NCBI Conserved Domain Search

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

108-202

3.72e-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: 3.72e-43

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   108 PWAVKPEDKAKYDAIFDSLSP-VNGFLSGDKVKPVLLNSKLPVDILGRVWELSDIDHDGMLDRDEFAVAMFLVYCALEKE 186
Cdd:smart00027   1 PWAISPEDKAKYEQIFRSLDKnQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGY 80

                           90
                   ....*....|....*.
gi 119627229   187 PVPMSLPPALVPPSKR 202
Cdd:smart00027  81 PIPASLPPSLIPPSKR 96

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

205-300

2.51e-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: 146.27 E-value: 2.51e-41

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   205 WVVSPAEKAKYDEIFLKTDKDMDGFVSGLEVREIFLKTGLPSTLLAHIWSLCDTKDCGKLSKDQFALAFHLISQKLIkGI 284
Cdd:smart00027   2 WAISPEDKAKYEQIFRSLDKNQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLN-GY 80

                           90
                   ....*....|....*.
gi 119627229   285 DPPHVLTPEMIPPSDR 300
Cdd:smart00027  81 PIPASLPPSLIPPSKR 96

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

11-90

1.76e-24

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: 98.12 E-value: 1.76e-24

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229    11 QQVDTGNTGRVLASDAAAFLKKSGLPDLILGKIWDLADTDGKGILNKQEFFVALRLVACAQNGLEVSLSSLNLAVPPPRF 90
Cdd:smart00027  17 RSLDKNQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGYPIPASLPPSLIPPSKR 96

COG4372

Uncharacterized protein, contains DUF3084 domain [Function unknown];

317-480

1.20e-16

Uncharacterized protein, contains DUF3084 domain [Function unknown];

Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 82.64 E-value: 1.20e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 317 SAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLE 396
Cdd:COG4372   35 KALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQ 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 397 EQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQL--EPLQQHLQDSQQ 474
Cdd:COG4372  115 EELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEaeQALDELLKEANR 194


                 ....*.
gi 119627229 475 EISSMQ 480
Cdd:COG4372  195 NAEKEE 200

Name

Accession

Description

Interval

E-value

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

108-202

3.72e-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: 3.72e-43

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   108 PWAVKPEDKAKYDAIFDSLSP-VNGFLSGDKVKPVLLNSKLPVDILGRVWELSDIDHDGMLDRDEFAVAMFLVYCALEKE 186
Cdd:smart00027   1 PWAISPEDKAKYEQIFRSLDKnQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGY 80

                           90
                   ....*....|....*.
gi 119627229   187 PVPMSLPPALVPPSKR 202
Cdd:smart00027  81 PIPASLPPSLIPPSKR 96

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

205-300

2.51e-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: 146.27 E-value: 2.51e-41

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   205 WVVSPAEKAKYDEIFLKTDKDMDGFVSGLEVREIFLKTGLPSTLLAHIWSLCDTKDCGKLSKDQFALAFHLISQKLIkGI 284
Cdd:smart00027   2 WAISPEDKAKYEQIFRSLDKNQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLN-GY 80

                           90
                   ....*....|....*.
gi 119627229   285 DPPHVLTPEMIPPSDR 300
Cdd:smart00027  81 PIPASLPPSLIPPSKR 96

Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...

215-280

1.81e-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: 1.81e-26

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119627229 215 YDEIFLKTDKDMDGFVSGLEVREIFLKTGLPSTLLAHIWSLCDTKDCGKLSKDQFALAFHLISQKL 280
Cdd:cd00052    1 YDQIFRSLDPDGDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALAL 66

EF-hand_4

Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ...

108-202

2.82e-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: 103.61 E-value: 2.82e-26

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  108 PWAVKpedkaKYDAIFDSLSPVNGFLSGDKVKPVLLNSKLPVDILGRVWELSDIDHDGMLDRDEFAVAMFLVYCALEKE- 186
Cdd:pfam12763   6 EWEIK-----KYWEIFSGLKPENNKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLIFDLVNGNi 80

                          90
                  ....*....|....*..
gi 119627229  187 -PVPMSLPPALVPPSKR 202
Cdd:pfam12763  81 aDVPDELPDWLVPGSKA 97

Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...

119-184

6.76e-25

Pssm-ID: 238009 [Multi-domain] Cd Length: 67 Bit Score: 98.45 E-value: 6.76e-25

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119627229 119 YDAIFDSLSPVN-GFLSGDKVKPVLLNSKLPVDILGRVWELSDIDHDGMLDRDEFAVAMFLVYCALE 184
Cdd:cd00052    1 YDQIFRSLDPDGdGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67

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

11-90

1.76e-24

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: 98.12 E-value: 1.76e-24

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229    11 QQVDTGNTGRVLASDAAAFLKKSGLPDLILGKIWDLADTDGKGILNKQEFFVALRLVACAQNGLEVSLSSLNLAVPPPRF 90
Cdd:smart00027  17 RSLDKNQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGYPIPASLPPSLIPPSKR 96

Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...

11-72

2.97e-21

Pssm-ID: 238009 [Multi-domain] Cd Length: 67 Bit Score: 88.05 E-value: 2.97e-21

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119627229  11 QQVDTGNTGRVLASDAAAFLKKSGLPDLILGKIWDLADTDGKGILNKQEFFVALRLVACAQN 72
Cdd:cd00052    6 RSLDPDGDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67

COG4372

Uncharacterized protein, contains DUF3084 domain [Function unknown];

317-480

1.20e-16

Uncharacterized protein, contains DUF3084 domain [Function unknown];

Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 82.64 E-value: 1.20e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 317 SAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLE 396
Cdd:COG4372   35 KALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQ 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 397 EQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQL--EPLQQHLQDSQQ 474
Cdd:COG4372  115 EELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEaeQALDELLKEANR 194


                 ....*.
gi 119627229 475 EISSMQ 480
Cdd:COG4372  195 NAEKEE 200

Mplasa_alph_rch

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

320-497

2.09e-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: 77.37 E-value: 2.09e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  320 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQL 399
Cdd:TIGR04523 335 KIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQI 414

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  400 KEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSm 479
Cdd:TIGR04523 415 KKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKS- 493

                         170
                  ....*....|....*...
gi 119627229  480 qmKLMEMKDLENHNSQLN 497
Cdd:TIGR04523 494 --KEKELKKLNEEKKELE 509

ATG16

pfam08614

Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...

342-496

6.37e-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: 6.37e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  342 DLKEKEDTIKQRTsevQDLQDEVQRE-NTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAEL 420
Cdd:pfam08614  11 RLLDRTALLEAEN---AKLQSEPESVlPSTSSSKLSKASPQSASIQSLEQLLAQLREELAELYRSRGELAQRLVDLNEEL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  421 TSQESQISTYEEELAKAREELSRLQQETAELEESVEsGKAQLeplqqhLQDSQQEISSMQMKL--ME--MKDLENHNSQL 496
Cdd:pfam08614  88 QELEKKLREDERRLAALEAERAQLEEKLKDREEELR-EKRKL------NQDLQDELVALQLQLnmAEekLRKLEKENREL 160

PRK03918

DNA double-strand break repair ATPase Rad50;

317-490

5.00e-11

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 66.63 E-value: 5.00e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 317 SAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRT-SEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKaQL 395
Cdd:PRK03918 546 KELEKLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEPFYNEYLELKDAEKELEREEKELK-KL 624

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 396 EEQLKEVRKKCAEEAQLISSLKAELTSQESQIStyEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQE 475
Cdd:PRK03918 625 EEELDKAFEELAETEKRLEELRKELEELEKKYS--EEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEE 702

                        170
                 ....*....|....*
gi 119627229 476 ISSMQMKLMEMKDLE 490
Cdd:PRK03918 703 LEEREKAKKELEKLE 717

EF-hand_4

Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ...

19-67

3.08e-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: 49.29 E-value: 3.08e-07

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 119627229   19 GRVLASDAAAFLKKSGLPDLILGKIWDLADTDGKGILNKQEFFVALRLV 67
Cdd:pfam12763  24 NKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLI 72

EF-hand_4

Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ...

209-306

7.41e-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: 7.41e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  209 PAEKAKYDEIFlKTDKDMDGFVSGLEVREIFLKTGLPSTLLAHIWSLCDTKDCGKLSKDQFALAFHLISQkLIKGI--DP 286
Cdd:pfam12763   6 EWEIKKYWEIF-SGLKPENNKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLIFD-LVNGNiaDV 83

                          90       100
                  ....*....|....*....|
gi 119627229  287 PHVLTPEMIPPSDRASLQKN 306
Cdd:pfam12763  84 PDELPDWLVPGSKAHLIQAN 103

FRQ1

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

152-274

1.66e-04

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

Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 42.47 E-value: 1.66e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 152 LGRVWELSDIDHDGMLDRDEFAvAMFLVYCALEKEPVPmSLPPALVPPSKRKTWVVSPAEK---AKYDEIFLKTDKDMDG 228
Cdd:COG5126    7 LDRRFDLLDADGDGVLERDDFE-ALFRRLWATLFSEAD-TDGDGRISREEFVAGMESLFEAtvePFARAAFDLLDTDGDG 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 119627229 229 FVSGLEVREIFLKTGLPSTLLAHIWSLCDTKDCGKLSKDQFALAFH 274
Cdd:COG5126   85 KISADEFRRLLTALGVSEEEADELFARLDTDGDGKISFEEFVAAVR 130

STAT5_CCD

cd16855

Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family ...

393-496

1.86e-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: 1.86e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 393 AQLEEQLKEVRKKCAEEAQLISSLKAEltsQESQISTYEEeLAKAREELSRLQ-QETAELEESVESGKAQLEPLQQHLQD 471
Cdd:cd16855    4 LEIRQQLEELRQRTQETENDLRNLQQK---QESFVIQYQE-SQKIQAQLQQLQqQPQNERIELEQQLQQQKEQLEQLLNA 79

                         90       100
                 ....*....|....*....|....*.
gi 119627229 472 SQQEISSMQMKLME-MKDLENHNSQL 496
Cdd:cd16855   80 KAQELLQLRMELADkFKKTIQLLSKL 105

Spc7

smart00787

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

383-492

3.38e-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: 3.38e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   383 ELLDELDEQKAQL---EEQLKEVRKKCAEEAQLISSLKAELTSQESQISTY-EEELAKAREELSRLQQE-------TAEL 451
Cdd:smart00787 151 ENLEGLKEDYKLLmkeLELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCdPTELDRAKEKLKKLLQEimikvkkLEEL 230

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 119627229   452 EESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKDLENH 492
Cdd:smart00787 231 EEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGFTFK 271

growth_prot_Scy

polarized growth protein Scy;

343-480

1.32e-03

polarized growth protein Scy;

Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 42.51 E-value: 1.32e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  343 LKEKEDTIKQR-TSEVQDLQDEVQRENTNLQKLQAqkqqvqELLDEL----DEQKAQLEEQLKEVRKKCAEEAqliSSLK 417
Cdd:NF041483 1119 IRERAEELRDRiTGEIEELHERARRESAEQMKSAG------ERCDALvkaaEEQLAEAEAKAKELVSDANSEA---SKVR 1189

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119627229  418 -AELTSQESQISTYEEELAKAREELSRLQQET-AELEESVESGKAQLEPLQQHLQDSQQEISSMQ 480
Cdd:NF041483 1190 iAAVKKAEGLLKEAEQKKAELVREAEKIKAEAeAEAKRTVEEGKRELDVLVRRREDINAEISRVQ 1254

FRQ1

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

40-176

1.62e-03

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

Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 39.78 E-value: 1.62e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  40 LGKIWDLADTDGKGILNKQEFfVALRLVACAQNGLEvslsslnlavppprfHDTSSPLLISGTSAAELPWAVKPED-KAK 118
Cdd:COG5126    7 LDRRFDLLDADGDGVLERDDF-EALFRRLWATLFSE---------------ADTDGDGRISREEFVAGMESLFEATvEPF 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 119627229 119 YDAIFDSLSP-VNGFLSGDKVKPVLLNSKLPVDILGRVWELSDIDHDGMLDRDEFAVAM 176
Cdd:COG5126   71 ARAAFDLLDTdGDGKISADEFRRLLTALGVSEEEADELFARLDTDGDGKISFEEFVAAV 129

growth_prot_Scy

polarized growth protein Scy;

344-467

5.58e-03

polarized growth protein Scy;

Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 40.58 E-value: 5.58e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  344 KEKEDTIKQRTSEVQDLQDEVQREntnlqklqaqkqqVQELLDELDEQKAQL-EEQLKEVRKKCAEEAQLISSLKAElts 422
Cdd:NF041483  520 RQAEETLERTRAEAERLRAEAEEQ-------------AEEVRAAAERAARELrEETERAIAARQAEAAEELTRLHTE--- 583

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 119627229  423 QESQISTYEEELAKAREELSRLQQETAELEESVESGKAQ-LEPLQQ 467
Cdd:NF041483  584 AEERLTAAEEALADARAEAERIRREAAEETERLRTEAAErIRTLQA 629

Name

Accession

Description

Interval

E-value

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

108-202

3.72e-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: 3.72e-43

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   108 PWAVKPEDKAKYDAIFDSLSP-VNGFLSGDKVKPVLLNSKLPVDILGRVWELSDIDHDGMLDRDEFAVAMFLVYCALEKE 186
Cdd:smart00027   1 PWAISPEDKAKYEQIFRSLDKnQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGY 80

                           90
                   ....*....|....*.
gi 119627229   187 PVPMSLPPALVPPSKR 202
Cdd:smart00027  81 PIPASLPPSLIPPSKR 96

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

205-300

2.51e-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: 146.27 E-value: 2.51e-41

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   205 WVVSPAEKAKYDEIFLKTDKDMDGFVSGLEVREIFLKTGLPSTLLAHIWSLCDTKDCGKLSKDQFALAFHLISQKLIkGI 284
Cdd:smart00027   2 WAISPEDKAKYEQIFRSLDKNQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLN-GY 80

                           90
                   ....*....|....*.
gi 119627229   285 DPPHVLTPEMIPPSDR 300
Cdd:smart00027  81 PIPASLPPSLIPPSKR 96

Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...

215-280

1.81e-26

Pssm-ID: 238009 [Multi-domain] Cd Length: 67 Bit Score: 103.07 E-value: 1.81e-26

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119627229 215 YDEIFLKTDKDMDGFVSGLEVREIFLKTGLPSTLLAHIWSLCDTKDCGKLSKDQFALAFHLISQKL 280
Cdd:cd00052    1 YDQIFRSLDPDGDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALAL 66

EF-hand_4

Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ...

108-202

2.82e-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: 103.61 E-value: 2.82e-26

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  108 PWAVKpedkaKYDAIFDSLSPVNGFLSGDKVKPVLLNSKLPVDILGRVWELSDIDHDGMLDRDEFAVAMFLVYCALEKE- 186
Cdd:pfam12763   6 EWEIK-----KYWEIFSGLKPENNKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLIFDLVNGNi 80

                          90
                  ....*....|....*..
gi 119627229  187 -PVPMSLPPALVPPSKR 202
Cdd:pfam12763  81 aDVPDELPDWLVPGSKA 97

Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...

119-184

6.76e-25

Pssm-ID: 238009 [Multi-domain] Cd Length: 67 Bit Score: 98.45 E-value: 6.76e-25

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119627229 119 YDAIFDSLSPVN-GFLSGDKVKPVLLNSKLPVDILGRVWELSDIDHDGMLDRDEFAVAMFLVYCALE 184
Cdd:cd00052    1 YDQIFRSLDPDGdGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67

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

11-90

1.76e-24

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: 98.12 E-value: 1.76e-24

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229    11 QQVDTGNTGRVLASDAAAFLKKSGLPDLILGKIWDLADTDGKGILNKQEFFVALRLVACAQNGLEVSLSSLNLAVPPPRF 90
Cdd:smart00027  17 RSLDKNQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGYPIPASLPPSLIPPSKR 96

Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...

11-72

2.97e-21

Pssm-ID: 238009 [Multi-domain] Cd Length: 67 Bit Score: 88.05 E-value: 2.97e-21

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119627229  11 QQVDTGNTGRVLASDAAAFLKKSGLPDLILGKIWDLADTDGKGILNKQEFFVALRLVACAQN 72
Cdd:cd00052    6 RSLDPDGDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67

COG4372

Uncharacterized protein, contains DUF3084 domain [Function unknown];

317-480

1.20e-16

Uncharacterized protein, contains DUF3084 domain [Function unknown];

Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 82.64 E-value: 1.20e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 317 SAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLE 396
Cdd:COG4372   35 KALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQ 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 397 EQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQL--EPLQQHLQDSQQ 474
Cdd:COG4372  115 EELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEaeQALDELLKEANR 194


                 ....*.
gi 119627229 475 EISSMQ 480
Cdd:COG4372  195 NAEKEE 200

DR0291

COG1579

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

320-476

8.31e-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: 77.66 E-value: 8.31e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 320 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNlqklqaqkqqvqelLDELDEQKAQLEEQL 399
Cdd:COG1579   17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELE--------------IEEVEARIKKYEEQL 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119627229 400 KEVRKkcAEEAQlisSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEI 476
Cdd:COG1579   83 GNVRN--NKEYE---ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAEL 154

Smc

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

320-496

5.46e-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: 5.46e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 320 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQL 399
Cdd:COG1196  246 AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEEL 325

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 400 KEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGK-AQLEPLQQHLQDSQQEISS 478
Cdd:COG1196  326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAeELLEALRAAAELAAQLEEL 405

                        170
                 ....*....|....*...
gi 119627229 479 MQMKLMEMKDLENHNSQL 496
Cdd:COG1196  406 EEAEEALLERLERLEEEL 423

Mplasa_alph_rch

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

320-497

2.09e-14

Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 77.37 E-value: 2.09e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  320 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQL 399
Cdd:TIGR04523 335 KIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQI 414

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  400 KEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSm 479
Cdd:TIGR04523 415 KKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKS- 493

                         170
                  ....*....|....*...
gi 119627229  480 qmKLMEMKDLENHNSQLN 497
Cdd:TIGR04523 494 --KEKELKKLNEEKKELE 509

SMC_prok_B

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

321-485

4.75e-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: 4.75e-14

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   321 ELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLK 400
Cdd:TIGR02168  268 KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLE 347

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   401 EVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQ 480
Cdd:TIGR02168  348 ELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELL 427


                   ....*
gi 119627229   481 MKLME 485
Cdd:TIGR02168  428 KKLEE 432

COG4913

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

311-480

1.50e-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: 1.50e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  311 SPVADFSAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLqklqaqkqqvqelLDELDE 390
Cdd:COG4913   279 AALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDR-------------LEQLER 345

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  391 QKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQistYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQ 470
Cdd:COG4913   346 EIERLERELEERERRRARLEALLAALGLPLPASAEE---FAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELR 422

                         170
                  ....*....|
gi 119627229  471 DSQQEISSMQ 480
Cdd:COG4913   423 ELEAEIASLE 432

SMC_prok_B

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

321-488

2.35e-13

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 74.32 E-value: 2.35e-13

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   321 ELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLK 400
Cdd:TIGR02168  776 ELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIE 855

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   401 EVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQ 480
Cdd:TIGR02168  856 SLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLE 935


                   ....*...
gi 119627229   481 MKLMEMKD 488
Cdd:TIGR02168  936 VRIDNLQE 943

SMC_prok_B

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

316-495

5.65e-13

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 73.17 E-value: 5.65e-13

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   316 FSAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQL 395
Cdd:TIGR02168  291 YALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL 370

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   396 EEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGK-----AQLEPLQQHLQ 470
Cdd:TIGR02168  371 ESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAElkelqAELEELEEELE 450

                          170       180
                   ....*....|....*....|....*
gi 119627229   471 DSQQEISSMQMKLMEMKDLENHNSQ 495
Cdd:TIGR02168  451 ELQEELERLEEALEELREELEEAEQ 475

Smc

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

320-497

9.30e-13

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 72.28 E-value: 9.30e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 320 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENtnlqklqaqkqqvqELLDELDEQKAQLEEQL 399
Cdd:COG1196  239 AELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQ--------------AEEYELLAELARLEQDI 304

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 400 KEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSM 479
Cdd:COG1196  305 ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384

                        170
                 ....*....|....*....
gi 119627229 480 QMKLME-MKDLENHNSQLN 497
Cdd:COG1196  385 AEELLEaLRAAAELAAQLE 403

SMC_prok_B

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

320-488

1.02e-12

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 72.40 E-value: 1.02e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   320 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENtnlqklqAQKQQVQELLDELDEQKAQLEEQL 399
Cdd:TIGR02168  705 KELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS-------KELTELEAEIEELEERLEEAEEEL 777

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   400 KEVRKKCAEEAQLISSLKAELTSQESQISTYEEEL-------AKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDS 472
Cdd:TIGR02168  778 AEAEAEIEELEAQIEQLKEELKALREALDELRAELtllneeaANLRERLESLERRIAATERRLEDLEEQIEELSEDIESL 857

                          170
                   ....*....|....*.
gi 119627229   473 QQEISSMQMKLMEMKD 488
Cdd:TIGR02168  858 AAEIEELEELIEELES 873

Mplasa_alph_rch

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

319-497

1.95e-12

Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 71.20 E-value: 1.95e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  319 IKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQ-------DLQDEVQRENTNLQKLQAQKQQVQELLDELDEQ 391
Cdd:TIGR04523 210 IQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISntqtqlnQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQ 289

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  392 KAQLEEQLKEVRKKcaEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQD 471
Cdd:TIGR04523 290 LNQLKSEISDLNNQ--KEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEE 367

                         170       180       190
                  ....*....|....*....|....*....|
gi 119627229  472 SQQEISSM----QMKLMEMKDLENHNSQLN 497
Cdd:TIGR04523 368 KQNEIEKLkkenQSYKQEIKNLESQINDLE 397

SMC_prok_B

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

317-497

3.80e-12

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 70.47 E-value: 3.80e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   317 SAIKELDTLNNEIVDLQREKNNVEQDLKEKE---DTIKQRTSEVQDLQDEVQRENTNLQklqaqkqqvqELLDELDEQKA 393
Cdd:TIGR02168  236 ELREELEELQEELKEAEEELEELTAELQELEeklEELRLEVSELEEEIEELQKELYALA----------NEISRLEQQKQ 305

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   394 QLEEQLKEVRKKcaeeaqlISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQ 473
Cdd:TIGR02168  306 ILRERLANLERQ-------LEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELE 378

                          170       180
                   ....*....|....*....|....*
gi 119627229   474 QEISSMQMKLMEMK-DLENHNSQLN 497
Cdd:TIGR02168  379 EQLETLRSKVAQLElQIASLNNEIE 403

ATG16

pfam08614

Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...

342-496

6.37e-12

Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 64.95 E-value: 6.37e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  342 DLKEKEDTIKQRTsevQDLQDEVQRE-NTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAEL 420
Cdd:pfam08614  11 RLLDRTALLEAEN---AKLQSEPESVlPSTSSSKLSKASPQSASIQSLEQLLAQLREELAELYRSRGELAQRLVDLNEEL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  421 TSQESQISTYEEELAKAREELSRLQQETAELEESVEsGKAQLeplqqhLQDSQQEISSMQMKL--ME--MKDLENHNSQL 496
Cdd:pfam08614  88 QELEKKLREDERRLAALEAERAQLEEKLKDREEELR-EKRKL------NQDLQDELVALQLQLnmAEekLRKLEKENREL 160

YhaN

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

318-461

8.46e-12

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 69.03 E-value: 8.46e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 318 AIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRT--SEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQL 395
Cdd:COG4717   93 LQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEERLEELRELEEELEELEAEL 172

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 396 EE---QLKEVRKKCAEEA-QLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQ 461
Cdd:COG4717  173 AElqeELEELLEQLSLATeEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242

DR0291

COG1579

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

297-456

9.08e-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: 65.72 E-value: 9.08e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 297 PSDRASLQKNIIGsspvadfsAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTS---------EVQDLQDEvqre 367
Cdd:COG1579   30 PAELAELEDELAA--------LEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlgnvrnnkEYEALQKE---- 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 368 ntnlqklqaqkqqvqelLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQIST----YEEELAKAREELSR 443
Cdd:COG1579   98 -----------------IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEkkaeLDEELAELEAELEE 160

                        170
                 ....*....|...
gi 119627229 444 LQQETAELEESVE 456
Cdd:COG1579  161 LEAEREELAAKIP 173

Smc

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

318-495

1.10e-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: 1.10e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 318 AIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEE 397
Cdd:COG1196  230 LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE 309

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 398 QLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEIS 477
Cdd:COG1196  310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389

                        170
                 ....*....|....*...
gi 119627229 478 SMQMKLMEMKDLENHNSQ 495
Cdd:COG1196  390 EALRAAAELAAQLEELEE 407

Smc

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

316-476

1.16e-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: 1.16e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 316 FSAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQL 395
Cdd:COG1196  291 YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA 370

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 396 EEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQE 475
Cdd:COG1196  371 EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450


                 .
gi 119627229 476 I 476
Cdd:COG1196  451 E 451

COG4372

Uncharacterized protein, contains DUF3084 domain [Function unknown];

329-488

1.38e-11

Uncharacterized protein, contains DUF3084 domain [Function unknown];

Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 67.23 E-value: 1.38e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 329 IVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNlqklqaqkqqvqelLDELDEQKAQLEEQLKEVRKKcae 408
Cdd:COG4372   26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEE--------------LEQARSELEQLEEELEELNEQ--- 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 409 eaqlISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKD 488
Cdd:COG4372   89 ----LQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQE 164

SMC_prok_A

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

316-497

1.91e-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: 1.91e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   316 FSAIKELDTLNNEIVDLQREKnnveQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLqaqkqqvqelLDELDEQKAQL 395
Cdd:TIGR02169  705 DELSQELSDASRKIGEIEKEI----EQLEQEEEKLKERLEELEEDLSSLEQEIENVKSE----------LKELEARIEEL 770

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   396 EEQLKEVRKKCAE-EAQL----ISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQ 470
Cdd:TIGR02169  771 EEDLHKLEEALNDlEARLshsrIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIK 850

                          170       180
                   ....*....|....*....|....*...
gi 119627229   471 DSQQEISSMQMKLMEMK-DLENHNSQLN 497
Cdd:TIGR02169  851 SIEKEIENLNGKKEELEeELEELEAALR 878

SMC_prok_A

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

321-491

2.19e-11

Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 68.17 E-value: 2.19e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   321 ELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQ---DEVQREntnlqklqaqkqqvqelLDELDEQKAQLEE 397
Cdd:TIGR02169  675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASrkiGEIEKE-----------------IEQLEQEEEKLKE 737

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   398 QLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRL------------QQETAELEESVESGKAQLEPL 465
Cdd:TIGR02169  738 RLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLearlshsripeiQAELSKLEEEVSRIEARLREI 817

                          170       180       190
                   ....*....|....*....|....*....|
gi 119627229   466 QQHLQDSQQEI----SSMQMKLMEMKDLEN 491
Cdd:TIGR02169  818 EQKLNRLTLEKeyleKEIQELQEQRIDLKE 847

EnvC

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

320-480

2.72e-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: 2.72e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 320 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNlqklqaqkqqvqelLDELDEQKAQLEEQL 399
Cdd:COG4942   34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAE--------------LAELEKEIAELRAEL 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 400 KEVRKKCAE---EAQLISS-------LKAELTSQESQISTYEEELAKAR----EELSRLQQETAELEESVESGKAQLEPL 465
Cdd:COG4942  100 EAQKEELAEllrALYRLGRqpplallLSPEDFLDAVRRLQYLKYLAPARreqaEELRADLAELAALRAELEAERAELEAL 179

                        170
                 ....*....|....*
gi 119627229 466 QQHLQDSQQEISSMQ 480
Cdd:COG4942  180 LAELEEERAALEALK 194

Smc

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

320-478

3.15e-11

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.27 E-value: 3.15e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 320 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENtnlqklqaqkqqvqELLDELDEQKAQLEEQL 399
Cdd:COG1196  281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELE--------------EELEELEEELEELEEEL 346

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119627229 400 KEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISS 478
Cdd:COG1196  347 EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425

EnvC

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

320-478

4.36e-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: 4.36e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 320 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDL-----------QDEVQRENTNLQKLQAQKQQVQELLDEL 388
Cdd:COG4942   76 QELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLgrqpplalllsPEDFLDAVRRLQYLKYLAPARREQAEEL 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 389 DEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQH 468
Cdd:COG4942  156 RADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235

                        170
                 ....*....|
gi 119627229 469 LQDSQQEISS 478
Cdd:COG4942  236 AAAAAERTPA 245

PRK03918

DNA double-strand break repair ATPase Rad50;

317-490

5.00e-11

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 66.63 E-value: 5.00e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 317 SAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRT-SEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKaQL 395
Cdd:PRK03918 546 KELEKLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEPFYNEYLELKDAEKELEREEKELK-KL 624

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 396 EEQLKEVRKKCAEEAQLISSLKAELTSQESQIStyEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQE 475
Cdd:PRK03918 625 EEELDKAFEELAETEKRLEELRKELEELEKKYS--EEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEE 702

                        170
                 ....*....|....*
gi 119627229 476 ISSMQMKLMEMKDLE 490
Cdd:PRK03918 703 LEEREKAKKELEKLE 717

SMC_prok_B

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

320-492

1.97e-10

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 64.69 E-value: 1.97e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   320 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQL 399
Cdd:TIGR02168  754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   400 KEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSM 479
Cdd:TIGR02168  834 AATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSEL 913

                          170
                   ....*....|...
gi 119627229   480 QMKLMEMKDLENH 492
Cdd:TIGR02168  914 RRELEELREKLAQ 926

Smc

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

318-480

3.01e-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: 3.01e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 318 AIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEE 397
Cdd:COG1196  349 AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE 428

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 398 QLKEVRKKCAEEAQLISSLKAELTSQEsqistyeEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEIS 477
Cdd:COG1196  429 ALAELEEEEEEEEEALEEAAEEEAELE-------EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501


                 ...
gi 119627229 478 SMQ 480
Cdd:COG1196  502 DYE 504

Cast

pfam10174

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...

322-585

3.90e-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: 63.69 E-value: 3.90e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  322 LDTLNNEIVD---------------------LQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEvqrentnlqkLQAQKQQ 380
Cdd:pfam10174 312 LETLTNQNSDckqhievlkesltakeqraaiLQTEVDALRLRLEEKESFLNKKTKQLQDLTEE----------KSTLAGE 381

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  381 VQELLDELD--EQKA--------QLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETaE 450
Cdd:pfam10174 382 IRDLKDMLDvkERKInvlqkkieNLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQR-E 460

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  451 LEESVEsgKAQLEPLQQHLQDSQQEISSMQMKLME----MKDLENHNSQLNwcSSPHSIlvngatdycsLSTSSSETANL 526
Cdd:pfam10174 461 REDRER--LEELESLKKENKDLKEKVSALQPELTEkessLIDLKEHASSLA--SSGLKK----------DSKLKSLEIAV 526

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119627229  527 NEHVEGQSNLESE--PIHQ-ESPARSSPELLPSGVTDENEVTTAVTE--KVCSELD----------NNRHSKEE 585
Cdd:pfam10174 527 EQKKEECSKLENQlkKAHNaEEAVRTNPEINDRIRLLEQEVARYKEEsgKAQAEVErllgilreveNEKNDKDK 600

COG4372

Uncharacterized protein, contains DUF3084 domain [Function unknown];

383-497

5.43e-10

Uncharacterized protein, contains DUF3084 domain [Function unknown];

Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 62.23 E-value: 5.43e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 383 ELLDELDEQKAQLEEQLKEVRKKcaeeaqlISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQL 462
Cdd:COG4372   24 ILIAALSEQLRKALFELDKLQEE-------LEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAEL 96

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 119627229 463 EPLQQHLQDSQQEISSMQMKLM----EMKDLENHNSQLN 497
Cdd:COG4372   97 AQAQEELESLQEEAEELQEELEelqkERQDLEQQRKQLE 135

Mplasa_alph_rch

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

325-477

6.72e-10

Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 62.73 E-value: 6.72e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  325 LNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRK 404
Cdd:TIGR04523 438 NNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTK 517

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  405 KCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSR---------LQQETAELEESVESGKAQLEPLQQHLQDSQQE 475
Cdd:TIGR04523 518 KISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKenlekeideKNKEIEELKQTQKSLKKKQEEKQELIDQKEKE 597


                  ..
gi 119627229  476 IS 477
Cdd:TIGR04523 598 KK 599

EnvC

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

390-479

8.99e-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: 8.99e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 390 EQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHL 469
Cdd:COG4942   20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99

                         90
                 ....*....|
gi 119627229 470 QDSQQEISSM 479
Cdd:COG4942  100 EAQKEELAEL 109

SMC_prok_A

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

320-470

9.63e-10

Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 62.78 E-value: 9.63e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   320 KELDTLNNEIVDLQREKNNVEQDLKEKE-------DTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELD--- 389
Cdd:TIGR02169  350 KRRDKLTEEYAELKEELEDLRAELEEVDkefaetrDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNaai 429

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   390 ----EQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELE-------ESVESG 458
Cdd:TIGR02169  430 agieAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEaqaraseERVRGG 509

                          170
                   ....*....|..
gi 119627229   459 KAQLEPLQQHLQ 470
Cdd:TIGR02169  510 RAVEEVLKASIQ 521

Mplasa_alph_rch

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

319-497

2.57e-09

Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 61.19 E-value: 2.57e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  319 IKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKlqaqkqqvqELLDELDEQKAQLEEQ 398
Cdd:TIGR04523 259 KDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELK---------SELKNQEKKLEEIQNQ 329

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  399 LKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDS------ 472
Cdd:TIGR04523 330 ISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQeklnqq 409

                         170       180       190
                  ....*....|....*....|....*....|
gi 119627229  473 -QQEISSMQ----MKLMEMKDLENHNSQLN 497
Cdd:TIGR04523 410 kDEQIKKLQqekeLLEKEIERLKETIIKNN 439

Mplasa_alph_rch

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

319-498

3.21e-09

Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 60.80 E-value: 3.21e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  319 IKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQ 398
Cdd:TIGR04523 376 KKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELI 455

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  399 LKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISS 478
Cdd:TIGR04523 456 IKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKE 535

                         170       180
                  ....*....|....*....|.
gi 119627229  479 MQMKLMEMKD-LENHNSQLNW 498
Cdd:TIGR04523 536 KESKISDLEDeLNKDDFELKK 556

Mplasa_alph_rch

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

305-497

3.32e-09

Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 60.80 E-value: 3.32e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  305 KNIIGSSPVADFSAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQ----RENTNLQKLQAQKQQ 380
Cdd:TIGR04523  25 KNIANKQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKdlndKLKKNKDKINKLNSD 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  381 VQELLDELDEQKAQ----------LEEQLKEVRKKCA--------EEAQL-------------ISSLKAELTSQESQIST 429
Cdd:TIGR04523 105 LSKINSEIKNDKEQknklevelnkLEKQKKENKKNIDkflteikkKEKELeklnnkyndlkkqKEELENELNLLEKEKLN 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  430 YEEELAKAREELSR-----------------LQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKDLENH 492
Cdd:TIGR04523 185 IQKNIDKIKNKLLKlelllsnlkkkiqknksLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNK 264


                  ....*.
gi 119627229  493 N-SQLN 497
Cdd:TIGR04523 265 IkKQLS 270

TPR_MLP1_2

pfam07926

TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...

390-496

3.84e-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: 3.84e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  390 EQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQeSQIST-----YEEELAK----------AREELSRLQQETAELEES 454
Cdd:pfam07926   1 AELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQ-AEIAReaqqnYERELVLhaedikalqaLREELNELKAEIAELKAE 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 119627229  455 VESGKAQLEPLQQHLQDS----QQEISSMQMKLmemKDLENHNSQL 496
Cdd:pfam07926  80 AESAKAELEESEESWEEQkkelEKELSELEKRI---EDLNEQNKLL 122

COG4913

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

317-485

5.11e-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: 5.11e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  317 SAIKELDTLNN--EIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRenTNLQKLQAQKQQVQELLDELDEQKAQ 394
Cdd:COG4913   229 ALVEHFDDLERahEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAA--LRLWFAQRRLELLEAELEELRAELAR 306

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  395 LEEQLKEVRKKCAEEAQLISSLKAELTSQ--------ESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQ 466
Cdd:COG4913   307 LEAELERLEARLDALREELDELEAQIRGNggdrleqlEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALR 386

                         170
                  ....*....|....*....
gi 119627229  467 QHLQDSQQEISSMQMKLME 485
Cdd:COG4913   387 AEAAALLEALEEELEALEE 405

EnvC

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

385-474

5.60e-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: 5.60e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 385 LDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEP 464
Cdd:COG4942   29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE 108

                         90
                 ....*....|
gi 119627229 465 LQQHLQDSQQ 474
Cdd:COG4942  109 LLRALYRLGR 118

SMC_prok_B

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

320-480

5.66e-09

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.07 E-value: 5.66e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   320 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTnlqklqaQKQQVQELLDELDEQKAQLEEQL 399
Cdd:TIGR02168  677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSR-------QISALRKDLARLEAEVEQLEERI 749

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   400 KEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSM 479
Cdd:TIGR02168  750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESL 829


                   .
gi 119627229   480 Q 480
Cdd:TIGR02168  830 E 830

Myosin_tail_1

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

332-496

7.46e-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: 7.46e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   332 LQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQ 411
Cdd:pfam01576   94 LQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEE 173

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   412 LISSLKAELTSQESQISTYEEEL---AKAREELS----RLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLM 484
Cdd:pfam01576  174 KAKSLSKLKNKHEAMISDLEERLkkeEKGRQELEkakrKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLE 253

                          170       180
                   ....*....|....*....|...
gi 119627229   485 E-----------MKDLENHNSQL 496
Cdd:pfam01576  254 EetaqknnalkkIRELEAQISEL 276

HAP1_N

pfam04849

HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ...

321-488

9.03e-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: 57.73 E-value: 9.03e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  321 ELDTLNNEIVDLQREknnveqdLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLK 400
Cdd:pfam04849 109 QLGSAREEILQLRHE-------LSKKDDLLQIYSNDAEESETESSCSTPLRRNESFSSLHGCVQLDALQEKLRGLEEENL 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  401 EVRKKC-----------AEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETA-------ELEESVESGKAQL 462
Cdd:pfam04849 182 KLRSEAshlktetdtyeEKEQQLMSDCVEQLSEANQQMAELSEELARKMEENLRQQEEITsllaqivDLQHKCKELGIEN 261

                         170       180
                  ....*....|....*....|....*.
gi 119627229  463 EPLQQHLQDSQQEISSMQMKLMEMKD 488
Cdd:pfam04849 262 EELQQHLQASKEAQRQLTSELQELQD 287

PRK03918

DNA double-strand break repair ATPase Rad50;

319-490

1.16e-08

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.92 E-value: 1.16e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 319 IKELDTLNNEIVDLQREKNNVEQDLKEKED---TIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQL 395
Cdd:PRK03918 171 IKEIKRRIERLEKFIKRTENIEELIKEKEKeleEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESL 250

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 396 EEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEE--ELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQ 473
Cdd:PRK03918 251 EGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERI 330

                        170
                 ....*....|....*..
gi 119627229 474 QEISSMQMKLMEMKDLE 490
Cdd:PRK03918 331 KELEEKEERLEELKKKL 347

SMC_prok_A

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

317-496

1.81e-08

Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.54 E-value: 1.81e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   317 SAIKELDTLN--------NEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRentnlqklqaqkqqVQELLDEL 388
Cdd:TIGR02169  269 EIEQLLEELNkkikdlgeEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAK--------------LEAEIDKL 334

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   389 DEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELS-------------------------- 442
Cdd:TIGR02169  335 LAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKdyrekleklkreinelkreldrlqee 414

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 119627229   443 --RLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMK-DLENHNSQL 496
Cdd:TIGR02169  415 lqRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAaDLSKYEQEL 471

CwlO1

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

317-478

1.95e-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: 1.95e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 317 SAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQ-------------------DL--------------QDE 363
Cdd:COG3883   55 ELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYrsggsvsyldvllgsesfsDFldrlsalskiadadADL 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 364 VQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSR 443
Cdd:COG3883  135 LEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 119627229 444 LQQETAELEESVESGKAQLEPLQQHLQDSQQEISS 478
Cdd:COG3883  215 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGA 249

GumC

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

320-490

2.04e-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: 2.04e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 320 KELDTLNNEIVDLQREKNNVeqDLKEKEDTIKQRTSEVQDLQDEVQREntnlqklqaqkqqvqelLDELDEQKAQLEEQL 399
Cdd:COG3206  189 KELEEAEAALEEFRQKNGLV--DLSEEAKLLLQQLSELESQLAEARAE-----------------LAEAEARLAALRAQL 249

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 400 KEVRKKCAEEAQ--LISSLKAELTSQESQI----STY----------EEELAKAREEL-SRLQQETAELEESVESGKAQL 462
Cdd:COG3206  250 GSGPDALPELLQspVIQQLRAQLAELEAELaelsARYtpnhpdvialRAQIAALRAQLqQEAQRILASLEAELEALQARE 329

                        170       180
                 ....*....|....*....|....*...
gi 119627229 463 EPLQQHLQDSQQEISSMQMKLMEMKDLE 490
Cdd:COG3206  330 ASLQAQLAQLEARLAELPELEAELRRLE 357

PspA

COG1842

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

383-487

2.43e-08

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

Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 55.22 E-value: 2.43e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 383 ELLDE-------LDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEE--ELA--KAREELSR--LQQEtA 449
Cdd:COG1842   16 ALLDKaedpekmLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEkaRLAleKGREDLAReaLERK-A 94

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 119627229 450 ELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMK 487
Cdd:COG1842   95 ELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELK 132

GumC

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

304-486

2.98e-08

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

Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 57.33 E-value: 2.98e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 304 QKNIIGSSPVADfSAIKELDtLNNEIVDLQREKNNVEQDLKEK----------------EDTIKQRTSEV--------QD 359
Cdd:COG3206   86 QIEILKSRPVLE-RVVDKLN-LDEDPLGEEASREAAIERLRKNltvepvkgsnvieisyTSPDPELAAAVanalaeayLE 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 360 LQDEVQRENTNlqklqaqkqqvqELLDELDEQKAQLEEQLKEVRKKCAE--EAQLISSLKAELTSQESQISTYEEELAKA 437
Cdd:COG3206  164 QNLELRREEAR------------KALEFLEEQLPELRKELEEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESQLAEA 231

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 119627229 438 REELSRLQQETAELEESVESGKAQLEPLQQH--LQDSQQEISSMQMKLMEM 486
Cdd:COG3206  232 RAELAEAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAEL 282

YhaN

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

322-490

3.13e-08

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.47 E-value: 3.13e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 322 LDTLNNEIVDLQRE-----KNNVEQ--DLKEKEDTIKQRTSEVQDLQDEVQRENT----------------NLQKLQAQK 378
Cdd:COG4717   48 LERLEKEADELFKPqgrkpELNLKElkELEEELKEAEEKEEEYAELQEELEELEEeleeleaeleelreelEKLEKLLQL 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 379 QQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQL---ISSLKAELTSQESQISTYEEEL-AKAREELSRLQQETAELEES 454
Cdd:COG4717  128 LPLYQELEALEAELAELPERLEELEERLEELRELeeeLEELEAELAELQEELEELLEQLsLATEEELQDLAEELEELQQR 207

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 119627229 455 VESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKDLE 490
Cdd:COG4717  208 LAELEEELEEAQEELEELEEELEQLENELEAAALEE 243

PRK03918

DNA double-strand break repair ATPase Rad50;

320-468

3.77e-08

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.38 E-value: 3.77e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 320 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVqRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQL 399
Cdd:PRK03918 231 KELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEI-EELEEKVKELKELKEKAEEYIKLSEFYEEYLDEL 309

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119627229 400 KEVRKKCAEEAQLISSLKAELTSQESQistyEEELAKAREELSRLQQETAELEESV---ESGKAQLEPLQQH 468
Cdd:PRK03918 310 REIEKRLSRLEEEINGIEERIKELEEK----EERLEELKKKLKELEKRLEELEERHelyEEAKAKKEELERL 377

Lebercilin

pfam15619

Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...

343-495

4.03e-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: 54.14 E-value: 4.03e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  343 LKEKEDTIKQRTSEVQDLQ---DEVQRENtnlqklqaqkqqvqELLDELdeQKAQlEEQLKEVRKKCAEEAQLISSLKAE 419
Cdd:pfam15619   6 LSARLHKIKELQNELAELQsklEELRKEN--------------RLLKRL--QKRQ-EKALGKYEGTESELPQLIARHNEE 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  420 L--------------TSQESQISTYEEELAKAREELSRLQQ--------ETAELEEsvesgkaQLEPLQQHLQDSQQEIS 477
Cdd:pfam15619  69 VrvlrerlrrlqekeRDLERKLKEKEAELLRLRDQLKRLEKlsedknlaEREELQK-------KLEQLEAKLEDKDEKIQ 141

                         170
                  ....*....|....*...
gi 119627229  478 SMQMKLmemkDLENHNSQ 495
Cdd:pfam15619 142 DLERKL----ELENKSFR 155

PRK02224

DNA double-strand break repair Rad50 ATPase;

321-491

5.00e-08

DNA double-strand break repair Rad50 ATPase;

Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.97 E-value: 5.00e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 321 ELDTLNNEIVDLQ-------REKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENtnlqklqAQKQQVQELLDELDEQKA 393
Cdd:PRK02224 252 ELETLEAEIEDLRetiaeteREREELAEEVRDLRERLEELEEERDDLLAEAGLDD-------ADAEAVEARREELEDRDE 324

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 394 QLEEQLKEVRKKCAEEAQLISSLKAELTSQES-------QISTYEEELAKAREELSRLQQETAELEESVESGKA------ 460
Cdd:PRK02224 325 ELRDRLEECRVAAQAHNEEAESLREDADDLEEraeelreEAAELESELEEAREAVEDRREEIEELEEEIEELRErfgdap 404

                        170       180       190
                 ....*....|....*....|....*....|...
gi 119627229 461 -QLEPLQQHLQDSQQEISSMQMKLMEMK-DLEN 491
Cdd:PRK02224 405 vDLGNAEDFLEELREERDELREREAELEaTLRT 437

COG4913

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

300-480

6.12e-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: 6.12e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  300 RASLQKNIIGsspvadFSAIKELDTLNNEIVDLQREKNNVE---QDLKEKEDTIKQR--------------------TSE 356
Cdd:COG4913   596 RRIRSRYVLG------FDNRAKLAALEAELAELEEELAEAEerlEALEAELDALQERrealqrlaeyswdeidvasaERE 669

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  357 VQDLQDEVQR-ENTNLQklqaqkqqvqelLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELA 435
Cdd:COG4913   670 IAELEAELERlDASSDD------------LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE 737

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 119627229  436 KAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQ 480
Cdd:COG4913   738 AAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARL 782

SMC_prok_A

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

321-479

6.74e-08

Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 56.61 E-value: 6.74e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   321 ELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLK 400
Cdd:TIGR02169  792 RIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELE 871

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   401 EVRKKCAE-EAQL------ISSLKAELTSQESQISTYEEELAKAREELSRLQ-------QETAELEESVESGK------A 460
Cdd:TIGR02169  872 ELEAALRDlESRLgdlkkeRDELEAQLRELERKIEELEAQIEKKRKRLSELKaklealeEELSEIEDPKGEDEeipeeeL 951

                          170
                   ....*....|....*....
gi 119627229   461 QLEPLQQHLQDSQQEISSM 479
Cdd:TIGR02169  952 SLEDVQAELQRVEEEIRAL 970

COG4913

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

320-451

1.24e-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: 1.24e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  320 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRentNLQKLQAQKQQVQELLDELDEQKAQLEEQL 399
Cdd:COG4913   338 DRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAA---LRAEAAALLEALEEELEALEEALAEAEAAL 414

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 119627229  400 KEVRKKcaeeaqlISSLKAELTSQESQISTYEEELAKAREELSR-LQQETAEL 451
Cdd:COG4913   415 RDLRRE-------LRELEAEIASLERRKSNIPARLLALRDALAEaLGLDEAEL 460

COG4372

Uncharacterized protein, contains DUF3084 domain [Function unknown];

320-476

1.39e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];

Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 54.52 E-value: 1.39e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 320 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQL 399
Cdd:COG4372   87 EQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEEL 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 400 KEVRKKCA--EEAQLISSLKaELTSQESQISTYEEELAKA---REELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQ 474
Cdd:COG4372  167 AALEQELQalSEAEAEQALD-ELLKEANRNAEKEEELAEAeklIESLPRELAEELLEAKDSLEAKLGLALSALLDALELE 245


                 ..
gi 119627229 475 EI 476
Cdd:COG4372  246 ED 247

Mplasa_alph_rch

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

320-497

1.44e-07

Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 55.41 E-value: 1.44e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  320 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEqkaqLEEQL 399
Cdd:TIGR04523 152 KELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISE----LKKQN 227

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  400 KEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQET-------AELEESVESGKAQLEPL-QQHLQD 471
Cdd:TIGR04523 228 NQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELeqnnkkiKELEKQLNQLKSEISDLnNQKEQD 307

                         170       180
                  ....*....|....*....|....*.
gi 119627229  472 SQQEISSmQMKLMEmKDLENHNSQLN 497
Cdd:TIGR04523 308 WNKELKS-ELKNQE-KKLEEIQNQIS 331

PRK02224

DNA double-strand break repair Rad50 ATPase;

317-482

1.50e-07

DNA double-strand break repair Rad50 ATPase;

Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.43 E-value: 1.50e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 317 SAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDE------------VQRENtnlqkLQAQKQQVQEL 384
Cdd:PRK02224 346 SLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEieelrerfgdapVDLGN-----AEDFLEELREE 420

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 385 LDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEP 464
Cdd:PRK02224 421 RDELREREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLER 500

                        170
                 ....*....|....*...
gi 119627229 465 LQQhLQDSQQEISSMQMK 482
Cdd:PRK02224 501 AED-LVEAEDRIERLEER 517

YhaN

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

316-479

1.70e-07

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.16 E-value: 1.70e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 316 FSAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTnlqklqaqkqqVQELLDELDEQKAQL 395
Cdd:COG4717  343 LDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEE-----------YQELKEELEELEEQL 411

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 396 EEQLKEVRKkcAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVEsgkaqLEPLQQHLQDSQQE 475
Cdd:COG4717  412 EELLGELEE--LLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGE-----LAELLQELEELKAE 484


                 ....
gi 119627229 476 ISSM 479
Cdd:COG4717  485 LREL 488

PRK04778

septation ring formation regulator EzrA; Provisional

316-497

1.71e-07

septation ring formation regulator EzrA; Provisional

Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 54.84 E-value: 1.71e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 316 FSAIKELDTLNneIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLqDEVQRENtnlqklqaqkqqvqelldelDEQKAQL 395
Cdd:PRK04778  89 FEAEELNDKFR--FRKAKHEINEIESLLDLIEEDIEQILEELQEL-LESEEKN--------------------REEVEQL 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 396 EEQLKEVRKKCAEEA----QLISSLKAELTSQESQISTYEEELA-----KAREELSRLQQETAELEESVESGKAQLEPLQ 466
Cdd:PRK04778 146 KDLYRELRKSLLANRfsfgPALDELEKQLENLEEEFSQFVELTEsgdyvEAREILDQLEEELAALEQIMEEIPELLKELQ 225

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 119627229 467 QHLQDSQQEISS----MQMK---------LMEMKDLENHNSQLN 497
Cdd:PRK04778 226 TELPDQLQELKAgyreLVEEgyhldhldiEKEIQDLKEQIDENL 269

GumC

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

304-478

1.94e-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: 1.94e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 304 QKNIIGSSPVADFSAIKELDTLNNEIVDLQREK-------NNVEQDLKEKEDTIKQ--RTSEVQDLQDEVQRENTNLQKL 374
Cdd:COG3206  203 QKNGLVDLSEEAKLLLQQLSELESQLAEARAELaeaearlAALRAQLGSGPDALPEllQSPVIQQLRAQLAELEAELAEL 282

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 375 QAQKQQV----QELLDELDEQKAQLEEqlkevrkkcaEEAQLISSLKAELTSQESQISTYEEELAKAREELSRL---QQE 447
Cdd:COG3206  283 SARYTPNhpdvIALRAQIAALRAQLQQ----------EAQRILASLEAELEALQAREASLQAQLAQLEARLAELpelEAE 352

                        170       180       190
                 ....*....|....*....|....*....|.
gi 119627229 448 TAELEESVESGKAQLEPLQQHLQDSQQEISS 478
Cdd:COG3206  353 LRRLEREVEVARELYESLLQRLEEARLAEAL 383

PRK04778

septation ring formation regulator EzrA; Provisional

318-472

2.04e-07

septation ring formation regulator EzrA; Provisional

Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 54.46 E-value: 2.04e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 318 AIKELDTLNNEIVDL----QRE---KNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDe 390
Cdd:PRK04778 280 AEEKNEEIQERIDQLydilEREvkaRKYVEKNSDTLPDFLEHAKEQNKELKEEIDRVKQSYTLNESELESVRQLEKQLE- 358

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 391 qkaQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQ 470
Cdd:PRK04778 359 ---SLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKLHEIKRYLE 435


                 ..
gi 119627229 471 DS 472
Cdd:PRK04778 436 KS 437

COG2433

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

296-460

2.09e-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: 2.09e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 296 PPSDRASLQKNIIGSSPVADfsAIKEL--DTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQR-ENTnlq 372
Cdd:COG2433  361 PDVDRDEVKARVIRGLSIEE--ALEELieKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEElEAE--- 435

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 373 klqaqkqqvqelLDELDEQKAQLEEQLKEVRKKCAEEAQL---ISSLKAELTSQESQISTYEEELAKAREELSRLQqeta 449
Cdd:COG2433  436 ------------LEEKDERIERLERELSEARSEERREIRKdreISRLDREIERLERELEEERERIEELKRKLERLK---- 499

                        170
                 ....*....|.
gi 119627229 450 ELEESVESGKA 460
Cdd:COG2433  500 ELWKLEHSGEL 510

PRK03918

DNA double-strand break repair ATPase Rad50;

318-488

2.16e-07

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.68 E-value: 2.16e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 318 AIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQ-------------RENTNLQKLQAQKQQVQEL 384
Cdd:PRK03918 382 TGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEelkkakgkcpvcgRELTEEHRKELLEEYTAEL 461

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 385 ------LDELDEQKAQLEEQLKEVRKKCAEEAQLIS--SLKAELTSQESQISTYE-EELAKAREELSRLQQETAELE--- 452
Cdd:PRK03918 462 kriekeLKEIEEKERKLRKELRELEKVLKKESELIKlkELAEQLKELEEKLKKYNlEELEKKAEEYEKLKEKLIKLKgei 541

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 119627229 453 ESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKD 488
Cdd:PRK03918 542 KSLKKELEKLEELKKKLAELEKKLDELEEELAELLK 577

EnvC

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

348-451

2.28e-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: 2.28e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 348 DTIKQRTSEVQDLQDEVQRENtnlqklqaqkqqvqELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQI 427
Cdd:COG4942   20 DAAAEAEAELEQLQQEIAELE--------------KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL 85

                         90       100
                 ....*....|....*....|....
gi 119627229 428 STYEEELAKAREELSRLQQETAEL 451
Cdd:COG4942   86 AELEKEIAELRAELEAQKEELAEL 109

CwlO1

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

317-488

2.40e-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: 2.40e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 317 SAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEvqrentnlqklqaqkqqvqelldeLDEQKAQLE 396
Cdd:COG3883   34 AAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAE------------------------IEERREELG 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 397 EQLKEVRKKCAEE------------AQLISSLKA-------------ELTSQESQISTYEEELAKAREELSRLQQETAEL 451
Cdd:COG3883   90 ERARALYRSGGSVsyldvllgsesfSDFLDRLSAlskiadadadlleELKADKAELEAKKAELEAKLAELEALKAELEAA 169

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 119627229 452 EESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKD 488
Cdd:COG3883  170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELA 206

EF-hand_4

Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ...

19-67

3.08e-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: 49.29 E-value: 3.08e-07

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 119627229   19 GRVLASDAAAFLKKSGLPDLILGKIWDLADTDGKGILNKQEFFVALRLV 67
Cdd:pfam12763  24 NKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLI 72

EnvC

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

339-458

3.72e-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: 3.72e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 339 VEQDLKEKEDTIKQRTSEVQDLQDEVQREntnlqklqaqkqqvqelLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKA 418
Cdd:COG4942  144 LAPARREQAEELRADLAELAALRAELEAE-----------------RAELEALLAELEEERAALEALKAERQKLLARLEK 206

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 119627229 419 ELTSQESQISTYEEELAKAREELSRLQQETAELEESVESG 458
Cdd:COG4942  207 ELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246

CwlO1

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

317-483

4.21e-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: 4.21e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 317 SAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENtnlqklqaqkqqvqELLDELDEQKAQLE 396
Cdd:COG3883   13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQ--------------AEIDKLQAEIAEAE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 397 EQLKEVRKKCAEEAQ-------LISSLKAELTSQE-----------SQISTYE----EELAKAREELSRLQQETAELEES 454
Cdd:COG3883   79 AEIEERREELGERARalyrsggSVSYLDVLLGSESfsdfldrlsalSKIADADadllEELKADKAELEAKKAELEAKLAE 158

                        170       180
                 ....*....|....*....|....*....
gi 119627229 455 VESGKAQLEPLQQHLQDSQQEISSMQMKL 483
Cdd:COG3883  159 LEALKAELEAAKAELEAQQAEQEALLAQL 187

Smc

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

384-496

4.67e-07

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.79 E-value: 4.67e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 384 LLDELDEQKAQLEEQlkevRKKcAEEAQLISS----LKAELT-----SQESQISTYEEELAKAREELSRLQQETAELEES 454
Cdd:COG1196  194 ILGELERQLEPLERQ----AEK-AERYRELKEelkeLEAELLllklrELEAELEELEAELEELEAELEELEAELAELEAE 268

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 119627229 455 VESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKDLENHNSQL 496
Cdd:COG1196  269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER 310

COG1340

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

319-487

5.63e-07

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

Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 52.22 E-value: 5.63e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 319 IKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDEL---------- 388
Cdd:COG1340   52 VKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLewrqqtevls 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 389 -DEQK------AQLEEQLKEvRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAEL---------- 451
Cdd:COG1340  132 pEEEKelvekiKELEKELEK-AKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELykeadelrke 210

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 119627229 452 -----EESVESGKA------QLEPLQQHLQDSQQEISSMQMKLMEMK 487
Cdd:COG1340  211 adelhKEIVEAQEKadelheEIIELQKELRELRKELKKLRKKQRALK 257

COG4372

Uncharacterized protein, contains DUF3084 domain [Function unknown];

389-488

5.72e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];

Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.60 E-value: 5.72e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 389 DEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQH 468
Cdd:COG4372    2 DRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEE 81

                         90       100
                 ....*....|....*....|
gi 119627229 469 LQDSQQEISSMQMKLMEMKD 488
Cdd:COG4372   82 LEELNEQLQAAQAELAQAQE 101

MAD

pfam05557

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...

328-497

5.76e-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: 53.21 E-value: 5.76e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  328 EIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQD-EVQRENTNLQK--LQAQKQQVQELLDELDEQKAQLEEQLKEV-- 402
Cdd:pfam05557  28 ARIELEKKASALKRQLDRESDRNQELQKRIRLLEKrEAEAEEALREQaeLNRLKKKYLEALNKKLNEKESQLADAREVis 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  403 --RKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKA---QLEPLQQHLQ---DSQQ 474
Cdd:pfam05557 108 clKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEaeqRIKELEFEIQsqeQDSE 187

                         170       180       190
                  ....*....|....*....|....*....|
gi 119627229  475 EISSMQMKLMEMKDLEN-------HNSQLN 497
Cdd:pfam05557 188 IVKNSKSELARIPELEKelerlreHNKHLN 217

COG4913

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

314-473

6.07e-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: 6.07e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  314 ADFSAIKE-LDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRentnlqklqAQKQQVQELLDELDEQK 392
Cdd:COG4913   685 DDLAALEEqLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA---------AEDLARLELRALLEERF 755

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  393 AQL--EEQLKEVRKKCAEEAQLISSLKAELTSQ-ESQISTY-----------------------------EEELAKAREE 440
Cdd:COG4913   756 AAAlgDAVERELRENLEERIDALRARLNRAEEElERAMRAFnrewpaetadldadleslpeylalldrleEDGLPEYEER 835

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 119627229  441 LSRLQQET---------AELEESVESGKAQLEPLQQHLQDSQ 473
Cdd:COG4913   836 FKELLNENsiefvadllSKLRRAIREIKERIDPLNDSLKRIP 877

PRK02224

DNA double-strand break repair Rad50 ATPase;

308-491

6.17e-07

DNA double-strand break repair Rad50 ATPase;

Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.51 E-value: 6.17e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 308 IGSSPVADfsAIKE----LDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRtSEVQDLQDevQRENTNlqklqaqkqqvqE 383
Cdd:PRK02224 461 VEGSPHVE--TIEEdrerVEELEAELEDLEEEVEEVEERLERAEDLVEAE-DRIERLEE--RREDLE------------E 523

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 384 LLDELDEQKAQLEEQLKEVRKKCAEeaqlissLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESgKAQLE 463
Cdd:PRK02224 524 LIAERRETIEEKRERAEELRERAAE-------LEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIES-LERIR 595

                        170       180
                 ....*....|....*....|....*...
gi 119627229 464 PLQQHLQDSQQEISSMQMKLMEMKDLEN 491
Cdd:PRK02224 596 TLLAAIADAEDEIERLREKREALAELND 623

UPF0242

pfam06785

Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ...

341-479

6.49e-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: 6.49e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  341 QDLKEKEDTIKQRTSEVQDLQDEVQRENtnlqklqaqkqqvqELLDELDEQKAQLEEQLKEVRKKCAEEaqlisslkael 420
Cdd:pfam06785  83 EGFKILEETLEELQSEEERLEEELSQKE--------------EELRRLTEENQQLQIQLQQISQDFAEF----------- 137

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 119627229  421 tSQESqistyEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSM 479
Cdd:pfam06785 138 -RLES-----EEQLAEKQLLINEYQQTIEEQRSVLEKRQDQIENLESKVRDLNYEIKTL 190

CCDC22

pfam05667

Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...

320-467

7.05e-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: 7.05e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  320 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQdlqdEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQL 399
Cdd:pfam05667 335 EELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELE----ELKEQNEELEKQYKVKKKTLDLLPDAEENIAKLQALV 410

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119627229  400 KEVRKKCAEEAQL-----------ISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQ 467
Cdd:pfam05667 411 DASAQRLVELAGQwekhrvplieeYRALKEAKSNKEDESQRKLEEIKELREKIKEVAEEAKQKEELYKQLVAEYERLPK 489

Mplasa_alph_rch

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

320-497

8.37e-07

Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 52.72 E-value: 8.37e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  320 KELDTLNNEIVDLQREKnnvEQDL-KEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQ 398
Cdd:TIGR04523 288 KQLNQLKSEISDLNNQK---EQDWnKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRE 364

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  399 LKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAreelsrlQQETAELEESVESGKAQLEPLQQHLQDSQQEISS 478
Cdd:TIGR04523 365 LEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQ-------EKLNQQKDEQIKKLQQEKELLEKEIERLKETIIK 437

                         170
                  ....*....|....*....
gi 119627229  479 MQmklMEMKDLENHNSQLN 497
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 ...

383-452

9.71e-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: 46.92 E-value: 9.71e-07

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  383 ELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELE 452
Cdd:pfam12329   5 KLLKEKDEQIAQLMEEGEKLSKKELKLNNTIKKLRAKNKELEKEIAELKKKLEKLEKELENLEERLKRAE 74

MscS_porin

pfam12795

Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...

317-477

1.26e-06

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: 50.38 E-value: 1.26e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  317 SAIKELDTLNNEIVDLQREKNNV------EQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDE 390
Cdd:pfam12795  48 DAPAELRELRQELAALQAKAEAApkeilaSLSLEELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQ 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  391 QKAQLEEQLK--EVRKKCAEEAQLIsSLKAELTSQESQISTYEEELAKA--REELSRLQQETAeleesvesgKAQLEPLQ 466
Cdd:pfam12795 128 RLQQIRNRLNgpAPPGEPLSEAQRW-ALQAELAALKAQIDMLEQELLSNnnRQDLLKARRDLL---------TLRIQRLE 197

                         170
                  ....*....|.
gi 119627229  467 QHLQDSQQEIS 477
Cdd:pfam12795 198 QQLQALQELLN 208

Mplasa_alph_rch

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

319-488

1.63e-06

Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.94 E-value: 1.63e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  319 IKELDT----LNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQ 394
Cdd:TIGR04523 456 IKNLDNtresLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKE 535

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  395 LEEQLKEVRKKcaeeaqlISSLKAELTSqesqiSTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQ 474
Cdd:TIGR04523 536 KESKISDLEDE-------LNKDDFELKK-----ENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIK 603

                         170
                  ....*....|....
gi 119627229  475 EISSMQMKLMEMKD 488
Cdd:TIGR04523 604 EIEEKEKKISSLEK 617

Mplasa_alph_rch

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

320-488

1.95e-06

Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.56 E-value: 1.95e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  320 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTnlqklqaqkqQVQELLDELDE-----QKAQ 394
Cdd:TIGR04523 489 KELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKES----------KISDLEDELNKddfelKKEN 558

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  395 LEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEplqqhlqdsqq 474
Cdd:TIGR04523 559 LEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENE----------- 627

                         170
                  ....*....|....
gi 119627229  475 EISSMQMKLMEMKD 488
Cdd:TIGR04523 628 KLSSIIKNIKSKKN 641

GumC

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

300-462

2.73e-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: 2.73e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 300 RASLQKNI-IGSSPVADFSAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQREntnlqklqaqk 378
Cdd:COG3206  242 LAALRAQLgSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQE----------- 310

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 379 qqVQELLDELDEQKAQLEEQLKEVRkkcAEEAQLISSLKaELTSQESQISTYEEELAKAREELSRLQQ--ETAELEESVE 456
Cdd:COG3206  311 --AQRILASLEAELEALQAREASLQ---AQLAQLEARLA-ELPELEAELRRLEREVEVARELYESLLQrlEEARLAEALT 384


                 ....*.
gi 119627229 457 SGKAQL 462
Cdd:COG3206  385 VGNVRV 390

SMC_prok_B

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

384-497

4.02e-06

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.83 E-value: 4.02e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   384 LLDELDEQKAQLEEQLKEV----RKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVE--- 456
Cdd:TIGR02168  194 ILNELERQLKSLERQAEKAerykELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEelr 273

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 119627229   457 ----SGKAQLEPLQQHLQDSQQEISSMQMKLM----EMKDLENHNSQLN 497
Cdd:TIGR02168  274 levsELEEEIEELQKELYALANEISRLEQQKQilreRLANLERQLEELE 322

YhaN

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

385-496

4.07e-06

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 4.07e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 385 LDELDEqkaqLEEQLKEVRKKCAEEAQLIsslkAELTSQESQISTYEEELAKAREELSRLQQ--ETAELEESVESGKAQL 462
Cdd:COG4717   70 LKELKE----LEEELKEAEEKEEEYAELQ----EELEELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAEL 141

                         90       100       110
                 ....*....|....*....|....*....|....
gi 119627229 463 EPLQQHLQDSQQEISSMQMKLMEMKDLENHNSQL 496
Cdd:COG4717  142 AELPERLEELEERLEELRELEEELEELEAELAEL 175

CwlO1

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

419-489

5.04e-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: 5.04e-06

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119627229 419 ELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKDL 489
Cdd:COG3883   17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREE 87

Golgin_A5

pfam09787

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...

324-572

5.12e-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: 5.12e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  324 TLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQREntnlqklqaqkqqvqelLDELDEQKAQLEEQLKEVR 403
Cdd:pfam09787  44 ALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEE-----------------AESSREQLQELEEQLATER 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  404 kkcaeeaqlisSLKAELtsqESQISTYEEELAKAREELSR----LQQETAELEESVESGKAQLEPLQQHlQDSQQEISSM 479
Cdd:pfam09787 107 -----------SARREA---EAELERLQEELRYLEEELRRskatLQSRIKDREAEIEKLRNQLTSKSQS-SSSQSELENR 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  480 QMKLMEmkDLENHNSQLNWCSSPHSILVngatdyCSLSTSSSETANLNEHVEGQSNLESEPIHQESPARSSPelLPSGVT 559
Cdd:pfam09787 172 LHQLTE--TLIQKQTMLEALSTEKNSLV------LQLERMEQQIKELQGEGSNGTSINMEGISDGEGTRLRN--VPGLFS 241

                         250
                  ....*....|...
gi 119627229  560 DENEVTTAVTEKV 572
Cdd:pfam09787 242 ESDSDRAGMYGKV 254

MAD

pfam05557

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...

320-495

5.29e-06

Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 50.12 E-value: 5.29e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  320 KELDTLNNEIVDLQREKNNVEQDlKEKEDTIKQRTSEVQDLQDEVQR---ENtnlqklqaqkqqvqELLDELDEQKAQLE 396
Cdd:pfam05557 163 SSLAEAEQRIKELEFEIQSQEQD-SEIVKNSKSELARIPELEKELERlreHN--------------KHLNENIENKLLLK 227

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  397 EQLKEVRKKC-------AEEAQL---ISSLKAELTSQESQISTYEEELAK---AREELSRLQQETAELEESVESGKAQLE 463
Cdd:pfam05557 228 EEVEDLKRKLereekyrEEAATLeleKEKLEQELQSWVKLAQDTGLNLRSpedLSRRIEQLQQREIVLKEENSSLTSSAR 307

                         170       180       190
                  ....*....|....*....|....*....|...
gi 119627229  464 PLQQHLQDSQQEISSMQMKLMEM-KDLENHNSQ 495
Cdd:pfam05557 308 QLEKARRELEQELAQYLKKIEDLnKKLKRHKAL 340

EzrA

pfam06160

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

341-493

6.21e-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: 6.21e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  341 QDLKEKEDTIKQRTSEVQDLQDEVQrentnlqklqaqkqqvqELLDELDEQKA---QLEEQLKEVRKKCAEEA----QLI 413
Cdd:pfam06160  86 KALDEIEELLDDIEEDIKQILEELD-----------------ELLESEEKNREeveELKDKYRELRKTLLANRfsygPAI 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  414 SSLKAELTSQESQISTYEEELA-----KAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMK- 487
Cdd:pfam06160 149 DELEKQLAEIEEEFSQFEELTEsgdylEAREVLEKLEEETDALEELMEDIPPLYEELKTELPDQLEELKEGYREMEEEGy 228


                  ....*.
gi 119627229  488 DLENHN 493
Cdd:pfam06160 229 ALEHLN 234

SCP-1

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

329-495

6.71e-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: 6.71e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  329 IVDLQREK-NNVEQDLKEKEDTIKQR-------TSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKaqlEEQLK 400
Cdd:pfam05483 262 LLEESRDKaNQLEEKTKLQDENLKELiekkdhlTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEK---EAQME 338

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  401 EVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELS----RLQQETAELEE--------SVE------------ 456
Cdd:pfam05483 339 ELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKiitmELQKKSSELEEmtkfknnkEVEleelkkilaede 418

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 119627229  457 ---SGKAQLEPLQQHLQDSQQ-----------EISSMQMKLMEMKDLENHNSQ 495
Cdd:pfam05483 419 kllDEKKQFEKIAEELKGKEQelifllqarekEIHDLEIQLTAIKTSEEHYLK 471

EF-hand_4

Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ...

209-306

7.41e-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: 7.41e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  209 PAEKAKYDEIFlKTDKDMDGFVSGLEVREIFLKTGLPSTLLAHIWSLCDTKDCGKLSKDQFALAFHLISQkLIKGI--DP 286
Cdd:pfam12763   6 EWEIKKYWEIF-SGLKPENNKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLIFD-LVNGNiaDV 83

                          90       100
                  ....*....|....*....|
gi 119627229  287 PHVLTPEMIPPSDRASLQKN 306
Cdd:pfam12763  84 PDELPDWLVPGSKAHLIQAN 103

PRK03918

DNA double-strand break repair ATPase Rad50;

319-453

7.61e-06

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.68 E-value: 7.61e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 319 IKELDTLNNEIVDLQreknNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTnlqklqaqkqQVQELLDELDE-QKAQLEE 397
Cdd:PRK03918 594 LKELEPFYNEYLELK----DAEKELEREEKELKKLEEELDKAFEELAETEK----------RLEELRKELEElEKKYSEE 659

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119627229 398 QLKEVRKKCAEEAQLISSLKAELTSQESQISTYE----------EELAKAREELSRLQQETAELEE 453
Cdd:PRK03918 660 EYEELREEYLELSRELAGLRAELEELEKRREEIKktleklkeelEEREKAKKELEKLEKALERVEE 725

MAP7

pfam05672

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...

332-451

7.67e-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: 46.57 E-value: 7.67e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  332 LQREKNNVEQDLKE------KEDTIKQRTSEVQDLQDEVQRentnlqklqaqkqqvqelLDEldEQKAQLEEQLKEVRKK 405
Cdd:pfam05672  25 EQREREEQERLEKEeeerlrKEELRRRAEEERARREEEARR------------------LEE--ERRREEEERQRKAEEE 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 119627229  406 CAEEAQlisslkAELTSQESQISTYEEELAKAREELSRLQQETAEL 451
Cdd:pfam05672  85 AEEREQ------REQEEQERLQKQKEEAEAKAREEAERQRQEREKI 124

PRK12704

phosphodiesterase; Provisional

386-491

8.49e-06

phosphodiesterase; Provisional

Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 49.39 E-value: 8.49e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 386 DELDEQKAQLEEQLKEVRKKcaeeaqlISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPL 465
Cdd:PRK12704  64 EEIHKLRNEFEKELRERRNE-------LQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEEL 136

                         90       100
                 ....*....|....*....|....*....
gi 119627229 466 QQHLQDSQQEISSMQM---KLMEMKDLEN 491
Cdd:PRK12704 137 IEEQLQELERISGLTAeeaKEILLEKVEE 165

COG4913

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

383-483

8.89e-06

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

Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 8.89e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  383 ELLDELDEQKAQLEEQLKEVRKKCAEEAQL---------ISSLKAELTSQESQISTYEE---ELAKAREELSRLQQETAE 450
Cdd:COG4913   624 EELAEAEERLEALEAELDALQERREALQRLaeyswdeidVASAEREIAELEAELERLDAssdDLAALEEQLEELEAELEE 703

                          90       100       110
                  ....*....|....*....|....*....|...
gi 119627229  451 LEESVESGKAQLEPLQQHLQDSQQEISSMQMKL 483
Cdd:COG4913   704 LEEELDELKGEIGRLEKELEQAEEELDELQDRL 736

MukB

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

385-496

9.31e-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: 49.57 E-value: 9.31e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  385 LDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQ--- 461
Cdd:COG3096   524 LEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARapa 603

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 119627229  462 -------LEPLQQH----LQDSQQEISSMQMKLMEMKDLENHNSQL 496
Cdd:COG3096   604 wlaaqdaLERLREQsgeaLADSQEVTAAMQQLLEREREATVERDEL 649

CwlO1

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

340-488

1.17e-05

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

Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 1.17e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 340 EQDLKEKEDTIKQRTSEVQDLQDEvqrentnlqklqaqkqqvqelLDELDEQKAQLEEQLKEVRKKcaeeaqlISSLKAE 419
Cdd:COG3883   15 DPQIQAKQKELSELQAELEAAQAE---------------------LDALQAELEELNEEYNELQAE-------LEALQAE 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 420 LTSQESQISTYEEELAKAREEL------------------------------------SRLQQETAELEESVESGKAQLE 463
Cdd:COG3883   67 IDKLQAEIAEAEAEIEERREELgeraralyrsggsvsyldvllgsesfsdfldrlsalSKIADADADLLEELKADKAELE 146

                        170       180
                 ....*....|....*....|....*
gi 119627229 464 PLQQHLQDSQQEISSMQMKLMEMKD 488
Cdd:COG3883  147 AKKAELEAKLAELEALKAELEAAKA 171

HOOK

pfam05622

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...

261-480

1.17e-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: 1.17e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  261 CGKLSKDQFALAFHLISqkliKGIDPPHVLTPEMIPPsdraslqkniigsspvadfsAIKEldtlnnEIVDLQREkNNVe 340
Cdd:pfam05622 246 CAQLQQAELSQADALLS----PSSDPGDNLAAEIMPA--------------------EIRE------KLIRLQHE-NKM- 293

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  341 qdLKEK-EDTIKQRTSEVQdlqdevqrentnlqklqaqkqqvqELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAE 419
Cdd:pfam05622 294 --LRLGqEGSYRERLTELQ------------------------QLLEDANRRKNELETQNRLANQRILELQQQVEELQKA 347

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119627229  420 LTSQESQ----------ISTYEEELAKAREELSRLQQETAELEESVESGKAQ-LEPLQQHLQDSQQEISSMQ 480
Cdd:pfam05622 348 LQEQGSKaedssllkqkLEEHLEKLHEAQSELQKKKEQIEELEPKQDSNLAQkIDELQEALRKKDEDMKAME 419

PRK12704

phosphodiesterase; Provisional

318-487

1.23e-05

phosphodiesterase; Provisional

Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 49.01 E-value: 1.23e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 318 AIKELDTLNNEIV-----DLQREKNNVEQDLKEKEDTIKQRTSEVQdlqdevQRENtnlqklqaqkqqvqelldeldeqk 392
Cdd:PRK12704  47 AKKEAEAIKKEALleakeEIHKLRNEFEKELRERRNELQKLEKRLL------QKEE------------------------ 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 393 aQLEEQLKEVRKKcaeeaqlisslKAELTSQESQISTYEEELAKAREELSRLQQET-AELEE----SVESGKAQLepLQQ 467
Cdd:PRK12704  97 -NLDRKLELLEKR-----------EEELEKKEKELEQKQQELEKKEEELEELIEEQlQELERisglTAEEAKEIL--LEK 162

                        170       180
                 ....*....|....*....|
gi 119627229 468 HLQDSQQEISSMqMKLMEMK 487
Cdd:PRK12704 163 VEEEARHEAAVL-IKEIEEE 181

PTZ00121

MAEBL; Provisional

333-605

1.42e-05

MAEBL; Provisional

Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 1.42e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  333 QREKNNVEQdLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLK----------EV 402
Cdd:PTZ00121 1629 EEEKKKVEQ-LKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKkeaeeakkaeEL 1707

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  403 RKKCAEE---------AQLISSLKAE-LTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDS 472
Cdd:PTZ00121 1708 KKKEAEEkkkaeelkkAEEENKIKAEeAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDE 1787

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  473 QQEISSMQMKlMEMKDLENHNSQLNWCSSPHSILVN-------GATDYCSLSTSS--SETANLNEHVEGQSNLESEPIHQ 543
Cdd:PTZ00121 1788 EDEKRRMEVD-KKIKDIFDNFANIIEGGKEGNLVINdskemedSAIKEVADSKNMqlEEADAFEKHKFNKNNENGEDGNK 1866

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119627229  544 ESPARSSPELLPSgvtDENEVTTAvteKVCSELDNNrhSKEEDPFNVDSSSLTGPVADTNLD 605
Cdd:PTZ00121 1867 EADFNKEKDLKED---DEEEIEEA---DEIEKIDKD--DIEREIPNNNMAGKNNDIIDDKLD 1920

ERM_helical

pfam20492

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...

391-490

1.50e-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: 44.91 E-value: 1.50e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  391 QKAQLEEQLKEVRkkcaEEAQLIsslKAELTSQESQISTYEEELAKAREELSRLQQ-------ETAELEESVESGKAQLE 463
Cdd:pfam20492   7 EKQELEERLKQYE----EETKKA---QEELEESEETAEELEEERRQAEEEAERLEQkrqeaeeEKERLEESAEMEAEEKE 79

                          90       100
                  ....*....|....*....|....*..
gi 119627229  464 PLQQHLQDSQQEISSMQMKlMEMKDLE 490
Cdd:pfam20492  80 QLEAELAEAQEEIARLEEE-VERKEEE 105

Nuf2_DHR10-like

pfam18595

Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ...

331-467

1.50e-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: 44.88 E-value: 1.50e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  331 DLQREKNNVE------QDLKEKEDTIKQRTSEV-------QDLQDEVQRENtnlqklqaqkqqvqELLDELDEQKAQLEE 397
Cdd:pfam18595   3 TLAEEKEELAelerkaRELQAKIDALQVVEKDLrscikllEEIEAELAKLE--------------EAKKKLKELRDALEE 68

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  398 QLKEVRkkcaeeaqlisslkaELTSQESQIstyEEELAKAREELSRLQQETaelEESVESGKAQLEPLQQ 467
Cdd:pfam18595  69 KEIELR---------------ELERREERL---QRQLENAQEKLERLREQA---EEKREAAQARLEELRE 117

DR0291

COG1579

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

383-483

1.76e-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: 1.76e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 383 ELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKARE---------ELSRLQQETA---- 449
Cdd:COG1579   24 HRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlgnvrnnkEYEALQKEIEslkr 103

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 119627229 450 ----------ELEESVESGKAQLEPLQQHLQDSQQEISSMQMKL 483
Cdd:COG1579  104 risdledeilELMERIEELEEELAELEAELAELEAELEEKKAEL 147

SMC_prok_A

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

307-491

1.77e-05

Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.53 E-value: 1.77e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   307 IIGSSPVADFSAIKELDTlnneIVDLQREKnnveQDLKEKEDTIKQRTSEVQDLQDEVQREntnlqklqaqkqqvqelLD 386
Cdd:TIGR02169  147 FISMSPVERRKIIDEIAG----VAEFDRKK----EKALEELEEVEENIERLDLIIDEKRQQ-----------------LE 201

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   387 ELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQ----ESQISTYEEELAKAREELSRLQQETAELEESVESGKAQL 462
Cdd:TIGR02169  202 RLRREREKAERYQALLKEKREYEGYELLKEKEALERQkeaiERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKI 281

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 119627229   463 EPL--------QQHLQDSQQEISSMQ----MKLMEMKDLEN 491
Cdd:TIGR02169  282 KDLgeeeqlrvKEKIGELEAEIASLErsiaEKERELEDAEE 322

rad50

rad50; All proteins in this family for which functions are known are involvedin recombination, ...

319-495

1.81e-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: 1.81e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   319 IKELDTLNNEI----VDLQREKNNVEQDLKEKEdTIKQRTSEVQDLQDEV------QRENTNLQKLQAQKQQVQELLD-- 386
Cdd:TIGR00606  743 EKEIPELRNKLqkvnRDIQRLKNDIEEQETLLG-TIMPEEESAKVCLTDVtimerfQMELKDVERKIAQQAAKLQGSDld 821

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   387 ----ELDEQKAQLEEQLK------EVRKKCAEEAQ-LISSLKA---ELTSQESQISTYEEELAKAREELSRLQQETAELE 452
Cdd:TIGR00606  822 rtvqQVNQEKQEKQHELDtvvskiELNRKLIQDQQeQIQHLKSktnELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLI 901

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 119627229   453 ESVESGKAQLEPLQQHLQDSQQEissmQMKLMEMKDLENHNSQ 495
Cdd:TIGR00606  902 REIKDAKEQDSPLETFLEKDQQE----KEELISSKETSNKKAQ 940

Apolipoprotein

pfam01442

Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...

322-474

1.86e-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: 1.86e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  322 LDTLNNEIVDLQREKNNVEQDLKEKedtikqRTSEVQDLQDEVQREntnlqklqaqkqqvqelldeLDEQKAQLEEQLKE 401
Cdd:pfam01442   6 LDELSTYAEELQEQLGPVAQELVDR------LEKETEALRERLQKD--------------------LEEVRAKLEPYLEE 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  402 VRKKCAEEAQLissLKAELtsqESQISTYEEELAKAREELSR-LQQETAELEESVESG----KAQLEP--------LQQH 468
Cdd:pfam01442  60 LQAKLGQNVEE---LRQRL---EPYTEELRKRLNADAEELQEkLAPYGEELRERLEQNvdalRARLAPyaeelrqkLAER 133


                  ....*.
gi 119627229  469 LQDSQQ 474
Cdd:pfam01442 134 LEELKE 139

PspA_IM30

pfam04012

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

336-483

1.96e-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: 46.60 E-value: 1.96e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  336 KNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEaqLISS 415
Cdd:pfam04012  10 RANIHEGLDKAEDPEKMLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGNEE--LARE 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119627229  416 LKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQqhlqdSQQEISSMQMKL 483
Cdd:pfam04012  88 ALAEKKSLEKQAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLK-----ARLKAAKAQEAV 150

YhaN

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

384-496

2.23e-05

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 2.23e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 384 LLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLE 463
Cdd:COG4717   47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 119627229 464 P---------LQQHLQDSQQEISSMQMKLMEMKDLENHNSQL 496
Cdd:COG4717  127 LlplyqeleaLEAELAELPERLEELEERLEELRELEEELEEL 168

ClpA

COG0542

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

321-455

2.35e-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: 2.35e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 321 ELDTLNNEIVDLQREKNNVEqdlKEKEDTIKQRtsevqdlqdevqrentnlqklqaqkqqvqelLDELDEQKAQLEEQLK 400
Cdd:COG0542  412 ELDELERRLEQLEIEKEALK---KEQDEASFER-------------------------------LAELRDELAELEEELE 457

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 119627229 401 EVRKKCAEEAQLIS---SLKAELTSQESQISTYEEELAKAREELSrlqQETAELEESV 455
Cdd:COG0542  458 ALKARWEAEKELIEeiqELKEELEQRYGKIPELEKELAELEEELA---ELAPLLREEV 512

SMC_prok_A

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

313-487

2.66e-05

Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.14 E-value: 2.66e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   313 VADFSAikELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQK 392
Cdd:TIGR02169  296 IGELEA--EIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAEL 373

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   393 AQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTY-------EEELAKAREELSRLQQETAELEESVESGKAQLEPL 465
Cdd:TIGR02169  374 EEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLqeelqrlSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQ 453

                          170       180
                   ....*....|....*....|..
gi 119627229   466 QQHLQDSQQEISSMQMKLMEMK 487
Cdd:TIGR02169  454 EWKLEQLAADLSKYEQELYDLK 475

EnvC

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

406-496

2.75e-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: 2.75e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 406 CAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLME 485
Cdd:COG4942   15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94

                         90
                 ....*....|..
gi 119627229 486 M-KDLENHNSQL 496
Cdd:COG4942   95 LrAELEAQKEEL 106

PRK03918

DNA double-strand break repair ATPase Rad50;

320-497

2.77e-05

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.14 E-value: 2.77e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 320 KELDTLNNEIVDLQR---EKNNVE---QDLKEKEDTIKQRTSE----VQDLQD----EVQRENTNLQKLQAQKQQVQELL 385
Cdd:PRK03918 314 KRLSRLEEEINGIEErikELEEKEerlEELKKKLKELEKRLEEleerHELYEEakakKEELERLKKRLTGLTPEKLEKEL 393

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 386 DELDEQKAQLEEQLKEVRKKCAEEAQLISSLKA-----------------ELTSQESqistyEEELAKAREELSRLQQET 448
Cdd:PRK03918 394 EELEKAKEEIEEEISKITARIGELKKEIKELKKaieelkkakgkcpvcgrELTEEHR-----KELLEEYTAELKRIEKEL 468

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 119627229 449 AELEESVESGKAQLEPLQQHLQDsQQEISSMQMKLMEMKDLENHNSQLN 497
Cdd:PRK03918 469 KEIEEKERKLRKELRELEKVLKK-ESELIKLKELAEQLKELEEKLKKYN 516

PHA02562

endonuclease subunit; Provisional

321-485

3.56e-05

endonuclease subunit; Provisional

Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 47.32 E-value: 3.56e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 321 ELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQ--RENTNLQKLQAQKQQVQELLDELDEQKAQLEEQ 398
Cdd:PHA02562 235 EIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKmyEKGGVCPTCTQQISEGPDRITKIKDKLKELQHS 314

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 399 LKEVRKKCAEEAQLISSLKA---ELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQE 475
Cdd:PHA02562 315 LEKLDTAIDELEEIMDEFNEqskKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKT 394

                        170
                 ....*....|
gi 119627229 476 ISSMQMKLME 485
Cdd:PHA02562 395 KSELVKEKYH 404

CALCOCO1

pfam07888

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...

323-492

3.84e-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: 3.84e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  323 DTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRentnlqkLQAQKQQVQELLDELDEQKAQLEEQLKEV 402
Cdd:pfam07888 111 EELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELER-------MKERAKKAGAQRKEEEAERKQLQAKLQQT 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  403 RKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESvesgKAQLEPLQQHLQDSQQEISSMQMK 482
Cdd:pfam07888 184 EEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEAL----LEELRSLQERLNASERKVEGLGEE 259

                         170
                  ....*....|
gi 119627229  483 LMEMKDLENH 492
Cdd:pfam07888 260 LSSMAAQRDR 269

PHA02562

endonuclease subunit; Provisional

315-496

4.72e-05

endonuclease subunit; Provisional

Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.93 E-value: 4.72e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 315 DFSAIKELDTLNNeivDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENT-NLQKLQAQKQQVQELLDELDEQKA 393
Cdd:PHA02562 161 DISVLSEMDKLNK---DKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGeNIARKQNKYDELVEEAKTIKAEIE 237

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 394 QLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKARE---------ELSRLQQETAELEESVESGKAQLEP 464
Cdd:PHA02562 238 ELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKggvcptctqQISEGPDRITKIKDKLKELQHSLEK 317

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 119627229 465 LQQHLQDSQQ---EISSMQMKLMEMK-DLENHNSQL 496
Cdd:PHA02562 318 LDTAIDELEEimdEFNEQSKKLLELKnKISTNKQSL 353

Apolipoprotein

pfam01442

Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...

385-476

4.91e-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: 4.91e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  385 LDELDEQKAQLEEQL----KEVRKKCAEEAQ-LISSLKAELTSQESQISTYEEEL-AKAREELSRLQQETAEL-EESVES 457
Cdd:pfam01442   6 LDELSTYAEELQEQLgpvaQELVDRLEKETEaLRERLQKDLEEVRAKLEPYLEELqAKLGQNVEELRQRLEPYtEELRKR 85

                          90
                  ....*....|....*....
gi 119627229  458 GKAQLEPLQQHLQDSQQEI 476
Cdd:pfam01442  86 LNADAEELQEKLAPYGEEL 104

PRK02224

DNA double-strand break repair Rad50 ATPase;

331-495

4.95e-05

DNA double-strand break repair Rad50 ATPase;

Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.34 E-value: 4.95e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 331 DLQREKNNVeqdLKEKEDTIKQRtsEVQDLQDEVQRENTnlqklqaQKQQVQELLDELDEQKAQLEEQL---KEVRKKCA 407
Cdd:PRK02224 180 RVLSDQRGS---LDQLKAQIEEK--EEKDLHERLNGLES-------ELAELDEEIERYEEQREQARETRdeaDEVLEEHE 247

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 408 EEAQLISSLKAELTSQESQISTYE-------EELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQ 480
Cdd:PRK02224 248 ERREELETLEAEIEDLRETIAETErereelaEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELR 327

                        170
                 ....*....|....*.
gi 119627229 481 MKLMEMK-DLENHNSQ 495
Cdd:PRK02224 328 DRLEECRvAAQAHNEE 343

sbcc

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

317-504

5.30e-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: 5.30e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   317 SAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQREntnlqklqaqKQQVQELLDELDEQKAQLE 396
Cdd:TIGR00618  553 SERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKL----------SEAEDMLACEQHALLRKLQ 622

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   397 EQLKEVRKKcAEEAQLISSLKAELTSQESqistYEEELAKAREELS--RLQQETAELEESVESGKAQLEPLQQHLQDSQQ 474
Cdd:TIGR00618  623 PEQDLQDVR-LHLQQCSQELALKLTALHA----LQLTLTQERVREHalSIRVLPKELLASRQLALQKMQSEKEQLTYWKE 697

                          170       180       190
                   ....*....|....*....|....*....|..
gi 119627229   475 EISSMQMKLMEMKDLENHNSQL--NWCSSPHS 504
Cdd:TIGR00618  698 MLAQCQTLLRELETHIEEYDREfnEIENASSS 729

CENP-F_leu_zip

pfam10473

Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ...

389-489

5.39e-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: 43.82 E-value: 5.39e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  389 DEQKAQLEEQLKEVRKKCAEEAQLISSLKAEL-TSQESQ------ISTYEEELAKAREELSRLQQETAELEESVESGKAQ 461
Cdd:pfam10473   2 EKKQLHVLEKLKESERKADSLKDKVENLERELeMSEENQelaileAENSKAEVETLKAEIEEMAQNLRDLELDLVTLRSE 81

                          90       100
                  ....*....|....*....|....*...
gi 119627229  462 LEPLQQHLQDSQQEISSMQMKLMEMKDL 489
Cdd:pfam10473  82 KENLTKELQKKQERVSELESLNSSLENL 109

Mplasa_alph_rch

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

320-455

5.67e-05

Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.94 E-value: 5.67e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  320 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEvqrentnlqklqaqkqqvqelLDELDEQKAQLEEQL 399
Cdd:TIGR04523 561 KEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKE---------------------IEEKEKKISSLEKEL 619

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 119627229  400 KEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESV 455
Cdd:TIGR04523 620 EKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKI 675

DUF3450

pfam11932

Protein of unknown function (DUF3450); This family of proteins are functionally ...

386-476

5.71e-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: 5.71e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  386 DELDEQKAQLEEQLKevrkkcaeeaqlisSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEEsvesGKAQLEPL 465
Cdd:pfam11932  37 DKWDDEKQELLAEYR--------------ALKAELESLEVYNRQLERLVASQEQEIASLERQIEEIER----TERELVPL 98

                          90
                  ....*....|.
gi 119627229  466 QQHLQDSQQEI 476
Cdd:pfam11932  99 MLKMLDRLEQF 109

SMC_prok_B

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

385-488

6.34e-05

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.97 E-value: 6.34e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   385 LDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEP 464
Cdd:TIGR02168  679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758

                           90       100
                   ....*....|....*....|....
gi 119627229   465 LQQHLQDSQQEISSMQMKLMEMKD 488
Cdd:TIGR02168  759 LEAEIEELEERLEEAEEELAEAEA 782

hsdR

PRK11448

type I restriction enzyme EcoKI subunit R; Provisional

383-481

6.75e-05

type I restriction enzyme EcoKI subunit R; Provisional

Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 46.87 E-value: 6.75e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  383 ELLDELDEQKAQLEEQLKEVrkkcAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAEleesvesgkAQL 462
Cdd:PRK11448  146 ALQQEVLTLKQQLELQAREK----AQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAE---------TSQ 212

                          90
                  ....*....|....*....
gi 119627229  463 EPLQQHLQDSQQEISSMQM 481
Cdd:PRK11448  213 ERKQKRKEITDQAAKRLEL 231

ERM_helical

pfam20492

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...

333-475

7.40e-05

Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 42.98 E-value: 7.40e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  333 QREKNNVEQDLKEKEDTIKQRTsevQDLQDEVQRentnlqklqaqkqqvqelLDELDEQ--KAQLEEQLKEVRKKCAEEA 410
Cdd:pfam20492   5 EREKQELEERLKQYEEETKKAQ---EELEESEET------------------AEELEEErrQAEEEAERLEQKRQEAEEE 63

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119627229  411 qlisslKAELtsQESQISTyEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQE 475
Cdd:pfam20492  64 ------KERL--EESAEME-AEEKEQLEAELAEAQEEIARLEEEVERKEEEARRLQEELEEAREE 119

PRK02224

DNA double-strand break repair Rad50 ATPase;

321-476

7.90e-05

DNA double-strand break repair Rad50 ATPase;

Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.57 E-value: 7.90e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 321 ELDTLNNEIVDLQREknNVEQDLKEKEDTIKQRTSEVQDLQDEVQREntnlqklqaqkqqvQELLDELDEQKAQLEEQLK 400
Cdd:PRK02224 303 GLDDADAEAVEARRE--ELEDRDEELRDRLEECRVAAQAHNEEAESL--------------REDADDLEERAEELREEAA 366

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119627229 401 EVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEI 476
Cdd:PRK02224 367 ELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERV 442

SCP-1

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

315-492

8.58e-05

Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 46.25 E-value: 8.58e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  315 DFSAIKELDTlnneivDLQREKNNVEQDLK-------EKEDTIKQRTSEVQDLQDEVQR--ENTNlqklqaqkqQVQELL 385
Cdd:pfam05483 220 DHEKIQHLEE------EYKKEINDKEKQVSllliqitEKENKMKDLTFLLEESRDKANQleEKTK---------LQDENL 284

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  386 DELDEQKAQLEEQLKEVR----------KKCAEEAQLISSLKAELTSQ-ESQIstyeEELAKAREE----LSRLQQETAE 450
Cdd:pfam05483 285 KELIEKKDHLTKELEDIKmslqrsmstqKALEEDLQIATKTICQLTEEkEAQM----EELNKAKAAhsfvVTEFEATTCS 360

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 119627229  451 LEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKDLENH 492
Cdd:pfam05483 361 LEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNN 402

CCDC158

pfam15921

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...

320-570

8.77e-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: 46.26 E-value: 8.77e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   320 KELDTLNNEIVDLQREKNNVEQDLK-----------EKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQEL---- 384
Cdd:pfam15921  653 QERDQLLNEVKTSRNELNSLSEDYEvlkrnfrnkseEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVamgm 732

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   385 ----------LDELDEQKAQLEEQLKEVRKkcaeEAQLISSLKAELTSQESQISTYEE----ELAKAREELSRLQQETAE 450
Cdd:pfam15921  733 qkqitakrgqIDALQSKIQFLEEAMTNANK----EKHFLKEEKNKLSQELSTVATEKNkmagELEVLRSQERRLKEKVAN 808

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   451 LEESVESGKAQLEPLQQHLQDSQQEisSMQMKL---MEMKDLENHNSQLNWCSSPHSILVNGATDYCSLSTSSSETANLN 527
Cdd:pfam15921  809 MEVALDKASLQFAECQDIIQRQEQE--SVRLKLqhtLDVKELQGPGYTSNSSMKPRLLQPASFTRTHSNVPSSQSTASFL 886

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 119627229   528 EHVEGQSNlesepIHQESPARSSPELLP---SGVTDENEVTTAVTE 570
Cdd:pfam15921  887 SHHSRKTN-----ALKEDPTRDLKQLLQelrSVINEEPTVQLSKAE 927

DUF4515

pfam14988

Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ...

336-481

8.84e-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: 44.37 E-value: 8.84e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  336 KNNVEQDLKEKEDTIKQRTSEVQDLQDEVQrentnlqklqaqkqqvqELLDELDEQKAQLEEQLKEVRKkcaEEAQL--- 412
Cdd:pfam14988  10 AKKTEEKQKKIEKLWNQYVQECEEIERRRQ-----------------ELASRYTQQTAELQTQLLQKEK---EQASLkke 69

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119627229  413 ------ISSLKAeltSQESQISTYEEELAKAREELSRLQQETaeleesvesgKAQLEPLQQHLQDSQQEISSMQM 481
Cdd:pfam14988  70 lqalrpFAKLKE---SQEREIQDLEEEKEKVRAETAEKDREA----------HLQFLKEKALLEKQLQELRILEL 131

TPH

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

329-488

1.01e-04

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

Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 45.29 E-value: 1.01e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  329 IVDLQREKNNVEQDLK-EKEDTIKQRTSEVQDLQDEVQREntnlqklqaqkQQVQELLDELDEQKAQlEEQLKEVRKKCA 407
Cdd:pfam13868 157 ILEYLKEKAEREEEREaEREEIEEEKEREIARLRAQQEKA-----------QDEKAERDELRAKLYQ-EEQERKERQKER 224

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  408 EEAQLISSLKAELT-SQESQIS----TYEEELAKAREELSRLQQETAELEEsvesgKAQLEPLQQHLQDSQ--QEISSM- 479
Cdd:pfam13868 225 EEAEKKARQRQELQqAREEQIElkerRLAEEAEREEEEFERMLRKQAEDEE-----IEQEEAEKRRMKRLEhrRELEKQi 299

                         170
                  ....*....|...
gi 119627229  480 ----QMKLMEMKD 488
Cdd:pfam13868 300 eereEQRAAEREE 312

PRK09039

peptidoglycan -binding protein;

320-497

1.20e-04

peptidoglycan -binding protein;

Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 45.34 E-value: 1.20e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 320 KELDTLNNEIVDL------QREKNnveQDLKEKEDTIKQRTSEVQDLQDEVQrentnlqklqaqkqqvqELLDELDEQKA 393
Cdd:PRK09039  53 SALDRLNSQIAELadllslERQGN---QDLQDSVANLRASLSAAEAERSRLQ-----------------ALLAELAGAGA 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 394 QLEEQLKEvrkkcaeeaqlissLKAELTSQEsQIStyeeelAKAREELSRLQQETAELeesvesgKAQLEPLQQHLQDSQ 473
Cdd:PRK09039 113 AAEGRAGE--------------LAQELDSEK-QVS------ARALAQVELLNQQIAAL-------RRQLAALEAALDASE 164

                        170       180
                 ....*....|....*....|....
gi 119627229 474 QEISSMQMKLmemKDLenhNSQLN 497
Cdd:PRK09039 165 KRDRESQAKI---ADL---GRRLN 182

YscO-like

pfam16789

YscO-like protein; This family of proteins is similar to the type III secretion protein YscO. ...

332-475

1.33e-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: 1.33e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  332 LQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNlqklqaqkqqvqellDELDEQKA---QLEEQLKEVRKKCAE 408
Cdd:pfam16789  30 LEKEKEKLAELEAERDKVRKHKKAKMQQLRDEMDRGTTS---------------DKILQMKRyikVVKERLKQEEKKVQD 94

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119627229  409 eaqlisslkaeltsQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQE 475
Cdd:pfam16789  95 --------------QKEQVRTAARNLEIAREELKKKRQEVEKLEKHKKEWVKEMKKEEEDQEEREQD 147

HMMR_N

pfam15905

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...

301-477

1.36e-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: 1.36e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  301 ASLQKNIIGSSPVADFSAIKELDT-----LNNEIVDLQREKNNVEQdlKEKEDTIKQRTSEVQdLQdEVQREntnlqklq 375
Cdd:pfam15905 125 ASLEKQLLELTRVNELLKAKFSEDgtqkkMSSLSMELMKLRNKLEA--KMKEVMAKQEGMEGK-LQ-VTQKN-------- 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  376 aqkqqvqelLDELDEQKAQLEEQLKEVRKKCAEEaqlisslkaelTSQESQISTYEEELAKAREELSRLQQETAELEESV 455
Cdd:pfam15905 193 ---------LEHSKGKVAQLEEKLVSTEKEKIEE-----------KSETEKLLEYITELSCVSEQVEKYKLDIAQLEELL 252

                         170       180
                  ....*....|....*....|..
gi 119627229  456 ESGKAQLEPLQQHLQDSQQEIS 477
Cdd:pfam15905 253 KEKNDEIESLKQSLEEKEQELS 274

PRK02224

DNA double-strand break repair Rad50 ATPase;

328-493

1.46e-04

DNA double-strand break repair Rad50 ATPase;

Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.80 E-value: 1.46e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 328 EIVDLQREKNNVEQDLkEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVR---- 403
Cdd:PRK02224 573 EVAELNSKLAELKERI-ESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARieea 651

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 404 ---KKCAEEAQL-----ISSLKAELTSQESQISTYEEELakarEELSRLQQETAELEESV---ESGKAQLEPLQQHLQD- 471
Cdd:PRK02224 652 redKERAEEYLEqveekLDELREERDDLQAEIGAVENEL----EELEELRERREALENRVealEALYDEAEELESMYGDl 727

                        170       180
                 ....*....|....*....|....*.
gi 119627229 472 ----SQQEISSMQMKLMEMKDLENHN 493
Cdd:PRK02224 728 raelRQRNVETLERMLNETFDLVYQN 753

GAS

pfam13851

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

384-483

1.52e-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: 1.52e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  384 LLDELDEQKaQLEEQLKEVRKKCAEEAQLISSlkaelTSQESQISTyeEELAKAREELSRLQQETAELE---ESVESGKA 460
Cdd:pfam13851  21 TRNNLELIK-SLKEEIAELKKKEERNEKLMSE-----IQQENKRLT--EPLQKAQEEVEELRKQLENYEkdkQSLKNLKA 92

                          90       100
                  ....*....|....*....|...
gi 119627229  461 QLEPLQQHLQDSQQEISSMQMKL 483
Cdd:pfam13851  93 RLKVLEKELKDLKWEHEVLEQRF 115

FRQ1

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

152-274

1.66e-04

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

Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 42.47 E-value: 1.66e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 152 LGRVWELSDIDHDGMLDRDEFAvAMFLVYCALEKEPVPmSLPPALVPPSKRKTWVVSPAEK---AKYDEIFLKTDKDMDG 228
Cdd:COG5126    7 LDRRFDLLDADGDGVLERDDFE-ALFRRLWATLFSEAD-TDGDGRISREEFVAGMESLFEAtvePFARAAFDLLDTDGDG 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 119627229 229 FVSGLEVREIFLKTGLPSTLLAHIWSLCDTKDCGKLSKDQFALAFH 274
Cdd:COG5126   85 KISADEFRRLLTALGVSEEEADELFARLDTDGDGKISFEEFVAAVR 130

SCP-1

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

325-496

1.67e-04

Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 45.48 E-value: 1.67e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  325 LNNEI---------VDLQREKNNVEQDLKEKEDTIKqrtseVQDLQDEVQRE-NTNLQKLQAQKQQVQE----------L 384
Cdd:pfam05483 188 LNNNIekmilafeeLRVQAENARLEMHFKLKEDHEK-----IQHLEEEYKKEiNDKEKQVSLLLIQITEkenkmkdltfL 262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  385 LDELDEQKAQLEEQ-------LKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQET-AELEES-- 454
Cdd:pfam05483 263 LEESRDKANQLEEKtklqdenLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKeAQMEELnk 342

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 119627229  455 --------VESGKAQLEPLQQHLQDSQQ--EISSMQMKLMEMkDLENHNSQL 496
Cdd:pfam05483 343 akaahsfvVTEFEATTCSLEELLRTEQQrlEKNEDQLKIITM-ELQKKSSEL 393

CCDC158

pfam15921

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...

320-496

1.73e-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: 1.73e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   320 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLD----ELDEQKAQ- 394
Cdd:pfam15921  349 KQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDhlrrELDDRNMEv 428

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   395 --LEEQLKEVRKKCA--------------EEAQLISSLKAELTSQesqistyEEELAKAREELSRLQQETAELEESVESG 458
Cdd:pfam15921  429 qrLEALLKAMKSECQgqmerqmaaiqgknESLEKVSSLTAQLEST-------KEMLRKVVEELTAKKMTLESSERTVSDL 501

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 119627229   459 KAQLEPLQQHLQDSQQEISSMQ----MKLMEMKDLENHNSQL 496
Cdd:pfam15921  502 TASLQEKERAIEATNAEITKLRsrvdLKLQELQHLKNEGDHL 543

STAT5_CCD

cd16855

Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family ...

393-496

1.86e-04

Pssm-ID: 341080 [Multi-domain] Cd Length: 194 Bit Score: 43.41 E-value: 1.86e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 393 AQLEEQLKEVRKKCAEEAQLISSLKAEltsQESQISTYEEeLAKAREELSRLQ-QETAELEESVESGKAQLEPLQQHLQD 471
Cdd:cd16855    4 LEIRQQLEELRQRTQETENDLRNLQQK---QESFVIQYQE-SQKIQAQLQQLQqQPQNERIELEQQLQQQKEQLEQLLNA 79

                         90       100
                 ....*....|....*....|....*.
gi 119627229 472 SQQEISSMQMKLME-MKDLENHNSQL 496
Cdd:cd16855   80 KAQELLQLRMELADkFKKTIQLLSKL 105

SPEC

cd00176

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...

327-486

1.90e-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: 43.59 E-value: 1.90e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 327 NEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQV-QELLDELDEQKAQLEEQLKEVRK- 404
Cdd:cd00176   33 ESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLEELNQRwEELRELAEERRQRLEEALDLQQFf 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 405 -KCAEEAQLISSLKAELTSQE------------SQISTYEEELAKAREELSRLQQETAELEESVESG-----KAQLEPLQ 466
Cdd:cd00176  113 rDADDLEQWLEEKEAALASEDlgkdlesveellKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDadeeiEEKLEELN 192

                        170       180
                 ....*....|....*....|
gi 119627229 467 QHLQDSQQEISSMQMKLMEM 486
Cdd:cd00176  193 ERWEELLELAEERQKKLEEA 212

PRK04778

septation ring formation regulator EzrA; Provisional

320-493

2.00e-04

septation ring formation regulator EzrA; Provisional

Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.83 E-value: 2.00e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 320 KELDTLNNEIVDLqrEKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQL 399
Cdd:PRK04778 256 KEIQDLKEQIDEN--LALLEELDLDEAEEKNEEIQERIDQLYDILEREVKARKYVEKNSDTLPDFLEHAKEQNKELKEEI 333

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 400 KEVRKK---CAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQ------ 470
Cdd:PRK04778 334 DRVKQSytlNESELESVRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQEKLSEMLQglrkde 413

                        170       180
                 ....*....|....*....|....*
gi 119627229 471 -DSQQEISSMQMKLMEMK-DLENHN 493
Cdd:PRK04778 414 lEAREKLERYRNKLHEIKrYLEKSN 438

DUF4618

pfam15397

Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins ...

300-476

2.06e-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: 2.06e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  300 RASLQKNII--GSSPVADFSAIKELDTLnneIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQ 377
Cdd:pfam15397  41 RKLLQQYEKfgTIISILEYSNKKQLQQA---KAELQEWEEKEESKLNKLEQQLEQLNAKIQKTQEELNFLSTYKDKEYPV 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  378 KQQVQELL------------DELDEqkaqLEEQLKEVRKKCAEEAQLISslKAELTS-QESQISTYEEEL-AKARE---- 439
Cdd:pfam15397 118 KAVQIANLvrqlqqlkdsqqDELDE----LEEMRRMVLESLSRKIQKKK--EKILSSlAEKTLSPYQESLlQKTRDnqvm 191

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 119627229  440 --ELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEI 476
Cdd:pfam15397 192 lkEIEQFREFIDELEEEIPKLKAEVQQLQAQRQEPREVI 230

EmrA

COG1566

Multidrug resistance efflux pump EmrA [Defense mechanisms];

391-497

2.12e-04

Multidrug resistance efflux pump EmrA [Defense mechanisms];

Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 44.27 E-value: 2.12e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 391 QKAQLEEQLKEVrkkcaEEAQLISSLKAELTSQESQISTYEEELAKAREELSR---LQQETAELEESVESGKAQLEPLQQ 467
Cdd:COG1566   88 AEAQLAAAEAQL-----ARLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERyqaLYKKGAVSQQELDEARAALDAAQA 162

                         90       100       110
                 ....*....|....*....|....*....|
gi 119627229 468 HLQDSQQEISSMQMKLMEMKDLENHNSQLN 497
Cdd:COG1566  163 QLEAAQAQLAQAQAGLREEEELAAAQAQVA 192

DUF1090

pfam06476

Protein of unknown function (DUF1090); This family consists of several bacterial proteins of ...

391-476

2.14e-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: 41.46 E-value: 2.14e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  391 QKAQLEEQLKEVRKKCAEEaqlisSLKAEltsqesqistYEEELAKAREELSRLQqetAELEESVESGKAQL-EPLQQHL 469
Cdd:pfam06476  39 RVAGLEKALAEVRAHCTDA-----GLRAE----------RQQKVAEKREEVAERE---AELAEAQAKGDADKiAKRQRKL 100


                  ....*..
gi 119627229  470 QDSQQEI 476
Cdd:pfam06476 101 AEARQEL 107

PRK03918

DNA double-strand break repair ATPase Rad50;

334-491

2.19e-04

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 2.19e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 334 REKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTnlqklqaqKQQVQELLDELDEqkaqLEEQLKEVRKKCAEE-AQL 412
Cdd:PRK03918 459 AELKRIEKELKEIEEKERKLRKELRELEKVLKKESE--------LIKLKELAEQLKE----LEEKLKKYNLEELEKkAEE 526

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 413 ISSLKAELTSQESQISTYEEELAKARE----------ELSRLQQETAELE-----------ESVESGKAQLEPLQQH--- 468
Cdd:PRK03918 527 YEKLKEKLIKLKGEIKSLKKELEKLEElkkklaelekKLDELEEELAELLkeleelgfesvEELEERLKELEPFYNEyle 606

                        170       180
                 ....*....|....*....|...
gi 119627229 469 LQDSQQEIssmQMKLMEMKDLEN 491
Cdd:PRK03918 607 LKDAEKEL---EREEKELKKLEE 626

mukB

chromosome partition protein MukB;

385-491

2.36e-04

chromosome partition protein MukB;

Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.95 E-value: 2.36e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  385 LDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKaeltsqeSQISTYEEELAKAREELSRLQ-QETAELEESVESGKaqlE 463
Cdd:PRK04863  994 LEQAEQERTRAREQLRQAQAQLAQYNQVLASLK-------SSYDAKRQMLQELKQELQDLGvPADSGAEERARARR---D 1063

                          90       100       110
                  ....*....|....*....|....*....|..
gi 119627229  464 PLQQHLQDSQQEISSMQMKL----MEMKDLEN 491
Cdd:PRK04863 1064 ELHARLSANRSRRNQLEKQLtfceAEMDNLTK 1095

PRK03918

DNA double-strand break repair ATPase Rad50;

320-456

2.39e-04

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 2.39e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 320 KELDTLNNEIVDLQREKNNVEQDLKEKEDTiKQRTSEVQDLQDEVQREntnlqklqaqkqqvqelLDELDE-----QKA- 393
Cdd:PRK03918 307 DELREIEKRLSRLEEEINGIEERIKELEEK-EERLEELKKKLKELEKR-----------------LEELEErhelyEEAk 368

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119627229 394 QLEEQLKEVRKKCAEEAqlISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVE 456
Cdd:PRK03918 369 AKKEELERLKKRLTGLT--PEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIE 429

CALCOCO1

pfam07888

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...

321-490

2.73e-04

Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 44.50 E-value: 2.73e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  321 ELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRentnlqklqaqkqqVQELLDELDEQKAQLE---E 397
Cdd:pfam07888 172 ERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITT--------------LTQKLTTAHRKEAENEallE 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  398 QLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAR------------------EELSRLQQETAELEESVESGK 459
Cdd:pfam07888 238 ELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARlqaaqltlqladaslalrEGRARWAQERETLQQSAEADK 317

                         170       180       190
                  ....*....|....*....|....*....|.
gi 119627229  460 AQLEPLQQHLQDSQQeisSMQMKLMEMKDLE 490
Cdd:pfam07888 318 DRIEKLSAELQRLEE---RLQEERMEREKLE 345

Myosin_tail_1

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

340-497

2.74e-04

Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.78 E-value: 2.74e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   340 EQDLKEKEDTIKQrtseVQDLQDEVQRENTNLQKLQAqkqqvqelldELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAE 419
Cdd:pfam01576    4 EEEMQAKEEELQK----VKERQQKAESELKELEKKHQ----------QLCEEKNALQEQLQAETELCAEAEEMRARLAAR 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   420 -------LTSQESQISTYEEELAKAREELSRLQQETAELEEsvesgkaQLEPLQQHLQDSQQEISSMQMKLMEMKD---- 488
Cdd:pfam01576   70 kqeleeiLHELESRLEEEEERSQQLQNEKKKMQQHIQDLEE-------QLDEEEAARQKLQLEKVTTEAKIKKLEEdill 142


                   ....*....
gi 119627229   489 LENHNSQLN 497
Cdd:pfam01576  143 LEDQNSKLS 151

sbcc

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

319-475

2.97e-04

Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.57 E-value: 2.97e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   319 IKELDTLNNEIvdlQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLD--------ELDE 390
Cdd:TIGR00618  713 IEEYDREFNEI---ENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGaelshlaaEIQF 789

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   391 QKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQE-TAELEESVESGKAQLEPLQQHL 469
Cdd:TIGR00618  790 FNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEiTHQLLKYEECSKQLAQLTQEQA 869


                   ....*.
gi 119627229   470 QDSQQE 475
Cdd:TIGR00618  870 KIIQLS 875

FapA

pfam03961

Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta ...

387-460

2.99e-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: 2.99e-04

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119627229  387 ELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQ-----ESQISTYEEELAKAREELSRLQQETAELEESVESGKA 460
Cdd:pfam03961 153 ELKEKLEELEKELEELEEELEKLKKRLKKLPKKARGQlppekREQLEKLLETKNKLSEELEELEEELKELKEELESLLG 231

Uso1_p115_C

pfam04871

Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ...

397-496

3.00e-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: 41.23 E-value: 3.00e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  397 EQLKEVRKKCAEEAQLISSLKAELTSQESQIstyeEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEI 476
Cdd:pfam04871   1 AKKSELESEASSLKNENTELKAELQELSKQY----NSLEQKESQAKELEAEVKKLEEALKKLKAELSEEKQKEKEKQSEL 76

                          90       100
                  ....*....|....*....|
gi 119627229  477 SSMqmkLMEMKDLENHNSQL 496
Cdd:pfam04871  77 DDL---LLLLGDLEEKVEKY 93

CwlO1

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

424-497

3.00e-04

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

Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 3.00e-04

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119627229 424 ESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEM-KDLENHNSQLN 497
Cdd:COG3883   15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAeAEIEERREELG 89

COG1340

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

383-490

3.29e-04

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

Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.75 E-value: 3.29e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 383 ELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQL 462
Cdd:COG1340    8 SSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKL 87

                         90       100
                 ....*....|....*....|....*...
gi 119627229 463 EPLQQHLQDSQQEISSMQMKLMEMKDLE 490
Cdd:COG1340   88 NELREELDELRKELAELNKAGGSIDKLR 115

Spc7

smart00787

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

383-492

3.38e-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: 3.38e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   383 ELLDELDEQKAQL---EEQLKEVRKKCAEEAQLISSLKAELTSQESQISTY-EEELAKAREELSRLQQE-------TAEL 451
Cdd:smart00787 151 ENLEGLKEDYKLLmkeLELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCdPTELDRAKEKLKKLLQEimikvkkLEEL 230

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 119627229   452 EESVESGKAQLEPLQQHLQDSQQEISSMQMKLMEMKDLENH 492
Cdd:smart00787 231 EEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGFTFK 271

COG1340

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

320-485

3.59e-04

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

Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.36 E-value: 3.59e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 320 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENtnlqklqaqkqqvqELLDELDEQKAQLEEQL 399
Cdd:COG1340   15 EKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELR--------------EKRDELNEKVKELKEER 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 400 KEVRKKCAEEAQLISSLKAELtsqeSQISTYEEELAKAREELSRL--QQET---------------AELEESVESGKAQL 462
Cdd:COG1340   81 DELNEKLNELREELDELRKEL----AELNKAGGSIDKLRKEIERLewRQQTevlspeeekelvekiKELEKELEKAKKAL 156

                        170       180
                 ....*....|....*....|...
gi 119627229 463 EpLQQHLQDSQQEISSMQMKLME 485
Cdd:COG1340  157 E-KNEKLKELRAELKELRKEAEE 178

mukB

chromosome partition protein MukB;

390-496

4.10e-04

chromosome partition protein MukB;

Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.18 E-value: 4.10e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  390 EQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQ-------- 461
Cdd:PRK04863  530 RQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARapawlaaq 609

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 119627229  462 --LEPLQQH----LQDSQQEISSMQMKLMEMKDLENHNSQL 496
Cdd:PRK04863  610 daLARLREQsgeeFEDSQDVTEYMQQLLERERELTVERDEL 650

COG1340

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

327-463

4.29e-04

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

Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.36 E-value: 4.29e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 327 NEIVDLQREKNNVEQDLKEKEDtIKQRTSEVQDLQDEVQRENTNLQKLQaqkqqvqELLDELDEQKAQLEEQLKEVRKKc 406
Cdd:COG1340  140 EKIKELEKELEKAKKALEKNEK-LKELRAELKELRKEAEEIHKKIKELA-------EEAQELHEEMIELYKEADELRKE- 210

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 119627229 407 AEEA-QLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLE 463
Cdd:COG1340  211 ADELhKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEK 268

PRK01156

chromosome segregation protein; Provisional

303-495

4.35e-04

chromosome segregation protein; Provisional

Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.12 E-value: 4.35e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 303 LQKNIIGSSP----VADFSAIKELDTL-------NNEIVDLQREKNNVEQD---LKEKEDTIKQRTSEVQDLQDEVQREN 368
Cdd:PRK01156 117 IEKNILGISKdvflNSIFVGQGEMDSLisgdpaqRKKILDEILEINSLERNydkLKDVIDMLRAEISNIDYLEEKLKSSN 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 369 TNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKkcaEEAQLISSLKaELTSQESQISTYEEELAKAREELSRLQQET 448
Cdd:PRK01156 197 LELENIKKQIADDEKSHSITLKEIERLSIEYNNAMD---DYNNLKSALN-ELSSLEDMKNRYESEIKTAESDLSMELEKN 272

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119627229 449 AELEESVE---------------------SGKAQLEPLQQHLQDSQQEISSMQMKLMEMKDLENHNSQ 495
Cdd:PRK01156 273 NYYKELEErhmkiindpvyknrnyindyfKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYND 340

COG1340

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

383-497

4.48e-04

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

Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.36 E-value: 4.48e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 383 ELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQL 462
Cdd:COG1340   22 EEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKEL 101

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119627229 463 EPLQ-------------QHLQDSQQ--------------EISSMQMKLMEMKDLENHNSQLN 497
Cdd:COG1340  102 AELNkaggsidklrkeiERLEWRQQtevlspeeekelveKIKELEKELEKAKKALEKNEKLK 163

rad50

rad50; All proteins in this family for which functions are known are involvedin recombination, ...

394-496

4.51e-04

Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 44.27 E-value: 4.51e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   394 QLEEQLKEVRKKCAEEAQLISslKAELtsQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLE---PLQQHLQ 470
Cdd:TIGR00606  710 KLKSTESELKKKEKRRDEMLG--LAPG--RQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGtimPEEESAK 785

                           90       100
                   ....*....|....*....|....*.
gi 119627229   471 DSQQEISSMQMKLMEMKDLENHNSQL 496
Cdd:TIGR00606  786 VCLTDVTIMERFQMELKDVERKIAQQ 811

MAP7

pfam05672

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...

387-475

5.34e-04

Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 41.18 E-value: 5.34e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  387 ELDEQKAQLEEQLK----EVRKKCAEEAQLissLKAELTSQESQISTYEEELAK-----AREELSRLQQ--ETAELEESV 455
Cdd:pfam05672  36 EKEEEERLRKEELRrraeEERARREEEARR---LEEERRREEEERQRKAEEEAEereqrEQEEQERLQKqkEEAEAKARE 112

                          90       100
                  ....*....|....*....|
gi 119627229  456 ESGKAQLEpLQQHLQDSQQE 475
Cdd:pfam05672 113 EAERQRQE-REKIMQQEEQE 131

PRK01156

chromosome segregation protein; Provisional

328-480

5.37e-04

chromosome segregation protein; Provisional

Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.74 E-value: 5.37e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 328 EIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCA 407
Cdd:PRK01156 581 DIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIA 660

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119627229 408 EEAQLISSlKAELTSQESQIstyEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQ 480
Cdd:PRK01156 661 EIDSIIPD-LKEITSRINDI---EDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMK 729

SCP-1

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

278-547

6.19e-04

Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 43.56 E-value: 6.19e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  278 QKLIKGIDPPHVLTPEMIPPSDRASLQKNIIGSSPVAdfsaIKELDTLNNEIVDLQREKNNVE---QDLKEKEDTI---- 350
Cdd:pfam05483 370 QRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVE----LEELKKILAEDEKLLDEKKQFEkiaEELKGKEQELifll 445

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  351 KQRTSEVQDLQDEVQRENTNLQklqaqkqqvqELLDELDEQKAQLE-EQLKEVrkKCAEEAQLISSLKAELTSQES---- 425
Cdd:pfam05483 446 QAREKEIHDLEIQLTAIKTSEE----------HYLKEVEDLKTELEkEKLKNI--ELTAHCDKLLLENKELTQEASdmtl 513

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  426 QISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEIssmQMKLmemkdlenHNSQLNWCSSPHSI 505
Cdd:pfam05483 514 ELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEV---KCKL--------DKSEENARSIEYEV 582

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 119627229  506 LVNGAtdycSLSTSSSETANLNEHVEGQSNlESEPIHQESPA 547
Cdd:pfam05483 583 LKKEK----QMKILENKCNNLKKQIENKNK-NIEELHQENKA 619

rad50

rad50; All proteins in this family for which functions are known are involvedin recombination, ...

315-565

6.33e-04

Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.50 E-value: 6.33e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   315 DFSAIKELDTLNNEIVDLQR----EKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRentnlqklqaqkqqvqelldelde 390
Cdd:TIGR00606  686 VFQTEAELQEFISDLQSKLRlapdKLKSTESELKKKEKRRDEMLGLAPGRQSIIDL------------------------ 741

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   391 qkaqLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTY--EEELAKAREE----LSRLQQETAELEESVESGKAQLE- 463
Cdd:TIGR00606  742 ----KEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTImpEEESAKVCLTdvtiMERFQMELKDVERKIAQQAAKLQg 817

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   464 --------PLQQHLQDSQQEISSMQMKLMEMKDL-ENHNSQLNWCSSPHSILvngATDYCSLSTSSSETANLNEHVEGQS 534
Cdd:TIGR00606  818 sdldrtvqQVNQEKQEKQHELDTVVSKIELNRKLiQDQQEQIQHLKSKTNEL---KSEKLQIGTNLQRRQQFEEQLVELS 894

                          250       260       270
                   ....*....|....*....|....*....|.
gi 119627229   535 NLESEPIHQESPARSspELLPSGVTDENEVT 565
Cdd:TIGR00606  895 TEVQSLIREIKDAKE--QDSPLETFLEKDQQ 923

HCR

pfam07111

Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...

397-489

6.74e-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: 6.74e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  397 EQLKEVRKKCAEEAQLisslKAELTSQEsqISTYEEELAKAREELS----RLQQETAELEESVESGKAQLEPLQQHLQDS 472
Cdd:pfam07111 484 EQLREERNRLDAELQL----SAHLIQQE--VGRAREQGEAERQQLSevaqQLEQELQRAQESLASVGQQLEVARQGQQES 557

                          90
                  ....*....|....*..
gi 119627229  473 QQEISSMQMKLMEMKDL 489
Cdd:pfam07111 558 TEEAASLRQELTQQQEI 574

HlpA

COG2825

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

383-485

7.01e-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: 7.01e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 383 ELLDELDEQK---AQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQIStyEEELAKAREELSRLQQEtaeleesvesgk 459
Cdd:COG2825   33 RILQESPEGKaaqKKLEKEFKKRQAELQKLEKELQALQEKLQKEAATLS--EEERQKKERELQKKQQE------------ 98

                         90       100
                 ....*....|....*....|....*.
gi 119627229 460 aqlepLQQHLQDSQQEISSMQMKLME 485
Cdd:COG2825   99 -----LQRKQQEAQQDLQKRQQELLQ 119

sbcc

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

383-489

7.43e-04

Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.42 E-value: 7.43e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   383 ELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQiSTYEEELAKAREELSRLQQETAELEESVES----- 457
Cdd:TIGR00618  212 CMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQ-LKKQQLLKQLRARIEELRAQEAVLEETQERinrar 290

                           90       100       110
                   ....*....|....*....|....*....|..
gi 119627229   458 GKAQLEPLQQHLQDSQQEISSMQMKLMEMKDL 489
Cdd:TIGR00618  291 KAAPLAAHIKAVTQIEQQAQRIHTELQSKMRS 322

MukB

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

321-475

7.89e-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: 7.89e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  321 ELDTLNNEIVDLQREKNN---VEQDLKEKEDTIKQRTSEVQDLQDEVqrentnlqkLQAQKQQVQELLDELDEQKAQLEE 397
Cdd:COG3096   837 ELAALRQRRSELERELAQhraQEQQLRQQLDQLKEQLQLLNKLLPQA---------NLLADETLADRLEELREELDAAQE 907

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  398 QLKEVRKKCAEEAQL---ISSLKAELTSQESQISTYEEelakAREELSRLQQETAELEESVE-------SGKAQL----- 462
Cdd:COG3096   908 AQAFIQQHGKALAQLeplVAVLQSDPEQFEQLQADYLQ----AKEQQRRLKQQIFALSEVVQrrphfsyEDAVGLlgens 983

                         170
                  ....*....|....*.
gi 119627229  463 ---EPLQQHLQDSQQE 475
Cdd:COG3096   984 dlnEKLRARLEQAEEA 999

Atg16_CCD

cd22887

Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...

415-496

8.10e-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: 8.10e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 415 SLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVEsgkaqleplqqHLQDsqqEISSMQM--KLME--MKDLE 490
Cdd:cd22887    1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANE-----------ILND---ELIALQIenNLLEekLRKLQ 66


                 ....*.
gi 119627229 491 NHNSQL 496
Cdd:cd22887   67 EENDEL 72

Myosin_tail_1

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

277-480

8.54e-04

Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 43.24 E-value: 8.54e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   277 SQKLIKGIDPPHVLTPEMIPPSDRASLQkniigsspvadfsAIKELDTLNNEIVD-------LQREKNNVEQDLKEKEDT 349
Cdd:pfam01576  831 SEKKLKNLEAELLQLQEDLAASERARRQ-------------AQQERDELADEIASgasgksaLQDEKRRLEARIAQLEEE 897

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   350 IKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAE-EAQLISSLKAELTSQESQIS 428
Cdd:pfam01576  898 LEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEmEGTVKSKFKSSIAALEAKIA 977

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119627229   429 TYEEEL-AKARE-----ELSR----------LQQE-----TAELEESVESGKAQLEPLQQHLQDSQQEISSMQ 480
Cdd:pfam01576  978 QLEEQLeQESRErqaanKLVRrtekklkevlLQVEderrhADQYKDQAEKGNSRMKQLKRQLEEAEEEASRAN 1050

HBM

pfam16591

Helical bimodular sensor domain; The HBM sensor domain has been identified primarily in ...

319-488

8.61e-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: 8.61e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  319 IKELDTLNNEIVDLQREKNNVE--QDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLE 396
Cdd:pfam16591  42 QKKLDELKQQLQQLKTTFTSPEnvRLLQEQLQLIQAYRKSFNELRAAYESRNASRQVMDSAAERALEAIDQLEAEVLQTP 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  397 EQLKEVrkkcAEEAQLISSLKAEL-------------TSQES------QISTYEEELAKAREEL-----SRLQQETAELE 452
Cdd:pfam16591 122 EADSRR----AAQYQAISELKRQVqmaryqvrgytftPNEDSeqaayqQLDAALASLDQLRQALagdpgAALQQLTSALQ 197

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 119627229  453 E---SVEsgkaQLEPLQQHLQDSQQEISSMQMKLMEMKD 488
Cdd:pfam16591 198 GyrdALD----TFKAAVAAIEQARQEMTSQGDEIVRISD 232

EnvC

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

418-497

9.09e-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: 9.09e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 418 AELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKL----MEMKDLENHN 493
Cdd:COG4942   13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELaaleAELAELEKEI 92


                 ....
gi 119627229 494 SQLN 497
Cdd:COG4942   93 AELR 96

DUF3584

pfam12128

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...

320-483

9.14e-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: 9.14e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   320 KELDTLNNEIVDLQREKN----NVEQDLKEKEDTIKQRTS---EVQDLQDEVQRentnlqklQAQKQQVQELLDELDEQK 392
Cdd:pfam12128  361 ERLKALTGKHQDVTAKYNrrrsKIKEQNNRDIAGIKDKLAkirEARDRQLAVAE--------DDLQALESELREQLEAGK 432

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   393 AQLEEQLKEVRKKCAEE------AQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQ 466
Cdd:pfam12128  433 LEFNEEEYRLKSRLGELklrlnqATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQAS 512

                          170
                   ....*....|....*..
gi 119627229   467 QHLQDSQQEISSMQMKL 483
Cdd:pfam12128  513 RRLEERQSALDELELQL 529

PRK11281

mechanosensitive channel MscK;

322-497

9.63e-04

mechanosensitive channel MscK;

Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.98 E-value: 9.63e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  322 LDTLNnEIVDLQREKNNVEQDLKEKEDTIKQRtsevqdlqDEVQRENtnlqklqaqkqqvqellDELDEQKAQLEEQLKE 401
Cdd:PRK11281   45 LDALN-KQKLLEAEDKLVQQDLEQTLALLDKI--------DRQKEET-----------------EQLKQQLAQAPAKLRQ 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  402 VRKKcaeeaqlISSLKAELTSQESQ------ISTYEEELAKAREELSRLQQETAELEesvesgkAQLEPLQQHLQDSQQE 475
Cdd:PRK11281   99 AQAE-------LEALKDDNDEETREtlstlsLRQLESRLAQTLDQLQNAQNDLAEYN-------SQLVSLQTQPERAQAA 164

                         170       180
                  ....*....|....*....|..
gi 119627229  476 ISSMQMKLMEMkdlenhNSQLN 497
Cdd:PRK11281  165 LYANSQRLQQI------RNLLK 180

CCCAP

pfam15964

Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ...

314-487

9.87e-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: 9.87e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  314 ADFSAIKEL---DTLNNEivdLQREKNNVEQDLKEKEDtikQRTSEVQDLQDEVQRENTNLQKLqaqkqqvqelLDELDE 390
Cdd:pfam15964 347 ANFEKTKALiqcEQLKSE---LERQKERLEKELASQQE---KRAQEKEALRKEMKKEREELGAT----------MLALSQ 410

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  391 QKAQLEEQLKEVRKkcaEEAQLISSLKA---ELTSQESQISTYEEELakaREELSRLQQETAELEESVESGKAQlepLQQ 467
Cdd:pfam15964 411 NVAQLEAQVEKVTR---EKNSLVSQLEEaqkQLASQEMDVTKVCGEM---RYQLNQTKMKKDEAEKEHREYRTK---TGR 481

                         170       180
                  ....*....|....*....|
gi 119627229  468 HLQDSQQEISSMQMKLMEMK 487
Cdd:pfam15964 482 QLEIKDQEIEKLGLELSESK 501

rad50

rad50; All proteins in this family for which functions are known are involvedin recombination, ...

320-465

1.08e-03

Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 42.73 E-value: 1.08e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   320 KELDTLNNEIVDLQREKNNVEQDLKEKE---DTIKQRTSEVQDLQDEVQR----------ENTNLQKLQAQKQQVQELLD 386
Cdd:TIGR00606  501 KEVKSLQNEKADLDRKLRKLDQEMEQLNhhtTTRTQMEMLTKDKMDKDEQirkiksrhsdELTSLLGYFPNKKQLEDWLH 580

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   387 ELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKA---REELSRLQQetaeLEESVESGKAQLE 463
Cdd:TIGR00606  581 SKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVcgsQDEESDLER----LKEEIEKSSKQRA 656


                   ..
gi 119627229   464 PL 465
Cdd:TIGR00606  657 ML 658

rad50

rad50; All proteins in this family for which functions are known are involvedin recombination, ...

330-492

1.13e-03

Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 42.73 E-value: 1.13e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   330 VDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQkqqvqelLDELDEQKAQLEEQLKEvRKKCAEE 409
Cdd:TIGR00606  818 SDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSK-------TNELKSEKLQIGTNLQR-RQQFEEQ 889

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   410 AQLISSlkaELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQlepLQQHLQDSQQEISSmqmKLMEMKDL 489
Cdd:TIGR00606  890 LVELST---EVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKK---AQDKVNDIKEKVKN---IHGYMKDI 960


                   ...
gi 119627229   490 ENH 492
Cdd:TIGR00606  961 ENK 963

Filament

pfam00038

Intermediate filament protein;

314-491

1.17e-03

Intermediate filament protein;

Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 41.83 E-value: 1.17e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  314 ADFSAI-KELDTLNNEIVDLQREKnnveQDLKEKEDTIKQ-RTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQ 391
Cdd:pfam00038 103 NDLVGLrKDLDEATLARVDLEAKI----ESLKEELAFLKKnHEEEVRELQAQVSDTQVNVEMDAARKLDLTSALAEIRAQ 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  392 --------KAQLEE----QLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGK 459
Cdd:pfam00038 179 yeeiaaknREEAEEwyqsKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEERYELQL 258

                         170       180       190
                  ....*....|....*....|....*....|...
gi 119627229  460 AQLEPLQQHLQDSQQEI-SSMQMKLMEMKDLEN 491
Cdd:pfam00038 259 ADYQELISELEAELQETrQEMARQLREYQELLN 291

growth_prot_Scy

polarized growth protein Scy;

343-480

1.32e-03

polarized growth protein Scy;

Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 42.51 E-value: 1.32e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  343 LKEKEDTIKQR-TSEVQDLQDEVQRENTNLQKLQAqkqqvqELLDEL----DEQKAQLEEQLKEVRKKCAEEAqliSSLK 417
Cdd:NF041483 1119 IRERAEELRDRiTGEIEELHERARRESAEQMKSAG------ERCDALvkaaEEQLAEAEAKAKELVSDANSEA---SKVR 1189

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119627229  418 -AELTSQESQISTYEEELAKAREELSRLQQET-AELEESVESGKAQLEPLQQHLQDSQQEISSMQ 480
Cdd:NF041483 1190 iAAVKKAEGLLKEAEQKKAELVREAEKIKAEAeAEAKRTVEEGKRELDVLVRRREDINAEISRVQ 1254

PRK11637

AmiB activator; Provisional

398-481

1.36e-03

AmiB activator; Provisional

Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 41.99 E-value: 1.36e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 398 QLKEVRKKCAE-------EAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVesgkAQLEplQQhlQ 470
Cdd:PRK11637  48 QLKSIQQDIAAkeksvrqQQQQRASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASI----AKLE--QQ--Q 119

                         90
                 ....*....|.
gi 119627229 471 DSQQEISSMQM 481
Cdd:PRK11637 120 AAQERLLAAQL 130

Rcc_KIF21

cd22248

regulatory coiled-coil domain found in the kinesin-like KIF21 family; The KIF21 family ...

432-481

1.40e-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: 1.40e-03

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 119627229 432 EELAKAREELSRLQQE---TAELEESVESGKAQLEPLQQHLQDSQQEIssMQM 481
Cdd:cd22248   27 EKLEKKRERALDEGKDesvLRDLEEEIDSLKANIDYVQENITECQSNI--MQM 77

ALIX_LYPXL_bnd

pfam13949

ALIX V-shaped domain binding to HIV; The binding of the LYPxL motif of late HIV p6Gag and EIAV ...

339-491

1.41e-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: 41.45 E-value: 1.41e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  339 VEQDLKEKEDTIKQRTSEVQDLQDEV--QRENTNLQKLQAQKQQVQELLDELDE---QKAQLEEQLKEVRKKCAEEAQLI 413
Cdd:pfam13949  98 VRSKFREHEEDLELLSGPDEDLEAFLpsSRRAKNSPSVEEQVAKLRELLNKLNElkrEREQLLKDLKEKARNDDISPKLL 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  414 SSLKAEL-TSQESQIstYEEELAKAREELSRLQQETA---ELEESVESGKAQLEPLQQHLQDSQQEISSMqmklmeMKDL 489
Cdd:pfam13949 178 LEKARLIaPNQEEQL--FEEELEKYDPLQNRLEQNLHkqeELLKEITEANNEFLQDKRVDSEKQRQREEA------LQKL 249


                  ..
gi 119627229  490 EN 491
Cdd:pfam13949 250 EN 251

TPH

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

319-490

1.47e-03

Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 41.83 E-value: 1.47e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  319 IKELDTL-----NNEIVDLQ-REKNNVEQDLKEKEDTIKQRTSE--VQDLQDEVQREntnlqklqaqkqqvQELLDELDE 390
Cdd:pfam13868   8 LRELNSKllaakCNKERDAQiAEKKRIKAEEKEEERRLDEMMEEerERALEEEEEKE--------------EERKEERKR 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  391 QKAQLEEQLKEvRKKCAEEAQLISSLKAELTsQESQISTYEEELAKAREELSRLQQETAELEESVEsgkaqlepLQQHLQ 470
Cdd:pfam13868  74 YRQELEEQIEE-REQKRQEEYEEKLQEREQM-DEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNE--------EQAEWK 143

                         170       180
                  ....*....|....*....|
gi 119627229  471 DSQQEissmQMKLMEMKDLE 490
Cdd:pfam13868 144 ELEKE----EEREEDERILE 159

Myosin_tail_1

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

325-482

1.47e-03

Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.47 E-value: 1.47e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   325 LNNEIVDLQREKNNVEQDLKEKE-DTIK------QRTSEVQDLQDEVQRENTNLQKLQAQkqqvqelLDELDEQKAQLEE 397
Cdd:pfam01576  431 LAEKLSKLQSELESVSSLLNEAEgKNIKlskdvsSLESQLQDTQELLQEETRQKLNLSTR-------LRQLEDERNSLQE 503

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   398 QL-KEVRKKCAEEAQL------ISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHL- 469
Cdd:pfam01576  504 QLeEEEEAKRNVERQLstlqaqLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELd 583

                          170
                   ....*....|....*....
gi 119627229   470 -----QDSQ-QEISSMQMK 482
Cdd:pfam01576  584 dllvdLDHQrQLVSNLEKK 602

DUF5401

pfam17380

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

332-450

1.48e-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: 1.48e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  332 LQREKNNVEQDLKEKEDTikqRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELL--DELDEQKAQ--------------- 394
Cdd:pfam17380 415 IQQQKVEMEQIRAEQEEA---RQREVRRLEEERAREMERVRLEEQERQQQVERLrqQEEERKRKKlelekekrdrkraee 491

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119627229  395 -----LEEQLKEVRKKCAEEAQLISSLKAELtsQESQISTYEEELAKAREELSRLQQETAE 450
Cdd:pfam17380 492 qrrkiLEKELEERKQAMIEEERKRKLLEKEM--EERQKAIYEEERRREAEEERRKQQEMEE 550

TPR_MLP1_2

pfam07926

TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...

327-446

1.61e-03

Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 39.54 E-value: 1.61e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  327 NEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKc 406
Cdd:pfam07926   1 AELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQNYERELVLHAEDIKALQALREELNELKAEIAELKAE- 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 119627229  407 AEEAQliSSLKAELTSQESQISTYEEELAKAREELSRLQQ 446
Cdd:pfam07926  80 AESAK--AELEESEESWEEQKKELEKELSELEKRIEDLNE 117

DUF4201

pfam13870

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

320-483

1.61e-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: 1.61e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  320 KELDTLNNEIVDLQREKNNVEQDLKEKEDtIKQRTSEVQDLQdeVQRENTnlqklqaqkqqvqELLDELDEQKAQLEE-- 397
Cdd:pfam13870   6 NELSKLRLELITLKHTLAKIQEKLEQKEE-LGEGLTMIDFLQ--LQIENQ-------------ALNEKIEERNKELKRlk 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  398 --------QLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESveSG----------- 458
Cdd:pfam13870  70 lkvtntvhALTHLKEKLHFLSAELSRLKKELRERQELLAKLRKELYRVKLERDKLRKQNKKLRQQ--GGllhvpallhdy 147

                         170       180
                  ....*....|....*....|....*...
gi 119627229  459 ---KAQLEPLQQHLQDSQQEISSMQMKL 483
Cdd:pfam13870 148 dktKAEVEEKRKSVKKLRRKVKILEMRI 175

FRQ1

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

40-176

1.62e-03

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

Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 39.78 E-value: 1.62e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  40 LGKIWDLADTDGKGILNKQEFfVALRLVACAQNGLEvslsslnlavppprfHDTSSPLLISGTSAAELPWAVKPED-KAK 118
Cdd:COG5126    7 LDRRFDLLDADGDGVLERDDF-EALFRRLWATLFSE---------------ADTDGDGRISREEFVAGMESLFEATvEPF 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 119627229 119 YDAIFDSLSP-VNGFLSGDKVKPVLLNSKLPVDILGRVWELSDIDHDGMLDRDEFAVAM 176
Cdd:COG5126   71 ARAAFDLLDTdGDGKISADEFRRLLTALGVSEEEADELFARLDTDGDGKISFEEFVAAV 129

End3

pfam12761

Actin cytoskeleton-regulatory complex protein END3; Endocytosis is accomplished through the ...

310-445

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 119627229  310 SSPVADFSAIKELDtlnNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDE---VQREntnlqklqaqkqqvqelLD 386
Cdd:pfam12761  84 SEKGTDFSATKGTD---WEEVRLKRELAELEEKLEKVEQAASKRRGGNRDESSKpalVKRE-----------------FE 143

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119627229  387 ELDEQKaqlEEQLKEVR--KKCAEEAQLiSSLKAELTSQESQISTYEEELAKAREELSRLQ 445
Cdd:pfam12761 144 QLLDYK---ERQLRELEegSGKSKPINL-KSVREDIDTVEEQVDGLESHLSSRKQELQQLR 200

APG6_N

pfam17675

Apg6 coiled-coil region; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. ...

384-488

1.67e-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: 1.67e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  384 LLDELDEQKAQLEEQ-------LKEVRKKCAEEaqlISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEEsve 456
Cdd:pfam17675  10 LLEELDKQLEDAEKErdayisfLKKLEKETPEE---LEELEKELEKLEKEEEELLQELEELEKEREELDAELEALEE--- 83

                          90       100       110
                  ....*....|....*....|....*....|..
gi 119627229  457 sgkaQLEPLQQHLQDSQQEISSMQMKLMEMKD 488
Cdd:pfam17675  84 ----ELEALDEEEEEFWREYNALQLQLLEFQD 111

Uso1_p115_C

pfam04871

Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ...

331-458

1.70e-03

Pssm-ID: 461461 [Multi-domain] Cd Length: 121 Bit Score: 39.30 E-value: 1.70e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  331 DLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEvqrentnlqklqaqkqqvQELLDELDEQKAQLEEQLKEVRKKCAEEA 410
Cdd:pfam04871   5 ELESEASSLKNENTELKAELQELSKQYNSLEQK------------------ESQAKELEAEVKKLEEALKKLKAELSEEK 66

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 119627229  411 QLISSLKAEL-------TSQESQISTYEEELAKAREELSRLQQETAELEESVESG 458
Cdd:pfam04871  67 QKEKEKQSELddlllllGDLEEKVEKYKARLKELGEEVLSDDEDDDEDDEEDDEE 121

Myosin_tail_1

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

321-488

1.71e-03

Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.08 E-value: 1.71e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   321 ELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQREntnlqklqaqkqqvQELLDELDE-------QKA 393
Cdd:pfam01576    6 EMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAE--------------TELCAEAEEmrarlaaRKQ 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   394 QLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQ 473
Cdd:pfam01576   72 ELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLS 151

                          170
                   ....*....|....*
gi 119627229   474 QEISSMQMKLMEMKD 488
Cdd:pfam01576  152 KERKLLEERISEFTS 166

Nnf1

pfam03980

Nnf1; NNF1 is an essential yeast gene that is necessary for chromosome segregation. It is ...

383-458

1.72e-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: 1.72e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  383 ELLDELDEqkaqLEEQLKEvRKKCAEEAQLISSLKAEltsqesQI------STYEEELAKAREELSRLQQETAELEESVE 456
Cdd:pfam03980  33 AKLNELDE----LIEEAKE-RREEGEGPAWRPSVPPE------ELirahlaPYKQKQLEQLNARLQKLEAENAALAEEVQ 101


                  ..
gi 119627229  457 SG 458
Cdd:pfam03980 102 AQ 103

PRK00409

recombination and DNA strand exchange inhibitor protein; Reviewed

325-488

1.72e-03

recombination and DNA strand exchange inhibitor protein; Reviewed

Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.12 E-value: 1.72e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 325 LNNEIVD-----LQREKNNVEQ---DLKEKEDTIKQRTSEVQDLQDEVQRentnlqklqaqkqqvqeLLDELDEQKAQLE 396
Cdd:PRK00409 499 LPENIIEeakklIGEDKEKLNEliaSLEELERELEQKAEEAEALLKEAEK-----------------LKEELEEKKEKLQ 561

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 397 EQLKEVRKKCAEEAQlisslkaeltsqesqistyeEELAKAREELSRLQQETAELE-ESVESGKAQ-LEPLQQHLQDSQQ 474
Cdd:PRK00409 562 EEEDKLLEEAEKEAQ--------------------QAIKEAKKEADEIIKELRQLQkGGYASVKAHeLIEARKRLNKANE 621

                        170
                 ....*....|....
gi 119627229 475 EISSMQMKLMEMKD 488
Cdd:PRK00409 622 KKEKKKKKQKEKQE 635

HCR

pfam07111

Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...

328-487

1.75e-03

Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 42.05 E-value: 1.75e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  328 EIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLD---ELDEQKAQLEE--QLKEV 402
Cdd:pfam07111 191 QLAEAQKEAELLRKQLSKTQEELEAQVTLVESLRKYVGEQVPPEVHSQTWELERQELLDtmqHLQEDRADLQAtvELLQV 270

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  403 R------------KKCAEEAQLISSLKAELTSQ-ESQISTYEEEL------AKA-----REELSRLQQETAELEESVESG 458
Cdd:pfam07111 271 RvqslthmlalqeEELTRKIQPSDSLEPEFPKKcRSLLNRWREKVfalmvqLKAqdlehRDSVKQLRGQVAELQEQVTSQ 350

                         170       180       190
                  ....*....|....*....|....*....|.
gi 119627229  459 KAQLEPLQQHLQD--SQQEISSMQMKLMEMK 487
Cdd:pfam07111 351 SQEQAILQRALQDkaAEVEVERMSAKGLQME 381

MscS_porin

pfam12795

Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...

385-497

1.80e-03

Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 40.75 E-value: 1.80e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  385 LDELDEQKaQLEEQLKEVRKKcAEEAQL----ISSLKAELTSQESQISTYEEELAKAREELSRLQQeTAELEESVESGKA 460
Cdd:pfam12795   2 LDELEKAK-LDEAAKKKLLQD-LQQALSlldkIDASKQRAAAYQKALDDAPAELRELRQELAALQA-KAEAAPKEILASL 78

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 119627229  461 QLEPLQQHLQDSQQEISSMQmklmemKDLENHNSQLN 497
Cdd:pfam12795  79 SLEELEQRLLQTSAQLQELQ------NQLAQLNSQLI 109

ClpA

COG0542

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

383-496

1.85e-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: 1.85e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 383 ELLDELDEQKAQLEEqlkevrkkcaEEAQLIsslkaeltsQESQISTYEEeLAKAREELSRLQQETAELEESVESGKAQL 462
Cdd:COG0542  411 EELDELERRLEQLEI----------EKEALK---------KEQDEASFER-LAELRDELAELEEELEALKARWEAEKELI 470

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 119627229 463 EPLQ---QHLQDSQQEISSMQMKLMEMKDLENHNSQL 496
Cdd:COG0542  471 EEIQelkEELEQRYGKIPELEKELAELEEELAELAPL 507

Myosin_tail_1

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

320-504

2.17e-03

Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 41.70 E-value: 2.17e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   320 KELDTLNNE----IVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRentnlqklqaqkqqVQELLDELDEQKAQL 395
Cdd:pfam01576  176 KSLSKLKNKheamISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAE--------------LQAQIAELRAQLAKK 241

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   396 EEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLE------PLQQHL 469
Cdd:pfam01576  242 EEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEdtldttAAQQEL 321

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 119627229   470 QDS-QQEISSMQMKLMEmkDLENHNSQLNWCSSPHS 504
Cdd:pfam01576  322 RSKrEQEVTELKKALEE--ETRSHEAQLQEMRQKHT 355

WEMBL

pfam05701

Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ...

384-487

2.19e-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: 41.55 E-value: 2.19e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  384 LLDELDEQKAQLEEqlkeVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSR----LQQETAELEESVESGK 459
Cdd:pfam05701 326 LRSELEKEKAELAS----LRQREGMASIAVSSLEAELNRTKSEIALVQAKEKEAREKMVElpkqLQQAAQEAEEAKSLAQ 401

                          90       100       110
                  ....*....|....*....|....*....|.
gi 119627229  460 AQLEPLQQHLQDSQQ---EISSMQMKLMEMK 487
Cdd:pfam05701 402 AAREELRKAKEEAEQakaAASTVESRLEAVL 432

UPF0242

pfam06785

Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ...

383-493

2.21e-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: 2.21e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  383 ELLDELDEQKAQLEEQLkevRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVES----- 457
Cdd:pfam06785  58 EDALKEKFEKSFLEEKE---AKLTELDAEGFKILEETLEELQSEEERLEEELSQKEEELRRLTEENQQLQIQLQQisqdf 134

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 119627229  458 ------GKAQLEPLQQHLQDSQQEISSmQMKLMEMKDLENHN 493
Cdd:pfam06785 135 aefrleSEEQLAEKQLLINEYQQTIEE-QRSVLEKRQDQIEN 175

CEP63

pfam17045

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

387-531

2.37e-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: 2.37e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  387 ELDEQKAQLEEQLKEVRKKCA--EEAQlisSLKAELTSQesqistYEEELAKAREELSRLQ------------------- 445
Cdd:pfam17045  43 ELLSARNTLERKHKEIGLLRQqlEELE---KGKQELVAK------YEQQLQKLQEELSKLKrsyeklqrkqlkeareeak 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  446 -QETAELEESVESGKAQ------LEPLQQHLQdSQQEISSMQmklMEMKDLENHNSQLNwcSSPHSILVNGATdyCSLST 518
Cdd:pfam17045 114 sREEDRSELSRLNGKLEefrqksLEWEQQRLQ-YQQQVASLE---AQRKALAEQSSLIQ--SAAYQVQLEGRK--QCLEA 185

                         170
                  ....*....|...
gi 119627229  519 SSSETANLNEHVE 531
Cdd:pfam17045 186 SQSEIQRLRSKLE 198

SMC_prok_B

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

321-451

2.43e-03

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.58 E-value: 2.43e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   321 ELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLk 400
Cdd:TIGR02168  867 LIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL- 945

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 119627229   401 evrkkcAEEAQLisslkaELTSQESQISTYEEELAKAREELSRLQQETAEL 451
Cdd:TIGR02168  946 ------SEEYSL------TLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984

PRK03918

DNA double-strand break repair ATPase Rad50;

320-467

2.46e-03

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 2.46e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 320 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRT--SEVQDLQDEVqrENTNLQKLQAQKQQVQELLDELDEQKAQ--- 394
Cdd:PRK03918 466 KELKEIEEKERKLRKELRELEKVLKKESELIKLKElaEQLKELEEKL--KKYNLEELEKKAEEYEKLKEKLIKLKGEiks 543

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 395 --------------LEEQLKEVRKKCAEEAQLISSLKA------------------------ELTSQESQISTYEEELAK 436
Cdd:PRK03918 544 lkkelekleelkkkLAELEKKLDELEEELAELLKELEElgfesveeleerlkelepfyneylELKDAEKELEREEKELKK 623

                        170       180       190
                 ....*....|....*....|....*....|.
gi 119627229 437 AREELSRLQQETAELEESVESGKAQLEPLQQ 467
Cdd:PRK03918 624 LEEELDKAFEELAETEKRLEELRKELEELEK 654

GAS

pfam13851

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

336-497

2.51e-03

Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 40.27 E-value: 2.51e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  336 KNNVE--QDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQklqaqkqqvqELLDELDEQKAQLEEQLKEVRKkcaeeaqli 413
Cdd:pfam13851  22 RNNLEliKSLKEEIAELKKKEERNEKLMSEIQQENKRLT----------EPLQKAQEEVEELRKQLENYEK--------- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  414 ssLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLE-PLQQHLQDSQQEISSMQMKLMEM-KDLEN 491
Cdd:pfam13851  83 --DKQSLKNLKARLKVLEKELKDLKWEHEVLEQRFEKVERERDELYDKFEaAIQDVQQKTGLKNLLLEKKLQALgETLEK 160


                  ....*.
gi 119627229  492 HNSQLN 497
Cdd:pfam13851 161 KEAQLN 166

OmpH

pfam03938

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

383-485

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 119627229  383 ELLDELDEQK---AQLEEQLKEVRKKCAEEAQLISSLKAELtsqESQISTYEEELAKAREELSRLQQEtaeleesvesgk 459
Cdd:pfam03938   9 KILEESPEGKaaqAQLEKKFKKRQAELEAKQKELQKLYEEL---QKDGALLEEEREEKEQELQKKEQE------------ 73

                          90       100
                  ....*....|....*....|....*.
gi 119627229  460 aqlepLQQHLQDSQQEISSMQMKLME 485
Cdd:pfam03938  74 -----LQQLQQKAQQELQKKQQELLQ 94

sbcc

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

332-496

2.63e-03

Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.49 E-value: 2.63e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   332 LQREKNNVEQ---DLKEKEDTIKQRTSEVQDLQ--DEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKC 406
Cdd:TIGR00618  641 LALKLTALHAlqlTLTQERVREHALSIRVLPKEllASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREF 720

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   407 AEEAQLISSLKAELTSQES-----------------QISTYEEELAKARE--------ELSRLQQETA----ELEESVES 457
Cdd:TIGR00618  721 NEIENASSSLGSDLAAREDalnqslkelmhqartvlKARTEAHFNNNEEVtaalqtgaELSHLAAEIQffnrLREEDTHL 800

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 119627229   458 GKAQLEPLQQHLQDSQQEISSMQMKLmeMKDLENHNSQL 496
Cdd:TIGR00618  801 LKTLEAEIGQEIPSDEDILNLQCETL--VQEEEQFLSRL 837

Kre28

pfam17097

Spindle pole body component; In Saccharomyces cerevisae Kre28 and Spc105 form a kinetochore ...

320-453

2.71e-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: 40.95 E-value: 2.71e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  320 KELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQrentnlqklqaqkqqvqELLDELDeqkaQLEEQL 399
Cdd:pfam17097 133 DTLTVLNQEIDQIKGDILQVAQEIADKQDQVNELCLETSNELDECW-----------------ELLNELE----RLRDQR 191

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 119627229  400 KEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEE 453
Cdd:pfam17097 192 ITVEEQTSNEKDTELDPVEETYEEWKSLQESLQQLEHLKEELDQLQKQKDSLEK 245

PRK09039

peptidoglycan -binding protein;

396-481

2.85e-03

peptidoglycan -binding protein;

Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.72 E-value: 2.85e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 396 EEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLqDSQQE 475
Cdd:PRK09039  52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQEL-DSEKQ 130


                 ....*.
gi 119627229 476 ISSMQM 481
Cdd:PRK09039 131 VSARAL 136

ZapB

pfam06005

Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is ...

419-485

3.12e-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: 36.86 E-value: 3.12e-03

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119627229  419 ELTSQ-ESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEISSMQMKLME 485
Cdd:pfam06005   4 ELLEQlETKIQAAVDTIALLQMENEELKEENEELKEEANELEEENQQLKQERNQWQERIRGLLGKLDE 71

mukB

chromosome partition protein MukB;

340-480

3.18e-03

chromosome partition protein MukB;

Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.48 E-value: 3.18e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  340 EQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKA- 418
Cdd:PRK04863  515 LQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQAr 594

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119627229  419 --ELTSQESQISTYEEELAKARE----------ELSRLQQETAELEESVESGKAQLEPLQQHLqdsQQEISSMQ 480
Cdd:PRK04863  595 iqRLAARAPAWLAAQDALARLREqsgeefedsqDVTEYMQQLLERERELTVERDELAARKQAL---DEEIERLS 665

Myosin_tail_1

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

321-497

3.32e-03

Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 41.31 E-value: 3.32e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   321 ELDTLNNEIVDLQREKNNVEQDLKEKEDTIK-----------QRT----------SEVQDLQDEVQRENtnlQKLQAQKQ 379
Cdd:pfam01576  216 ESTDLQEQIAELQAQIAELRAQLAKKEEELQaalarleeetaQKNnalkkireleAQISELQEDLESER---AARNKAEK 292

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   380 QVQELLDELDEQKAQLEEQL------KEVR-KKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSR--------- 443
Cdd:pfam01576  293 QRRDLGEELEALKTELEDTLdttaaqQELRsKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEqleqakrnk 372

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119627229   444 ---------LQQETAELEE---SVESGK-----------AQLEPLQQHLQDSQQEISSMQMKLMEMK-DLENHNSQLN 497
Cdd:pfam01576  373 anlekakqaLESENAELQAelrTLQQAKqdsehkrkkleGQLQELQARLSESERQRAELAEKLSKLQsELESVSSLLN 450

Tektin

pfam03148

Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ...

320-491

3.33e-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: 40.61 E-value: 3.33e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  320 KELDTLNNEIVDLQREKNNVEQDLKEKEDTI----------KQRTSEvqDL-QDEVQRentnlqklqaqkqqvqELLDEL 388
Cdd:pfam03148  64 KELEELDEEIELLLEEKRRLEKALEALEEPLhiaqecltlrEKRQGI--DLvHDEVEK----------------ELLKEV 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  389 D----------EQKAQLEEQL---KEVRKKCA------EEAQLI----------S---SLKAELTSQESQISTYEE---- 432
Cdd:pfam03148 126 EliegiqellqRTLEQAWEQLrllRAARHKLEkdlsdkKEALEIdekclslnntSpniSYKPGPTRIPPNSSTPEEwekf 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  433 ----------ELAKA---REELSRLQQETAELEES---------------VESGKAQLEplqQHLQDSQQEISSMQmklM 484
Cdd:pfam03148 206 tqdnieraekERAASaqlRELIDSILEQTANDLRAqadavnfalrkrieeTEDAKNKLE---WQLKKTLQEIAELE---K 279


                  ....*..
gi 119627229  485 EMKDLEN 491
Cdd:pfam03148 280 NIEALEK 286

sbcc

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

332-495

3.61e-03

Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.11 E-value: 3.61e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   332 LQREKNNVEQDLKEKEDTIKQRtsevQDLQDEVQRENTNLQKLQAQKQQVQE---LLDELDEQKA------QLEEQLKEV 402
Cdd:TIGR00618  316 LQSKMRSRAKLLMKRAAHVKQQ----SSIEEQRRLLQTLHSQEIHIRDAHEVatsIREISCQQHTltqhihTLQQQKTTL 391

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   403 RKKCAEEAQLISSLKAELTSQESQISTYEEE---LAKAREELsRLQQETAELEESVESGKAQLEPLQQ-HLQDSQQEISS 478
Cdd:TIGR00618  392 TQKLQSLCKELDILQREQATIDTRTSAFRDLqgqLAHAKKQQ-ELQQRYAELCAAAITCTAQCEKLEKiHLQESAQSLKE 470

                          170
                   ....*....|....*..
gi 119627229   479 MQMKLmemKDLENHNSQ 495
Cdd:TIGR00618  471 REQQL---QTKEQIHLQ 484

SCP-1

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

323-488

3.70e-03

Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 40.86 E-value: 3.70e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  323 DTLNNEIVDLQREKNNVEQDLK-EKEDTIKQRTSEVQDLQdevQRENTNLQKLqaqkqqvqELLDELDEQKAQLEEQLKE 401
Cdd:pfam05483 495 DKLLLENKELTQEASDMTLELKkHQEDIINCKKQEERMLK---QIENLEEKEM--------NLRDELESVREEFIQKGDE 563

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  402 VRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREE-------LSRLQQETAELEESVESGKAQLEPLQQHLQDSQQ 474
Cdd:pfam05483 564 VKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQienknknIEELHQENKALKKKGSAENKQLNAYEIKVNKLEL 643

                         170
                  ....*....|....
gi 119627229  475 EISSMQMKLMEMKD 488
Cdd:pfam05483 644 ELASAKQKFEEIID 657

COG2433

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

395-497

3.80e-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: 3.80e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 395 LEEQLKEVRKKcaEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQ 474
Cdd:COG2433  378 IEEALEELIEK--ELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARS 455

                         90       100
                 ....*....|....*....|...
gi 119627229 475 EISSMQMKLMEMKDLENHNSQLN 497
Cdd:COG2433  456 EERREIRKDREISRLDREIERLE 478

flagell_FliJ

TIGR02473

flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ...

383-497

3.87e-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: 38.45 E-value: 3.87e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  383 ELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSlKAELTSQESQISTYEEELAKAREELSRLQQetaeleesvesgkaQL 462
Cdd:TIGR02473  27 AEFERLETQLQQLIKYREEYEQQALEKVGAGTS-ALELSNYQRFIRQLDQRIQQQQQELALLQQ--------------EV 91

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 119627229  463 EPLQQHLQDSQQEIssMQMKLMEMKDLENHNSQLN 497
Cdd:TIGR02473  92 EAKRERLLEARREL--KALEKLKEKKQKEYRAEEA 124

Smc

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

383-479

3.99e-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: 3.99e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 383 ELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELEESVESGKAQL 462
Cdd:COG1196  683 ELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL 762

                         90
                 ....*....|....*..
gi 119627229 463 EPLQQHLQDSQQEISSM 479
Cdd:COG1196  763 EELERELERLEREIEAL 779

CCDC158

pfam15921

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...

312-494

4.10e-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: 40.87 E-value: 4.10e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   312 PVADfsaikELDTLNNEivdlqrEKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDE-LDE 390
Cdd:pfam15921  242 PVED-----QLEALKSE------SQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEqARN 310

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   391 QKAQLEEQLKEVRKKCAeeaQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAELeeSVESGKA--QLEPLQQH 468
Cdd:pfam15921  311 QNSMYMRQLSDLESTVS---QLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQF--SQESGNLddQLQKLLAD 385

                          170       180
                   ....*....|....*....|....*.
gi 119627229   469 LQDSQQEISSMQMKLMEMKDLENHNS 494
Cdd:pfam15921  386 LHKREKELSLEKEQNKRLWDRDTGNS 411

MukB

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

388-474

4.59e-03

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

Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 40.71 E-value: 4.59e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  388 LDEQKAQLEEQ--LKEVRKKCAEEAQLISSLKAELTS-------------QESQISTYEEEL--------------AKAR 438
Cdd:COG3096   295 FGARRQLAEEQyrLVEMARELEELSARESDLEQDYQAasdhlnlvqtalrQQEKIERYQEDLeelterleeqeevvEEAA 374

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 119627229  439 EELSRLQQETAELEESVESGKAQLEPLQQHLqDSQQ 474
Cdd:COG3096   375 EQLAEAEARLEAAEEEVDSLKSQLADYQQAL-DVQQ 409

FliJ

pfam02050

Flagellar FliJ protein;

385-480

4.65e-03

Flagellar FliJ protein;

Pssm-ID: 426581 [Multi-domain] Cd Length: 123 Bit Score: 38.03 E-value: 4.65e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  385 LDELDEQKAQLEEQLKEVRKKCAEEA-----QLISSLKAELTSQESQISTYEEELAKAREELSRLQQEtaelEESVE--S 457
Cdd:pfam02050  21 LEELQQYRAEYQQQLSGAGQGISAAElrnyqAFISQLDEAIAQQQQELAQAEAQVEKAREEWQEARQE----RKSLEklR 96

                          90       100
                  ....*....|....*....|....*...
gi 119627229  458 GKAQLEplQQHLQDSQQ-----EISSMQ 480
Cdd:pfam02050  97 EREKKE--ERKEQNRREqkqldELAARL 122

PRK10246

exonuclease subunit SbcC; Provisional

390-496

5.23e-03

exonuclease subunit SbcC; Provisional

Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 40.55 E-value: 5.23e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  390 EQKAQLEEQLKEVRKK-----------CAEE-----AQLISS--LKAELTSQESQISTYEEELAKAREELSRLQQETAEL 451
Cdd:PRK10246  380 EQLRQWQQQLTHAEQKlnalpaitltlTADEvaaalAQHAEQrpLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQR 459

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 119627229  452 EESVESGKAQLEPLQQHLQD----SQQEissmqmklMEMKDLENHNSQL 496
Cdd:PRK10246  460 NAALNEMRQRYKEKTQQLADvktiCEQE--------ARIKDLEAQRAQL 500

fliH

PRK06669

flagellar assembly protein H; Validated

303-483

5.27e-03

flagellar assembly protein H; Validated

Pssm-ID: 235850 [Multi-domain] Cd Length: 281 Bit Score: 39.61 E-value: 5.27e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 303 LQKNIIGSSPVADFSAIKELDTLNNEIVDLQREKNNveqdlKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQA--QKQQ 380
Cdd:PRK06669   1 MPKVIFKRSNVINKEKLKTHEIQKYRFKVLSIKEKE-----RLREEEEEQVEQLREEANDEAKEIIEEAEEDAFeiVEAA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 381 VQELLDELDEQKAQLEEQLKEVRKKCA-EEAQLISSLKAELtsQESQISTYEEELAKAREE-LSRLQQETAELEESVESG 458
Cdd:PRK06669  76 EEEAKEELLKKTDEASSIIEKLQMQIErEQEEWEEELERLI--EEAKAEGYEEGYEKGREEgLEEVRELIEQLNKIIEKL 153

                        170       180
                 ....*....|....*....|....*
gi 119627229 459 KAQLEplqQHLQDSQQEISSMQMKL 483
Cdd:PRK06669 154 IKKRE---EILESSEEEIVELALDI 175

Myosin_tail_1

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

322-496

5.48e-03

Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.54 E-value: 5.48e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   322 LDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKE 401
Cdd:pfam01576  358 LEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSK 437

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   402 VRKKC--------AEEAQLISSLKaELTSQESQISTYEEELA-KAREEL---SRLQQ---ETAELEESVESGKAQLEPLQ 466
Cdd:pfam01576  438 LQSELesvssllnEAEGKNIKLSK-DVSSLESQLQDTQELLQeETRQKLnlsTRLRQledERNSLQEQLEEEEEAKRNVE 516

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 119627229   467 QHLQDSQQEISSMQMKLMEM---------------KDLENHNSQL 496
Cdd:pfam01576  517 RQLSTLQAQLSDMKKKLEEDagtlealeegkkrlqRELEALTQQL 561

BBC

smart00502

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

383-488

5.57e-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: 5.57e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   383 ELLDELDEQKAQLEEQLKEVRKKCaeeaQLISSLKAELTSQ-ESQISTYEEELAKAREEL-SRLQQETAELEESVESGKA 460
Cdd:smart00502   7 ELLTKLRKKAAELEDALKQLISII----QEVEENAADVEAQiKAAFDELRNALNKRKKQLlEDLEEQKENKLKVLEQQLE 82

                           90       100
                   ....*....|....*....|....*...
gi 119627229   461 QLEPLQQHLQDSQQEISsmqmKLMEMKD 488
Cdd:smart00502  83 SLTQKQEKLSHAINFTE----EALNSGD 106

growth_prot_Scy

polarized growth protein Scy;

344-467

5.58e-03

polarized growth protein Scy;

Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 40.58 E-value: 5.58e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  344 KEKEDTIKQRTSEVQDLQDEVQREntnlqklqaqkqqVQELLDELDEQKAQL-EEQLKEVRKKCAEEAQLISSLKAElts 422
Cdd:NF041483  520 RQAEETLERTRAEAERLRAEAEEQ-------------AEEVRAAAERAARELrEETERAIAARQAEAAEELTRLHTE--- 583

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 119627229  423 QESQISTYEEELAKAREELSRLQQETAELEESVESGKAQ-LEPLQQ 467
Cdd:NF041483  584 AEERLTAAEEALADARAEAERIRREAAEETERLRTEAAErIRTLQA 629

CusB_dom_1

pfam00529

Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...

319-445

5.69e-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: 5.69e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  319 IKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEE- 397
Cdd:pfam00529  81 LDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLLAt 160

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 119627229  398 --QLKEVRK-KCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQ 445
Cdd:pfam00529 161 vaQLDQIYVqITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLERTE 211

CCDC-167

pfam15188

Coiled-coil domain-containing protein 167; The function of this family of coiled-coil domains, ...

385-440

6.11e-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: 6.11e-03

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  385 LDELDEQKAQLEEQLKEVRKKcAEEAQLI----SSLKAELTSQESQISTYEEELAKAREE 440
Cdd:pfam15188   5 IDRLEEKIASCRDRLERIEKK-LRREELSeedrRSLEKELLLLKKRLEKNEEELKLLRKE 63

Macoilin

pfam09726

Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ...

320-486

6.17e-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: 6.17e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  320 KELDTLNNEIVDL----QREKNNV---EQDLKEKEDTikqRTSEVQDLQDEVQR----ENTNLQKLQAQKQQVQELLDEL 388
Cdd:pfam09726 444 QENDLLQTKLHNAvsakQKDKQTVqqlEKRLKAEQEA---RASAEKQLAEEKKRkkeeEATAARAVALAAASRGECTESL 520

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  389 DEQKAQLEEQLKEVRKKCAEEAQLISSLkaELTSQEsqISTYEEElAKARE----ELSRLQQETAELEESVES------- 457
Cdd:pfam09726 521 KQRKRELESEIKKLTHDIKLKEEQIREL--EIKVQE--LRKYKES-EKDTEvlmsALSAMQDKNQHLENSLSAetrikld 595

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 119627229  458 -------GKAQLEPLQQHLQDSQQEISSMQMKLMEM 486
Cdd:pfam09726 596 lfsalgdAKRQLEIAQGQIYQKDQEIKDLKQKIAEV 631

Prefoldin_2

pfam01920

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

385-482

6.22e-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: 6.22e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  385 LDELDEQKAQLEEQLKEVrkKCAEEAqlISSLKAELTSQESqIST--YEEELAKAREElsrLQQETAELEESVESGKAQL 462
Cdd:pfam01920  11 LQLLAQQIKQLETQLKEL--ELALEE--LELLDEDTKVYKL-IGDvlVKQDKEEVKEQ---LEERKETLEKEIKTLEKQL 82

                          90       100
                  ....*....|....*....|
gi 119627229  463 EPLQQHLQDSQQEISSMQMK 482
Cdd:pfam01920  83 EKLEKELEELKEELYKKFGQ 102

ClyA_Cry6Aa-like

cd22656

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...

383-498

6.74e-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: 6.74e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 383 ELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTY--EEELAKAREELSRLQQETAEL-EESVESGK 459
Cdd:cd22656  121 ALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLltDEGGAIARKEIKDLQKELEKLnEEYAAKLK 200

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 119627229 460 AQLEPLQQHLQDSQQEIssmQMKLMEMKDLENHNSQLNW 498
Cdd:cd22656  201 AKIDELKALIADDEAKL---AAALRLIADLTAADTDLDN 236

PRK12705

hypothetical protein; Provisional

317-446

6.81e-03

hypothetical protein; Provisional

Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 40.08 E-value: 6.81e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229 317 SAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTikqrtSEVQDLQDE----VQRENTNLQKLQAQKQQVQELLD------ 386
Cdd:PRK12705  41 EAQKEAEEKLEAALLEAKELLLRERNQQRQEAR-----REREELQREeerlVQKEEQLDARAEKLDNLENQLEErekals 115

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119627229 387 ----ELDEQKAQLEEQLKEVRKKCAEEA--QLISSLKAELTSQESQISTYEEElaKAREELSRLQQ 446
Cdd:PRK12705 116 arelELEELEKQLDNELYRVAGLTPEQArkLLLKLLDAELEEEKAQRVKKIEE--EADLEAERKAQ 179

sbcc

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

321-476

7.36e-03

Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 39.95 E-value: 7.36e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   321 ELDTLNNEIVDLQR--EKNNVEQDLKEKEDTIKQRTSEVQ-DLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKaqLEE 397
Cdd:TIGR00618  585 DIPNLQNITVRLQDltEKLSEAEDMLACEQHALLRKLQPEqDLQDVRLHLQQCSQELALKLTALHALQLTLTQER--VRE 662

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119627229   398 QLKEVRKkcaEEAQLISSLKAELTSQESQIstyeEELAKAREELSRLQQETAELEESVESGKAQLEPLQQHLQDSQQEI 476
Cdd:TIGR00618  663 HALSIRV---LPKELLASRQLALQKMQSEK----EQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDL 734

mukB

chromosome partition protein MukB;

387-474

7.82e-03

chromosome partition protein MukB;

Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.94 E-value: 7.82e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  387 ELDEQKAQLEEQ---LKEVRKKCAEEAQLISSLKAELTS-------------QESQISTYEEELAK-------------- 436
Cdd:PRK04863  294 ELYTSRRQLAAEqyrLVEMARELAELNEAESDLEQDYQAasdhlnlvqtalrQQEKIERYQADLEEleerleeqnevvee 373

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 119627229  437 AREELSRLQQETAELEESVESGKAQLEPLQQHLqDSQQ 474
Cdd:PRK04863  374 ADEQQEENEARAEAAEEEVDELKSQLADYQQAL-DVQQ 410

DUF4686

pfam15742

Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ...

343-483

8.11e-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: 8.11e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  343 LKEKEDTIKQRTSEVQDLQDEVQRentnlqKLQAQKQQVQELLDE-------------LDEQKAQLEEQLKEVRKKCAEE 409
Cdd:pfam15742   1 VSSGEKLKYQQQEEVQQLRQNLQR------LQILCTSAEKELRYErgknldlkqhnslLQEENIKIKAELKQAQQKLLDS 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  410 AQLISSLKAELtsqesqistyeeelakareelSRLQQETAELE----ESVESGKAQ---LEPLQQH---LQDSQQEISSM 479
Cdd:pfam15742  75 TKMCSSLTAEW---------------------KHCQQKIRELElevlKQAQSIKSQnslQEKLAQEksrVADAEEKILEL 133


                  ....
gi 119627229  480 QMKL 483
Cdd:pfam15742 134 QQKL 137

DUF3584

pfam12128

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...

317-497

8.36e-03

Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 39.82 E-value: 8.36e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   317 SAIKELDTLNNEIVDLQREknnVEQDLKEKEDTIKQRTSEVQDLQDEVQ--RENTNLQKLQAqK---QQVQELLDELDEQ 391
Cdd:pfam12128  255 SAELRLSHLHFGYKSDETL---IASRQEERQETSAELNQLLRTLDDQWKekRDELNGELSAA-DaavAKDRSELEALEDQ 330

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   392 KAQLEEQLKEVRKKCAEEAQLISS--------LKAELTSQESQISTYEEELAKAREE----LSRLQQETAELEESVESGK 459
Cdd:pfam12128  331 HGAFLDADIETAAADQEQLPSWQSelenleerLKALTGKHQDVTAKYNRRRSKIKEQnnrdIAGIKDKLAKIREARDRQL 410

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 119627229   460 A-------QLE-PLQQHLQDSQQEISSMQMKLMEmkDLENHNSQLN 497
Cdd:pfam12128  411 AvaeddlqALEsELREQLEAGKLEFNEEEYRLKS--RLGELKLRLN 454

MukB

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

386-476

8.60e-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: 8.60e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  386 DELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETAeLEESVESGKAQLEPL 465
Cdd:COG3096   281 RELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTALR-QQEKIERYQEDLEEL 359

                          90
                  ....*....|.
gi 119627229  466 QQHLqDSQQEI 476
Cdd:COG3096   360 TERL-EEQEEV 369

TPH

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

333-462

8.80e-03

Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 39.13 E-value: 8.80e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  333 QREKNNVEQDLKEKEDTIKQRTSEVQD----LQDEVQREntnlqklQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAE 408
Cdd:pfam13868 221 QKEREEAEKKARQRQELQQAREEQIELkerrLAEEAERE-------EEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRR 293

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 119627229  409 EaqlisslkaeltsQESQI----STYEEELAKAREELSRLQQETAELEESVESGKAQL 462
Cdd:pfam13868 294 E-------------LEKQIeereEQRAAEREEELEEGERLREEEAERRERIEEERQKK 338

CALCOCO1

pfam07888

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...

331-496

8.96e-03

Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 39.49 E-value: 8.96e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  331 DLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEA 410
Cdd:pfam07888  56 QREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELE 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  411 QLISSLKAELTSQESQISTYEEELAKA----REELSRLQQETAELEESVE----------SGKAQLEPLQQHLQDSQQEI 476
Cdd:pfam07888 136 EDIKTLTQRVLERETELERMKERAKKAgaqrKEEEAERKQLQAKLQQTEEelrslskefqELRNSLAQRDTQVLQLQDTI 215

                         170       180
                  ....*....|....*....|
gi 119627229  477 SSMQMKLMEMKDLENHNSQL 496
Cdd:pfam07888 216 TTLTQKLTTAHRKEAENEAL 235

Leu_zip

pfam15294

Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ...

325-449

9.54e-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: 9.54e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229  325 LNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQ---DEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKE 401
Cdd:pfam15294 131 LHMEIERLKEENEKLKERLKTLESQATQALDEKSKLEkalKDLQKEQGAKKDVKSNLKEISDLEEKMAALKSDLEKTLNA 210

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 119627229  402 vrkkcaeEAQLISSLKAELTSQESQISTYEEELAKAREELSRLQQETA 449
Cdd:pfam15294 211 -------STALQKSLEEDLASTKHELLKVQEQLEMAEKELEKKFQQTA 251

OmpH

smart00935

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

392-485

9.56e-03

Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 37.56 E-value: 9.56e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627229   392 KAQLEEQLKEVRKKCAEEAQLISSLKAELTSQESQIStyEEELAKAREELSRLQQEtaeleesvesgkaqlepLQQHLQD 471
Cdd:smart00935  20 QKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLS--EAAREKKEKELQKKVQE-----------------FQRKQQK 80

                           90
                   ....*....|....
gi 119627229   472 SQQEISSMQMKLME 485
Cdd:smart00935  81 LQQDLQKRQQEELQ 94

TPH