LNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQ 407
Cdd:TIGR04523 456 IKNLDNtresLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKE 535

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   408 LEEQLKEVRKKcaeeaqlISSLKAELTSqesqiSTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQ 487
Cdd:TIGR04523 536 KESKISDLEDE-------LNKDDFELKK-----ENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIK 603

                         170
                  ....*....|....
gi 67476728   488 EISSMQMKLMEMKD 501
Cdd:TIGR04523 604 EIEEKEKKISSLEK 617
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 333-501 1.75e-06

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 51.94  E-value: 1.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   333 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTnlqklqaqkqQVQELLDELDE-----QKAQ 407
Cdd:TIGR04523 489 KELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKES----------KISDLEDELNKddfelKKEN 558

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   408 LEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEplqqhlqdsqq 487
Cdd:TIGR04523 559 LEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENE----------- 627

                         170
                  ....*....|....
gi 67476728   488 EISSMQMKLMEMKD 501
Cdd:TIGR04523 628 KLSSIIKNIKSKKN 641
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
313-475 2.57e-06

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 51.17  E-value: 2.57e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 313 RASLQKNI-IGSSPVADFSAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQREntnlqklqaqk 391
Cdd:COG3206 242 LAALRAQLgSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQE----------- 310

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 392 qqVQELLDELDEQKAQLEEQLKEVRkkcAEEAQLISSLKaELTSQESQISTYEEELAKAREELSRLQQ--ETAELEESVE 469
Cdd:COG3206 311 --AQRILASLEAELEALQAREASLQ---AQLAQLEARLA-ELPELEAELRRLEREVEVARELYESLLQrlEEARLAEALT 384


                ....*.
gi 67476728 470 SGKAQL 475
Cdd:COG3206 385 VGNVRV 390
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
398-509 3.64e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 50.54  E-value: 3.64e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 398 LDELDEqkaqLEEQLKEVRKKCAEEAQLIsslkAELTSQESQISTYEEELAKAREELSRLQQ--ETAELEESVESGKAQL 475
Cdd:COG4717  70 LKELKE----LEEELKEAEEKEEEYAELQ----EELEELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAEL 141

                        90       100       110
                ....*....|....*....|....*....|....
gi 67476728 476 EPLQQHLQDSQQEISSMQMKLMEMKDLENHNSQL 509
Cdd:COG4717 142 AELPERLEELEERLEELRELEEELEELEAELAEL 175
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 397-510 3.73e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.83  E-value: 3.73e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    397 LLDELDEQKAQLEEQLKEV----RKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVE--- 469
Cdd:TIGR02168  194 ILNELERQLKSLERQAEKAerykELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEelr 273

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 67476728    470 ----SGKAQLEPLQQHLQDSQQEISSMQMKLM----EMKDLENHNSQLN 510
Cdd:TIGR02168  274 levsELEEEIEELQKELYALANEISRLEQQKQilreRLANLERQLEELE 322
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
 337-585 4.52e-06

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 49.37  E-value: 4.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   337 TLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQREntnlqklqaqkqqvqelLDELDEQKAQLEEQLKEVR 416
Cdd:pfam09787  44 ALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEE-----------------AESSREQLQELEEQLATER 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   417 kkcaeeaqlisSLKAELtsqESQISTYEEELAKAREELSR----LQQETAELEESVESGKAQLEPLQQHlQDSQQEISSM 492
Cdd:pfam09787 107 -----------SARREA---EAELERLQEELRYLEEELRRskatLQSRIKDREAEIEKLRNQLTSKSQS-SSSQSELENR 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   493 QMKLMEmkDLENHNSQLNWCSSPHSILVngatdyCSLSTSSSETANLNEHVEGQSNLESEPIHQESPARSSPelLPSGVT 572
Cdd:pfam09787 172 LHQLTE--TLIQKQTMLEALSTEKNSLV------LQLERMEQQIKELQGEGSNGTSINMEGISDGEGTRLRN--VPGLFS 241

                         250
                  ....*....|...
gi 67476728   573 DENEVTTAVTEKV 585
Cdd:pfam09787 242 ESDSDRAGMYGKV 254
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 432-502 4.62e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 49.83  E-value: 4.62e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 67476728 432 ELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKDL 502
Cdd:COG3883  17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREE 87
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 333-508 4.66e-06

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


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 50.51  E-value: 4.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   333 KELDTLNNEIVDLQREKNNVEQDlKEKEDTIKQRTSEVQDLQDEVQR---ENtnlqklqaqkqqvqELLDELDEQKAQLE 409
Cdd:pfam05557 163 SSLAEAEQRIKELEFEIQSQEQD-SEIVKNSKSELARIPELEKELERlreHN--------------KHLNENIENKLLLK 227

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   410 EQLKEVRKKC-------AEEAQL---ISSLKAELTSQESQISTYEEELAK---AREELSRLQQETAELEESVESGKAQLE 476
Cdd:pfam05557 228 EEVEDLKRKLereekyrEEAATLeleKEKLEQELQSWVKLAQDTGLNLRSpedLSRRIEQLQQREIVLKEENSSLTSSAR 307

                         170       180       190
                  ....*....|....*....|....*....|...
gi 67476728   477 PLQQHLQDSQQEISSMQMKLMEM-KDLENHNSQ 508
Cdd:pfam05557 308 QLEKARRELEQELAQYLKKIEDLnKKLKRHKAL 340
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 342-508 6.01e-06

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 50.11  E-value: 6.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   342 IVDLQREK-NNVEQDLKEKEDTIKQR-------TSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKaqlEEQLK 413
Cdd:pfam05483 262 LLEESRDKaNQLEEKTKLQDENLKELiekkdhlTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEK---EAQME 338

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   414 EVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELS----RLQQETAELEE--------SVE------------ 469
Cdd:pfam05483 339 ELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKiitmELQKKSSELEEmtkfknnkEVEleelkkilaede 418

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 67476728   470 ---SGKAQLEPLQQHLQDSQQ-----------EISSMQMKLMEMKDLENHNSQ 508
Cdd:pfam05483 419 kllDEKKQFEKIAEELKGKEQelifllqarekEIHDLEIQLTAIKTSEEHYLK 471
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 354-506 6.06e-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: 49.85  E-value: 6.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   354 QDLKEKEDTIKQRTSEVQDLQDEVQrentnlqklqaqkqqvqELLDELDEQKA---QLEEQLKEVRKKCAEEA----QLI 426
Cdd:pfam06160  86 KALDEIEELLDDIEEDIKQILEELD-----------------ELLESEEKNREeveELKDKYRELRKTLLANRfsygPAI 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   427 SSLKAELTSQESQISTYEEELA-----KAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMK- 500
Cdd:pfam06160 149 DELEKQLAEIEEEFSQFEELTEsgdylEAREVLEKLEEETDALEELMEDIPPLYEELKTELPDQLEELKEGYREMEEEGy 228


                  ....*.
gi 67476728   501 DLENHN 506
Cdd:pfam06160 229 ALEHLN 234
EF-hand_4 pfam12763
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ...
 222-319 6.96e-06

Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin cytoskeleton-regulatory complex END3 and similar proteins from fungi and closely related species.


Pssm-ID: 289529  Cd Length: 104  Bit Score: 45.44  E-value: 6.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   222 PAEKAKYDEIFlKTDKDMDGFVSGLEVREIFLKTGLPSTLLAHIWSLCDTKDCGKLSKDQFALAFHLISQkLIKGI--DP 299
Cdd:pfam12763   6 EWEIKKYWEIF-SGLKPENNKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLIFD-LVNGNiaDV 83

                          90       100
                  ....*....|....*....|
gi 67476728   300 PHVLTPEMIPPSDRASLQKN 319
Cdd:pfam12763  84 PDELPDWLVPGSKAHLIQAN 103
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 345-464 7.22e-06

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 46.96  E-value: 7.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   345 LQREKNNVEQDLKE------KEDTIKQRTSEVQDLQDEVQRentnlqklqaqkqqvqelLDEldEQKAQLEEQLKEVRKK 418
Cdd:pfam05672  25 EQREREEQERLEKEeeerlrKEELRRRAEEERARREEEARR------------------LEE--ERRREEEERQRKAEEE 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 67476728   419 CAEEAQlisslkAELTSQESQISTYEEELAKAREELSRLQQETAEL 464
Cdd:pfam05672  85 AEEREQ------REQEEQERLQKQKEEAEAKAREEAERQRQEREKI 124
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
332-466 7.89e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 49.68  E-value: 7.89e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728  332 IKELDTLNNEIVDLQreknNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTnlqklqaqkqQVQELLDELDE-QKAQLEE 410
Cdd:PRK03918 594 LKELEPFYNEYLELK----DAEKELEREEKELKKLEEELDKAFEELAETEK----------RLEELRKELEElEKKYSEE 659

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 67476728  411 QLKEVRKKCAEEAQLISSLKAELTSQESQISTYE----------EELAKAREELSRLQQETAELEE 466
Cdd:PRK03918 660 EYEELREEYLELSRELAGLRAELEELEKRREEIKktleklkeelEEREKAKKELEKLEKALERVEE 725
PRK12704 PRK12704
phosphodiesterase; Provisional
 399-504 7.93e-06

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 49.39  E-value: 7.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728  399 DELDEQKAQLEEQLKEVRKKcaeeaqlISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPL 478
Cdd:PRK12704  64 EEIHKLRNEFEKELRERRNE-------LQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEEL 136

                         90       100
                 ....*....|....*....|....*....
gi 67476728  479 QQHLQDSQQEISSMQM---KLMEMKDLEN 504
Cdd:PRK12704 137 IEEQLQELERISGLTAeeaKEILLEKVEE 165
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
396-496 8.61e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.91  E-value: 8.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728  396 ELLDELDEQKAQLEEQLKEVRKKCAEEAQL---------ISSLKAELTSQESQISTYEE---ELAKAREELSRLQQETAE 463
Cdd:COG4913  624 EELAEAEERLEALEAELDALQERREALQRLaeyswdeidVASAEREIAELEAELERLDAssdDLAALEEQLEELEAELEE 703

                         90       100       110
                 ....*....|....*....|....*....|...
gi 67476728  464 LEESVESGKAQLEPLQQHLQDSQQEISSMQMKL 496
Cdd:COG4913  704 LEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 398-509 8.71e-06

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: 49.95  E-value: 8.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728  398 LDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQ--- 474
Cdd:COG3096  524 LEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARapa 603

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 67476728  475 -------LEPLQQH----LQDSQQEISSMQMKLMEMKDLENHNSQL 509
Cdd:COG3096  604 wlaaqdaLERLREQsgeaLADSQEVTAAMQQLLEREREATVERDEL 649
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 353-501 9.14e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 49.06  E-value: 9.14e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 353 EQDLKEKEDTIKQRTSEVQDLQDEvqrentnlqklqaqkqqvqelLDELDEQKAQLEEQLKEVRKKcaeeaqlISSLKAE 432
Cdd:COG3883  15 DPQIQAKQKELSELQAELEAAQAE---------------------LDALQAELEELNEEYNELQAE-------LEALQAE 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 433 LTSQESQISTYEEELAKAREEL------------------------------------SRLQQETAELEESVESGKAQLE 476
Cdd:COG3883  67 IDKLQAEIAEAEAEIEERREELgeraralyrsggsvsyldvllgsesfsdfldrlsalSKIADADADLLEELKADKAELE 146

                       170       180
                ....*....|....*....|....*
gi 67476728 477 PLQQHLQDSQQEISSMQMKLMEMKD 501
Cdd:COG3883 147 AKKAELEAKLAELEALKAELEAAKA 171
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 274-493 1.05e-05

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


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 48.92  E-value: 1.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   274 CGKLSKDQFALAFHLISqkliKGIDPPHVLTPEMIPPsdraslqkniigsspvadfsAIKEldtlnnEIVDLQREkNNVe 353
Cdd:pfam05622 246 CAQLQQAELSQADALLS----PSSDPGDNLAAEIMPA--------------------EIRE------KLIRLQHE-NKM- 293

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   354 qdLKEK-EDTIKQRTSEVQdlqdevqrentnlqklqaqkqqvqELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAE 432
Cdd:pfam05622 294 --LRLGqEGSYRERLTELQ------------------------QLLEDANRRKNELETQNRLANQRILELQQQVEELQKA 347

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 67476728   433 LTSQESQ----------ISTYEEELAKAREELSRLQQETAELEESVESGKAQ-LEPLQQHLQDSQQEISSMQ 493
Cdd:pfam05622 348 LQEQGSKaedssllkqkLEEHLEKLHEAQSELQKKKEQIEELEPKQDSNLAQkIDELQEALRKKDEDMKAME 419
PRK12704 PRK12704
phosphodiesterase; Provisional
 331-500 1.16e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 49.01  E-value: 1.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728  331 AIKELDTLNNEIV-----DLQREKNNVEQDLKEKEDTIKQRTSEVQdlqdevQRENtnlqklqaqkqqvqelldeldeqk 405
Cdd:PRK12704  47 AKKEAEAIKKEALleakeEIHKLRNEFEKELRERRNELQKLEKRLL------QKEE------------------------ 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728  406 aQLEEQLKEVRKKcaeeaqlisslKAELTSQESQISTYEEELAKAREELSRLQQET-AELEE----SVESGKAQLepLQQ 480
Cdd:PRK12704  97 -NLDRKLELLEKR-----------EEELEKKEKELEQKQQELEKKEEELEELIEEQlQELERisglTAEEAKEIL--LEK 162

                        170       180
                 ....*....|....*....|
gi 67476728  481 HLQDSQQEISSMqMKLMEMK 500
Cdd:PRK12704 163 VEEEARHEAAVL-IKEIEEE 181
Nuf2_DHR10-like pfam18595
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ...
 344-480 1.23e-05

Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This domain was identified as MazG related domain also designated as Designed helical repeat protein 10 (DHR10) that actually adopts a coiled-coil structure. Nuf2 is part of the Ndc80 complex, which binds to the spindle and is required for chromosome segregation and spindle checkpoint activity.


Pssm-ID: 465814 [Multi-domain]  Cd Length: 117  Bit Score: 45.27  E-value: 1.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   344 DLQREKNNVE------QDLKEKEDTIKQRTSEV-------QDLQDEVQRENtnlqklqaqkqqvqELLDELDEQKAQLEE 410
Cdd:pfam18595   3 TLAEEKEELAelerkaRELQAKIDALQVVEKDLrscikllEEIEAELAKLE--------------EAKKKLKELRDALEE 68

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   411 QLKEVRkkcaeeaqlisslkaELTSQESQIstyEEELAKAREELSRLQQETaelEESVESGKAQLEPLQQ 480
Cdd:pfam18595  69 KEIELR---------------ELERREERL---QRQLENAQEKLERLREQA---EEKREAAQARLEELRE 117
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 404-503 1.24e-05

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 45.29  E-value: 1.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   404 QKAQLEEQLKEVRkkcaEEAQLIsslKAELTSQESQISTYEEELAKAREELSRLQQ-------ETAELEESVESGKAQLE 476
Cdd:pfam20492   7 EKQELEERLKQYE----EETKKA---QEELEESEETAEELEEERRQAEEEAERLEQkrqeaeeEKERLEESAEMEAEEKE 79

                          90       100
                  ....*....|....*....|....*..
gi 67476728   477 PLQQHLQDSQQEISSMQMKlMEMKDLE 503
Cdd:pfam20492  80 QLEAELAEAQEEIARLEEE-VERKEEE 105
PTZ00121 PTZ00121
MAEBL; Provisional
 346-618 1.44e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.98  E-value: 1.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   346 QREKNNVEQdLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLK----------EV 415
Cdd:PTZ00121 1629 EEEKKKVEQ-LKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKkeaeeakkaeEL 1707

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   416 RKKCAEE---------AQLISSLKAE-LTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDS 485
Cdd:PTZ00121 1708 KKKEAEEkkkaeelkkAEEENKIKAEeAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDE 1787

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   486 QQEISSMQMKlMEMKDLENHNSQLNWCSSPHSILVN-------GATDYCSLSTSS--SETANLNEHVEGQSNLESEPIHQ 556
Cdd:PTZ00121 1788 EDEKRRMEVD-KKIKDIFDNFANIIEGGKEGNLVINdskemedSAIKEVADSKNMqlEEADAFEKHKFNKNNENGEDGNK 1866

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 67476728   557 ESPARSSPELLPSgvtDENEVTTAvteKVCSELDNNrhSKEEDPFNVDSSSLTGPVADTNLD 618
Cdd:PTZ00121 1867 EADFNKEKDLKED---DEEEIEEA---DEIEKIDKD--DIEREIPNNNMAGKNNDIIDDKLD 1920
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 332-508 1.44e-05

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 48.89  E-value: 1.44e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    332 IKELDTLNNEI----VDLQREKNNVEQDLKEKEdTIKQRTSEVQDLQDEV------QRENTNLQKLQAQKQQVQELLD-- 399
Cdd:TIGR00606  743 EKEIPELRNKLqkvnRDIQRLKNDIEEQETLLG-TIMPEEESAKVCLTDVtimerfQMELKDVERKIAQQAAKLQGSDld 821

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    400 ----ELDEQKAQLEEQLK------EVRKKCAEEAQ-LISSLKA---ELTSQESQISTYEEELAKAREELSRLQQETAELE 465
Cdd:TIGR00606  822 rtvqQVNQEKQEKQHELDtvvskiELNRKLIQDQQeQIQHLKSktnELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLI 901

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 67476728    466 ESVESGKAQLEPLQQHLQDSQQEissmQMKLMEMKDLENHNSQ 508
Cdd:TIGR00606  902 REIKDAKEQDSPLETFLEKDQQE----KEELISSKETSNKKAQ 940
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 396-496 1.48e-05

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: 47.23  E-value: 1.48e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 396 ELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKARE---------ELSRLQQETA---- 462
Cdd:COG1579  24 HRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlgnvrnnkEYEALQKEIEslkr 103

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 67476728 463 ----------ELEESVESGKAQLEPLQQHLQDSQQEISSMQMKL 496
Cdd:COG1579 104 risdledeilELMERIEELEEELAELEAELAELEAELEEKKAEL 147
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
 335-487 1.56e-05

Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.


Pssm-ID: 460211 [Multi-domain]  Cd Length: 175  Bit Score: 46.10  E-value: 1.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   335 LDTLNNEIVDLQREKNNVEQDLKEKedtikqRTSEVQDLQDEVQREntnlqklqaqkqqvqelldeLDEQKAQLEEQLKE 414
Cdd:pfam01442   6 LDELSTYAEELQEQLGPVAQELVDR------LEKETEALRERLQKD--------------------LEEVRAKLEPYLEE 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   415 VRKKCAEEAQLissLKAELtsqESQISTYEEELAKAREELSR-LQQETAELEESVESG----KAQLEP--------LQQH 481
Cdd:pfam01442  60 LQAKLGQNVEE---LRQRL---EPYTEELRKRLNADAEELQEkLAPYGEELRERLEQNvdalRARLAPyaeelrqkLAER 133


                  ....*.
gi 67476728   482 LQDSQQ 487
Cdd:pfam01442 134 LEELKE 139
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 320-504 1.63e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 48.91  E-value: 1.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    320 IIGSSPVADFSAIKELdtlnNEIVDLQREKnnveQDLKEKEDTIKQRTSEVQDLQDEVQREntnlqklqaqkqqvqelLD 399
Cdd:TIGR02169  147 FISMSPVERRKIIDEI----AGVAEFDRKK----EKALEELEEVEENIERLDLIIDEKRQQ-----------------LE 201

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    400 ELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQ----ESQISTYEEELAKAREELSRLQQETAELEESVESGKAQL 475
Cdd:TIGR02169  202 RLRREREKAERYQALLKEKREYEGYELLKEKEALERQkeaiERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKI 281

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 67476728    476 EPL--------QQHLQDSQQEISSMQ----MKLMEMKDLEN 504
Cdd:TIGR02169  282 KDLgeeeqlrvKEKIGELEAEIASLErsiaEKERELEDAEE 322
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 349-496 1.74e-05

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: 46.98  E-value: 1.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   349 KNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEaqLISS 428
Cdd:pfam04012  10 RANIHEGLDKAEDPEKMLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGNEE--LARE 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 67476728   429 LKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQqhlqdSQQEISSMQMKL 496
Cdd:pfam04012  88 ALAEKKSLEKQAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLK-----ARLKAAKAQEAV 150
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
397-509 2.14e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.23  E-value: 2.14e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 397 LLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLE 476
Cdd:COG4717  47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 67476728 477 P---------LQQHLQDSQQEISSMQMKLMEMKDLENHNSQL 509
Cdd:COG4717 127 LlplyqeleaLEAELAELPERLEELEERLEELRELEEELEEL 168
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 334-468 2.16e-05

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 48.15  E-value: 2.16e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 334 ELDTLNNEIVDLQREKNNVEqdlKEKEDTIKQRtsevqdlqdevqrentnlqklqaqkqqvqelLDELDEQKAQLEEQLK 413
Cdd:COG0542 412 ELDELERRLEQLEIEKEALK---KEQDEASFER-------------------------------LAELRDELAELEEELE 457

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 67476728 414 EVRKKCAEEAQLIS---SLKAELTSQESQISTYEEELAKAREELSrlqQETAELEESV 468
Cdd:COG0542 458 ALKARWEAEKELIEeiqELKEELEQRYGKIPELEKELAELEEELA---ELAPLLREEV 512
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 326-500 2.60e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 48.14  E-value: 2.60e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    326 VADFSAikELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQK 405
Cdd:TIGR02169  296 IGELEA--EIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAEL 373

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    406 AQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTY-------EEELAKAREELSRLQQETAELEESVESGKAQLEPL 478
Cdd:TIGR02169  374 EEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLqeelqrlSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQ 453

                          170       180
                   ....*....|....*....|..
gi 67476728    479 QQHLQDSQQEISSMQMKLMEMK 500
Cdd:TIGR02169  454 EWKLEQLAADLSKYEQELYDLK 475
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 419-509 2.80e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 47.45  E-value: 2.80e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 419 CAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLME 498
Cdd:COG4942  15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94

                        90
                ....*....|..
gi 67476728 499 M-KDLENHNSQL 509
Cdd:COG4942  95 LrAELEAQKEEL 106
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
333-510 2.88e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.14  E-value: 2.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728  333 KELDTLNNEIVDLQR---EKNNVE---QDLKEKEDTIKQRTSE----VQDLQD----EVQRENTNLQKLQAQKQQVQELL 398
Cdd:PRK03918 314 KRLSRLEEEINGIEErikELEEKEerlEELKKKLKELEKRLEEleerHELYEEakakKEELERLKKRLTGLTPEKLEKEL 393

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728  399 DELDEQKAQLEEQLKEVRKKCAEEAQLISSLKA-----------------ELTSQESqistyEEELAKAREELSRLQQET 461
Cdd:PRK03918 394 EELEKAKEEIEEEISKITARIGELKKEIKELKKaieelkkakgkcpvcgrELTEEHR-----KELLEEYTAELKRIEKEL 468

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 67476728  462 AELEESVESGKAQLEPLQQHLQDsQQEISSMQMKLMEMKDLENHNSQLN 510
Cdd:PRK03918 469 KEIEEKERKLRKELRELEKVLKK-ESELIKLKELAEQLKELEEKLKKYN 516
46 PHA02562
endonuclease subunit; Provisional
 334-498 3.44e-05

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 47.32  E-value: 3.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728  334 ELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQ--RENTNLQKLQAQKQQVQELLDELDEQKAQLEEQ 411
Cdd:PHA02562 235 EIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKmyEKGGVCPTCTQQISEGPDRITKIKDKLKELQHS 314

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728  412 LKEVRKKCAEEAQLISSLKA---ELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQE 488
Cdd:PHA02562 315 LEKLDTAIDELEEIMDEFNEqskKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKT 394

                        170
                 ....*....|
gi 67476728  489 ISSMQMKLME 498
Cdd:PHA02562 395 KSELVKEKYH 404
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 336-505 3.62e-05

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


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 47.20  E-value: 3.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   336 DTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRentnlqkLQAQKQQVQELLDELDEQKAQLEEQLKEV 415
Cdd:pfam07888 111 EELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELER-------MKERAKKAGAQRKEEEAERKQLQAKLQQT 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   416 RKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESvesgKAQLEPLQQHLQDSQQEISSMQMK 495
Cdd:pfam07888 184 EEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEAL----LEELRSLQERLNASERKVEGLGEE 259

                         170
                  ....*....|
gi 67476728   496 LMEMKDLENH 505
Cdd:pfam07888 260 LSSMAAQRDR 269
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
 398-489 4.05e-05

Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.


Pssm-ID: 460211 [Multi-domain]  Cd Length: 175  Bit Score: 44.95  E-value: 4.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   398 LDELDEQKAQLEEQL----KEVRKKCAEEAQ-LISSLKAELTSQESQISTYEEEL-AKAREELSRLQQETAEL-EESVES 470
Cdd:pfam01442   6 LDELSTYAEELQEQLgpvaQELVDRLEKETEaLRERLQKDLEEVRAKLEPYLEELqAKLGQNVEELRQRLEPYtEELRKR 85

                          90
                  ....*....|....*....
gi 67476728   471 GKAQLEPLQQHLQDSQQEI 489
Cdd:pfam01442  86 LNADAEELQEKLAPYGEEL 104
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 330-517 4.55e-05

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: 47.27  E-value: 4.55e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    330 SAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQREntnlqklqaqKQQVQELLDELDEQKAQLE 409
Cdd:TIGR00618  553 SERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKL----------SEAEDMLACEQHALLRKLQ 622

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    410 EQLKEVRKKcAEEAQLISSLKAELTSQESqistYEEELAKAREELS--RLQQETAELEESVESGKAQLEPLQQHLQDSQQ 487
Cdd:TIGR00618  623 PEQDLQDVR-LHLQQCSQELALKLTALHA----LQLTLTQERVREHalSIRVLPKELLASRQLALQKMQSEKEQLTYWKE 697

                          170       180       190
                   ....*....|....*....|....*....|..
gi 67476728    488 EISSMQMKLMEMKDLENHNSQL--NWCSSPHS 517
Cdd:TIGR00618  698 MLAQCQTLLRELETHIEEYDREfnEIENASSS 729
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
344-508 4.71e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 47.34  E-value: 4.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728  344 DLQREKNNVeqdLKEKEDTIKQRtsEVQDLQDEVQRENTnlqklqaQKQQVQELLDELDEQKAQLEEQL---KEVRKKCA 420
Cdd:PRK02224 180 RVLSDQRGS---LDQLKAQIEEK--EEKDLHERLNGLES-------ELAELDEEIERYEEQREQARETRdeaDEVLEEHE 247

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728  421 EEAQLISSLKAELTSQESQISTYE-------EELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQ 493
Cdd:PRK02224 248 ERREELETLEAEIEDLRETIAETErereelaEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELR 327

                        170
                 ....*....|....*.
gi 67476728  494 MKLMEMK-DLENHNSQ 508
Cdd:PRK02224 328 DRLEECRvAAQAHNEE 343
46 PHA02562
endonuclease subunit; Provisional
 328-509 4.73e-05

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 46.93  E-value: 4.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728  328 DFSAIKELDTLNNeivDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENT-NLQKLQAQKQQVQELLDELDEQKA 406
Cdd:PHA02562 161 DISVLSEMDKLNK---DKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGeNIARKQNKYDELVEEAKTIKAEIE 237

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728  407 QLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKARE---------ELSRLQQETAELEESVESGKAQLEP 477
Cdd:PHA02562 238 ELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKggvcptctqQISEGPDRITKIKDKLKELQHSLEK 317

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 67476728  478 LQQHLQDSQQ---EISSMQMKLMEMK-DLENHNSQL 509
Cdd:PHA02562 318 LDTAIDELEEimdEFNEQSKKLLELKnKISTNKQSL 353
CENP-F_leu_zip pfam10473
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ...
 402-502 4.83e-05

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


Pssm-ID: 463102 [Multi-domain]  Cd Length: 140  Bit Score: 44.21  E-value: 4.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   402 DEQKAQLEEQLKEVRKKCAEEAQLISSLKAEL-TSQESQ------ISTYEEELAKAREELSRLQQETAELEESVESGKAQ 474
Cdd:pfam10473   2 EKKQLHVLEKLKESERKADSLKDKVENLERELeMSEENQelaileAENSKAEVETLKAEIEEMAQNLRDLELDLVTLRSE 81

                          90       100
                  ....*....|....*....|....*...
gi 67476728   475 LEPLQQHLQDSQQEISSMQMKLMEMKDL 502
Cdd:pfam10473  82 KENLTKELQKKQERVSELESLNSSLENL 109
DUF3450 pfam11932
Protein of unknown function (DUF3450); This family of proteins are functionally ...
 396-489 5.11e-05

Protein of unknown function (DUF3450); This family of proteins are functionally uncharacterized. This protein is found in bacteria and eukaryotes. Proteins in this family are about 260 amino acids in length.


Pssm-ID: 432198 [Multi-domain]  Cd Length: 238  Bit Score: 45.69  E-value: 5.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   396 ELLDELDEQKAQLEEQLKevrkkcaeeaqlisSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEEsvesGKAQL 475
Cdd:pfam11932  34 KKIDKWDDEKQELLAEYR--------------ALKAELESLEVYNRQLERLVASQEQEIASLERQIEEIER----TEREL 95

                          90
                  ....*....|....
gi 67476728   476 EPLQQHLQDSQQEI 489
Cdd:pfam11932  96 VPLMLKMLDRLEQF 109
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 333-468 5.26e-05

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 46.94  E-value: 5.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   333 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEvqrentnlqklqaqkqqvqelLDELDEQKAQLEEQL 412
Cdd:TIGR04523 561 KEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKE---------------------IEEKEKKISSLEKEL 619

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 67476728   413 KEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESV 468
Cdd:TIGR04523 620 EKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKI 675
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 398-501 5.88e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.97  E-value: 5.88e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    398 LDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEP 477
Cdd:TIGR02168  679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758

                           90       100
                   ....*....|....*....|....
gi 67476728    478 LQQHLQDSQQEISSMQMKLMEMKD 501
Cdd:TIGR02168  759 LEAEIEELEERLEEAEEELAEAEA 782
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 346-488 6.26e-05

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 43.37  E-value: 6.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   346 QREKNNVEQDLKEKEDTIKQRTsevQDLQDEVQRentnlqklqaqkqqvqelLDELDEQ--KAQLEEQLKEVRKKCAEEA 423
Cdd:pfam20492   5 EREKQELEERLKQYEEETKKAQ---EELEESEET------------------AEELEEErrQAEEEAERLEQKRQEAEEE 63

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 67476728   424 qlisslKAELtsQESQISTyEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQE 488
Cdd:pfam20492  64 ------KERL--EESAEME-AEEKEQLEAELAEAQEEIARLEEEVERKEEEARRLQEELEEAREE 119
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
 396-494 6.76e-05

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 46.87  E-value: 6.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   396 ELLDELDEQKAQLEEQLKEVrkkcAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAEleesvesgkAQL 475
Cdd:PRK11448  146 ALQQEVLTLKQQLELQAREK----AQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAE---------TSQ 212

                          90
                  ....*....|....*....
gi 67476728   476 EPLQQHLQDSQQEISSMQM 494
Cdd:PRK11448  213 ERKQKRKEITDQAAKRLEL 231
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
334-489 7.08e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 46.57  E-value: 7.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728  334 ELDTLNNEIVDLQREknNVEQDLKEKEDTIKQRTSEVQDLQDEVQREntnlqklqaqkqqvQELLDELDEQKAQLEEQLK 413
Cdd:PRK02224 303 GLDDADAEAVEARRE--ELEDRDEELRDRLEECRVAAQAHNEEAESL--------------REDADDLEERAEELREEAA 366

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 67476728  414 EVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEI 489
Cdd:PRK02224 367 ELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERV 442
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 333-583 7.34e-05

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 46.65  E-value: 7.34e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    333 KELDTLNNEIVDLQREKNNVEQDLK-----------EKEDTIKQRTSEVQDLQDEVQR--------ENTNLQKLQAQKQQ 393
Cdd:pfam15921  653 QERDQLLNEVKTSRNELNSLSEDYEvlkrnfrnkseEMETTTNKLKMQLKSAQSELEQtrntlksmEGSDGHAMKVAMGM 732

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    394 VQEL------LDELDEQKAQLEEQLKEVRKkcaeEAQLISSLKAELTSQESQISTYEEELAKAREEL----SRLQQETAE 463
Cdd:pfam15921  733 QKQItakrgqIDALQSKIQFLEEAMTNANK----EKHFLKEEKNKLSQELSTVATEKNKMAGELEVLrsqeRRLKEKVAN 808

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    464 LEESVESGKAQLEPLQQHLQDSQQEisSMQMKL---MEMKDLENHNSQLNWCSSPHSILVNGATDYCSLSTSSSETANLN 540
Cdd:pfam15921  809 MEVALDKASLQFAECQDIIQRQEQE--SVRLKLqhtLDVKELQGPGYTSNSSMKPRLLQPASFTRTHSNVPSSQSTASFL 886

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 67476728    541 EHVEGQSNlesepIHQESPARSSPELLP---SGVTDENEVTTAVTE 583
Cdd:pfam15921  887 SHHSRKTN-----ALKEDPTRDLKQLLQelrSVINEEPTVQLSKAE 927
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 328-505 7.82e-05

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 46.64  E-value: 7.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   328 DFSAIKELDTlnneivDLQREKNNVEQDLK-------EKEDTIKQRTSEVQDLQDEVQR--ENTNlqklqaqkqQVQELL 398
Cdd:pfam05483 220 DHEKIQHLEE------EYKKEINDKEKQVSllliqitEKENKMKDLTFLLEESRDKANQleEKTK---------LQDENL 284

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   399 DELDEQKAQLEEQLKEVR----------KKCAEEAQLISSLKAELTSQ-ESQIstyeEELAKAREE----LSRLQQETAE 463
Cdd:pfam05483 285 KELIEKKDHLTKELEDIKmslqrsmstqKALEEDLQIATKTICQLTEEkEAQM----EELNKAKAAhsfvVTEFEATTCS 360

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 67476728   464 LEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKDLENH 505
Cdd:pfam05483 361 LEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNN 402
DUF4515 pfam14988
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ...
 349-494 8.43e-05

Domain of unknown function (DUF4515); This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 198 and 469 amino acids in length. There are two completely conserved L residues that may be functionally important.


Pssm-ID: 405647 [Multi-domain]  Cd Length: 206  Bit Score: 44.76  E-value: 8.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   349 KNNVEQDLKEKEDTIKQRTSEVQDLQDEVQrentnlqklqaqkqqvqELLDELDEQKAQLEEQLKEVRKkcaEEAQL--- 425
Cdd:pfam14988  10 AKKTEEKQKKIEKLWNQYVQECEEIERRRQ-----------------ELASRYTQQTAELQTQLLQKEK---EQASLkke 69

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 67476728   426 ------ISSLKAeltSQESQISTYEEELAKAREELSRLQQETaeleesvesgKAQLEPLQQHLQDSQQEISSMQM 494
Cdd:pfam14988  70 lqalrpFAKLKE---SQEREIQDLEEEKEKVRAETAEKDREA----------HLQFLKEKALLEKQLQELRILEL 131
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 342-501 8.71e-05

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: 45.68  E-value: 8.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   342 IVDLQREKNNVEQDLK-EKEDTIKQRTSEVQDLQDEVQREntnlqklqaqkQQVQELLDELDEQKAQlEEQLKEVRKKCA 420
Cdd:pfam13868 157 ILEYLKEKAEREEEREaEREEIEEEKEREIARLRAQQEKA-----------QDEKAERDELRAKLYQ-EEQERKERQKER 224

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   421 EEAQLISSLKAELT-SQESQIS----TYEEELAKAREELSRLQQETAELEEsvesgKAQLEPLQQHLQDSQ--QEISSM- 492
Cdd:pfam13868 225 EEAEKKARQRQELQqAREEQIElkerRLAEEAEREEEEFERMLRKQAEDEE-----IEQEEAEKRRMKRLEhrRELEKQi 299

                         170
                  ....*....|...
gi 67476728   493 ----QMKLMEMKD 501
Cdd:pfam13868 300 eereEQRAAEREE 312
PRK09039 PRK09039
peptidoglycan -binding protein;
333-510 1.05e-04

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 45.34  E-value: 1.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728  333 KELDTLNNEIVDL------QREKNnveQDLKEKEDTIKQRTSEVQDLQDEVQrentnlqklqaqkqqvqELLDELDEQKA 406
Cdd:PRK09039  53 SALDRLNSQIAELadllslERQGN---QDLQDSVANLRASLSAAEAERSRLQ-----------------ALLAELAGAGA 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728  407 QLEEQLKEvrkkcaeeaqlissLKAELTSQEsQIStyeeelAKAREELSRLQQETAELeesvesgKAQLEPLQQHLQDSQ 486
Cdd:PRK09039 113 AAEGRAGE--------------LAQELDSEK-QVS------ARALAQVELLNQQIAAL-------RRQLAALEAALDASE 164

                        170       180
                 ....*....|....*....|....
gi 67476728  487 QEISSMQMKLmemKDLenhNSQLN 510
Cdd:PRK09039 165 KRDRESQAKI---ADL---GRRLN 182
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 314-509 1.23e-04

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 45.19  E-value: 1.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   314 ASLQKNIIGSSPVADFSAIKELDT-----LNNEIVDLQREKNNVEQdlKEKEDTIKQRTSEVQdLQdEVQREntnlqklq 388
Cdd:pfam15905 125 ASLEKQLLELTRVNELLKAKFSEDgtqkkMSSLSMELMKLRNKLEA--KMKEVMAKQEGMEGK-LQ-VTQKN-------- 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   389 aqkqqvqelLDELDEQKAQLEEQLKEVRKKCAEEaqlisslkaelTSQESQISTYEEELAKAREELSRLQQETAELEESV 468
Cdd:pfam15905 193 ---------LEHSKGKVAQLEEKLVSTEKEKIEE-----------KSETEKLLEYITELSCVSEQVEKYKLDIAQLEELL 252

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 67476728   469 ESGKAQLEPLQQHLQDSQQEISSMQMKLME-MKDLENHNSQL 509
Cdd:pfam15905 253 KEKNDEIESLKQSLEEKEQELSKQIKDLNEkCKLLESEKEEL 294
YscO-like pfam16789
YscO-like protein; This family of proteins is similar to the type III secretion protein YscO. ...
 345-501 1.25e-04

YscO-like protein; This family of proteins is similar to the type III secretion protein YscO. The family includes Chlamydia trachomatis CT670 which is found in a type III secretion gene cluster. CT670 interacts with CT671, a putative YscP homolog and CT670 and CT671 may form a chaperone-effector pair.


Pssm-ID: 435583 [Multi-domain]  Cd Length: 160  Bit Score: 43.29  E-value: 1.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   345 LQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNlqklqaqkqqvqellDELDEQKA---QLEEQLKEVRKKCAE 421
Cdd:pfam16789  30 LEKEKEKLAELEAERDKVRKHKKAKMQQLRDEMDRGTTS---------------DKILQMKRyikVVKERLKQEEKKVQD 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   422 eaqlisslkaeltsQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKD 501
Cdd:pfam16789  95 --------------QKEQVRTAARNLEIAREELKKKRQEVEKLEKHKKEWVKEMKKEEEDQEEREQDEIGSALHLANQRK 160
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
341-506 1.32e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 45.80  E-value: 1.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728  341 EIVDLQREKNNVEQDLkEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVR---- 416
Cdd:PRK02224 573 EVAELNSKLAELKERI-ESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARieea 651

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728  417 ---KKCAEEAQL-----ISSLKAELTSQESQISTYEEELakarEELSRLQQETAELEESV---ESGKAQLEPLQQHLQD- 484
Cdd:PRK02224 652 redKERAEEYLEqveekLDELREERDDLQAEIGAVENEL----EELEELRERREALENRVealEALYDEAEELESMYGDl 727

                        170       180
                 ....*....|....*....|....*.
gi 67476728  485 ----SQQEISSMQMKLMEMKDLENHN 506
Cdd:PRK02224 728 raelRQRNVETLERMLNETFDLVYQN 753
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
165-287 1.39e-04

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 42.86  E-value: 1.39e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 165 LGRVWELSDIDHDGMLDRDEFAvAMFLVYCALEKEPVPmSLPPALVPPSKRKTWVVSPAEK---AKYDEIFLKTDKDMDG 241
Cdd:COG5126   7 LDRRFDLLDADGDGVLERDDFE-ALFRRLWATLFSEAD-TDGDGRISREEFVAGMESLFEAtvePFARAAFDLLDTDGDG 84

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 67476728 242 FVSGLEVREIFLKTGLPSTLLAHIWSLCDTKDCGKLSKDQFALAFH 287
Cdd:COG5126  85 KISADEFRRLLTALGVSEEEADELFARLDTDGDGKISFEEFVAAVR 130
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 397-496 1.42e-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: 1.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   397 LLDELDEQKaQLEEQLKEVRKKCAEEAQLISSlkaelTSQESQISTyeEELAKAREELSRLQQETAELE---ESVESGKA 473
Cdd:pfam13851  21 TRNNLELIK-SLKEEIAELKKKEERNEKLMSE-----IQQENKRLT--EPLQKAQEEVEELRKQLENYEkdkQSLKNLKA 92

                          90       100
                  ....*....|....*....|...
gi 67476728   474 QLEPLQQHLQDSQQEISSMQMKL 496
Cdd:pfam13851  93 RLKVLEKELKDLKWEHEVLEQRF 115
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 340-499 1.48e-04

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 43.97  E-value: 1.48e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 340 NEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQV-QELLDELDEQKAQLEEQLKEVRK- 417
Cdd:cd00176  33 ESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLEELNQRwEELRELAEERRQRLEEALDLQQFf 112

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 418 -KCAEEAQLISSLKAELTSQE------------SQISTYEEELAKAREELSRLQQETAELEESVESG-----KAQLEPLQ 479
Cdd:cd00176 113 rDADDLEQWLEEKEAALASEDlgkdlesveellKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDadeeiEEKLEELN 192

                       170       180
                ....*....|....*....|
gi 67476728 480 QHLQDSQQEISSMQMKLMEM 499
Cdd:cd00176 193 ERWEELLELAEERQKKLEEA 212
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 338-509 1.53e-04

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 45.48  E-value: 1.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   338 LNNEI---------VDLQREKNNVEQDLKEKEDTIKqrtseVQDLQDEVQRE-NTNLQKLQAQKQQVQE----------L 397
Cdd:pfam05483 188 LNNNIekmilafeeLRVQAENARLEMHFKLKEDHEK-----IQHLEEEYKKEiNDKEKQVSLLLIQITEkenkmkdltfL 262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   398 LDELDEQKAQLEEQ-------LKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQET-AELEES-- 467
Cdd:pfam05483 263 LEESRDKANQLEEKtklqdenLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKeAQMEELnk 342

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 67476728   468 --------VESGKAQLEPLQQHLQDSQQ--EISSMQMKLMEMkDLENHNSQL 509
Cdd:pfam05483 343 akaahsfvVTEFEATTCSLEELLRTEQQrlEKNEDQLKIITM-ELQKKSSEL 393
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 336-509 1.67e-04

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 45.49  E-value: 1.67e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    336 DTLNNEIVDL-QREKnnvEQDLKEKED------------TIKQRTSEVQDLQDEVQRentnlqklqaqkqqVQELLDEL- 401
Cdd:pfam15921  377 DQLQKLLADLhKREK---ELSLEKEQNkrlwdrdtgnsiTIDHLRRELDDRNMEVQR--------------LEALLKAMk 439

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    402 DEQKAQLEEQLKEVRKKcAEEAQLISSLKAELTSQesqistyEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQH 481
Cdd:pfam15921  440 SECQGQMERQMAAIQGK-NESLEKVSSLTAQLEST-------KEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERA 511

                          170       180       190
                   ....*....|....*....|....*....|..
gi 67476728    482 LQDSQQEISSMQ----MKLMEMKDLENHNSQL 509
Cdd:pfam15921  512 IEATNAEITKLRsrvdLKLQELQHLKNEGDHL 543
STAT5_CCD cd16855
Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family ...
 406-509 1.69e-04

Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family consists of the coiled-coil (alpha) domain of the STAT5 proteins (Signal Transducer and Activator of Transcription 5, or Signal Transduction And Transcription 5) which include STAT5A and STAT5B, both of which are >90% identical despite being encoded by separate genes. The coiled-coil domain (CCD) of STAT5A and STAT5B appears to be required for constitutive nuclear localization signals (NLS) function; small deletions within the CCD can abrogate nuclear import. Studies show that the CCD binds to the importin-alpha3 NLS adapter in most cells. STAT5A and STAT5B regulate erythropoiesis, lymphopoiesis, and the maintenance of the hematopoietic stem cell population. STAT5A and STAT5B have overlapping and redundant functions; both isoforms can be activated by the same set of cytokines, but some cytokines preferentially activate either STAT5A or STAT5B, e.g. during pregnancy and lactation, STAT5A rather than STAT5B is required for the production of luminal progenitor cells from mammary stem cells and is essential for the differentiation of milk producing alveolar cells during pregnancy. STAT5 has been found to be constitutively phosphorylated in cancer cells, and therefore constantly activated, either by aberrant cell signaling expression or by mutations. It differentially regulates cellular behavior in human mammary carcinoma. Prolactin (PRL) in the prostate gland can induce growth and survival of prostate cancer cells and tissues through the activation of STAT5, its downstream target; PRL expression and STAT5 activation correlates with disease severity. STAT5A and STAT5B are central signaling molecules in leukemias driven by Abelson fusion tyrosine kinases, displaying unique nuclear shuttling mechanisms and having a key role in resistance of leukemic cells against treatment with tyrosine kinase inhibitors (TKI). In addition, STAT5A and STAT5B promote survival of leukemic stem cells. STAT5 is a key transcription factor for IL-3-mediated inhibition of RANKL-induced osteoclastogenesis via the induction of the expression of Id genes. Autosomal recessive STAT5B mutations are associated with severe growth failure, insulin-like growth factor (IGF) deficiency and growth hormone insensitivity (GHI) syndrome. STAT5B deficiency can lead to potentially fatal primary immunodeficiency.


Pssm-ID: 341080 [Multi-domain]  Cd Length: 194  Bit Score: 43.41  E-value: 1.69e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 406 AQLEEQLKEVRKKCAEEAQLISSLKAEltsQESQISTYEEeLAKAREELSRLQ-QETAELEESVESGKAQLEPLQQHLQD 484
Cdd:cd16855   4 LEIRQQLEELRQRTQETENDLRNLQQK---QESFVIQYQE-SQKIQAQLQQLQqQPQNERIELEQQLQQQKEQLEQLLNA 79

                        90       100
                ....*....|....*....|....*.
gi 67476728 485 SQQEISSMQMKLME-MKDLENHNSQL 509
Cdd:cd16855  80 KAQELLQLRMELADkFKKTIQLLSKL 105
DUF1090 pfam06476
Protein of unknown function (DUF1090); This family consists of several bacterial proteins of ...
 404-489 1.74e-04

Protein of unknown function (DUF1090); This family consists of several bacterial proteins of unknown function and is known as YqjC in E. coli.


Pssm-ID: 428965 [Multi-domain]  Cd Length: 109  Bit Score: 41.84  E-value: 1.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   404 QKAQLEEQLKEVRKKCAEEaqlisSLKAEltsqesqistYEEELAKAREELSRLQqetAELEESVESGKAQL-EPLQQHL 482
Cdd:pfam06476  39 RVAGLEKALAEVRAHCTDA-----GLRAE----------RQQKVAEKREEVAERE---AELAEAQAKGDADKiAKRQRKL 100


                  ....*..
gi 67476728   483 QDSQQEI 489
Cdd:pfam06476 101 AEARQEL 107
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 333-506 1.93e-04

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 45.21  E-value: 1.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728  333 KELDTLNNEIVDLqrEKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQL 412
Cdd:PRK04778 256 KEIQDLKEQIDEN--LALLEELDLDEAEEKNEEIQERIDQLYDILEREVKARKYVEKNSDTLPDFLEHAKEQNKELKEEI 333

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728  413 KEVRKK---CAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQ------ 483
Cdd:PRK04778 334 DRVKQSytlNESELESVRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQEKLSEMLQglrkde 413

                        170       180
                 ....*....|....*....|....*
gi 67476728  484 -DSQQEISSMQMKLMEMK-DLENHN 506
Cdd:PRK04778 414 lEAREKLERYRNKLHEIKrYLEKSN 438
DUF4618 pfam15397
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins ...
 313-489 1.95e-04

Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins in this family are typically between 238 and 363 amino acids in length. There are two conserved sequence motifs: EYP and KCTPD.


Pssm-ID: 464704 [Multi-domain]  Cd Length: 258  Bit Score: 44.17  E-value: 1.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   313 RASLQKNII--GSSPVADFSAIKELDTLnneIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQ 390
Cdd:pfam15397  41 RKLLQQYEKfgTIISILEYSNKKQLQQA---KAELQEWEEKEESKLNKLEQQLEQLNAKIQKTQEELNFLSTYKDKEYPV 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   391 KQQVQELL------------DELDEqkaqLEEQLKEVRKKCAEEAQLISslKAELTS-QESQISTYEEEL-AKARE---- 452
Cdd:pfam15397 118 KAVQIANLvrqlqqlkdsqqDELDE----LEEMRRMVLESLSRKIQKKK--EKILSSlAEKTLSPYQESLlQKTRDnqvm 191

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 67476728   453 --ELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEI 489
Cdd:pfam15397 192 lkEIEQFREFIDELEEEIPKLKAEVQQLQAQRQEPREVI 230
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
404-510 2.15e-04

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 44.27  E-value: 2.15e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 404 QKAQLEEQLKEVrkkcaEEAQLISSLKAELTSQESQISTYEEELAKAREELSR---LQQETAELEESVESGKAQLEPLQQ 480
Cdd:COG1566  88 AEAQLAAAEAQL-----ARLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERyqaLYKKGAVSQQELDEARAALDAAQA 162

                        90       100       110
                ....*....|....*....|....*....|
gi 67476728 481 HLQDSQQEISSMQMKLMEMKDLENHNSQLN 510
Cdd:COG1566 163 QLEAAQAQLAQAQAGLREEEELAAAQAQVA 192
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
347-504 2.23e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.05  E-value: 2.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728  347 REKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTnlqklqaqKQQVQELLDELDEqkaqLEEQLKEVRKKCAEE-AQL 425
Cdd:PRK03918 459 AELKRIEKELKEIEEKERKLRKELRELEKVLKKESE--------LIKLKELAEQLKE----LEEKLKKYNLEELEKkAEE 526

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728  426 ISSLKAELTSQESQISTYEEELAKARE----------ELSRLQQETAELE-----------ESVESGKAQLEPLQQH--- 481
Cdd:PRK03918 527 YEKLKEKLIKLKGEIKSLKKELEKLEElkkklaelekKLDELEEELAELLkeleelgfesvEELEERLKELEPFYNEyle 606

                        170       180
                 ....*....|....*....|...
gi 67476728  482 LQDSQQEIssmQMKLMEMKDLEN 504
Cdd:PRK03918 607 LKDAEKEL---EREEKELKKLEE 626
mukB PRK04863
chromosome partition protein MukB;
398-504 2.39e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 44.95  E-value: 2.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   398 LDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKaeltsqeSQISTYEEELAKAREELSRLQ-QETAELEESVESGKaqlE 476
Cdd:PRK04863  994 LEQAEQERTRAREQLRQAQAQLAQYNQVLASLK-------SSYDAKRQMLQELKQELQDLGvPADSGAEERARARR---D 1063

                          90       100       110
                  ....*....|....*....|....*....|..
gi 67476728   477 PLQQHLQDSQQEISSMQMKL----MEMKDLEN 504
Cdd:PRK04863 1064 ELHARLSANRSRRNQLEKQLtfceAEMDNLTK 1095
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 334-503 2.40e-04

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


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 44.50  E-value: 2.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   334 ELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRentnlqklqaqkqqVQELLDELDEQKAQLE---E 410
Cdd:pfam07888 172 ERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITT--------------LTQKLTTAHRKEAENEallE 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   411 QLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAR------------------EELSRLQQETAELEESVESGK 472
Cdd:pfam07888 238 ELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARlqaaqltlqladaslalrEGRARWAQERETLQQSAEADK 317

                         170       180       190
                  ....*....|....*....|....*....|.
gi 67476728   473 AQLEPLQQHLQDSQQeisSMQMKLMEMKDLE 503
Cdd:pfam07888 318 DRIEKLSAELQRLEE---RLQEERMEREKLE 345
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 353-510 2.41e-04

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 45.17  E-value: 2.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    353 EQDLKEKEDTIKQrtseVQDLQDEVQRENTNLQKLQAqkqqvqelldELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAE 432
Cdd:pfam01576    4 EEEMQAKEEELQK----VKERQQKAESELKELEKKHQ----------QLCEEKNALQEQLQAETELCAEAEEMRARLAAR 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    433 -------LTSQESQISTYEEELAKAREELSRLQQETAELEEsvesgkaQLEPLQQHLQDSQQEISSMQMKLMEMKD---- 501
Cdd:pfam01576   70 kqeleeiLHELESRLEEEEERSQQLQNEKKKMQQHIQDLEE-------QLDEEEAARQKLQLEKVTTEAKIKKLEEdill 142


                   ....*....
gi 67476728    502 LENHNSQLN 510
Cdd:pfam01576  143 LEDQNSKLS 151
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
333-469 2.45e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.05  E-value: 2.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728  333 KELDTLNNEIVDLQREKNNVEQDLKEKEDTiKQRTSEVQDLQDEVQREntnlqklqaqkqqvqelLDELDE-----QKA- 406
Cdd:PRK03918 307 DELREIEKRLSRLEEEINGIEERIKELEEK-EERLEELKKKLKELEKR-----------------LEELEErhelyEEAk 368

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 67476728  407 QLEEQLKEVRKKCAEEAqlISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVE 469
Cdd:PRK03918 369 AKKEELERLKKRLTGLT--PEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIE 429
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 332-488 2.57e-04

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 44.96  E-value: 2.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    332 IKELDTLNNEIvdlQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLD--------ELDE 403
Cdd:TIGR00618  713 IEEYDREFNEI---ENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGaelshlaaEIQF 789

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    404 QKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQE-TAELEESVESGKAQLEPLQQHL 482
Cdd:TIGR00618  790 FNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEiTHQLLKYEECSKQLAQLTQEQA 869


                   ....*.
gi 67476728    483 QDSQQE 488
Cdd:TIGR00618  870 KIIQLS 875
Uso1_p115_C pfam04871
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ...
 410-509 2.61e-04

Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular transport factor, Transcytosis associate protein (TAP) and Vesicle docking protein, this myosin-shaped molecule consists of an N-terminal globular head region, a coiled-coil tail which mediates dimerization, and a short C-terminal acidic region. p115 tethers COP1 vesicles to the Golgi by binding the coiled coil proteins giantin (on the vesicles) and GM130 (on the Golgi), via its C-terminal acidic region. It is required for intercisternal transport in the golgi stack. This family consists of the acidic C-terminus, which binds to the golgins giantin and GM130. p115 is thought to juxtapose two membranes by binding giantin with one acidic region, and GM130 with another.


Pssm-ID: 461461 [Multi-domain]  Cd Length: 121  Bit Score: 41.62  E-value: 2.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   410 EQLKEVRKKCAEEAQLISSLKAELTSQESQIstyeEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEI 489
Cdd:pfam04871   1 AKKSELESEASSLKNENTELKAELQELSKQY----NSLEQKESQAKELEAEVKKLEEALKKLKAELSEEKQKEKEKQSEL 76

                          90       100
                  ....*....|....*....|
gi 67476728   490 SSMqmkLMEMKDLENHNSQL 509
Cdd:pfam04871  77 DDL---LLLLGDLEEKVEKY 93
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 437-510 2.73e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.44  E-value: 2.73e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 67476728 437 ESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEM-KDLENHNSQLN 510
Cdd:COG3883  15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAeAEIEERREELG 89
FapA pfam03961
Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta ...
 400-473 3.05e-04

Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta solenoid domain of FapA and its homologs. Members of this family include FapA (flagellar assembly protein A) found in Vibrio vulnificus. The synthesis of flagella allows bacteria to respond to chemotaxis by facilitating motility. Studies examining the role of FapA show that the loss or delocalization of FapA results in a complete failure of the flagellar biosynthesis and motility in response to glucose mediated chemotaxis. The polar localization of FapA is required for flagellar synthesis, and dephosphorylated EIIAGlc (Glucose-permease IIA component) inhibited the polar localization of FapA through direct interaction. This entry shows similarity to pfam03775 suggesting a similar functional role.


Pssm-ID: 461111 [Multi-domain]  Cd Length: 272  Bit Score: 43.44  E-value: 3.05e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 67476728   400 ELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQ-----ESQISTYEEELAKAREELSRLQQETAELEESVESGKA 473
Cdd:pfam03961 153 ELKEKLEELEKELEELEEELEKLKKRLKKLPKKARGQlppekREQLEKLLETKNKLSEELEELEEELKELKEELESLLG 231
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
333-498 3.09e-04

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 43.75  E-value: 3.09e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 333 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENtnlqklqaqkqqvqELLDELDEQKAQLEEQL 412
Cdd:COG1340  15 EKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELR--------------EKRDELNEKVKELKEER 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 413 KEVRKKCAEEAQLISSLKAELtsqeSQISTYEEELAKAREELSRL--QQET---------------AELEESVESGKAQL 475
Cdd:COG1340  81 DELNEKLNELREELDELRKEL----AELNKAGGSIDKLRKEIERLewRQQTevlspeeekelvekiKELEKELEKAKKAL 156

                       170       180
                ....*....|....*....|...
gi 67476728 476 EpLQQHLQDSQQEISSMQMKLME 498
Cdd:COG1340 157 E-KNEKLKELRAELKELRKEAEE 178
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
396-503 3.12e-04

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 43.75  E-value: 3.12e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 396 ELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQL 475
Cdd:COG1340   8 SSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKL 87

                        90       100
                ....*....|....*....|....*...
gi 67476728 476 EPLQQHLQDSQQEISSMQMKLMEMKDLE 503
Cdd:COG1340  88 NELREELDELRKELAELNKAGGSIDKLR 115
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 396-505 3.32e-04

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 43.85  E-value: 3.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    396 ELLDELDEQKAQL---EEQLKEVRKKCAEEAQLISSLKAELTSQESQISTY-EEELAKAREELSRLQQE-------TAEL 464
Cdd:smart00787 151 ENLEGLKEDYKLLmkeLELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCdPTELDRAKEKLKKLLQEimikvkkLEEL 230

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 67476728    465 EESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKDLENH 505
Cdd:smart00787 231 EEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGFTFK 271
mukB PRK04863
chromosome partition protein MukB;
403-509 3.87e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 44.56  E-value: 3.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   403 EQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQ-------- 474
Cdd:PRK04863  530 RQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARapawlaaq 609

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 67476728   475 --LEPLQQH----LQDSQQEISSMQMKLMEMKDLENHNSQL 509
Cdd:PRK04863  610 daLARLREQsgeeFEDSQDVTEYMQQLLERERELTVERDEL 650
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
396-510 3.92e-04

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 43.36  E-value: 3.92e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 396 ELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQL 475
Cdd:COG1340  22 EEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKEL 101

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 67476728 476 EPLQ-------------QHLQDSQQ--------------EISSMQMKLMEMKDLENHNSQLN 510
Cdd:COG1340 102 AELNkaggsidklrkeiERLEWRQQtevlspeeekelveKIKELEKELEKAKKALEKNEKLK 163
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 407-509 3.97e-04

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 44.27  E-value: 3.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    407 QLEEQLKEVRKKCAEEAQLISslKAELtsQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLE---PLQQHLQ 483
Cdd:TIGR00606  710 KLKSTESELKKKEKRRDEMLG--LAPG--RQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGtimPEEESAK 785

                           90       100
                   ....*....|....*....|....*.
gi 67476728    484 DSQQEISSMQMKLMEMKDLENHNSQL 509
Cdd:TIGR00606  786 VCLTDVTIMERFQMELKDVERKIAQQ 811
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
340-476 4.03e-04

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 43.36  E-value: 4.03e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 340 NEIVDLQREKNNVEQDLKEKEDtIKQRTSEVQDLQDEVQRENTNLQKLQaqkqqvqELLDELDEQKAQLEEQLKEVRKKc 419
Cdd:COG1340 140 EKIKELEKELEKAKKALEKNEK-LKELRAELKELRKEAEEIHKKIKELA-------EEAQELHEEMIELYKEADELRKE- 210

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 67476728 420 AEEA-QLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLE 476
Cdd:COG1340 211 ADELhKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEK 268
PRK01156 PRK01156
chromosome segregation protein; Provisional
 316-508 4.50e-04

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 44.12  E-value: 4.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728  316 LQKNIIGSSP----VADFSAIKELDTL-------NNEIVDLQREKNNVEQD---LKEKEDTIKQRTSEVQDLQDEVQREN 381
Cdd:PRK01156 117 IEKNILGISKdvflNSIFVGQGEMDSLisgdpaqRKKILDEILEINSLERNydkLKDVIDMLRAEISNIDYLEEKLKSSN 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728  382 TNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKkcaEEAQLISSLKaELTSQESQISTYEEELAKAREELSRLQQET 461
Cdd:PRK01156 197 LELENIKKQIADDEKSHSITLKEIERLSIEYNNAMD---DYNNLKSALN-ELSSLEDMKNRYESEIKTAESDLSMELEKN 272

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 67476728  462 AELEESVE---------------------SGKAQLEPLQQHLQDSQQEISSMQMKLMEMKDLENHNSQ 508
Cdd:PRK01156 273 NYYKELEErhmkiindpvyknrnyindyfKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYND 340
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 400-488 4.58e-04

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 41.56  E-value: 4.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   400 ELDEQKAQLEEQLK----EVRKKCAEEAQLissLKAELTSQESQISTYEEELAK-----AREELSRLQQ--ETAELEESV 468
Cdd:pfam05672  36 EKEEEERLRKEELRrraeEERARREEEARR---LEEERRREEEERQRKAEEEAEereqrEQEEQERLQKqkEEAEAKARE 112

                          90       100
                  ....*....|....*....|
gi 67476728   469 ESGKAQLEpLQQHLQDSQQE 488
Cdd:pfam05672 113 EAERQRQE-REKIMQQEEQE 131
PRK01156 PRK01156
chromosome segregation protein; Provisional
 341-493 5.47e-04

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 43.74  E-value: 5.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728  341 EIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCA 420
Cdd:PRK01156 581 DIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIA 660

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 67476728  421 EEAQLISSlKAELTSQESQIstyEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQ 493
Cdd:PRK01156 661 EIDSIIPD-LKEITSRINDI---EDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMK 729
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 328-578 5.48e-04

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 43.88  E-value: 5.48e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    328 DFSAIKELDTLNNEIVDLQR----EKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRentnlqklqaqkqqvqelldelde 403
Cdd:TIGR00606  686 VFQTEAELQEFISDLQSKLRlapdKLKSTESELKKKEKRRDEMLGLAPGRQSIIDL------------------------ 741

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    404 qkaqLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTY--EEELAKAREE----LSRLQQETAELEESVESGKAQLE- 476
Cdd:TIGR00606  742 ----KEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTImpEEESAKVCLTdvtiMERFQMELKDVERKIAQQAAKLQg 817

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    477 --------PLQQHLQDSQQEISSMQMKLMEMKDL-ENHNSQLNWCSSPHSILvngATDYCSLSTSSSETANLNEHVEGQS 547
Cdd:TIGR00606  818 sdldrtvqQVNQEKQEKQHELDTVVSKIELNRKLiQDQQEQIQHLKSKTNEL---KSEKLQIGTNLQRRQQFEEQLVELS 894

                          250       260       270
                   ....*....|....*....|....*....|.
gi 67476728    548 NLESEPIHQESPARSspELLPSGVTDENEVT 578
Cdd:TIGR00606  895 TEVQSLIREIKDAKE--QDSPLETFLEKDQQ 923
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 291-560 5.79e-04

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 43.56  E-value: 5.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   291 QKLIKGIDPPHVLTPEMIPPSDRASLQKNIIGSSPVAdfsaIKELDTLNNEIVDLQREKNNVE---QDLKEKEDTI---- 363
Cdd:pfam05483 370 QRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVE----LEELKKILAEDEKLLDEKKQFEkiaEELKGKEQELifll 445

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   364 KQRTSEVQDLQDEVQRENTNLQklqaqkqqvqELLDELDEQKAQLE-EQLKEVrkKCAEEAQLISSLKAELTSQES---- 438
Cdd:pfam05483 446 QAREKEIHDLEIQLTAIKTSEE----------HYLKEVEDLKTELEkEKLKNI--ELTAHCDKLLLENKELTQEASdmtl 513

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   439 QISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEIssmQMKLmemkdlenHNSQLNWCSSPHSI 518
Cdd:pfam05483 514 ELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEV---KCKL--------DKSEENARSIEYEV 582

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 67476728   519 LVNGAtdycSLSTSSSETANLNEHVEGQSNlESEPIHQESPA 560
Cdd:pfam05483 583 LKKEK----QMKILENKCNNLKKQIENKNK-NIEELHQENKA 619
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
 410-502 6.25e-04

Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.


Pssm-ID: 284517 [Multi-domain]  Cd Length: 749  Bit Score: 43.59  E-value: 6.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   410 EQLKEVRKKCAEEAQLisslKAELTSQEsqISTYEEELAKAREELS----RLQQETAELEESVESGKAQLEPLQQHLQDS 485
Cdd:pfam07111 484 EQLREERNRLDAELQL----SAHLIQQE--VGRAREQGEAERQQLSevaqQLEQELQRAQESLASVGQQLEVARQGQQES 557

                          90
                  ....*....|....*..
gi 67476728   486 QQEISSMQMKLMEMKDL 502
Cdd:pfam07111 558 TEEAASLRQELTQQQEI 574
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
 396-498 6.31e-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: 41.36  E-value: 6.31e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 396 ELLDELDEQK---AQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQIStyEEELAKAREELSRLQQEtaeleesvesgk 472
Cdd:COG2825  33 RILQESPEGKaaqKKLEKEFKKRQAELQKLEKELQALQEKLQKEAATLS--EEERQKKERELQKKQQE------------ 98

                        90       100
                ....*....|....*....|....*.
gi 67476728 473 aqlepLQQHLQDSQQEISSMQMKLME 498
Cdd:COG2825  99 -----LQRKQQEAQQDLQKRQQELLQ 119
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 396-502 6.89e-04

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 43.42  E-value: 6.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    396 ELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQiSTYEEELAKAREELSRLQQETAELEESVES----- 470
Cdd:TIGR00618  212 CMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQ-LKKQQLLKQLRARIEELRAQEAVLEETQERinrar 290

                           90       100       110
                   ....*....|....*....|....*....|..
gi 67476728    471 GKAQLEPLQQHLQDSQQEISSMQMKLMEMKDL 502
Cdd:TIGR00618  291 KAAPLAAHIKAVTQIEQQAQRIHTELQSKMRS 322
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 428-509 7.53e-04

Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.


Pssm-ID: 439196 [Multi-domain]  Cd Length: 91  Bit Score: 39.47  E-value: 7.53e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 428 SLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVEsgkaqleplqqHLQDsqqEISSMQM--KLME--MKDLE 503
Cdd:cd22887   1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANE-----------ILND---ELIALQIenNLLEekLRKLQ 66


                ....*.
gi 67476728 504 NHNSQL 509
Cdd:cd22887  67 EENDEL 72
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 334-488 7.57e-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: 43.40  E-value: 7.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728  334 ELDTLNNEIVDLQREKNN---VEQDLKEKEDTIKQRTSEVQDLQDEVqrentnlqkLQAQKQQVQELLDELDEQKAQLEE 410
Cdd:COG3096  837 ELAALRQRRSELERELAQhraQEQQLRQQLDQLKEQLQLLNKLLPQA---------NLLADETLADRLEELREELDAAQE 907

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728  411 QLKEVRKKCAEEAQL---ISSLKAELTSQESQISTYEEelakAREELSRLQQETAELEESVE-------SGKAQL----- 475
Cdd:COG3096  908 AQAFIQQHGKALAQLeplVAVLQSDPEQFEQLQADYLQ----AKEQQRRLKQQIFALSEVVQrrphfsyEDAVGLlgens 983

                        170
                 ....*....|....*.
gi 67476728  476 ---EPLQQHLQDSQQE 488
Cdd:COG3096  984 dlnEKLRARLEQAEEA 999
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 290-493 7.59e-04

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 43.24  E-value: 7.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    290 SQKLIKGIDPPHVLTPEMIPPSDRASLQkniigsspvadfsAIKELDTLNNEIVD-------LQREKNNVEQDLKEKEDT 362
Cdd:pfam01576  831 SEKKLKNLEAELLQLQEDLAASERARRQ-------------AQQERDELADEIASgasgksaLQDEKRRLEARIAQLEEE 897

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    363 IKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAE-EAQLISSLKAELTSQESQIS 441
Cdd:pfam01576  898 LEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEmEGTVKSKFKSSIAALEAKIA 977

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 67476728    442 TYEEEL-AKARE-----ELSR----------LQQE-----TAELEESVESGKAQLEPLQQHLQDSQQEISSMQ 493
Cdd:pfam01576  978 QLEEQLeQESRErqaanKLVRrtekklkevlLQVEderrhADQYKDQAEKGNSRMKQLKRQLEEAEEEASRAN 1050
HBM pfam16591
Helical bimodular sensor domain; The HBM sensor domain has been identified primarily in ...
 332-501 8.00e-04

Helical bimodular sensor domain; The HBM sensor domain has been identified primarily in bacterial chemoreceptors but is also present on histidine kinases. characteriztic features of this domain are its size of approximately 250 amino acids and its location in the bacterial periplasm. The McpS chemoreceptor of Pseudomonas putida KT2440 was found to possess an HBM sensor domain and its 3D structure in complex with physiologically relevant ligands has been reported. This domain is composed of 2 long and 4 short helices that form two modules each composed of a 4-helix bundle. The McpS chemoreceptor mediates chemotaxis towards a number of organic acids. Both modules of the McpS HBM domain contain a ligand binding site. Chemo-attractants binds to each of these sites and their binding was shown to trigger a chemotactic response. This domain is primarily found in different proteobacteria but also in archaea. Interestingly, amino acids in both ligand binding sites showed a high degree of conservation suggesting that members of this family sense similar ligands. This domain recognizes Multiple TCA cycle intermediates, citrate and alpha-ketoglutarate (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 435446 [Multi-domain]  Cd Length: 246  Bit Score: 42.00  E-value: 8.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   332 IKELDTLNNEIVDLQREKNNVE--QDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLE 409
Cdd:pfam16591  42 QKKLDELKQQLQQLKTTFTSPEnvRLLQEQLQLIQAYRKSFNELRAAYESRNASRQVMDSAAERALEAIDQLEAEVLQTP 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   410 EQLKEVrkkcAEEAQLISSLKAEL-------------TSQES------QISTYEEELAKAREEL-----SRLQQETAELE 465
Cdd:pfam16591 122 EADSRR----AAQYQAISELKRQVqmaryqvrgytftPNEDSeqaayqQLDAALASLDQLRQALagdpgAALQQLTSALQ 197

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 67476728   466 E---SVEsgkaQLEPLQQHLQDSQQEISSMQMKLMEMKD 501
Cdd:pfam16591 198 GyrdALD----TFKAAVAAIEQARQEMTSQGDEIVRISD 232
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 333-496 8.19e-04

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 43.29  E-value: 8.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    333 KELDTLNNEIVDLQREKN----NVEQDLKEKEDTIKQRTS---EVQDLQDEVQRentnlqklQAQKQQVQELLDELDEQK 405
Cdd:pfam12128  361 ERLKALTGKHQDVTAKYNrrrsKIKEQNNRDIAGIKDKLAkirEARDRQLAVAE--------DDLQALESELREQLEAGK 432

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    406 AQLEEQLKEVRKKCAEE------AQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQ 479
Cdd:pfam12128  433 LEFNEEEYRLKSRLGELklrlnqATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQAS 512

                          170
                   ....*....|....*..
gi 67476728    480 QHLQDSQQEISSMQMKL 496
Cdd:pfam12128  513 RRLEERQSALDELELQL 529
PRK11281 PRK11281
mechanosensitive channel MscK;
335-510 9.08e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 42.98  E-value: 9.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   335 LDTLNnEIVDLQREKNNVEQDLKEKEDTIKQRtsevqdlqDEVQRENtnlqklqaqkqqvqellDELDEQKAQLEEQLKE 414
Cdd:PRK11281   45 LDALN-KQKLLEAEDKLVQQDLEQTLALLDKI--------DRQKEET-----------------EQLKQQLAQAPAKLRQ 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   415 VRKKcaeeaqlISSLKAELTSQESQ------ISTYEEELAKAREELSRLQQETAELEesvesgkAQLEPLQQHLQDSQQE 488
Cdd:PRK11281   99 AQAE-------LEALKDDNDEETREtlstlsLRQLESRLAQTLDQLQNAQNDLAEYN-------SQLVSLQTQPERAQAA 164

                         170       180
                  ....*....|....*....|..
gi 67476728   489 ISSMQMKLMEMkdlenhNSQLN 510
Cdd:PRK11281  165 LYANSQRLQQI------RNLLK 180
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 431-510 9.25e-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: 42.44  E-value: 9.25e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 431 AELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKL----MEMKDLENHN 506
Cdd:COG4942  13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELaaleAELAELEKEI 92


                ....
gi 67476728 507 SQLN 510
Cdd:COG4942  93 AELR 96
CCCAP pfam15964
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ...
 327-500 9.63e-04

Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.


Pssm-ID: 435040 [Multi-domain]  Cd Length: 703  Bit Score: 42.97  E-value: 9.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   327 ADFSAIKEL---DTLNNEivdLQREKNNVEQDLKEKEDtikQRTSEVQDLQDEVQRENTNLQKLqaqkqqvqelLDELDE 403
Cdd:pfam15964 347 ANFEKTKALiqcEQLKSE---LERQKERLEKELASQQE---KRAQEKEALRKEMKKEREELGAT----------MLALSQ 410

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   404 QKAQLEEQLKEVRKkcaEEAQLISSLKA---ELTSQESQISTYEEELakaREELSRLQQETAELEESVESGKAQlepLQQ 480
Cdd:pfam15964 411 NVAQLEAQVEKVTR---EKNSLVSQLEEaqkQLASQEMDVTKVCGEM---RYQLNQTKMKKDEAEKEHREYRTK---TGR 481

                         170       180
                  ....*....|....*....|
gi 67476728   481 HLQDSQQEISSMQMKLMEMK 500
Cdd:pfam15964 482 QLEIKDQEIEKLGLELSESK 501
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 333-478 9.76e-04

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 43.11  E-value: 9.76e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    333 KELDTLNNEIVDLQREKNNVEQDLKEKE---DTIKQRTSEVQDLQDEVQR----------ENTNLQKLQAQKQQVQELLD 399
Cdd:TIGR00606  501 KEVKSLQNEKADLDRKLRKLDQEMEQLNhhtTTRTQMEMLTKDKMDKDEQirkiksrhsdELTSLLGYFPNKKQLEDWLH 580

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    400 ELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKA---REELSRLQQetaeLEESVESGKAQLE 476
Cdd:TIGR00606  581 SKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVcgsQDEESDLER----LKEEIEKSSKQRA 656


                   ..
gi 67476728    477 PL 478
Cdd:TIGR00606  657 ML 658
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 343-505 1.00e-03

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 43.11  E-value: 1.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    343 VDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQkqqvqelLDELDEQKAQLEEQLKEvRKKCAEE 422
Cdd:TIGR00606  818 SDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSK-------TNELKSEKLQIGTNLQR-RQQFEEQ 889

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    423 AQLISSlkaELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQlepLQQHLQDSQQEISSmqmKLMEMKDL 502
Cdd:TIGR00606  890 LVELST---EVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKK---AQDKVNDIKEKVKN---IHGYMKDI 960


                   ...
gi 67476728    503 ENH 505
Cdd:TIGR00606  961 ENK 963
growth_prot_Scy NF041483
polarized growth protein Scy;
356-493 1.12e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 42.89  E-value: 1.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   356 LKEKEDTIKQR-TSEVQDLQDEVQRENTNLQKLQAqkqqvqELLDEL----DEQKAQLEEQLKEVRKKCAEEAqliSSLK 430
Cdd:NF041483 1119 IRERAEELRDRiTGEIEELHERARRESAEQMKSAG------ERCDALvkaaEEQLAEAEAKAKELVSDANSEA---SKVR 1189

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 67476728   431 -AELTSQESQISTYEEELAKAREELSRLQQET-AELEESVESGKAQLEPLQQHLQDSQQEISSMQ 493
Cdd:NF041483 1190 iAAVKKAEGLLKEAEQKKAELVREAEKIKAEAeAEAKRTVEEGKRELDVLVRRREDINAEISRVQ 1254
Filament pfam00038
Intermediate filament protein;
327-504 1.12e-03

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 42.21  E-value: 1.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   327 ADFSAI-KELDTLNNEIVDLQREKnnveQDLKEKEDTIKQ-RTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQ 404
Cdd:pfam00038 103 NDLVGLrKDLDEATLARVDLEAKI----ESLKEELAFLKKnHEEEVRELQAQVSDTQVNVEMDAARKLDLTSALAEIRAQ 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   405 --------KAQLEE----QLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGK 472
Cdd:pfam00038 179 yeeiaaknREEAEEwyqsKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEERYELQL 258

                         170       180       190
                  ....*....|....*....|....*....|...
gi 67476728   473 AQLEPLQQHLQDSQQEI-SSMQMKLMEMKDLEN 504
Cdd:pfam00038 259 ADYQELISELEAELQETrQEMARQLREYQELLN 291
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 338-495 1.23e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 42.85  E-value: 1.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    338 LNNEIVDLQREKNNVEQDLKEKE-DTIK------QRTSEVQDLQDEVQRENTNLQKLQAQkqqvqelLDELDEQKAQLEE 410
Cdd:pfam01576  431 LAEKLSKLQSELESVSSLLNEAEgKNIKlskdvsSLESQLQDTQELLQEETRQKLNLSTR-------LRQLEDERNSLQE 503

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    411 QL-KEVRKKCAEEAQL------ISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHL- 482
Cdd:pfam01576  504 QLeEEEEAKRNVERQLstlqaqLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELd 583

                          170
                   ....*....|....*....
gi 67476728    483 -----QDSQ-QEISSMQMK 495
Cdd:pfam01576  584 dllvdLDHQrQLVSNLEKK 602
Rcc_KIF21 cd22248
regulatory coiled-coil domain found in the kinesin-like KIF21 family; The KIF21 family ...
 445-494 1.28e-03

regulatory coiled-coil domain found in the kinesin-like KIF21 family; The KIF21 family includes KIF21A and KIF21B. KIF21A (also called kinesin-like protein KIF2, or renal carcinoma antigen NY-REN-62) is a microtubule-binding motor protein involved in neuronal axonal transport. It works as a microtubule stabilizer that regulates axonal morphology, suppressing cortical microtubule dynamics in neurons. Mutations in KIF21A cause congenital fibrosis of the extraocular muscles type 1 (CFEOM1). In vitro, it has a plus-end directed motor activity. KIF21B is a plus-end directed microtubule-dependent motor protein which displays processive activity. It is involved in regulation of microtubule dynamics, synapse function, and neuronal morphology, including dendritic tree branching and spine formation. KIF21B plays a role in learning and memory. It is involved in the delivery of gamma-aminobutyric acid (GABA(A)) receptors to the cell surface. This model corresponds to the regulatory coiled-coil domain of KIF21A/KIF21B, which folds into an intramolecular antiparallel coiled-coil monomer in solution but crystallizes into a dimeric domain-swapped antiparallel coiled-coil.


Pssm-ID: 410202 [Multi-domain]  Cd Length: 81  Bit Score: 38.34  E-value: 1.28e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 67476728 445 EELAKAREELSRLQQE---TAELEESVESGKAQLEPLQQHLQDSQQEIssMQM 494
Cdd:cd22248  27 EKLEKKRERALDEGKDesvLRDLEEEIDSLKANIDYVQENITECQSNI--MQM 77
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 332-503 1.30e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 41.83  E-value: 1.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   332 IKELDTL-----NNEIVDLQ-REKNNVEQDLKEKEDTIKQRTSE--VQDLQDEVQREntnlqklqaqkqqvQELLDELDE 403
Cdd:pfam13868   8 LRELNSKllaakCNKERDAQiAEKKRIKAEEKEEERRLDEMMEEerERALEEEEEKE--------------EERKEERKR 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   404 QKAQLEEQLKEvRKKCAEEAQLISSLKAELTsQESQISTYEEELAKAREELSRLQQETAELEESVEsgkaqlepLQQHLQ 483
Cdd:pfam13868  74 YRQELEEQIEE-REQKRQEEYEEKLQEREQM-DEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNE--------EQAEWK 143

                         170       180
                  ....*....|....*....|
gi 67476728   484 DSQQEissmQMKLMEMKDLE 503
Cdd:pfam13868 144 ELEKE----EEREEDERILE 159
Uso1_p115_C pfam04871
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ...
 344-471 1.35e-03

Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular transport factor, Transcytosis associate protein (TAP) and Vesicle docking protein, this myosin-shaped molecule consists of an N-terminal globular head region, a coiled-coil tail which mediates dimerization, and a short C-terminal acidic region. p115 tethers COP1 vesicles to the Golgi by binding the coiled coil proteins giantin (on the vesicles) and GM130 (on the Golgi), via its C-terminal acidic region. It is required for intercisternal transport in the golgi stack. This family consists of the acidic C-terminus, which binds to the golgins giantin and GM130. p115 is thought to juxtapose two membranes by binding giantin with one acidic region, and GM130 with another.


Pssm-ID: 461461 [Multi-domain]  Cd Length: 121  Bit Score: 39.69  E-value: 1.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   344 DLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEvqrentnlqklqaqkqqvQELLDELDEQKAQLEEQLKEVRKKCAEEA 423
Cdd:pfam04871   5 ELESEASSLKNENTELKAELQELSKQYNSLEQK------------------ESQAKELEAEVKKLEEALKKLKAELSEEK 66

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 67476728   424 QLISSLKAEL-------TSQESQISTYEEELAKAREELSRLQQETAELEESVESG 471
Cdd:pfam04871  67 QKEKEKQSELddlllllGDLEEKVEKYKARLKELGEEVLSDDEDDDEDDEEDDEE 121
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
53-189 1.35e-03

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 39.78  E-value: 1.35e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728  53 LGKIWDLADTDGKGILNKQEFfVALRLVACAQNGLEvslsslnlavppprfHDTSSPLLISGTSAAELPWAVKPED-KAK 131
Cdd:COG5126   7 LDRRFDLLDADGDGVLERDDF-EALFRRLWATLFSE---------------ADTDGDGRISREEFVAGMESLFEATvEPF 70

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 67476728 132 YDAIFDSLSP-VNGFLSGDKVKPVLLNSKLPVDILGRVWELSDIDHDGMLDRDEFAVAM 189
Cdd:COG5126  71 ARAAFDLLDTdGDGKISADEFRRLLTALGVSEEEADELFARLDTDGDGKISFEEFVAAV 129
ALIX_LYPXL_bnd pfam13949
ALIX V-shaped domain binding to HIV; The binding of the LYPxL motif of late HIV p6Gag and EIAV ...
 352-504 1.36e-03

ALIX V-shaped domain binding to HIV; The binding of the LYPxL motif of late HIV p6Gag and EIAV p9Gag to this domain is necessary for viral budding.This domain is generally central between an N-terminal Bro1 domain, pfam03097 and a C-terminal proline-rich domain. The retroviruses thus used this domain to hijack the ESCRT system of the cell.


Pssm-ID: 464053 [Multi-domain]  Cd Length: 294  Bit Score: 41.84  E-value: 1.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   352 VEQDLKEKEDTIKQRTSEVQDLQDEV--QRENTNLQKLQAQKQQVQELLDELDE---QKAQLEEQLKEVRKKCAEEAQLI 426
Cdd:pfam13949  98 VRSKFREHEEDLELLSGPDEDLEAFLpsSRRAKNSPSVEEQVAKLRELLNKLNElkrEREQLLKDLKEKARNDDISPKLL 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   427 SSLKAEL-TSQESQIstYEEELAKAREELSRLQQETA---ELEESVESGKAQLEPLQQHLQDSQQEISSMqmklmeMKDL 502
Cdd:pfam13949 178 LEKARLIaPNQEEQL--FEEELEKYDPLQNRLEQNLHkqeELLKEITEANNEFLQDKRVDSEKQRQREEA------LQKL 249


                  ..
gi 67476728   503 EN 504
Cdd:pfam13949 250 EN 251
PRK11637 PRK11637
AmiB activator; Provisional
 411-494 1.38e-03

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 41.99  E-value: 1.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728  411 QLKEVRKKCAE-------EAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVesgkAQLEplQQhlQ 483
Cdd:PRK11637  48 QLKSIQQDIAAkeksvrqQQQQRASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASI----AKLE--QQ--Q 119

                         90
                 ....*....|.
gi 67476728  484 DSQQEISSMQM 494
Cdd:PRK11637 120 AAQERLLAAQL 130
MscS_porin pfam12795
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...
 398-510 1.39e-03

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


Pssm-ID: 432790 [Multi-domain]  Cd Length: 238  Bit Score: 41.13  E-value: 1.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   398 LDELDEQKaQLEEQLKEVRKKcAEEAQL----ISSLKAELTSQESQISTYEEELAKAREELSRLQQeTAELEESVESGKA 473
Cdd:pfam12795   2 LDELEKAK-LDEAAKKKLLQD-LQQALSlldkIDASKQRAAAYQKALDDAPAELRELRQELAALQA-KAEAAPKEILASL 78

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 67476728   474 QLEPLQQHLQDSQQEISSMQmklmemKDLENHNSQLN 510
Cdd:pfam12795  79 SLEELEQRLLQTSAQLQELQ------NQLAQLNSQLI 109
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 334-501 1.46e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 42.47  E-value: 1.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    334 ELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQREntnlqklqaqkqqvQELLDELDE-------QKA 406
Cdd:pfam01576    6 EMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAE--------------TELCAEAEEmrarlaaRKQ 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    407 QLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQ 486
Cdd:pfam01576   72 ELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLS 151

                          170
                   ....*....|....*
gi 67476728    487 QEISSMQMKLMEMKD 501
Cdd:pfam01576  152 KERKLLEERISEFTS 166
Nnf1 pfam03980
Nnf1; NNF1 is an essential yeast gene that is necessary for chromosome segregation. It is ...
 396-471 1.49e-03

Nnf1; NNF1 is an essential yeast gene that is necessary for chromosome segregation. It is associated with the spindle poles and forms part of a kinetochore subcomplex called MIND.


Pssm-ID: 461118  Cd Length: 103  Bit Score: 38.77  E-value: 1.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   396 ELLDELDEqkaqLEEQLKEvRKKCAEEAQLISSLKAEltsqesQI------STYEEELAKAREELSRLQQETAELEESVE 469
Cdd:pfam03980  33 AKLNELDE----LIEEAKE-RREEGEGPAWRPSVPPE------ELirahlaPYKQKQLEQLNARLQKLEAENAALAEEVQ 101


                  ..
gi 67476728   470 SG 471
Cdd:pfam03980 102 AQ 103
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
 340-459 1.50e-03

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


Pssm-ID: 462316 [Multi-domain]  Cd Length: 129  Bit Score: 39.54  E-value: 1.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   340 NEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKc 419
Cdd:pfam07926   1 AELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQNYERELVLHAEDIKALQALREELNELKAEIAELKAE- 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 67476728   420 AEEAQliSSLKAELTSQESQISTYEEELAKAREELSRLQQ 459
Cdd:pfam07926  80 AESAK--AELEESEESWEEQKKELEKELSELEKRIEDLNE 117
DUF4201 pfam13870
Domain of unknown function (DUF4201); This is a family of coiled-coil proteins from eukaryotes. ...
 333-496 1.53e-03

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


Pssm-ID: 464008 [Multi-domain]  Cd Length: 177  Bit Score: 40.28  E-value: 1.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   333 KELDTLNNEIVDLQREKNNVEQDLKEKEDtIKQRTSEVQDLQdeVQRENTnlqklqaqkqqvqELLDELDEQKAQLEE-- 410
Cdd:pfam13870   6 NELSKLRLELITLKHTLAKIQEKLEQKEE-LGEGLTMIDFLQ--LQIENQ-------------ALNEKIEERNKELKRlk 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   411 --------QLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESveSG----------- 471
Cdd:pfam13870  70 lkvtntvhALTHLKEKLHFLSAELSRLKKELRERQELLAKLRKELYRVKLERDKLRKQNKKLRQQ--GGllhvpallhdy 147

                         170       180
                  ....*....|....*....|....*...
gi 67476728   472 ---KAQLEPLQQHLQDSQQEISSMQMKL 496
Cdd:pfam13870 148 dktKAEVEEKRKSVKKLRRKVKILEMRI 175
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 345-463 1.54e-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: 42.42  E-value: 1.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   345 LQREKNNVEQDLKEKEDTikqRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELL--DELDEQKAQ--------------- 407
Cdd:pfam17380 415 IQQQKVEMEQIRAEQEEA---RQREVRRLEEERAREMERVRLEEQERQQQVERLrqQEEERKRKKlelekekrdrkraee 491

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 67476728   408 -----LEEQLKEVRKKCAEEAQLISSLKAELtsQESQISTYEEELAKAREELSRLQQETAE 463
Cdd:pfam17380 492 qrrkiLEKELEERKQAMIEEERKRKLLEKEM--EERQKAIYEEERRREAEEERRKQQEMEE 550
APG6_N pfam17675
Apg6 coiled-coil region; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. ...
 397-501 1.57e-03

Apg6 coiled-coil region; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. Autophagy is a bulk degradation process induced by starvation in eukaryotic cells. Apg6/Vps30p has two distinct functions in the autophagic process, either associated with the membrane or in a retrieval step of the carboxypeptidase Y sorting pathway.


Pssm-ID: 465452 [Multi-domain]  Cd Length: 127  Bit Score: 39.50  E-value: 1.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   397 LLDELDEQKAQLEEQ-------LKEVRKKCAEEaqlISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEEsve 469
Cdd:pfam17675  10 LLEELDKQLEDAEKErdayisfLKKLEKETPEE---LEELEKELEKLEKEEEELLQELEELEKEREELDAELEALEE--- 83

                          90       100       110
                  ....*....|....*....|....*....|..
gi 67476728   470 sgkaQLEPLQQHLQDSQQEISSMQMKLMEMKD 501
Cdd:pfam17675  84 ----ELEALDEEEEEFWREYNALQLQLLEFQD 111
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 338-501 1.64e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 42.12  E-value: 1.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728  338 LNNEIVD-----LQREKNNVEQ---DLKEKEDTIKQRTSEVQDLQDEVQRentnlqklqaqkqqvqeLLDELDEQKAQLE 409
Cdd:PRK00409 499 LPENIIEeakklIGEDKEKLNEliaSLEELERELEQKAEEAEALLKEAEK-----------------LKEELEEKKEKLQ 561

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728  410 EQLKEVRKKCAEEAQlisslkaeltsqesqistyeEELAKAREELSRLQQETAELE-ESVESGKAQ-LEPLQQHLQDSQQ 487
Cdd:PRK00409 562 EEEDKLLEEAEKEAQ--------------------QAIKEAKKEADEIIKELRQLQkGGYASVKAHeLIEARKRLNKANE 621

                        170
                 ....*....|....
gi 67476728  488 EISSMQMKLMEMKD 501
Cdd:PRK00409 622 KKEKKKKKQKEKQE 635
End3 pfam12761
Actin cytoskeleton-regulatory complex protein END3; Endocytosis is accomplished through the ...
 323-458 1.65e-03

Actin cytoskeleton-regulatory complex protein END3; Endocytosis is accomplished through the sequential recruitment at endocytic sites of proteins that drive cargo sorting, membrane invagination and vesicle release. End3p is part of the coat module protein complex Pan1, along with Pan1p, Sla1p, and Sla2p. The proteins in this complex are regulated by phosphorylation events. End3p also regulates the cortical actin cytoskeleton. The subunits of the Pan1 complex are homologous to mammalian intersectin.


Pssm-ID: 432765 [Multi-domain]  Cd Length: 200  Bit Score: 40.75  E-value: 1.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   323 SSPVADFSAIKELDtlnNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDE---VQREntnlqklqaqkqqvqelLD 399
Cdd:pfam12761  84 SEKGTDFSATKGTD---WEEVRLKRELAELEEKLEKVEQAASKRRGGNRDESSKpalVKRE-----------------FE 143

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 67476728   400 ELDEQKaqlEEQLKEVR--KKCAEEAQLiSSLKAELTSQESQISTYEEELAKAREELSRLQ 458
Cdd:pfam12761 144 QLLDYK---ERQLRELEegSGKSKPINL-KSVREDIDTVEEQVDGLESHLSSRKQELQQLR 200
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
 341-500 1.65e-03

Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.


Pssm-ID: 284517 [Multi-domain]  Cd Length: 749  Bit Score: 42.05  E-value: 1.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   341 EIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLD---ELDEQKAQLEE--QLKEV 415
Cdd:pfam07111 191 QLAEAQKEAELLRKQLSKTQEELEAQVTLVESLRKYVGEQVPPEVHSQTWELERQELLDtmqHLQEDRADLQAtvELLQV 270

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   416 R------------KKCAEEAQLISSLKAELTSQ-ESQISTYEEEL------AKA-----REELSRLQQETAELEESVESG 471
Cdd:pfam07111 271 RvqslthmlalqeEELTRKIQPSDSLEPEFPKKcRSLLNRWREKVfalmvqLKAqdlehRDSVKQLRGQVAELQEQVTSQ 350

                         170       180       190
                  ....*....|....*....|....*....|.
gi 67476728   472 KAQLEPLQQHLQD--SQQEISSMQMKLMEMK 500
Cdd:pfam07111 351 SQEQAILQRALQDkaAEVEVERMSAKGLQME 381
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 396-509 1.82e-03

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 41.99  E-value: 1.82e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 396 ELLDELDEQKAQLEEqlkevrkkcaEEAQLIsslkaeltsQESQISTYEEeLAKAREELSRLQQETAELEESVESGKAQL 475
Cdd:COG0542 411 EELDELERRLEQLEI----------EKEALK---------KEQDEASFER-LAELRDELAELEEELEALKARWEAEKELI 470

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 67476728 476 EPLQ---QHLQDSQQEISSMQMKLMEMKDLENHNSQL 509
Cdd:COG0542 471 EEIQelkEELEQRYGKIPELEKELAELEEELAELAPL 507
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 333-517 1.87e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 42.08  E-value: 1.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    333 KELDTLNNE----IVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRentnlqklqaqkqqVQELLDELDEQKAQL 408
Cdd:pfam01576  176 KSLSKLKNKheamISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAE--------------LQAQIAELRAQLAKK 241

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    409 EEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLE------PLQQHL 482
Cdd:pfam01576  242 EEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEdtldttAAQQEL 321

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 67476728    483 QDS-QQEISSMQMKLMEmkDLENHNSQLNWCSSPHS 517
Cdd:pfam01576  322 RSKrEQEVTELKKALEE--ETRSHEAQLQEMRQKHT 355
WEMBL pfam05701
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ...
 397-500 2.03e-03

Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".


Pssm-ID: 461718 [Multi-domain]  Cd Length: 562  Bit Score: 41.94  E-value: 2.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   397 LLDELDEQKAQLEEqlkeVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSR----LQQETAELEESVESGK 472
Cdd:pfam05701 326 LRSELEKEKAELAS----LRQREGMASIAVSSLEAELNRTKSEIALVQAKEKEAREKMVElpkqLQQAAQEAEEAKSLAQ 401

                          90       100       110
                  ....*....|....*....|....*....|.
gi 67476728   473 AQLEPLQQHLQDSQQ---EISSMQMKLMEMK 500
Cdd:pfam05701 402 AAREELRKAKEEAEQakaAASTVESRLEAVL 432
CEP63 pfam17045
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ...
 400-544 2.07e-03

Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole activity.


Pssm-ID: 465338 [Multi-domain]  Cd Length: 264  Bit Score: 40.96  E-value: 2.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   400 ELDEQKAQLEEQLKEVRKKCA--EEAQlisSLKAELTSQesqistYEEELAKAREELSRLQ------------------- 458
Cdd:pfam17045  43 ELLSARNTLERKHKEIGLLRQqlEELE---KGKQELVAK------YEQQLQKLQEELSKLKrsyeklqrkqlkeareeak 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   459 -QETAELEESVESGKAQ------LEPLQQHLQdSQQEISSMQmklMEMKDLENHNSQLNwcSSPHSILVNGATdyCSLST 531
Cdd:pfam17045 114 sREEDRSELSRLNGKLEefrqksLEWEQQRLQ-YQQQVASLE---AQRKALAEQSSLIQ--SAAYQVQLEGRK--QCLEA 185

                         170
                  ....*....|...
gi 67476728   532 SSSETANLNEHVE 544
Cdd:pfam17045 186 SQSEIQRLRSKLE 198
UPF0242 pfam06785
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ...
 396-506 2.18e-03

Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal transmembrane region and a C-terminal coiled-coil.


Pssm-ID: 429117 [Multi-domain]  Cd Length: 194  Bit Score: 40.19  E-value: 2.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   396 ELLDELDEQKAQLEEQLkevRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVES----- 470
Cdd:pfam06785  58 EDALKEKFEKSFLEEKE---AKLTELDAEGFKILEETLEELQSEEERLEEELSQKEEELRRLTEENQQLQIQLQQisqdf 134

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 67476728   471 ------GKAQLEPLQQHLQDSQQEISSmQMKLMEMKDLENHN 506
Cdd:pfam06785 135 aefrleSEEQLAEKQLLINEYQQTIEE-QRSVLEKRQDQIEN 175
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 345-509 2.34e-03

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 41.88  E-value: 2.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    345 LQREKNNVEQ---DLKEKEDTIKQRTSEVQDLQ--DEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKC 419
Cdd:TIGR00618  641 LALKLTALHAlqlTLTQERVREHALSIRVLPKEllASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREF 720

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    420 AEEAQLISSLKAELTSQES-----------------QISTYEEELAKARE--------ELSRLQQETA----ELEESVES 470
Cdd:TIGR00618  721 NEIENASSSLGSDLAAREDalnqslkelmhqartvlKARTEAHFNNNEEVtaalqtgaELSHLAAEIQffnrLREEDTHL 800

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 67476728    471 GKAQLEPLQQHLQDSQQEISSMQMKLmeMKDLENHNSQL 509
Cdd:TIGR00618  801 LKTLEAEIGQEIPSDEDILNLQCETL--VQEEEQFLSRL 837
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 349-510 2.35e-03

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


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 40.27  E-value: 2.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   349 KNNVE--QDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQklqaqkqqvqELLDELDEQKAQLEEQLKEVRKkcaeeaqli 426
Cdd:pfam13851  22 RNNLEliKSLKEEIAELKKKEERNEKLMSEIQQENKRLT----------EPLQKAQEEVEELRKQLENYEK--------- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   427 ssLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLE-PLQQHLQDSQQEISSMQMKLMEM-KDLEN 504
Cdd:pfam13851  83 --DKQSLKNLKARLKVLEKELKDLKWEHEVLEQRFEKVERERDELYDKFEaAIQDVQQKTGLKNLLLEKKLQALgETLEK 160


                  ....*.
gi 67476728   505 HNSQLN 510
Cdd:pfam13851 161 KEAQLN 166
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 334-464 2.46e-03

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: 41.58  E-value: 2.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    334 ELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLk 413
Cdd:TIGR02168  867 LIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL- 945

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 67476728    414 evrkkcAEEAQLisslkaELTSQESQISTYEEELAKAREELSRLQQETAEL 464
Cdd:TIGR02168  946 ------SEEYSL------TLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
Kre28 pfam17097
Spindle pole body component; In Saccharomyces cerevisae Kre28 and Spc105 form a kinetochore ...
 333-466 2.46e-03

Spindle pole body component; In Saccharomyces cerevisae Kre28 and Spc105 form a kinetochore microtubule binding complex, which bridges between centromeric heterochromatin and kinetochore MAPs (microtubule associated protein, such as Bim1, Bik1 and SIk19) and motors (Cin8, Kar3). It may be regulated by sumoylation.


Pssm-ID: 407241 [Multi-domain]  Cd Length: 360  Bit Score: 41.33  E-value: 2.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   333 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQrentnlqklqaqkqqvqELLDELDeqkaQLEEQL 412
Cdd:pfam17097 133 DTLTVLNQEIDQIKGDILQVAQEIADKQDQVNELCLETSNELDECW-----------------ELLNELE----RLRDQR 191

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 67476728   413 KEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEE 466
Cdd:pfam17097 192 ITVEEQTSNEKDTELDPVEETYEEWKSLQESLQQLEHLKEELDQLQKQKDSLEK 245
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 334-510 2.51e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 41.70  E-value: 2.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    334 ELDTLNNEIVDLQREKNNVEQDLKEKEDTIK-----------QRT----------SEVQDLQDEVQRENtnlQKLQAQKQ 392
Cdd:pfam01576  216 ESTDLQEQIAELQAQIAELRAQLAKKEEELQaalarleeetaQKNnalkkireleAQISELQEDLESER---AARNKAEK 292

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    393 QVQELLDELDEQKAQLEEQL------KEVR-KKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSR--------- 456
Cdd:pfam01576  293 QRRDLGEELEALKTELEDTLdttaaqQELRsKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEqleqakrnk 372

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 67476728    457 ---------LQQETAELEE---SVESGK-----------AQLEPLQQHLQDSQQEISSMQMKLMEMK-DLENHNSQLN 510
Cdd:pfam01576  373 anlekakqaLESENAELQAelrTLQQAKqdsehkrkkleGQLQELQARLSESERQRAELAEKLSKLQsELESVSSLLN 450
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
333-480 2.57e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.59  E-value: 2.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728  333 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRT--SEVQDLQDEVqrENTNLQKLQAQKQQVQELLDELDEQKAQ--- 407
Cdd:PRK03918 466 KELKEIEEKERKLRKELRELEKVLKKESELIKLKElaEQLKELEEKL--KKYNLEELEKKAEEYEKLKEKLIKLKGEiks 543

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728  408 --------------LEEQLKEVRKKCAEEAQLISSLKA------------------------ELTSQESQISTYEEELAK 449
Cdd:PRK03918 544 lkkelekleelkkkLAELEKKLDELEEELAELLKELEElgfesveeleerlkelepfyneylELKDAEKELEREEKELKK 623

                        170       180       190
                 ....*....|....*....|....*....|.
gi 67476728  450 AREELSRLQQETAELEESVESGKAQLEPLQQ 480
Cdd:PRK03918 624 LEEELDKAFEELAETEKRLEELRKELEELEK 654
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 396-498 2.60e-03

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


Pssm-ID: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 39.10  E-value: 2.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   396 ELLDELDEQK---AQLEEQLKEVRKKCAEEAQLISSLKAELtsqESQISTYEEELAKAREELSRLQQEtaeleesvesgk 472
Cdd:pfam03938   9 KILEESPEGKaaqAQLEKKFKKRQAELEAKQKELQKLYEEL---QKDGALLEEEREEKEQELQKKEQE------------ 73

                          90       100
                  ....*....|....*....|....*.
gi 67476728   473 aqlepLQQHLQDSQQEISSMQMKLME 498
Cdd:pfam03938  74 -----LQQLQQKAQQELQKKQQELLQ 94
PRK09039 PRK09039
peptidoglycan -binding protein;
409-494 2.63e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 41.10  E-value: 2.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728  409 EEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLqDSQQE 488
Cdd:PRK09039  52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQEL-DSEKQ 130


                 ....*.
gi 67476728  489 ISSMQM 494
Cdd:PRK09039 131 VSARAL 136
ZapB pfam06005
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is ...
 432-498 2.87e-03

Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is required for proper Z-ring formation.


Pssm-ID: 428718 [Multi-domain]  Cd Length: 71  Bit Score: 37.25  E-value: 2.87e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 67476728   432 ELTSQ-ESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLME 498
Cdd:pfam06005   4 ELLEQlETKIQAAVDTIALLQMENEELKEENEELKEEANELEEENQQLKQERNQWQERIRGLLGKLDE 71
Tektin pfam03148
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ...
 333-504 2.88e-03

Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular sites as centrioles, basal bodies, and along ciliary and flagellar doublet microtubules. Tektins form unique protofilaments, organized as longitudinal polymers of tektin heterodimers with axial periodicity matching tubulin. Tektin polypeptides consist of several alpha-helical regions that are predicted to form coiled coils. Indeed, tektins share considerable structural similarities with intermediate filament proteins. Possible functional roles for tektins are: stabilization of tubulin protofilaments; attachment of A and B-tubules in ciliary/flagellar microtubule doublets and C-tubules in centrioles; binding of axonemal components.


Pssm-ID: 460827 [Multi-domain]  Cd Length: 383  Bit Score: 40.99  E-value: 2.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   333 KELDTLNNEIVDLQREKNNVEQDLKEKEDTI----------KQRTSEvqDL-QDEVQRentnlqklqaqkqqvqELLDEL 401
Cdd:pfam03148  64 KELEELDEEIELLLEEKRRLEKALEALEEPLhiaqecltlrEKRQGI--DLvHDEVEK----------------ELLKEV 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   402 D----------EQKAQLEEQL---KEVRKKCA------EEAQLI----------S---SLKAELTSQESQISTYEE---- 445
Cdd:pfam03148 126 EliegiqellqRTLEQAWEQLrllRAARHKLEkdlsdkKEALEIdekclslnntSpniSYKPGPTRIPPNSSTPEEwekf 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   446 ----------ELAKA---REELSRLQQETAELEES---------------VESGKAQLEplqQHLQDSQQEISSMQmklM 497
Cdd:pfam03148 206 tqdnieraekERAASaqlRELIDSILEQTANDLRAqadavnfalrkrieeTEDAKNKLE---WQLKKTLQEIAELE---K 279


                  ....*..
gi 67476728   498 EMKDLEN 504
Cdd:pfam03148 280 NIEALEK 286
mukB PRK04863
chromosome partition protein MukB;
353-493 3.06e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 41.48  E-value: 3.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   353 EQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKA- 431
Cdd:PRK04863  515 LQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQAr 594

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 67476728   432 --ELTSQESQISTYEEELAKARE----------ELSRLQQETAELEESVESGKAQLEPLQQHLqdsQQEISSMQ 493
Cdd:PRK04863  595 iqRLAARAPAWLAAQDALARLREqsgeefedsqDVTEYMQQLLERERELTVERDELAARKQAL---DEEIERLS 665
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 345-508 3.29e-03

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 41.49  E-value: 3.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    345 LQREKNNVEQDLKEKEDTIKQRtsevQDLQDEVQRENTNLQKLQAQKQQVQE---LLDELDEQKA------QLEEQLKEV 415
Cdd:TIGR00618  316 LQSKMRSRAKLLMKRAAHVKQQ----SSIEEQRRLLQTLHSQEIHIRDAHEVatsIREISCQQHTltqhihTLQQQKTTL 391

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    416 RKKCAEEAQLISSLKAELTSQESQISTYEEE---LAKAREELsRLQQETAELEESVESGKAQLEPLQQ-HLQDSQQEISS 491
Cdd:TIGR00618  392 TQKLQSLCKELDILQREQATIDTRTSAFRDLqgqLAHAKKQQ-ELQQRYAELCAAAITCTAQCEKLEKiHLQESAQSLKE 470

                          170
                   ....*....|....*..
gi 67476728    492 MQMKLmemKDLENHNSQ 508
Cdd:TIGR00618  471 REQQL---QTKEQIHLQ 484
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 336-501 3.52e-03

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 41.25  E-value: 3.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   336 DTLNNEIVDLQREKNNVEQDLK-EKEDTIKQRTSEVQDLQdevQRENTNLQKLqaqkqqvqELLDELDEQKAQLEEQLKE 414
Cdd:pfam05483 495 DKLLLENKELTQEASDMTLELKkHQEDIINCKKQEERMLK---QIENLEEKEM--------NLRDELESVREEFIQKGDE 563

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   415 VRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREE-------LSRLQQETAELEESVESGKAQLEPLQQHLQDSQQ 487
Cdd:pfam05483 564 VKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQienknknIEELHQENKALKKKGSAENKQLNAYEIKVNKLEL 643

                         170
                  ....*....|....
gi 67476728   488 EISSMQMKLMEMKD 501
Cdd:pfam05483 644 ELASAKQKFEEIID 657
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 325-507 3.67e-03

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 41.26  E-value: 3.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    325 PVADfsaikELDTLNNEivdlqrEKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDE-LDE 403
Cdd:pfam15921  242 PVED-----QLEALKSE------SQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEqARN 310

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    404 QKAQLEEQLKEVRKKCAeeaQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELeeSVESGKA--QLEPLQQH 481
Cdd:pfam15921  311 QNSMYMRQLSDLESTVS---QLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQF--SQESGNLddQLQKLLAD 385

                          170       180
                   ....*....|....*....|....*.
gi 67476728    482 LQDSQQEISSMQMKLMEMKDLENHNS 507
Cdd:pfam15921  386 LHKREKELSLEKEQNKRLWDRDTGNS 411
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 396-492 3.73e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 3.73e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 396 ELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQL 475
Cdd:COG1196 683 ELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL 762

                        90
                ....*....|....*..
gi 67476728 476 EPLQQHLQDSQQEISSM 492
Cdd:COG1196 763 EELERELERLEREIEAL 779
flagell_FliJ TIGR02473
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ...
 396-510 3.75e-03

flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly every case, in the midst of other flagellar biosynthesis genes in bacgterial genomes. Typically the fliJ gene is found adjacent to the gene for the flagellum-specific ATPase FliI. Sequence scoring in the gray zone between trusted and noise cutoffs include both probable FliJ proteins and components of bacterial type III secretion systems.


Pssm-ID: 131526 [Multi-domain]  Cd Length: 141  Bit Score: 38.84  E-value: 3.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   396 ELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSlKAELTSQESQISTYEEELAKAREELSRLQQetaeleesvesgkaQL 475
Cdd:TIGR02473  27 AEFERLETQLQQLIKYREEYEQQALEKVGAGTS-ALELSNYQRFIRQLDQRIQQQQQELALLQQ--------------EV 91

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 67476728   476 EPLQQHLQDSQQEIssMQMKLMEMKDLENHNSQLN 510
Cdd:TIGR02473  92 EAKRERLLEARREL--KALEKLKEKKQKEYRAEEA 124
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
408-510 3.87e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 41.00  E-value: 3.87e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 408 LEEQLKEVRKKcaEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQ 487
Cdd:COG2433 378 IEEALEELIEK--ELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARS 455

                        90       100
                ....*....|....*....|...
gi 67476728 488 EISSMQMKLMEMKDLENHNSQLN 510
Cdd:COG2433 456 EERREIRKDREISRLDREIERLE 478
BBC smart00502
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains
 396-501 4.40e-03

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


Pssm-ID: 128778  Cd Length: 127  Bit Score: 38.01  E-value: 4.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    396 ELLDELDEQKAQLEEQLKEVRKKCaeeaQLISSLKAELTSQ-ESQISTYEEELAKAREEL-SRLQQETAELEESVESGKA 473
Cdd:smart00502   7 ELLTKLRKKAAELEDALKQLISII----QEVEENAADVEAQiKAAFDELRNALNKRKKQLlEDLEEQKENKLKVLEQQLE 82

                           90       100
                   ....*....|....*....|....*...
gi 67476728    474 QLEPLQQHLQDSQQEISsmqmKLMEMKD 501
Cdd:smart00502  83 SLTQKQEKLSHAINFTE----EALNSGD 106
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 401-487 4.56e-03

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


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 41.09  E-value: 4.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728  401 LDEQKAQLEEQ--LKEVRKKCAEEAQLISSLKAELTS-------------QESQISTYEEEL--------------AKAR 451
Cdd:COG3096  295 FGARRQLAEEQyrLVEMARELEELSARESDLEQDYQAasdhlnlvqtalrQQEKIERYQEDLeelterleeqeevvEEAA 374

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 67476728  452 EELSRLQQETAELEESVESGKAQLEPLQQHLqDSQQ 487
Cdd:COG3096  375 EQLAEAEARLEAAEEEVDSLKSQLADYQQAL-DVQQ 409
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 335-509 4.63e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 40.93  E-value: 4.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    335 LDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKE 414
Cdd:pfam01576  358 LEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSK 437

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    415 VRKKC--------AEEAQLISSLKaELTSQESQISTYEEELA-KAREEL---SRLQQ---ETAELEESVESGKAQLEPLQ 479
Cdd:pfam01576  438 LQSELesvssllnEAEGKNIKLSK-DVSSLESQLQDTQELLQeETRQKLnlsTRLRQledERNSLQEQLEEEEEAKRNVE 516

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 67476728    480 QHLQDSQQEISSMQMKLMEM---------------KDLENHNSQL 509
Cdd:pfam01576  517 RQLSTLQAQLSDMKKKLEEDagtlealeegkkrlqRELEALTQQL 561
FliJ pfam02050
Flagellar FliJ protein;
398-493 4.72e-03

Flagellar FliJ protein;


Pssm-ID: 426581 [Multi-domain]  Cd Length: 123  Bit Score: 38.03  E-value: 4.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   398 LDELDEQKAQLEEQLKEVRKKCAEEA-----QLISSLKAELTSQESQISTYEEELAKAREELSRLQQEtaelEESVE--S 470
Cdd:pfam02050  21 LEELQQYRAEYQQQLSGAGQGISAAElrnyqAFISQLDEAIAQQQQELAQAEAQVEKAREEWQEARQE----RKSLEklR 96

                          90       100
                  ....*....|....*....|....*...
gi 67476728   471 GKAQLEplQQHLQDSQQ-----EISSMQ 493
Cdd:pfam02050  97 EREKKE--ERKEQNRREqkqldELAARL 122
PRK10246 PRK10246
exonuclease subunit SbcC; Provisional
 403-509 4.73e-03

exonuclease subunit SbcC; Provisional


Pssm-ID: 182330 [Multi-domain]  Cd Length: 1047  Bit Score: 40.94  E-value: 4.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   403 EQKAQLEEQLKEVRKK-----------CAEE-----AQLISS--LKAELTSQESQISTYEEELAKAREELSRLQQETAEL 464
Cdd:PRK10246  380 EQLRQWQQQLTHAEQKlnalpaitltlTADEvaaalAQHAEQrpLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQR 459

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 67476728   465 EESVESGKAQLEPLQQHLQD----SQQEissmqmklMEMKDLENHNSQL 509
Cdd:PRK10246  460 NAALNEMRQRYKEKTQQLADvktiCEQE--------ARIKDLEAQRAQL 500
fliH PRK06669
flagellar assembly protein H; Validated
 316-496 4.82e-03

flagellar assembly protein H; Validated


Pssm-ID: 235850 [Multi-domain]  Cd Length: 281  Bit Score: 40.00  E-value: 4.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728  316 LQKNIIGSSPVADFSAIKELDTLNNEIVDLQREKNNveqdlKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQA--QKQQ 393
Cdd:PRK06669   1 MPKVIFKRSNVINKEKLKTHEIQKYRFKVLSIKEKE-----RLREEEEEQVEQLREEANDEAKEIIEEAEEDAFeiVEAA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728  394 VQELLDELDEQKAQLEEQLKEVRKKCA-EEAQLISSLKAELtsQESQISTYEEELAKAREE-LSRLQQETAELEESVESG 471
Cdd:PRK06669  76 EEEAKEELLKKTDEASSIIEKLQMQIErEQEEWEEELERLI--EEAKAEGYEEGYEKGREEgLEEVRELIEQLNKIIEKL 153

                        170       180
                 ....*....|....*....|....*
gi 67476728  472 KAQLEplqQHLQDSQQEISSMQMKL 496
Cdd:PRK06669 154 IKKRE---EILESSEEEIVELALDI 175
growth_prot_Scy NF041483
polarized growth protein Scy;
357-480 4.96e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 40.58  E-value: 4.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   357 KEKEDTIKQRTSEVQDLQDEVQREntnlqklqaqkqqVQELLDELDEQKAQL-EEQLKEVRKKCAEEAQLISSLKAElts 435
Cdd:NF041483  520 RQAEETLERTRAEAERLRAEAEEQ-------------AEEVRAAAERAARELrEETERAIAARQAEAAEELTRLHTE--- 583

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 67476728   436 QESQISTYEEELAKAREELSRLQQETAELEESVESGKAQ-LEPLQQ 480
Cdd:NF041483  584 AEERLTAAEEALADARAEAERIRREAAEETERLRTEAAErIRTLQA 629
Prefoldin_2 pfam01920
Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996.
 398-495 5.79e-03

Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996.


Pssm-ID: 396482 [Multi-domain]  Cd Length: 102  Bit Score: 37.20  E-value: 5.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   398 LDELDEQKAQLEEQLKEVrkKCAEEAqlISSLKAELTSQESqIST--YEEELAKAREElsrLQQETAELEESVESGKAQL 475
Cdd:pfam01920  11 LQLLAQQIKQLETQLKEL--ELALEE--LELLDEDTKVYKL-IGDvlVKQDKEEVKEQ---LEERKETLEKEIKTLEKQL 82

                          90       100
                  ....*....|....*....|
gi 67476728   476 EPLQQHLQDSQQEISSMQMK 495
Cdd:pfam01920  83 EKLEKELEELKEELYKKFGQ 102
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 332-458 5.84e-03

Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.


Pssm-ID: 425733 [Multi-domain]  Cd Length: 322  Bit Score: 39.71  E-value: 5.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   332 IKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEE- 410
Cdd:pfam00529  81 LDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLLAt 160

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 67476728   411 --QLKEVRK-KCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQ 458
Cdd:pfam00529 161 vaQLDQIYVqITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLERTE 211
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 396-511 6.01e-03

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 39.66  E-value: 6.01e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 396 ELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTY--EEELAKAREELSRLQQETAEL-EESVESGK 472
Cdd:cd22656 121 ALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLltDEGGAIARKEIKDLQKELEKLnEEYAAKLK 200

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 67476728 473 AQLEPLQQHLQDSQQEIssmQMKLMEMKDLENHNSQLNW 511
Cdd:cd22656 201 AKIDELKALIADDEAKL---AAALRLIADLTAADTDLDN 236
CCDC-167 pfam15188
Coiled-coil domain-containing protein 167; The function of this family of coiled-coil domains, ...
 398-453 6.20e-03

Coiled-coil domain-containing protein 167; The function of this family of coiled-coil domains, has not, as yet, been determined. Members of this family remain uncharacterized. This family of proteins is found in eukaryotes. Proteins in this family are typically between and 103 amino acids in length.


Pssm-ID: 464553 [Multi-domain]  Cd Length: 82  Bit Score: 36.49  E-value: 6.20e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   398 LDELDEQKAQLEEQLKEVRKKcAEEAQLI----SSLKAELTSQESQISTYEEELAKAREE 453
Cdd:pfam15188   5 IDRLEEKIASCRDRLERIEKK-LRREELSeedrRSLEKELLLLKKRLEKNEEELKLLRKE 63
Macoilin pfam09726
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ...
 333-499 6.22e-03

Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.


Pssm-ID: 462859 [Multi-domain]  Cd Length: 670  Bit Score: 40.22  E-value: 6.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   333 KELDTLNNEIVDL----QREKNNV---EQDLKEKEDTikqRTSEVQDLQDEVQR----ENTNLQKLQAQKQQVQELLDEL 401
Cdd:pfam09726 444 QENDLLQTKLHNAvsakQKDKQTVqqlEKRLKAEQEA---RASAEKQLAEEKKRkkeeEATAARAVALAAASRGECTESL 520

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   402 DEQKAQLEEQLKEVRKKCAEEAQLISSLkaELTSQEsqISTYEEElAKARE----ELSRLQQETAELEESVES------- 470
Cdd:pfam09726 521 KQRKRELESEIKKLTHDIKLKEEQIREL--EIKVQE--LRKYKES-EKDTEvlmsALSAMQDKNQHLENSLSAetrikld 595

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 67476728   471 -------GKAQLEPLQQHLQDSQQEISSMQMKLMEM 499
Cdd:pfam09726 596 lfsalgdAKRQLEIAQGQIYQKDQEIKDLKQKIAEV 631
PRK12705 PRK12705
hypothetical protein; Provisional
 330-459 6.58e-03

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 40.08  E-value: 6.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728  330 SAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTikqrtSEVQDLQDE----VQRENTNLQKLQAQKQQVQELLD------ 399
Cdd:PRK12705  41 EAQKEAEEKLEAALLEAKELLLRERNQQRQEAR-----REREELQREeerlVQKEEQLDARAEKLDNLENQLEErekals 115

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 67476728  400 ----ELDEQKAQLEEQLKEVRKKCAEEA--QLISSLKAELTSQESQISTYEEElaKAREELSRLQQ 459
Cdd:PRK12705 116 arelELEELEKQLDNELYRVAGLTPEQArkLLLKLLDAELEEEKAQRVKKIEE--EADLEAERKAQ 179
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 334-489 6.59e-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: 40.34  E-value: 6.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    334 ELDTLNNEIVDLQR--EKNNVEQDLKEKEDTIKQRTSEVQ-DLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKaqLEE 410
Cdd:TIGR00618  585 DIPNLQNITVRLQDltEKLSEAEDMLACEQHALLRKLQPEqDLQDVRLHLQQCSQELALKLTALHALQLTLTQER--VRE 662

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 67476728    411 QLKEVRKkcaEEAQLISSLKAELTSQESQIstyeEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEI 489
Cdd:TIGR00618  663 HALSIRV---LPKELLASRQLALQKMQSEK----EQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDL 734
DUF4686 pfam15742
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ...
 356-496 7.06e-03

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


Pssm-ID: 464838 [Multi-domain]  Cd Length: 384  Bit Score: 39.66  E-value: 7.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   356 LKEKEDTIKQRTSEVQDLQDEVQRentnlqKLQAQKQQVQELLDE-------------LDEQKAQLEEQLKEVRKKCAEE 422
Cdd:pfam15742   1 VSSGEKLKYQQQEEVQQLRQNLQR------LQILCTSAEKELRYErgknldlkqhnslLQEENIKIKAELKQAQQKLLDS 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   423 AQLISSLKAELtsqesqistyeeelakareelSRLQQETAELE----ESVESGKAQ---LEPLQQH---LQDSQQEISSM 492
Cdd:pfam15742  75 TKMCSSLTAEW---------------------KHCQQKIRELElevlKQAQSIKSQnslQEKLAQEksrVADAEEKILEL 133


                  ....
gi 67476728   493 QMKL 496
Cdd:pfam15742 134 QQKL 137
mukB PRK04863
chromosome partition protein MukB;
400-487 7.50e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 40.33  E-value: 7.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   400 ELDEQKAQLEEQ---LKEVRKKCAEEAQLISSLKAELTS-------------QESQISTYEEELAK-------------- 449
Cdd:PRK04863  294 ELYTSRRQLAAEqyrLVEMARELAELNEAESDLEQDYQAasdhlnlvqtalrQQEKIERYQADLEEleerleeqnevvee 373

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 67476728   450 AREELSRLQQETAELEESVESGKAQLEPLQQHLqDSQQ 487
Cdd:PRK04863  374 ADEQQEENEARAEAAEEEVDELKSQLADYQQAL-DVQQ 410
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 330-510 7.68e-03

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 40.21  E-value: 7.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    330 SAIKELDTLNNEIVDLQREknnVEQDLKEKEDTIKQRTSEVQDLQDEVQ--RENTNLQKLQAqK---QQVQELLDELDEQ 404
Cdd:pfam12128  255 SAELRLSHLHFGYKSDETL---IASRQEERQETSAELNQLLRTLDDQWKekRDELNGELSAA-DaavAKDRSELEALEDQ 330

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    405 KAQLEEQLKEVRKKCAEEAQLISS--------LKAELTSQESQISTYEEELAKAREE----LSRLQQETAELEESVESGK 472
Cdd:pfam12128  331 HGAFLDADIETAAADQEQLPSWQSelenleerLKALTGKHQDVTAKYNRRRSKIKEQnnrdIAGIKDKLAKIREARDRQL 410

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 67476728    473 A-------QLE-PLQQHLQDSQQEISSMQMKLMEmkDLENHNSQLN 510
Cdd:pfam12128  411 AvaeddlqALEsELREQLEAGKLEFNEEEYRLKS--RLGELKLRLN 454
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 346-475 7.79e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 39.52  E-value: 7.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   346 QREKNNVEQDLKEKEDTIKQRTSEVQD----LQDEVQREntnlqklQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAE 421
Cdd:pfam13868 221 QKEREEAEKKARQRQELQQAREEQIELkerrLAEEAERE-------EEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRR 293

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 67476728   422 EaqlisslkaeltsQESQI----STYEEELAKAREELSRLQQETAELEESVESGKAQL 475
Cdd:pfam13868 294 E-------------LEKQIeereEQRAAEREEELEEGERLREEEAERRERIEEERQKK 338
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 399-489 8.46e-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: 8.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728  399 DELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAeLEESVESGKAQLEPL 478
Cdd:COG3096  281 RELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTALR-QQEKIERYQEDLEEL 359

                         90
                 ....*....|.
gi 67476728  479 QQHLqDSQQEI 489
Cdd:COG3096  360 TERL-EEQEEV 369
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 344-509 8.52e-03

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


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 39.49  E-value: 8.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   344 DLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEA 423
Cdd:pfam07888  56 QREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELE 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   424 QLISSLKAELTSQESQISTYEEELAKA----REELSRLQQETAELEESVE----------SGKAQLEPLQQHLQDSQQEI 489
Cdd:pfam07888 136 EDIKTLTQRVLERETELERMKERAKKAgaqrKEEEAERKQLQAKLQQTEEelrslskefqELRNSLAQRDTQVLQLQDTI 215

                         170       180
                  ....*....|....*....|
gi 67476728   490 SSMQMKLMEMKDLENHNSQL 509
Cdd:pfam07888 216 TTLTQKLTTAHRKEAENEAL 235
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 346-500 8.64e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 39.52  E-value: 8.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   346 QREKNNV--------EQDLKEKEdtikQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDE----QKAQLEEQLK 413
Cdd:pfam13868  97 LQEREQMdeiveriqEEDQAEAE----EKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILeylkEKAEREEERE 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   414 EVRKKCAEEAQLIsslKAELTSQESQISTYEEELAKAREELSRLQQETA----ELEEsVESGKAQLEPLQQHLQdsQQEI 489
Cdd:pfam13868 173 AEREEIEEEKERE---IARLRAQQEKAQDEKAERDELRAKLYQEEQERKerqkEREE-AEKKARQRQELQQARE--EQIE 246

                         170
                  ....*....|.
gi 67476728   490 SSMQMKLMEMK 500
Cdd:pfam13868 247 LKERRLAEEAE 257
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 398-475 8.82e-03

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 37.42  E-value: 8.82e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728 398 LDELDEQKAQLEEQLKEVRKKCAE---EAQLISSlKAELTSQEsqisTYEEELAKAREELSRLQQET-AELEESVESGKA 473
Cdd:cd06503  39 LEEAEKAKEEAEELLAEYEEKLAEaraEAQEIIE-EARKEAEK----IKEEILAEAKEEAERILEQAkAEIEQEKEKALA 113


                ..
gi 67476728 474 QL 475
Cdd:cd06503 114 EL 115
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 405-498 8.83e-03

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


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 37.56  E-value: 8.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728    405 KAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQIStyEEELAKAREELSRLQQEtaeleesvesgkaqlepLQQHLQD 484
Cdd:smart00935  20 QKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLS--EAAREKKEKELQKKVQE-----------------FQRKQQK 80

                           90
                   ....*....|....
gi 67476728    485 SQQEISSMQMKLME 498
Cdd:smart00935  81 LQQDLQKRQQEELQ 94
Leu_zip pfam15294
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ...
 338-462 9.36e-03

Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 (LZTFL1) and Leucine zipper protein 2 (LUZP2).


Pssm-ID: 464620 [Multi-domain]  Cd Length: 276  Bit Score: 38.92  E-value: 9.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67476728   338 LNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQ---DEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKE 414
Cdd:pfam15294 131 LHMEIERLKEENEKLKERLKTLESQATQALDEKSKLEkalKDLQKEQGAKKDVKSNLKEISDLEEKMAALKSDLEKTLNA 210

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 67476728   415 vrkkcaeEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETA 462
Cdd:pfam15294 211 -------STALQKSLEEDLASTKHELLKVQEQLEMAEKELEKKFQQTA 251
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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