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Conserved domains on  [gi|1958776456|ref|XP_038965890|]
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epidermal growth factor receptor substrate 15 isoform X6 [Rattus norvegicus]

Protein Classification

EH domain-containing protein( domain architecture ID 12184509)

EH (Eps15 homology) domain-containing protein 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+

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
121-215 4.45e-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: 151.28  E-value: 4.45e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  121 PWAVKSEDKAKYDAIFDSLSP-VDGFLSGDKVKPVLLNSKLPVEILGRVWELSDIDHDGKLDRDEFAVAMFLVYCALEKE 199
Cdd:smart00027   1 PWAISPEDKAKYEQIFRSLDKnQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGY 80
                           90
                   ....*....|....*.
gi 1958776456  200 PVPMSLPPALVPPSKR 215
Cdd:smart00027  81 PIPASLPPSLIPPSKR 96
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
253-349 6.92e-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: 144.73  E-value: 6.92e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  253 QWVVSPAEKAKYDEIFLKTDKDMDGYVSGLEVRETFLKTGLPSTLLAHIWALCDTKNCGKLSKDQFALAFHLINQKLIkG 332
Cdd:smart00027   1 PWAISPEDKAKYEQIFRSLDKNQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLN-G 79
                           90
                   ....*....|....*..
gi 1958776456  333 IDPPHSLTPEMIPPSDK 349
Cdd:smart00027  80 YPIPASLPPSLIPPSKR 96
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
13-103 7.55e-26

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: 101.97  E-value: 7.55e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456   13 SSGNPVYEKYYRQVEAGNTGRVLALDAAAFLKKSGLPDLILGKIWDLADTDGKGVLNKQEFFIALRLVACAQNGLEVSLS 92
Cdd:smart00027   6 PEDKAKYEQIFRSLDKNQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGYPIPAS 85
                           90
                   ....*....|.
gi 1958776456   93 SLNLAVPPPRF 103
Cdd:smart00027  86 LPPSLIPPSKR 96
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
366-529 1.22e-15

Uncharacterized protein, contains DUF3084 domain [Function unknown];


:

Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 79.56  E-value: 1.22e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 366 SAIKELDTLNNEIIDLQREKNNVEQDLKEKEDTVRQRTTEAQDLQDEVQRESLNLQKLQAQKQQVQELLDELDEQKAQLE 445
Cdd:COG4372    35 KALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQ 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 446 EQLKEVRKKCAEEAQLISSLKAEITSQESQISTYEEELSKAREELSRLQQETAQLEESVESGKAQL--EPLQQHLQDSQQ 523
Cdd:COG4372   115 EELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEaeQALDELLKEANR 194

                  ....*.
gi 1958776456 524 EISSMQ 529
Cdd:COG4372   195 NAEKEE 200
 
Name Accession Description Interval E-value
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
121-215 4.45e-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: 151.28  E-value: 4.45e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  121 PWAVKSEDKAKYDAIFDSLSP-VDGFLSGDKVKPVLLNSKLPVEILGRVWELSDIDHDGKLDRDEFAVAMFLVYCALEKE 199
Cdd:smart00027   1 PWAISPEDKAKYEQIFRSLDKnQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGY 80
                           90
                   ....*....|....*.
gi 1958776456  200 PVPMSLPPALVPPSKR 215
Cdd:smart00027  81 PIPASLPPSLIPPSKR 96
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
253-349 6.92e-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: 144.73  E-value: 6.92e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  253 QWVVSPAEKAKYDEIFLKTDKDMDGYVSGLEVRETFLKTGLPSTLLAHIWALCDTKNCGKLSKDQFALAFHLINQKLIkG 332
Cdd:smart00027   1 PWAISPEDKAKYEQIFRSLDKNQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLN-G 79
                           90
                   ....*....|....*..
gi 1958776456  333 IDPPHSLTPEMIPPSDK 349
Cdd:smart00027  80 YPIPASLPPSLIPPSKR 96
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
264-329 5.82e-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: 101.53  E-value: 5.82e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958776456 264 YDEIFLKTDKDMDGYVSGLEVRETFLKTGLPSTLLAHIWALCDTKNCGKLSKDQFALAFHLINQKL 329
Cdd:cd00052     1 YDQIFRSLDPDGDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALAL 66
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
13-103 7.55e-26

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: 101.97  E-value: 7.55e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456   13 SSGNPVYEKYYRQVEAGNTGRVLALDAAAFLKKSGLPDLILGKIWDLADTDGKGVLNKQEFFIALRLVACAQNGLEVSLS 92
Cdd:smart00027   6 PEDKAKYEQIFRSLDKNQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGYPIPAS 85
                           90
                   ....*....|.
gi 1958776456   93 SLNLAVPPPRF 103
Cdd:smart00027  86 LPPSLIPPSKR 96
EF-hand_4 pfam12763
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ...
121-218 1.93e-25

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: 101.30  E-value: 1.93e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 121 PWAVKsedkaKYDAIFDSLSPVDGFLSGDKVKPVLLNSKLPVEILGRVWELSDIDHDGKLDRDEFAVAMFLVYCALEKE- 199
Cdd:pfam12763   6 EWEIK-----KYWEIFSGLKPENNKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLIFDLVNGNi 80
                          90       100
                  ....*....|....*....|
gi 1958776456 200 -PVPMSLPPALVPPSKRKTV 218
Cdd:pfam12763  81 aDVPDELPDWLVPGSKAHLI 100
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
132-197 5.73e-25

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


Pssm-ID: 238009 [Multi-domain]  Cd Length: 67  Bit Score: 98.45  E-value: 5.73e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958776456 132 YDAIFDSLSPV-DGFLSGDKVKPVLLNSKLPVEILGRVWELSDIDHDGKLDRDEFAVAMFLVYCALE 197
Cdd:cd00052     1 YDQIFRSLDPDgDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
19-85 9.20e-23

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: 92.28  E-value: 9.20e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958776456  19 YEKYYRQVEAGNTGRVLALDAAAFLKKSGLPDLILGKIWDLADTDGKGVLNKQEFFIALRLVACAQN 85
Cdd:cd00052     1 YDQIFRSLDPDGDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
366-529 1.22e-15

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 79.56  E-value: 1.22e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 366 SAIKELDTLNNEIIDLQREKNNVEQDLKEKEDTVRQRTTEAQDLQDEVQRESLNLQKLQAQKQQVQELLDELDEQKAQLE 445
Cdd:COG4372    35 KALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQ 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 446 EQLKEVRKKCAEEAQLISSLKAEITSQESQISTYEEELSKAREELSRLQQETAQLEESVESGKAQL--EPLQQHLQDSQQ 523
Cdd:COG4372   115 EELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEaeQALDELLKEANR 194

                  ....*.
gi 1958776456 524 EISSMQ 529
Cdd:COG4372   195 NAEKEE 200
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
366-539 1.08e-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: 78.56  E-value: 1.08e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  366 SAIKELDTLNNEII-------DLQREKNNVEQDLKEKEDTVRQRTTEAQDLQDEVQ----------------RESLNLQK 422
Cdd:TIGR02168  236 ELREELEELQEELKeaeeeleELTAELQELEEKLEELRLEVSELEEEIEELQKELYalaneisrleqqkqilRERLANLE 315
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  423 LQAQKQQVQEL-----LDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAEITSQESQISTYEEELSKAREELSRLQQET 497
Cdd:TIGR02168  316 RQLEELEAQLEeleskLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQI 395
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1958776456  498 AQLEESVESGKAQLEPLQQHLQDSQQEISSMQMRLAMKDLET 539
Cdd:TIGR02168  396 ASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKE 437
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
370-540 4.44e-09

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 60.05  E-value: 4.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 370 ELDTLNNEIIDLQ-------REKNNVEQDLKEKEDTVRQRTTEAQDLQDEVQRESLNLQKLQaqkqqvqELLDELDEQKA 442
Cdd:PRK02224  252 ELETLEAEIEDLRetiaeteREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVE-------ARREELEDRDE 324
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 443 QLEEQLKEVRKKCAEEAQLISSLKAEITSQES-------QISTYEEELSKAREELSRLQQETAQLEESVESGKA------ 509
Cdd:PRK02224  325 ELRDRLEECRVAAQAHNEEAESLREDADDLEEraeelreEAAELESELEEAREAVEDRREEIEELEEEIEELRErfgdap 404
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1958776456 510 -QLEPLQQHLQDSQQEISSMQMRLAmkDLETD 540
Cdd:PRK02224  405 vDLGNAEDFLEELREERDELREREA--ELEAT 434
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
439-542 5.16e-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: 54.95  E-value: 5.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 439 EQKAQLEEQLKEVRKKCAEEAQLISSLKAEITSQeSQIST-----YEEE----------LSKAREELSRLQQETAQLEES 503
Cdd:pfam07926   1 AELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQ-AEIAReaqqnYERElvlhaedikaLQALREELNELKAEIAELKAE 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1958776456 504 VESGKAQLEPLQQHLQDS----QQEISSMQMRLamKDLETDNN 542
Cdd:pfam07926  80 AESAKAELEESEESWEEQkkelEKELSELEKRI--EDLNEQNK 120
EF-hand_4 pfam12763
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ...
39-80 1.18e-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: 50.45  E-value: 1.18e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1958776456  39 AAAFLKKSGLPDLILGKIWDLADTDGKGVLNKQEFFIALRLV 80
Cdd:pfam12763  31 VSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLI 72
EF-hand_4 pfam12763
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ...
251-355 3.05e-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: 46.60  E-value: 3.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 251 LRQWvvspaEKAKYDEIFlKTDKDMDGYVSGLEVRETFLKTGLPSTLLAHIWALCDTKNCGKLSKDQFALA----FHLIN 326
Cdd:pfam12763   4 LEEW-----EIKKYWEIF-SGLKPENNKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAmrliFDLVN 77
                          90       100
                  ....*....|....*....|....*....
gi 1958776456 327 QKLikgIDPPHSLTPEMIPPSDKSSLQKN 355
Cdd:pfam12763  78 GNI---ADVPDELPDWLVPGSKAHLIQAN 103
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
471-543 4.31e-05

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: 42.94  E-value: 4.31e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958776456 471 SQESQISTYEEELSKAREELSRLQQETAQLEESVEsgkaQLEPLQQHLQDsqqEISSMQMRLAM-----KDLETDNNQ 543
Cdd:cd22887     1 ELESELQELEKRLAELEAELASLEEEIKDLEEELK----EKNKANEILND---ELIALQIENNLleeklRKLQEENDE 71
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
53-189 6.04e-05

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 43.63  E-value: 6.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  53 LGKIWDLADTDGKGVLNKQEFfIALRLVACAQnglevslsslnLAVPPPRFHDSSsplLTSGTSVAELPWAVKSEDKAKY 132
Cdd:COG5126     7 LDRRFDLLDADGDGVLERDDF-EALFRRLWAT-----------LFSEADTDGDGR---ISREEFVAGMESLFEATVEPFA 71
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958776456 133 DAIFDSLSP-VDGFLSGDKVKPVLLNSKLPVEILGRVWELSDIDHDGKLDRDEFAVAM 189
Cdd:COG5126    72 RAAFDLLDTdGDGKISADEFRRLLTALGVSEEEADELFARLDTDGDGKISFEEFVAAV 129
growth_prot_Scy NF041483
polarized growth protein Scy;
393-516 2.84e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 41.35  E-value: 2.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  393 KEKEDTVRQRTTEAQDLQDEVQRESlnlqklqaqkqqvQELLDELDEQKAQL-EEQLKEVRKKCAEEAQLISSLKAEits 471
Cdd:NF041483   520 RQAEETLERTRAEAERLRAEAEEQA-------------EEVRAAAERAARELrEETERAIAARQAEAAEELTRLHTE--- 583
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1958776456  472 QESQISTYEEELSKAREELSRLQQETAQLEESVESGKAQ-LEPLQQ 516
Cdd:NF041483   584 AEERLTAAEEALADARAEAERIRREAAEETERLRTEAAErIRTLQA 629
growth_prot_Scy NF041483
polarized growth protein Scy;
392-529 2.94e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 41.35  E-value: 2.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  392 LKEKEDTVRQRTT-EAQDLQDEVQRESlnlqklQAQKQQVQELLDEL----DEQKAQLEEQLKEVRKKCAEEAqliSSLK 466
Cdd:NF041483  1119 IRERAEELRDRITgEIEELHERARRES------AEQMKSAGERCDALvkaaEEQLAEAEAKAKELVSDANSEA---SKVR 1189
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958776456  467 -AEITSQESQISTYEEELSKAREELSRLQQET-AQLEESVESGKAQLEPLQQHLQDSQQEISSMQ 529
Cdd:NF041483  1190 iAAVKKAEGLLKEAEQKKAELVREAEKIKAEAeAEAKRTVEEGKRELDVLVRRREDINAEISRVQ 1254
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
432-523 7.26e-03

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: 39.23  E-value: 7.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  432 ELLDELDEQKAQLEEQLKEVRKKCAEEAQlisSLKAEITSQESQIstyEEELSKareeLSRLQQETAQLEESVESGKAQL 511
Cdd:smart00787 179 DRKDALEEELRQLKQLEDELEDCDPTELD---RAKEKLKKLLQEI---MIKVKK----LEELEEELQELESKIEDLTNKK 248
                           90
                   ....*....|..
gi 1958776456  512 EPLQQHLQDSQQ 523
Cdd:smart00787 249 SELNTEIAEAEK 260
 
Name Accession Description Interval E-value
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
121-215 4.45e-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: 151.28  E-value: 4.45e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  121 PWAVKSEDKAKYDAIFDSLSP-VDGFLSGDKVKPVLLNSKLPVEILGRVWELSDIDHDGKLDRDEFAVAMFLVYCALEKE 199
Cdd:smart00027   1 PWAISPEDKAKYEQIFRSLDKnQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGY 80
                           90
                   ....*....|....*.
gi 1958776456  200 PVPMSLPPALVPPSKR 215
Cdd:smart00027  81 PIPASLPPSLIPPSKR 96
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
253-349 6.92e-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: 144.73  E-value: 6.92e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  253 QWVVSPAEKAKYDEIFLKTDKDMDGYVSGLEVRETFLKTGLPSTLLAHIWALCDTKNCGKLSKDQFALAFHLINQKLIkG 332
Cdd:smart00027   1 PWAISPEDKAKYEQIFRSLDKNQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLN-G 79
                           90
                   ....*....|....*..
gi 1958776456  333 IDPPHSLTPEMIPPSDK 349
Cdd:smart00027  80 YPIPASLPPSLIPPSKR 96
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
264-329 5.82e-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: 101.53  E-value: 5.82e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958776456 264 YDEIFLKTDKDMDGYVSGLEVRETFLKTGLPSTLLAHIWALCDTKNCGKLSKDQFALAFHLINQKL 329
Cdd:cd00052     1 YDQIFRSLDPDGDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALAL 66
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
13-103 7.55e-26

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: 101.97  E-value: 7.55e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456   13 SSGNPVYEKYYRQVEAGNTGRVLALDAAAFLKKSGLPDLILGKIWDLADTDGKGVLNKQEFFIALRLVACAQNGLEVSLS 92
Cdd:smart00027   6 PEDKAKYEQIFRSLDKNQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGYPIPAS 85
                           90
                   ....*....|.
gi 1958776456   93 SLNLAVPPPRF 103
Cdd:smart00027  86 LPPSLIPPSKR 96
EF-hand_4 pfam12763
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ...
121-218 1.93e-25

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: 101.30  E-value: 1.93e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 121 PWAVKsedkaKYDAIFDSLSPVDGFLSGDKVKPVLLNSKLPVEILGRVWELSDIDHDGKLDRDEFAVAMFLVYCALEKE- 199
Cdd:pfam12763   6 EWEIK-----KYWEIFSGLKPENNKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLIFDLVNGNi 80
                          90       100
                  ....*....|....*....|
gi 1958776456 200 -PVPMSLPPALVPPSKRKTV 218
Cdd:pfam12763  81 aDVPDELPDWLVPGSKAHLI 100
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
132-197 5.73e-25

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


Pssm-ID: 238009 [Multi-domain]  Cd Length: 67  Bit Score: 98.45  E-value: 5.73e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958776456 132 YDAIFDSLSPV-DGFLSGDKVKPVLLNSKLPVEILGRVWELSDIDHDGKLDRDEFAVAMFLVYCALE 197
Cdd:cd00052     1 YDQIFRSLDPDgDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
19-85 9.20e-23

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: 92.28  E-value: 9.20e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958776456  19 YEKYYRQVEAGNTGRVLALDAAAFLKKSGLPDLILGKIWDLADTDGKGVLNKQEFFIALRLVACAQN 85
Cdd:cd00052     1 YDQIFRSLDPDGDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
366-529 1.22e-15

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 79.56  E-value: 1.22e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 366 SAIKELDTLNNEIIDLQREKNNVEQDLKEKEDTVRQRTTEAQDLQDEVQRESLNLQKLQAQKQQVQELLDELDEQKAQLE 445
Cdd:COG4372    35 KALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQ 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 446 EQLKEVRKKCAEEAQLISSLKAEITSQESQISTYEEELSKAREELSRLQQETAQLEESVESGKAQL--EPLQQHLQDSQQ 523
Cdd:COG4372   115 EELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEaeQALDELLKEANR 194

                  ....*.
gi 1958776456 524 EISSMQ 529
Cdd:COG4372   195 NAEKEE 200
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
369-525 6.31e-15

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: 74.96  E-value: 6.31e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 369 KELDTLNNEIIDLQREKNNVEQDLKEKEDTVRQRTTEAQDLQDEVQRESLNlqklqaqkqqvqelLDELDEQKAQLEEQL 448
Cdd:COG1579    17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELE--------------IEEVEARIKKYEEQL 82
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958776456 449 KEVRKkcAEEAQlisSLKAEITSQESQISTYEEELSKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQDSQQEI 525
Cdd:COG1579    83 GNVRN--NKEYE---ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAEL 154
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
366-539 1.08e-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: 78.56  E-value: 1.08e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  366 SAIKELDTLNNEII-------DLQREKNNVEQDLKEKEDTVRQRTTEAQDLQDEVQ----------------RESLNLQK 422
Cdd:TIGR02168  236 ELREELEELQEELKeaeeeleELTAELQELEEKLEELRLEVSELEEEIEELQKELYalaneisrleqqkqilRERLANLE 315
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  423 LQAQKQQVQEL-----LDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAEITSQESQISTYEEELSKAREELSRLQQET 497
Cdd:TIGR02168  316 RQLEELEAQLEeleskLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQI 395
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1958776456  498 AQLEESVESGKAQLEPLQQHLQDSQQEISSMQMRLAMKDLET 539
Cdd:TIGR02168  396 ASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKE 437
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
369-545 1.39e-13

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 75.09  E-value: 1.39e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  369 KELDTLNNEIIDLQREKNNVEQDLKEKEDTVRQRTTEAQDLQDEVQRESLNLQKLQaqkqqvqELLDELDEQKAQLEEQL 448
Cdd:TIGR02168  705 KELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE-------AEIEELEERLEEAEEEL 777
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  449 KEVRKKcaeeaqlISSLKAEITSQESQISTYEEELSKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQDSQQEISSM 528
Cdd:TIGR02168  778 AEAEAE-------IEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEEL 850
                          170       180
                   ....*....|....*....|..
gi 1958776456  529 Q-----MRLAMKDLETDNNQSN 545
Cdd:TIGR02168  851 SediesLAAEIEELEELIEELE 872
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
369-533 2.35e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 74.20  E-value: 2.35e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 369 KELDTLNNEIIDLQREKNNVEQDLKEKEDTVRQRTTEAQDLQDEVQRESLNLQKLQAQKQQVQELLDELDEQKAQLEEQL 448
Cdd:COG1196   246 AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEEL 325
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 449 KEVRKKCAEEAQLISSLKAEITSQESQISTYEEELSKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQDSQQEISSM 528
Cdd:COG1196   326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL 405

                  ....*
gi 1958776456 529 QMRLA 533
Cdd:COG1196   406 EEAEE 410
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
360-531 9.59e-13

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 72.26  E-value: 9.59e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  360 SPVADFSAIKELDTLNNEIIDLQREKnnveQDLKEKEDTVRQRTTEAQDLQDEVQRESLNLQKlqaqkqqvqELLDELDE 439
Cdd:COG4913    279 AALRLWFAQRRLELLEAELEELRAEL----ARLEAELERLEARLDALREELDELEAQIRGNGG---------DRLEQLER 345
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  440 QKAQLEEQLKEVRKKCAEEAQLISSLKAEITSQESQistYEEELSKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQ 519
Cdd:COG4913    346 EIERLERELEERERRRARLEALLAALGLPLPASAEE---FAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELR 422
                          170
                   ....*....|..
gi 1958776456  520 DSQQEISSMQMR 531
Cdd:COG4913    423 ELEAEIASLERR 434
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
368-538 2.90e-12

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 70.18  E-value: 2.90e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 368 IKELDTLNNEIIDLQREKNNVEQDLKEKEDTvRQRTTEAQDLQDEVQREsLNLQKLQAQKQQVQELLDELDEQKAQLEEQ 447
Cdd:COG4717    70 LKELKELEEELKEAEEKEEEYAELQEELEEL-EEELEELEAELEELREE-LEKLEKLLQLLPLYQELEALEAELAELPER 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 448 LKEVRKKCAEEAQL---ISSLKAEITSQESQISTYEEELS-KAREELSRLQQETAQLEESVESGKAQLEPLQQHLQDSQQ 523
Cdd:COG4717   148 LEELEERLEELRELeeeLEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
                         170
                  ....*....|....*
gi 1958776456 524 EISSMQMRLAMKDLE 538
Cdd:COG4717   228 ELEQLENELEAAALE 242
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
365-533 5.00e-12

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 70.09  E-value: 5.00e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  365 FSAIKELDTLNNEIIDLQREKNNVEQDLKEKEDTVRQRTTEAQDLQDEVQRESLNLQKLQAQKQQVQELLDELDEQKAQL 444
Cdd:TIGR02168  291 YALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL 370
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  445 EEQLKEVRKKCAEEAQLISSLKAEITSQESQISTYEEELSKAREELSRLQQETAQLEESVESgkAQLEPLQQHLQDSQQE 524
Cdd:TIGR02168  371 ESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE--AELKELQAELEELEEE 448

                   ....*....
gi 1958776456  525 ISSMQMRLA 533
Cdd:TIGR02168  449 LEELQEELE 457
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
369-527 1.01e-11

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: 68.51  E-value: 1.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 369 KELDTLNNEIIDLQREKNNVEQDLKEKEDTVRQRTTEAQDLQDEVQRESLNLQKLQAQKQQVQELLDELDEQKAQLEEQL 448
Cdd:TIGR04523 335 KIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQI 414
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958776456 449 KEVRKKCAEEAQLISSLKAEITSQESQISTYEEELSKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQDSQQEISS 527
Cdd:TIGR04523 415 KKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKS 493
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
367-533 1.17e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 68.81  E-value: 1.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 367 AIKELDTLNNEIIDLQREKNNVEQDLKEKEDTVRQRTTEAQDLQDEVQRESLnlqklqaQKQQVQELLDELDEQKAQLEE 446
Cdd:COG1196   230 LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELEL-------ELEEAQAEEYELLAELARLEQ 302
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 447 QLKEVRKKCAEEAQLISSLKAEITSQESQISTYEEELSKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQDSQQEIS 526
Cdd:COG1196   303 DIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382

                  ....*..
gi 1958776456 527 SMQMRLA 533
Cdd:COG1196   383 ELAEELL 389
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
369-533 1.64e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 68.04  E-value: 1.64e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 369 KELDTLNNEIIDLQREKNNVEQDLKEKEDTVRQRTTEAQDLQDEVQRESLNLQKLQAQKQQVQELLDELDEQKAQLEEQL 448
Cdd:COG1196   239 AELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERL 318
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 449 KEVRKKCAEEAQLISSLKAEITSQESQISTYEEELSKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQDSQQEISSM 528
Cdd:COG1196   319 EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL 398

                  ....*
gi 1958776456 529 QMRLA 533
Cdd:COG1196   399 AAQLE 403
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
367-510 1.80e-11

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 67.87  E-value: 1.80e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 367 AIKELDTLNNEIIDLQREKNNVEQDLKEKEDTVRQRTTEAQDLQDEVQRESLnlQKLQAQKQQVQELLDELDEQKAQLEE 446
Cdd:COG4717    93 LQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAEL--PERLEELEERLEELRELEEELEELEA 170
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958776456 447 QLKEVRKKCAEEAQL--------ISSLKAEITSQESQISTYEEELSKAREELSRLQQETAQLEESVESGKAQ 510
Cdd:COG4717   171 ELAELQEELEELLEQlslateeeLQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
367-533 1.90e-11

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: 68.16  E-value: 1.90e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  367 AIKELDTLNNEIIDLQREKNNVEQDLKEKEDtvrqrttEAQDLQDEVQRESLNLQKLQAQKQQVQELLDELDEQKAQLEE 446
Cdd:TIGR02168  780 AEAEIEELEAQIEQLKEELKALREALDELRA-------ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSE 852
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  447 QLKEVRKKCAEEAQLISSLKAEITSQESQISTYEEELSKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQDSQQEIS 526
Cdd:TIGR02168  853 DIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLE 932

                   ....*..
gi 1958776456  527 SMQMRLA 533
Cdd:TIGR02168  933 GLEVRID 939
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
396-545 3.51e-11

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 65.69  E-value: 3.51e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 396 EDTVRQRTTEAQDLQDEVQ--RESLNlqklqaqkqqvqELLDELDEQKAQLEE---QLKEVRKKCAEEAQLISSLKAEIT 470
Cdd:COG4372    30 SEQLRKALFELDKLQEELEqlREELE------------QAREELEQLEEELEQarsELEQLEEELEELNEQLQAAQAELA 97
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958776456 471 SQESQISTYEEELSKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQDSQQEISSMQMRLAMKDLETDNNQSN 545
Cdd:COG4372    98 QAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQE 172
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
369-535 1.52e-10

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 65.08  E-value: 1.52e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  369 KELDTLNNEIIDLQREKNNVEQDLKEKEDTVRQRTTEAQDLQDEvqreslnlqklqaqkqqvqelLDELDEQKAQLEEQL 448
Cdd:TIGR02168  677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKE---------------------LEELSRQISALRKDL 735
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  449 KEVRKKCAEEAQLISSLKAEITSQESQISTYEEELSKAREELS--------------RLQQETAQLEESVESGKAQLEPL 514
Cdd:TIGR02168  736 ARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAeaeaeieeleaqieQLKEELKALREALDELRAELTLL 815
                          170       180
                   ....*....|....*....|.
gi 1958776456  515 QQHLQDSQQEISSMQMRLAMK 535
Cdd:TIGR02168  816 NEEAANLRERLESLERRIAAT 836
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
370-533 1.65e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 64.96  E-value: 1.65e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 370 ELDTLNNEIIDLQREKNNVEQDLKEKEDTVRQRTTEAQDLQDEVQRESLNLQKLQaqkqqvqELLDELDEQKAQLEEQLK 449
Cdd:COG1196   275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELE-------EELEELEEELEELEEELE 347
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 450 EVRKKCAEEAQLISSLKAEITSQESQISTYEEELSKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQDSQQEISSMQ 529
Cdd:COG1196   348 EAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE 427

                  ....
gi 1958776456 530 MRLA 533
Cdd:COG1196   428 EALA 431
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
369-527 2.03e-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: 63.63  E-value: 2.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 369 KELDTLNNEIIDLQREKNNVEQDLKEKEDTVRQRTTEAQDL-----------QDEVQRESLNLQKLQAQKQQVQELLDEL 437
Cdd:COG4942    76 QELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLgrqpplalllsPEDFLDAVRRLQYLKYLAPARREQAEEL 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 438 DEQKAQLEEQLKEVRKKCAEEAQLISSLKAEITSQESQISTYEEELSKAREELSRLQQETAQLEESVESGKAQLEPLQQH 517
Cdd:COG4942   156 RADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
                         170
                  ....*....|
gi 1958776456 518 LQDSQQEISS 527
Cdd:COG4942   236 AAAAAERTPA 245
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
369-505 2.05e-10

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: 61.86  E-value: 2.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 369 KELDTLNNEIIDLQREKNNVEQDLKEkedtVRQRTTEAQDLQDEV--QRESLNlqklqaqkqqvqeLLDELDEQK---AQ 443
Cdd:COG1579    45 ARLEAAKTELEDLEKEIKRLELEIEE----VEARIKKYEEQLGNVrnNKEYEA-------------LQKEIESLKrriSD 107
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958776456 444 LEEQLKEVRKKCAEEAQLISSLKAEITSQESQIST----YEEELSKAREELSRLQQETAQLEESVE 505
Cdd:COG1579   108 LEDEILELMERIEELEEELAELEAELAELEAELEEkkaeLDEELAELEAELEELEAEREELAAKIP 173
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
374-536 2.20e-10

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 64.27  E-value: 2.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 374 LNNEIIDLQREKNNVEQDLKEKEDTVRQRTTEAQDLQDEVQRESLNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRK 453
Cdd:TIGR04523 438 NNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTK 517
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 454 KCAEEAQLISSLKAEITSQESQISTYEEELSKAREELSR---------LQQETAQLEESVESGKAQLEPLQQHLQDSQQE 524
Cdd:TIGR04523 518 KISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKenlekeideKNKEIEELKQTQKSLKKKQEEKQELIDQKEKE 597
                         170
                  ....*....|..
gi 1958776456 525 ISSMQMRLAMKD 536
Cdd:TIGR04523 598 KKDLIKEIEEKE 609
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
369-543 2.46e-10

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 64.32  E-value: 2.46e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  369 KELDTLNNEIIDLQR---EKNNVEQDLKEKEDTVRQRTTEAQDLQDEVQRESLNLQKLqaqkqqvqelLDELDEQKAQLE 445
Cdd:TIGR02169  702 NRLDELSQELSDASRkigEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSE----------LKELEARIEELE 771
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  446 EQLKEVRKKCAE-EAQL----ISSLKAEITSQESQISTYEEELSKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQD 520
Cdd:TIGR02169  772 EDLHKLEEALNDlEARLshsrIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKS 851
                          170       180
                   ....*....|....*....|...
gi 1958776456  521 SQQEISSMQMRLAMKDLETDNNQ 543
Cdd:TIGR02169  852 IEKEIENLNGKKEELEEELEELE 874
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
439-528 3.71e-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: 62.47  E-value: 3.71e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 439 EQKAQLEEQLKEVRKKCAEEAQLISSLKAEITSQESQISTYEEELSKAREELSRLQQETAQLEESVESGKAQLEPLQQHL 518
Cdd:COG4942    20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
                          90
                  ....*....|
gi 1958776456 519 QDSQQEISSM 528
Cdd:COG4942   100 EAQKEELAEL 109
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
366-546 8.01e-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: 8.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 366 SAIKELDTLNNEIIDLQREKNNVEQDLKEKEDTVRQRTTEAQDLQD--EVQRESL-----------------------NL 420
Cdd:COG4942    52 ALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAelEAQKEELaellralyrlgrqpplalllspeDF 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 421 QKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAEITSQESQISTYEEELSKAREELSRLQQETAQL 500
Cdd:COG4942   132 LDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAEL 211
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1958776456 501 EESVESGKAQLEPLQQHLQDSQQEISSMQMRLAMKDLETDNNQSNW 546
Cdd:COG4942   212 AAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKLPW 257
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
366-533 8.19e-10

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 62.63  E-value: 8.19e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  366 SAIKELDTLNN--EIIDLQREKNNVEQDLKEKEDTVRQRTTEAQDLQDEvqRESLNLQKLQAQKQQVQELLDELDEQKAQ 443
Cdd:COG4913    229 ALVEHFDDLERahEALEDAREQIELLEPIRELAERYAAARERLAELEYL--RAALRLWFAQRRLELLEAELEELRAELAR 306
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  444 LEEQLKEVRKKCAEEAQLISSLKAEITSQ--------ESQISTYEEELSKAREELSRLQQETAQLEESVESGKAQLEPLQ 515
Cdd:COG4913    307 LEAELERLEARLDALREELDELEAQIRGNggdrleqlEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALR 386
                          170
                   ....*....|....*...
gi 1958776456  516 QHLQDSQQEISSMQMRLA 533
Cdd:COG4913    387 AEAAALLEALEEELEALE 404
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
367-529 8.21e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 62.65  E-value: 8.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 367 AIKELDTLNNEIIDLQREKNNVEQDLKEKEDTVRQRTTEAQDLQDEVQRESLNLQKLQAQKQQVQELLDELDEQKAQLEE 446
Cdd:COG1196   342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 447 QLKEVRKKCAEEAQLISSLKAEITSQESQISTYEEELSKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQDSQQEIS 526
Cdd:COG1196   422 ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501

                  ...
gi 1958776456 527 SMQ 529
Cdd:COG1196   502 DYE 504
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
369-545 1.45e-09

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 61.57  E-value: 1.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 369 KELDTLNNEIIDLQREKNNVEQDLKEKEDTVRQRTTEAQDLQDEVQResLNLQKLQAQKQQVQELLDELDEQKAQLEEQL 448
Cdd:TIGR04523 246 TEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQ--LKSEISDLNNQKEQDWNKELKSELKNQEKKL 323
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 449 KEVRKKCAEEAQLISSLKAEITSQESQISTYEEELSKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQDSQQEISSM 528
Cdd:TIGR04523 324 EEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQ 403
                         170
                  ....*....|....*..
gi 1958776456 529 QMRLAMKDLETDNNQSN 545
Cdd:TIGR04523 404 EKLNQQKDEQIKKLQQE 420
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
369-529 1.56e-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: 60.55  E-value: 1.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 369 KELDTLNNEIIDLQREKNNVEQDLKEKEDTVRQRTTEAQDLQDEVQReslnlqklqaqkqqVQELLDELDEQKAQLEEQL 448
Cdd:COG4942    34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA--------------LEAELAELEKEIAELRAEL 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 449 KEVRKKCAE---EAQLISS-------LKAEITSQESQISTYEEELSKAR----EELSRLQQETAQLEESVESGKAQLEPL 514
Cdd:COG4942   100 EAQKEELAEllrALYRLGRqpplallLSPEDFLDAVRRLQYLKYLAPARreqaEELRADLAELAALRAELEAERAELEAL 179
                         170
                  ....*....|....*
gi 1958776456 515 QQHLQDSQQEISSMQ 529
Cdd:COG4942   180 LAELEEERAALEALK 194
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
368-525 3.00e-09

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 60.80  E-value: 3.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 368 IKELDTLNNEIIDLQREKNNVEQDLKEKEDTVRQRTTEAQDLQDEVQRESLNLQKLQAQKQQVQELLDELDEQKAQLEEQ 447
Cdd:TIGR04523 210 IQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQ 289
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 448 LKEVRKKCAE-----EAQLISSLKAEITSQESQISTYEEELSKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQDSQ 522
Cdd:TIGR04523 290 LNQLKSEISDlnnqkEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQ 369

                  ...
gi 1958776456 523 QEI 525
Cdd:TIGR04523 370 NEI 372
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
434-523 3.07e-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: 59.78  E-value: 3.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 434 LDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAEITSQESQISTYEEELSKAREELSRLQQETAQLEESVESGKAQLEP 513
Cdd:COG4942    29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE 108
                          90
                  ....*....|
gi 1958776456 514 LQQHLQDSQQ 523
Cdd:COG4942   109 LLRALYRLGR 118
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
370-540 4.44e-09

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 60.05  E-value: 4.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 370 ELDTLNNEIIDLQ-------REKNNVEQDLKEKEDTVRQRTTEAQDLQDEVQRESLNLQKLQaqkqqvqELLDELDEQKA 442
Cdd:PRK02224  252 ELETLEAEIEDLRetiaeteREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVE-------ARREELEDRDE 324
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 443 QLEEQLKEVRKKCAEEAQLISSLKAEITSQES-------QISTYEEELSKAREELSRLQQETAQLEESVESGKA------ 509
Cdd:PRK02224  325 ELRDRLEECRVAAQAHNEEAESLREDADDLEEraeelreEAAELESELEEAREAVEDRREEIEELEEEIEELRErfgdap 404
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1958776456 510 -QLEPLQQHLQDSQQEISSMQMRLAmkDLETD 540
Cdd:PRK02224  405 vDLGNAEDFLEELREERDELREREA--ELEAT 434
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
439-542 5.16e-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: 54.95  E-value: 5.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 439 EQKAQLEEQLKEVRKKCAEEAQLISSLKAEITSQeSQIST-----YEEE----------LSKAREELSRLQQETAQLEES 503
Cdd:pfam07926   1 AELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQ-AEIAReaqqnYERElvlhaedikaLQALREELNELKAEIAELKAE 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1958776456 504 VESGKAQLEPLQQHLQDS----QQEISSMQMRLamKDLETDNN 542
Cdd:pfam07926  80 AESAKAELEESEESWEEQkkelEKELSELEKRI--EDLNEQNK 120
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
432-543 5.58e-09

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 58.76  E-value: 5.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 432 ELLDELDEQKAQLEEQLKEVRKKcaeeaqlISSLKAEITSQESQISTYEEELSKAREELSRLQQETAQLEESVESGKAQL 511
Cdd:COG4372    24 ILIAALSEQLRKALFELDKLQEE-------LEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAEL 96
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1958776456 512 EPLQQHLQDSQQEISSMQMRLA-----MKDLETDNNQ 543
Cdd:COG4372    97 AQAQEELESLQEEAEELQEELEelqkeRQDLEQQRKQ 133
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
369-519 5.79e-09

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: 60.08  E-value: 5.79e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  369 KELDTLNNEIIDLQREKNNVEQDLKEKE---DTVRQRTTEAQDLQDEVQRESLNLQKLQAQKQQVQELLDE--------- 436
Cdd:TIGR02169  350 KRRDKLTEEYAELKEELEDLRAELEEVDkefAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEeladlnaai 429
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  437 --LDEQKAQLEEQLKEVRKKCAEEAQLISSLKAEITSQESQISTYEEELSKAREELSRLQQETAQLE-------ESVESG 507
Cdd:TIGR02169  430 agIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEaqaraseERVRGG 509
                          170
                   ....*....|..
gi 1958776456  508 KAQLEPLQQHLQ 519
Cdd:TIGR02169  510 RAVEEVLKASIQ 521
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
370-542 6.92e-09

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: 59.70  E-value: 6.92e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  370 ELDTLNNEIIDLQREKNNVEQDLKEKEDTVRQRTTEAQDLQDEVQRESLNLQKLQAQKQQVQELLDELDEQKAQLEEQLK 449
Cdd:TIGR02169  675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIE 754
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  450 EVRKKCAEeaqlissLKAEITSQESQISTYEEELSK-----AREELSRLQQETAQLEESVESGKAQLEPLQQHLQDSQQE 524
Cdd:TIGR02169  755 NVKSELKE-------LEARIEELEEDLHKLEEALNDlearlSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLE 827
                          170
                   ....*....|....*...
gi 1958776456  525 ISSMQMrlAMKDLETDNN 542
Cdd:TIGR02169  828 KEYLEK--EIQELQEQRI 843
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
365-537 1.01e-08

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 59.01  E-value: 1.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 365 FSAIKELDTLNNEI------IDLQREKNNVEQDLK----EKEDTVRQRTTEAQDLQdevqreslnlqklqaqkqqvqELL 434
Cdd:COG4717   343 LDRIEELQELLREAeeleeeLQLEELEQEIAALLAeagvEDEEELRAALEQAEEYQ---------------------ELK 401
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 435 DELDEQKAQLEEQLKEVRKkcAEEAQLISSLKAEITSQESQISTYEEELSKAREELSRLQQETAQLEESVEsgkaqLEPL 514
Cdd:COG4717   402 EELEELEEQLEELLGELEE--LLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGE-----LAEL 474
                         170       180
                  ....*....|....*....|...
gi 1958776456 515 QQHLQDSQQEISSMQMRLAMKDL 537
Cdd:COG4717   475 LQELEELKAELRELAEEWAALKL 497
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
377-546 1.06e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.18  E-value: 1.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 377 EIIDLQREKNNVEQDLKEKEDTVRQRTTEAQDLQDEvqreslnlqklqaqkqqvqelLDELDEQKAQLEEQLKEVRKKCA 456
Cdd:COG1196   233 KLRELEAELEELEAELEELEAELEELEAELAELEAE---------------------LEELRLELEELELELEEAQAEEY 291
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 457 EEAQLISSLKAEITSQESQISTYEEELSKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQDSQQEISSMQMRLAMKD 536
Cdd:COG1196   292 ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
                         170
                  ....*....|
gi 1958776456 537 LETDNNQSNW 546
Cdd:COG1196   372 AELAEAEEEL 381
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
369-545 1.41e-08

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: 58.53  E-value: 1.41e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  369 KELDTLNNEIIDLQREKNNVEQDLKEKEDTVRQRTTEAQDLQDEVQRESLNLQKLQAQKQQVQELLDELDEQKAQLEEQL 448
Cdd:TIGR02168  754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  449 KEVRKKCAEEAQLISSLKAEITSQESQISTYEEELSKAREELSRLQQETAQLEESVESGKAQLE--------------PL 514
Cdd:TIGR02168  834 AATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEelseelreleskrsEL 913
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1958776456  515 QQHLQDSQQEISSMQMRLAMKDLETDNNQSN 545
Cdd:TIGR02168  914 RRELEELREKLAQLELRLEGLEVRIDNLQER 944
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
369-545 1.61e-08

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: 58.53  E-value: 1.61e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  369 KELDTLNNEIIDLQREKNNVEQDLKEKEDTVRQRTTEAQDLQDEV-----QRESLNLQKLQAQK---------------- 427
Cdd:TIGR02168  712 EELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELteleaEIEELEERLEEAEEelaeaeaeieeleaqi 791
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  428 QQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAEITSQESQISTYEEELSKAREELSRLQQETAQLEESVESG 507
Cdd:TIGR02168  792 EQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL 871
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1958776456  508 KAQLEPLQQHLQDSQQEIssMQMRLAMKDLETDNNQSN 545
Cdd:TIGR02168  872 ESELEALLNERASLEEAL--ALLRSELEELSEELRELE 907
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
366-538 2.10e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 58.15  E-value: 2.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 366 SAIKELDTLNNEIIDLQREKNNVEQDLKEKEDTVRQRTTEA-QDLQDEVQRESLNLQKLQAQKQQVQELLDELDEQKaQL 444
Cdd:PRK03918  546 KELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESvEELEERLKELEPFYNEYLELKDAEKELEREEKELK-KL 624
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 445 EEQLKEVRKKCAEEAQLISSLKAEITSQESQIS--TYE---EELSKAREELSRLQQETAQLEESVESGKAQLEPLQQHLq 519
Cdd:PRK03918  625 EEELDKAFEELAETEKRLEELRKELEELEKKYSeeEYEelrEEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEEL- 703
                         170       180
                  ....*....|....*....|....
gi 1958776456 520 dsqQEISSMQMRL-----AMKDLE 538
Cdd:PRK03918  704 ---EEREKAKKELeklekALERVE 724
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
336-538 2.69e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 57.62  E-value: 2.69e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  336 PHSLTPE-MIppSDKSSL-QKNT---IGSSPVADFSAIKELDTLNNEIIDLQREKNNVE---QDLKEKEDTVRQRTTEAQ 407
Cdd:COG4913    574 PRAITRAgQV--KGNGTRhEKDDrrrIRSRYVLGFDNRAKLAALEAELAELEEELAEAEerlEALEAELDALQERREALQ 651
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  408 DLQD------------------EVQRESLNLQKLQaqkqqvqelLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAEI 469
Cdd:COG4913    652 RLAEyswdeidvasaereiaelEAELERLDASSDD---------LAALEEQLEELEAELEELEEELDELKGEIGRLEKEL 722
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958776456  470 TSQESQISTYEEELSkAREELSRLQQEtAQLEE--SVESGKAQLEPLQQHLQDSQQEISSmQMRLAMKDLE 538
Cdd:COG4913    723 EQAEEELDELQDRLE-AAEDLARLELR-ALLEErfAAALGDAVERELRENLEERIDALRA-RLNRAEEELE 790
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
375-540 5.09e-08

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 56.56  E-value: 5.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 375 NNEIIDLQREKNNVEQDLKEKEDTVRQRTTEAQDLQDEVQ--RESLNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVR 452
Cdd:COG3206   204 KNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAalRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELS 283
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 453 KKCAEEAQLISSLKAEITSQESQIStyeeelskareelSRLQQETAQLEESVESGKAQLEPLQQHLQDSQQEISSMQMRL 532
Cdd:COG3206   284 ARYTPNHPDVIALRAQIAALRAQLQ-------------QEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELE 350

                  ....*....
gi 1958776456 533 A-MKDLETD 540
Cdd:COG3206   351 AeLRRLERE 359
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
366-572 9.41e-08

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 55.22  E-value: 9.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 366 SAIKELDTLNNEIIDLQREKNNVEQDLKEKEDTVRQRT----------------TEAQDLQD------------EVQRES 417
Cdd:COG3883    55 ELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAralyrsggsvsyldvlLGSESFSDfldrlsalskiaDADADL 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 418 LNL-----QKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAEITSQESQISTYEEELSKAREELSR 492
Cdd:COG3883   135 LEElkadkAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 493 LQQETAQLEESVESGKAQLEPLQQHLQDSQQEISSMQMRLAMKDLETDNNQSNWCSSPQSILVNGAADYCSLSTSSSETA 572
Cdd:COG3883   215 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGG 294
EF-hand_4 pfam12763
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ...
39-80 1.18e-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: 50.45  E-value: 1.18e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1958776456  39 AAAFLKKSGLPDLILGKIWDLADTDGKGVLNKQEFFIALRLV 80
Cdd:pfam12763  31 VSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLI 72
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
369-545 1.64e-07

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 55.03  E-value: 1.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 369 KELDTLNNEIIDLQREKN-------NVEQDLKEKEDTVRQRTTEAQDLQDEVQRESLNlqklqaqKQQVQELLDELDEQK 441
Cdd:TIGR04523 363 RELEEKQNEIEKLKKENQsykqeikNLESQINDLESKIQNQEKLNQQKDEQIKKLQQE-------KELLEKEIERLKETI 435
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 442 AQLEEQLKEVRKKCAEEAQLISSLKAEITSQESQISTYEEELSKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQDS 521
Cdd:TIGR04523 436 IKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDL 515
                         170       180
                  ....*....|....*....|....
gi 1958776456 522 QQEISSMQMRlaMKDLETDNNQSN 545
Cdd:TIGR04523 516 TKKISSLKEK--IEKLESEKKEKE 537
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
366-531 2.21e-07

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 54.66  E-value: 2.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 366 SAIKELDTLNNEIIDLQREKNNVEQDLKEKEDTVRQRTTEAQDLQDEVQ--RESLNLQKL-----QAQKQQVQELLDELD 438
Cdd:PRK02224  346 SLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEelRERFGDAPVdlgnaEDFLEELREERDELR 425
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 439 EQKAQLEEQLKEVRKKCAEEAQLISSLKAEITSQESQISTYEEELSKAREELSRLQQETAQLEESVESGKAQLEPLQQhL 518
Cdd:PRK02224  426 EREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAED-L 504
                         170
                  ....*....|...
gi 1958776456 519 QDSQQEISSMQMR 531
Cdd:PRK02224  505 VEAEDRIERLEER 517
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
381-541 3.72e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 53.62  E-value: 3.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 381 LQREKNNVEQDLKEKEDTVRQRTTEAQDLQDEVQRESLNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEE-- 458
Cdd:COG4717   293 LAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQei 372
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 459 AQLISSLKAEitsQESQISTYEEELSKAREELSRLQQETAQLEE------------SVESGKAQLEPLQQHLQDSQQEIS 526
Cdd:COG4717   373 AALLAEAGVE---DEEELRAALEQAEEYQELKEELEELEEQLEEllgeleellealDEEELEEELEELEEELEELEEELE 449
                         170       180
                  ....*....|....*....|
gi 1958776456 527 SMQMRLA-----MKDLETDN 541
Cdd:COG4717   450 ELREELAeleaeLEQLEEDG 469
HAP1_N pfam04849
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ...
370-538 3.76e-07

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: 52.72  E-value: 3.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 370 ELDTLNNEIIDLQREknnveqdLKEKEDTVRQRTTEAQDLQDEVQRESLNLQKLQAQKQQVQELLDELDEQKAQLEEQLK 449
Cdd:pfam04849 109 QLGSAREEILQLRHE-------LSKKDDLLQIYSNDAEESETESSCSTPLRRNESFSSLHGCVQLDALQEKLRGLEEENL 181
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 450 EVRKKC-----------AEEAQLISSLKAEITSQESQISTYEEELSKAREELSRLQQETAQL-------EESVESGKAQL 511
Cdd:pfam04849 182 KLRSEAshlktetdtyeEKEQQLMSDCVEQLSEANQQMAELSEELARKMEENLRQQEEITSLlaqivdlQHKCKELGIEN 261
                         170       180
                  ....*....|....*....|....*..
gi 1958776456 512 EPLQQHLQDSQQeiSSMQMRLAMKDLE 538
Cdd:pfam04849 262 EELQQHLQASKE--AQRQLTSELQELQ 286
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
367-528 4.43e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 53.92  E-value: 4.43e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  367 AIKELDTLNNEIIDLQREKNNVEQDLKEKEDT-----VRQRTTEAQDLQDEVQR--------------ESLNLQKLQAQK 427
Cdd:TIGR02169  756 VKSELKELEARIEELEEDLHKLEEALNDLEARlshsrIPEIQAELSKLEEEVSRiearlreieqklnrLTLEKEYLEKEI 835
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  428 QQVQELLDELDEQKA--------------QLEEQLKEVRKKCAE-EAQL------ISSLKAEITSQESQISTYEEELSKA 486
Cdd:TIGR02169  836 QELQEQRIDLKEQIKsiekeienlngkkeELEEELEELEAALRDlESRLgdlkkeRDELEAQLRELERKIEELEAQIEKK 915
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958776456  487 REELSRLQ-------QETAQLEESVESGK------AQLEPLQQHLQDSQQEISSM 528
Cdd:TIGR02169  916 RKRLSELKaklealeEELSEIEDPKGEDEeipeeeLSLEDVQAELQRVEEEIRAL 970
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
369-492 4.93e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.77  E-value: 4.93e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  369 KELDTLNNEIIDLQREKNNV--------EQDLKEKEDTVRQRTTEAQDLQDEVQR----ESLNLQKLQAQKQQVQELLDE 436
Cdd:COG4913    316 ARLDALREELDELEAQIRGNggdrleqlEREIERLERELEERERRRARLEALLAAlglpLPASAEEFAALRAEAAALLEA 395
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958776456  437 LDEQKAQLEEQLKEVRKKCAEEAQLISSLKAEITSQESQISTYEEELSKAREELSR 492
Cdd:COG4913    396 LEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAE 451
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
361-544 5.18e-07

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 53.51  E-value: 5.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 361 PVADFSAIKELDTLNNEIIDLQREKnnveQDLKEKEDTVRQRTTEAQDLQD-EVQRESLnlqklQAQKQQVQELLDELDE 439
Cdd:PRK02224  460 PVEGSPHVETIEEDRERVEELEAEL----EDLEEEVEEVEERLERAEDLVEaEDRIERL-----EERREDLEELIAERRE 530
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 440 QKAQLEEQLKEVRKKCAEeaqlissLKAEITSQESQISTYEEELSKAREELSRLQQETAQLEESVESgKAQLEPLQQHLQ 519
Cdd:PRK02224  531 TIEEKRERAEELRERAAE-------LEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIES-LERIRTLLAAIA 602
                         170       180
                  ....*....|....*....|....*
gi 1958776456 520 DSQQEISSMQMRLamKDLETDNNQS 544
Cdd:PRK02224  603 DAEDEIERLREKR--EALAELNDER 625
PTZ00121 PTZ00121
MAEBL; Provisional
382-634 5.36e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.61  E-value: 5.36e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  382 QREKNNVEQDLKEKEDTVRQrtteAQDLQDEVQRESLNLQKLQAQKQQVQELLDEL---DEQKAQLEEQLK--------- 449
Cdd:PTZ00121  1629 EEEKKKVEQLKKKEAEEKKK----AEELKKAEEENKIKAAEEAKKAEEDKKKAEEAkkaEEDEKKAAEALKkeaeeakka 1704
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  450 -EVRKKCAEE---------AQLISSLKAE-ITSQESQISTYEEELSKAREELSRLQQETAQLEESVESGKAQLEPLQQHL 518
Cdd:PTZ00121  1705 eELKKKEAEEkkkaeelkkAEEENKIKAEeAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEE 1784
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  519 QDSQQEISSMQMRLAMKDLETD-------NNQSNWCSSPQSILVNGAADYCSLSTSS--SETANLNEHAEGQNNLESEPI 589
Cdd:PTZ00121  1785 LDEEDEKRRMEVDKKIKDIFDNfaniiegGKEGNLVINDSKEMEDSAIKEVADSKNMqlEEADAFEKHKFNKNNENGEDG 1864
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958776456  590 HPESSVRSSPEIAPSDV-----TDESEVVTAADIEKVSPRFD---------DDKHSKEE 634
Cdd:PTZ00121  1865 NKEADFNKEKDLKEDDEeeieeADEIEKIDKDDIEREIPNNNmagknndiiDDKLDKDE 1923
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
433-545 6.43e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.40  E-value: 6.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 433 LLDELDEQKAQLEEQ---------LKEVRKKCAEEAQL--ISSLKAEITSQESQISTYEEELSKAREELSRLQQETAQLE 501
Cdd:COG1196   194 ILGELERQLEPLERQaekaeryreLKEELKELEAELLLlkLRELEAELEELEAELEELEAELEELEAELAELEAELEELR 273
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1958776456 502 ESVESGKAQLEPLQQHLQDSQQEISSMQMRLAMKDLETDNNQSN 545
Cdd:COG1196   274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
370-544 6.56e-07

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: 52.07  E-value: 6.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 370 ELDTLNNEIIDLQREKNNVEQDLKEKEDTVRQRTTEAQD-LQDEVQREslnlqklqaqkqqvQELLDELDEQKAQLEEQL 448
Cdd:pfam09787  62 EIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEEqLATERSAR--------------REAEAELERLQEELRYLE 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 449 KEVRKKCAEEAQLISSLKAEITSQESQISTYEEELSKAREELSRLQQET-------AQLEE-SVE--SGKAQLEPLQQHL 518
Cdd:pfam09787 128 EELRRSKATLQSRIKDREAEIEKLRNQLTSKSQSSSSQSELENRLHQLTetliqkqTMLEAlSTEknSLVLQLERMEQQI 207
                         170       180
                  ....*....|....*....|....*.
gi 1958776456 519 QDSQQEiSSMQMRLAMKDLETDNNQS 544
Cdd:pfam09787 208 KELQGE-GSNGTSINMEGISDGEGTR 232
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
366-604 6.95e-07

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 52.52  E-value: 6.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 366 SAIKELDTLNNEIIDLQREKNNVEQDLKEKEdtvrqrtTEAQDLQDEVQreslnlqklqaqkqqvqELLDELDEQKAQLE 445
Cdd:COG3883    34 AAQAELDALQAELEELNEEYNELQAELEALQ-------AEIDKLQAEIA-----------------EAEAEIEERREELG 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 446 EQLKEVRKKC--------------------------------AEEAQLISSLKAEITSQESQISTYEEELSKAREELSR- 492
Cdd:COG3883    90 ERARALYRSGgsvsyldvllgsesfsdfldrlsalskiadadADLLEELKADKAELEAKKAELEAKLAELEALKAELEAa 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 493 ---LQQETAQLEESVESGKAQLEPLQQHLQDSQQEISSMQMRLAMKDLETDNNQSNWCSSPQSILVNGAADYCSLSTSSS 569
Cdd:COG3883   170 kaeLEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGA 249
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1958776456 570 ETANLNEHAEGQNNLESEPIHPESSVRSSPEIAPS 604
Cdd:COG3883   250 GAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGG 284
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
369-541 7.34e-07

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 53.10  E-value: 7.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 369 KELDTLNNEIIDLQREK-----NNVEQDLKEKEDTVRQrtTEAQDLQDEVQRESLNLQKLQAQKQqvqelLDELDEQKAQ 443
Cdd:TIGR04523 288 KQLNQLKSEISDLNNQKeqdwnKELKSELKNQEKKLEE--IQNQISQNNKIISQLNEQISQLKKE-----LTNSESENSE 360
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 444 LEEQLKEVRKKCAEEAQLISSLKAEITSQESQISTYEEELSKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQDSQQ 523
Cdd:TIGR04523 361 KQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNS 440
                         170
                  ....*....|....*...
gi 1958776456 524 EISSMQMRLAMKDLETDN 541
Cdd:TIGR04523 441 EIKDLTNQDSVKELIIKN 458
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
353-527 9.11e-07

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 52.71  E-value: 9.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 353 QKNTIGSSPVADFSAIKELDTLNNEIIDLQREKNNVEQDLKEKEDTVRQRTTEAQDLQDEVQRESLNLQKLQAQKQQVQ- 431
Cdd:COG3206   203 QKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAEl 282
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 432 ------------ELLDELDEQKAQLEEqlkevrkkcaEEAQLISSLKAEITSQESQISTYEEELSKAREELSRL---QQE 496
Cdd:COG3206   283 sarytpnhpdviALRAQIAALRAQLQQ----------EAQRILASLEAELEALQAREASLQAQLAQLEARLAELpelEAE 352
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1958776456 497 TAQLEESVESGKAQLEPLQQHLQDSQQEISS 527
Cdd:COG3206   353 LRRLEREVEVARELYESLLQRLEEARLAEAL 383
TMF_DNA_bd pfam12329
TATA element modulatory factor 1 DNA binding; This is the middle region of a family of TATA ...
432-501 9.90e-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: 9.90e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 432 ELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAEITSQESQISTYEEELSKAREELSRLQQETAQLE 501
Cdd:pfam12329   5 KLLKEKDEQIAQLMEEGEKLSKKELKLNNTIKKLRAKNKELEKEIAELKKKLEKLEKELENLEERLKRAE 74
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
377-533 1.04e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 52.76  E-value: 1.04e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  377 EIIDLQREKNNVEQDLKEKEDTVRQRTTEAQDLQDEvqRESLNLQklqaqkqqvqelLDELDEQKAQLEEQLKEVRKK-- 454
Cdd:TIGR02169  330 EIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEE--LEDLRAE------------LEEVDKEFAETRDELKDYREKle 395
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  455 ---------------CAEEAQLISS----LKAEITSQESQISTYEEELSKAREELSRLQQETAQLEESVESGKAQLEPLQ 515
Cdd:TIGR02169  396 klkreinelkreldrLQEELQRLSEeladLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLK 475
                          170
                   ....*....|....*...
gi 1958776456  516 QHLQDSQQEISSMQMRLA 533
Cdd:TIGR02169  476 EEYDRVEKELSKLQRELA 493
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
348-526 1.29e-06

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 51.94  E-value: 1.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 348 DKSSLQKNTIgSSPVADFSAIK-ELDTLNNEIIDLQREKNNVEQDLKEKEDTVRQRTTEAQDLQDEVqrESLNLQklqaq 426
Cdd:TIGR04523  89 DKLKKNKDKI-NKLNSDLSKINsEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKEL--EKLNNK----- 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 427 kqqvqelLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAEITSQE---SQISTYEEELSKAREELSRLQQETAQLEES 503
Cdd:TIGR04523 161 -------YNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLElllSNLKKKIQKNKSLESQISELKKQNNQLKDN 233
                         170       180
                  ....*....|....*....|...
gi 1958776456 504 VESGKAQLEPLQQHLQDSQQEIS 526
Cdd:TIGR04523 234 IEKKQQEINEKTTEISNTQTQLN 256
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
438-533 1.47e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 51.44  E-value: 1.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 438 DEQKAQLEEQLKEVRKKCAEEAQLISSLKAEITSQESQISTYEEELSKAREELSRLQQETAQLEESVESGKAQLEPLQQH 517
Cdd:COG4372     2 DRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEE 81
                          90
                  ....*....|....*.
gi 1958776456 518 LQDSQQEISSMQMRLA 533
Cdd:COG4372    82 LEELNEQLQAAQAELA 97
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
371-536 1.60e-06

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: 51.75  E-value: 1.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 371 LDTLNNEIID---------------------LQREKNNVEQDLKEKEDTVRQRTTEAQDLQDEvqreslnlqkLQAQKQQ 429
Cdd:pfam10174 312 LETLTNQNSDckqhievlkesltakeqraaiLQTEVDALRLRLEEKESFLNKKTKQLQDLTEE----------KSTLAGE 381
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 430 VQELLDELD--EQKA--------QLEEQLKEVRKKCAEEAQLISSLKAEITSQESQISTYEEELSKA------------- 486
Cdd:pfam10174 382 IRDLKDMLDvkERKInvlqkkieNLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKeriierlkeqrer 461
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958776456 487 -----REELSRLQQETAQLEESVESGKAQLEPLQQHLQDSQQEISSMQMRLAMKD 536
Cdd:pfam10174 462 edrerLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKD 516
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
365-527 1.66e-06

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 51.76  E-value: 1.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 365 FSAIKELDTLNneIIDLQREKNNVEQDLKEKEDTVRQRTTEAQDL--QDEVQREslnlqklqaqkqqvqelldeldeQKA 442
Cdd:PRK04778   89 FEAEELNDKFR--FRKAKHEINEIESLLDLIEEDIEQILEELQELleSEEKNRE-----------------------EVE 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 443 QLEEQLKEVRKKCAEEA----QLISSLKAEITSQESQISTYEEELS-----KAREELSRLQQETAQLEESVESGKAQLEP 513
Cdd:PRK04778  144 QLKDLYRELRKSLLANRfsfgPALDELEKQLENLEEEFSQFVELTEsgdyvEAREILDQLEEELAALEQIMEEIPELLKE 223
                         170
                  ....*....|....
gi 1958776456 514 LQQHLQDSQQEISS 527
Cdd:PRK04778  224 LQTELPDQLQELKA 237
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
368-521 1.69e-06

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 51.38  E-value: 1.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 368 IKELDTLNNEI---ID-----LQRE---KNNVEQDLKEKEDTVRQRTTEAQDLQDEVQR--ES--LNLQKLqaqkqqvqE 432
Cdd:PRK04778  277 LDEAEEKNEEIqerIDqlydiLEREvkaRKYVEKNSDTLPDFLEHAKEQNKELKEEIDRvkQSytLNESEL--------E 348
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 433 LLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAEITSQESQISTYEEELSKAREELSRLQQETAQLEESVESGKAQLE 512
Cdd:PRK04778  349 SVRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKLH 428

                  ....*....
gi 1958776456 513 PLQQHLQDS 521
Cdd:PRK04778  429 EIKRYLEKS 437
MscS_porin pfam12795
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...
369-542 1.76e-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: 49.99  E-value: 1.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 369 KELDTLNNEII-DLQREKNNVE--QDLKEKEDTVRQRTTEAQDLQDEVQRESLNLQKLQAQKQQvqELLDELDeqKAQLE 445
Cdd:pfam12795   9 KLDEAAKKKLLqDLQQALSLLDkiDASKQRAAAYQKALDDAPAELRELRQELAALQAKAEAAPK--EILASLS--LEELE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 446 EQLKEVRKKCAEEAQLISSLKAEITSQESQISTyeeelskAREELSRLQQETAQLEESVESGKAQLEPLQQHLQDSQQ-E 524
Cdd:pfam12795  85 QRLLQTSAQLQELQNQLAQLNSQLIELQTRPER-------AQQQLSEARQRLQQIRNRLNGPAPPGEPLSEAQRWALQaE 157
                         170
                  ....*....|....*...
gi 1958776456 525 ISSMQMRLAMKDLETDNN 542
Cdd:pfam12795 158 LAALKAQIDMLEQELLSN 175
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
369-540 1.94e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 51.60  E-value: 1.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 369 KELDTLNNEIIDLQREKNNVEQDLKEKEDTVRQRTTEAQDLQDEVQRESLNLQKLQAQKQQVQELLDELDEQKAQLEEQL 448
Cdd:PRK03918  466 KELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLK 545
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 449 KEVRKkcaeeaqlISSLKAEITSQESQISTYEEELSKAREELSRLQQETaqlEESVESGKAQLEPLQQH---LQDSQQEI 525
Cdd:PRK03918  546 KELEK--------LEELKKKLAELEKKLDELEEELAELLKELEELGFES---VEELEERLKELEPFYNEyleLKDAEKEL 614
                         170
                  ....*....|....*
gi 1958776456 526 SSMQMRLamKDLETD 540
Cdd:PRK03918  615 EREEKEL--KKLEEE 627
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
369-524 2.14e-06

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 51.56  E-value: 2.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 369 KELDTLNNEIIDLQREKNNVEQDLKEKEDTVRQRTTEAQDLQDEVQRESLNLQKLQAQKQQVQELLDELDEqkaqLEEQL 448
Cdd:TIGR04523 152 KELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISE----LKKQN 227
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958776456 449 KEVRKKCAEEAQLISSLKAEITSQESQISTYEEELSKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQDSQQE 524
Cdd:TIGR04523 228 NQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQ 303
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
369-526 2.41e-06

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: 50.58  E-value: 2.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 369 KELDTLNNEIIDLQREKnnveqDLKEKEDTVRQRTTEAQdLQdEVQREslnlqklqaqkqqvqelLDELDEQKAQLEEQL 448
Cdd:pfam15905 152 KKMSSLSMELMKLRNKL-----EAKMKEVMAKQEGMEGK-LQ-VTQKN-----------------LEHSKGKVAQLEEKL 207
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958776456 449 KEVRKKCAEEaqlisslKAEITSQESQIstyeEELSKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQDSQQEIS 526
Cdd:pfam15905 208 VSTEKEKIEE-------KSETEKLLEYI----TELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELS 274
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
368-532 2.78e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 51.22  E-value: 2.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 368 IKELDTLNNEIIDLQREKNNVEQDLKEKED---TVRQRTTEAQDLQDEVQRESLNLQKLQAQKQQVQELLDELDEQKAQL 444
Cdd:PRK03918  171 IKEIKRRIERLEKFIKRTENIEELIKEKEKeleEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESL 250
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 445 EEQLKEVRKKCAEEAQLISSLKAEITSQESQISTYEE--ELSKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQDSQ 522
Cdd:PRK03918  251 EGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERI 330
                         170
                  ....*....|
gi 1958776456 523 QEISSMQMRL 532
Cdd:PRK03918  331 KELEEKEERL 340
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
369-534 2.87e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 51.22  E-value: 2.87e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  369 KELDTLNNEIIDLQREKNNVEQDLKEKEDTVRQRTTEAQDLQDEVQREslnlqklqaqkqqVQELLDELDEQKAQLEEQL 448
Cdd:TIGR02169  244 RQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLR-------------VKEKIGELEAEIASLERSI 310
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  449 KEVRKKCAEEAQLISSLKAEITSQESQISTYEEELSKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQDSQQEISSM 528
Cdd:TIGR02169  311 AEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDY 390

                   ....*.
gi 1958776456  529 QMRLAM 534
Cdd:TIGR02169  391 REKLEK 396
EF-hand_4 pfam12763
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ...
251-355 3.05e-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: 46.60  E-value: 3.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 251 LRQWvvspaEKAKYDEIFlKTDKDMDGYVSGLEVRETFLKTGLPSTLLAHIWALCDTKNCGKLSKDQFALA----FHLIN 326
Cdd:pfam12763   4 LEEW-----EIKKYWEIF-SGLKPENNKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAmrliFDLVN 77
                          90       100
                  ....*....|....*....|....*....
gi 1958776456 327 QKLikgIDPPHSLTPEMIPPSDKSSLQKN 355
Cdd:pfam12763  78 GNI---ADVPDELPDWLVPGSKAHLIQAN 103
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
379-539 3.08e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.21  E-value: 3.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  379 IDLQREKNNVE--------QDLKEKEDTVRQRTTEAQDLQDEVQRESlnlqklqaqkQQVQELLDELDEQKAQLEEQLKE 450
Cdd:TIGR02168  216 KELKAELRELElallvlrlEELREELEELQEELKEAEEELEELTAEL----------QELEEKLEELRLEVSELEEEIEE 285
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  451 VRKKCAEEAQLISSLKAEITSQ-------ESQISTYEEELSKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQDSQQ 523
Cdd:TIGR02168  286 LQKELYALANEISRLEQQKQILrerlanlERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEA 365
                          170
                   ....*....|....*.
gi 1958776456  524 EISsmQMRLAMKDLET 539
Cdd:TIGR02168  366 ELE--ELESRLEELEE 379
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
366-502 3.26e-06

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 50.63  E-value: 3.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 366 SAIKEL--DTLNNEIIDLQREKNNVEQDLKEKEDTVRQRTTEAQDLQDEVqrESLnlqklqaqkqqvQELLDELDEQKAQ 443
Cdd:COG2433   380 EALEELieKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEV--EEL------------EAELEEKDERIER 445
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958776456 444 LEEQLKEVRKKCAEEAQlissLKAEITSQESQISTYEEELSKAREELSRLQQETAQLEE 502
Cdd:COG2433   446 LERELSEARSEERREIR----KDREISRLDREIERLERELEEERERIEELKRKLERLKE 500
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
353-541 3.29e-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: 50.62  E-value: 3.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 353 QKNTIGSSPVAD-FSAIKEL----------DTLNNEIIDLQ-REKNNVEQDLKEKED--------TVRQRTTEAQDLQDE 412
Cdd:pfam06160  18 RKNELMNLPVQEeLSKVKKLnltgetqekfEEWRKKWDDIVtKSLPDIEELLFEAEElndkyrfkKAKKALDEIEELLDD 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 413 VQRESlnlqklqaqkqqvQELLDELDEQKAQ----------LEEQLKEVRKKCAEEA----QLISSLKAEITSQESQIST 478
Cdd:pfam06160  98 IEEDI-------------KQILEELDELLESeeknreeveeLKDKYRELRKTLLANRfsygPAIDELEKQLAEIEEEFSQ 164
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958776456 479 YEEELS-----KAREELSRLQQETAQLEESVESGKAQLEPLQQHLQDSQQEISSmqmrlAMKDLETDN 541
Cdd:pfam06160 165 FEELTEsgdylEAREVLEKLEEETDALEELMEDIPPLYEELKTELPDQLEELKE-----GYREMEEEG 227
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
433-538 3.31e-06

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 49.15  E-value: 3.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 433 LLD--ELDEQKAQLEEQLKEVRKKcaeeaqlISSLKAEITSQESQISTYEEELSKAREELSRLQQETAQLEESVESGKAQ 510
Cdd:COG1579     9 LLDlqELDSELDRLEHRLKELPAE-------LAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ 81
                          90       100       110
                  ....*....|....*....|....*....|
gi 1958776456 511 LEPL--QQHLQDSQQEISSMQMRLAmkDLE 538
Cdd:COG1579    82 LGNVrnNKEYEALQKEIESLKRRIS--DLE 109
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
440-540 3.93e-06

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: 46.45  E-value: 3.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 440 QKAQLEEQLKEVRkkcaEEAQLIsslKAEITSQESQISTYEEELSKAREELSRLQQ-------ETAQLEESVESGKAQLE 512
Cdd:pfam20492   7 EKQELEERLKQYE----EETKKA---QEELEESEETAEELEEERRQAEEEAERLEQkrqeaeeEKERLEESAEMEAEEKE 79
                          90       100
                  ....*....|....*....|....*...
gi 1958776456 513 PLQQHLQDSQQEISSMQMRLAMKDLETD 540
Cdd:pfam20492  80 QLEAELAEAQEEIARLEEEVERKEEEAR 107
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
369-469 4.24e-06

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 48.77  E-value: 4.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 369 KELDTLNNEIIDLQREKNNVEQDLKEKEDTVRQRTTEAQDLQDEV--QRESLNlqklqaqkqqvqELLDELDEQKAQLEE 446
Cdd:COG1579    89 KEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELaeLEAELE------------EKKAELDEELAELEA 156
                          90       100
                  ....*....|....*....|...
gi 1958776456 447 QLKEVRKKCAEeaqLISSLKAEI 469
Cdd:COG1579   157 ELEELEAEREE---LAAKIPPEL 176
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
468-533 5.97e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 49.44  E-value: 5.97e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958776456 468 EITSQESQISTYEEELSKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQDSQQEISSMQMRLA 533
Cdd:COG3883    17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIE 82
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
384-504 7.35e-06

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 49.69  E-value: 7.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 384 EKNNVEQDLKEKEDTVRQRTTEAQDLQDEVQRESlnlqklqaqkqqvQELLDELDEQKAQLEEQLKEVRKKCAEEAQLIS 463
Cdd:COG0542   405 EIDSKPEELDELERRLEQLEIEKEALKKEQDEAS-------------FERLAELRDELAELEEELEALKARWEAEKELIE 471
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1958776456 464 ---SLKAEITSQESQISTYEEELSKAREELSrlqQETAQLEESV 504
Cdd:COG0542   472 eiqELKEELEQRYGKIPELEKELAELEEELA---ELAPLLREEV 512
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
310-531 8.81e-06

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: 49.30  E-value: 8.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 310 CGKLSKDQFALAFHLinqkLIKGIDPPHSLTPEMIPPsdksslqkntigsspvadfsAIKEldtlnnEIIDLQREkNNVe 389
Cdd:pfam05622 246 CAQLQQAELSQADAL----LSPSSDPGDNLAAEIMPA--------------------EIRE------KLIRLQHE-NKM- 293
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 390 qdLKEK-EDTVRQRTTEAQdlqdevqreslnlqklqaqkqqvqELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAE 468
Cdd:pfam05622 294 --LRLGqEGSYRERLTELQ------------------------QLLEDANRRKNELETQNRLANQRILELQQQVEELQKA 347
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958776456 469 ITSQESQ----------ISTYEEELSKAREELSRLQQETAQLEESVESGKAQ-LEPLQQHLQDSQQEISSMQMR 531
Cdd:pfam05622 348 LQEQGSKaedssllkqkLEEHLEKLHEAQSELQKKKEQIEELEPKQDSNLAQkIDELQEALRKKDEDMKAMEER 421
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
434-545 1.06e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.28  E-value: 1.06e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  434 LDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAEITSQESQISTYEEELSKAREELSRLQQETAQLEESVESGKAQLEP 513
Cdd:TIGR02168  679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1958776456  514 LQQHLQDSQQEISSMQMRLA-----MKDLETDNNQSN 545
Cdd:TIGR02168  759 LEAEIEELEERLEEAEEELAeaeaeIEELEAQIEQLK 795
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
438-539 1.22e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 48.29  E-value: 1.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 438 DEQKAQLEEQLKEVRKKCAEEAQLISSLKAEITSQESQISTYEEELSKAREELSRLQQETAQLEESVESGKAQLEPLQQH 517
Cdd:COG3883    15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
                          90       100
                  ....*....|....*....|..
gi 1958776456 518 LQDSQQEISSMQMRLAMKDLET 539
Cdd:COG3883    95 LYRSGGSVSYLDVLLGSESFSD 116
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
367-522 1.25e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.14  E-value: 1.25e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  367 AIKELDTLNNEIIDLQREKNNVEQDLKEKEDTVRQRTTEAQDLQDEV-----QRESLNLQKLQAQKQQVQELLDELDEQK 441
Cdd:COG4913    676 ELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELeqaeeELDELQDRLEAAEDLARLELRALLEERF 755
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  442 AQL--EEQLKEVRKKCAEEaqlISSLKAEITSQESQIST-------------------------YEEELSK--------A 486
Cdd:COG4913    756 AAAlgDAVERELRENLEER---IDALRARLNRAEEELERamrafnrewpaetadldadleslpeYLALLDRleedglpeY 832
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1958776456  487 REELSRLQQET---------AQLEESVESGKAQLEPLQQHLQDSQ 522
Cdd:COG4913    833 EERFKELLNENsiefvadllSKLRRAIREIKERIDPLNDSLKRIP 877
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
432-540 1.47e-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: 1.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 432 ELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAEITSQESQISTYEEELSKARE---------ELSRLQQETAQLE- 501
Cdd:COG1579    24 HRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlgnvrnnkEYEALQKEIESLKr 103
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958776456 502 -------------ESVESGKAQLEPLQQHLQDSQQEISSMQMRL--AMKDLETD 540
Cdd:COG1579   104 risdledeilelmERIEELEEELAELEAELAELEAELEEKKAELdeELAELEAE 157
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
369-516 1.54e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.52  E-value: 1.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 369 KELDTLNNEIIDLQREKNNVEQDLKEKEDTVRQRTteaqdlqdEVQREslnlqklqaqkqqvqelLDELDEQKAQLEEQL 448
Cdd:PRK03918  525 EEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLA--------ELEKK-----------------LDELEEELAELLKEL 579
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958776456 449 KEVRKKCAEEAQL-ISSLKA------EITSQESQISTYEEELSKAREELSRLQQETAQLEESVESGKAQLEPLQQ 516
Cdd:PRK03918  580 EELGFESVEELEErLKELEPfyneylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEK 654
Nuf2_DHR10-like pfam18595
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ...
380-516 1.85e-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: 44.50  E-value: 1.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 380 DLQREKNNVE------QDLKEKEDT-------VRQRTTEAQDLQDEVQREslnlqklqaqkqqvQELLDELDEQKAQLEE 446
Cdd:pfam18595   3 TLAEEKEELAelerkaRELQAKIDAlqvvekdLRSCIKLLEEIEAELAKL--------------EEAKKKLKELRDALEE 68
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 447 QLKEVRkkcaeeaqlisslkaEITSQESQIstyEEELSKAREELSRLQQetaQLEESVESGKAQLEPLQQ 516
Cdd:pfam18595  69 KEIELR---------------ELERREERL---QRQLENAQEKLERLRE---QAEEKREAAQARLEELRE 117
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
434-532 2.12e-05

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: 48.41  E-value: 2.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  434 LDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAEITSQESQISTYEEELSKAREELSRLQQETAQLEESVESGKAQ--- 510
Cdd:COG3096    524 LEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARapa 603
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1958776456  511 -------LEPLQQH----LQDSQQEISSMQMRL 532
Cdd:COG3096    604 wlaaqdaLERLREQsgeaLADSQEVTAAMQQLL 636
PRK12704 PRK12704
phosphodiesterase; Provisional
435-530 2.12e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 47.85  E-value: 2.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 435 DELDEQKAQLEEQLKEVRKKcaeeaqlISSLKAEITSQESQISTYEEELSKAREELSRLQQETAQLEESVESGKAQLEPL 514
Cdd:PRK12704   64 EEIHKLRNEFEKELRERRNE-------LQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEEL 136
                          90
                  ....*....|....*.
gi 1958776456 515 QQHLQDSQQEISSMQM 530
Cdd:PRK12704  137 IEEQLQELERISGLTA 152
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
368-529 2.15e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.14  E-value: 2.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 368 IKELDTLNNEIIDLQREKNNVEQDLKEKEDTvRQRTTEAqdlqdEVQRESLNLQKLQAQkqqvqELLDELDEQKAQLEEQ 447
Cdd:PRK03918  206 LREINEISSELPELREELEKLEKEVKELEEL-KEEIEEL-----EKELESLEGSKRKLE-----EKIRELEERIEELKKE 274
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 448 LKEVRKKC---------AEEAQLISSLKAEITSQESQI----STYEEELS------KAREELSRLQQETAQLEESVESGK 508
Cdd:PRK03918  275 IEELEEKVkelkelkekAEEYIKLSEFYEEYLDELREIekrlSRLEEEINgieeriKELEEKEERLEELKKKLKELEKRL 354
                         170       180
                  ....*....|....*....|.
gi 1958776456 509 AQLEPLQQHLQDSQQEISSMQ 529
Cdd:PRK03918  355 EELEERHELYEEAKAKKEELE 375
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
369-529 2.23e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.59  E-value: 2.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 369 KELDTLNNEIIDLQREKNNVEQDLKEKEDTVRQRTTEAQDLQDEVQ--RESLNLQKLQAQKQQVQELLDELDEQKAQLEE 446
Cdd:COG4372   115 EELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLEslQEELAALEQELQALSEAEAEQALDELLKEANR 194
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 447 QLKEVRKKCAEEAQLISSLKAEITSQESQISTYEEELSKAREEL----SRLQQETAQLEESVESGKAQLEPLQQHLQDSQ 522
Cdd:COG4372   195 NAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALldalELEEDKEELLEEVILKEIEELELAILVEKDTE 274

                  ....*..
gi 1958776456 523 QEISSMQ 529
Cdd:COG4372   275 EEELEIA 281
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
368-533 2.37e-05

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 47.21  E-value: 2.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 368 IKELDTLNNEIIDLQREKNNVEQDLKEKEDTVRQRTTEA-----------------QDLQDEVQRESLNLQKLQAQKQQV 430
Cdd:COG1340    63 REKRDELNEKVKELKEERDELNEKLNELREELDELRKELaelnkaggsidklrkeiERLEWRQQTEVLSPEEEKELVEKI 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 431 QELLDELDEQKAQLE--EQLKEVRKKCAEEAQLISSLKAEIT--SQESQ------ISTYEE--ELSKAREELSRLQQEta 498
Cdd:COG1340   143 KELEKELEKAKKALEknEKLKELRAELKELRKEAEEIHKKIKelAEEAQelheemIELYKEadELRKEADELHKEIVE-- 220
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1958776456 499 qLEESVESGKAQLEPLQQHLQDSQQEISSMQMRLA 533
Cdd:COG1340   221 -AQEKADELHEEIIELQKELRELRKELKKLRKKQR 254
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
433-545 2.62e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 48.13  E-value: 2.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  433 LLDELDEQKAQLEEQLKEV----RKKCAEEAQLISSLKAEITSQESQISTYEEELSKAREELSRLQQETAQLEESVE--- 505
Cdd:TIGR02168  194 ILNELERQLKSLERQAEKAerykELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEelr 273
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1958776456  506 ----SGKAQLEPLQQHLQDSQQEISSMQMRLAMKDLETDNNQSN 545
Cdd:TIGR02168  274 levsELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQ 317
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
369-588 2.65e-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: 48.19  E-value: 2.65e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  369 KELDTLNNEIIDLQREKNNVEQDLK-----------EKEDTVRQRTTEAQDLQDEVQ--RESLNLQKLQAQKQQVQEL-- 433
Cdd:pfam15921  653 QERDQLLNEVKTSRNELNSLSEDYEvlkrnfrnkseEMETTTNKLKMQLKSAQSELEqtRNTLKSMEGSDGHAMKVAMgm 732
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  434 ----------LDELDEQKAQLEEQLKEVRKkcaeEAQLISSLKAEITSQESQISTYEE----ELSKAREELSRLQQETAQ 499
Cdd:pfam15921  733 qkqitakrgqIDALQSKIQFLEEAMTNANK----EKHFLKEEKNKLSQELSTVATEKNkmagELEVLRSQERRLKEKVAN 808
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  500 LEESVESGKAQLEPLQQHLQDSQQEISSMQMR--LAMKDLETDNNQSNWCSSPQsiLVNGAA---DYCSLSTSSSETANL 574
Cdd:pfam15921  809 MEVALDKASLQFAECQDIIQRQEQESVRLKLQhtLDVKELQGPGYTSNSSMKPR--LLQPASftrTHSNVPSSQSTASFL 886
                          250
                   ....*....|....
gi 1958776456  575 NEHAEGQNNLESEP 588
Cdd:pfam15921  887 SHHSRKTNALKEDP 900
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
373-527 2.67e-05

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: 47.06  E-value: 2.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 373 TLNNEIIDLQREKNNVEQDLKEKEDTVRQRTTEAQDLQDEVQRESlnlqklqaqkqqvqellDELDEQKAQLEEQLKEVR 452
Cdd:pfam09787  44 ALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEA-----------------ESSREQLQELEEQLATER 106
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958776456 453 kkcaeeaqlisSLKAEItsqESQISTYEEELSKAREELSR----LQQETAQLEESVESGKAQLEPLQQHlQDSQQEISS 527
Cdd:pfam09787 107 -----------SARREA---EAELERLQEELRYLEEELRRskatLQSRIKDREAEIEKLRNQLTSKSQS-SSSQSELEN 170
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
379-546 2.89e-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: 48.12  E-value: 2.89e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  379 IDLQREKNNVEQDLKEKE---DTVRQRTTEAQDLQDEVQRESLNLQKLQAQKQQVQELLDELDEQKAQLEEQL------- 448
Cdd:TIGR00606  818 SDLDRTVQQVNQEKQEKQhelDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLvelstev 897
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  449 ----KEVRKKCAEEAQLISSLKAEITSQESQISTYEEELSKAREELSRLQQETAQ-------LEESVESGK--------- 508
Cdd:TIGR00606  898 qsliREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNihgymkdIENKIQDGKddylkqket 977
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1958776456  509 ------AQLEPLQQHlqdsqQEISSMQMRLAMKDLETDNNQSNW 546
Cdd:TIGR00606  978 elntvnAQLEECEKH-----QEKINEDMRLMRQDIDTQKIQERW 1016
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
369-517 3.18e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 47.75  E-value: 3.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 369 KELDTLNNEIIDLQREKNNVEQD-------LKEKEDTVRQRTTEAQDLQDEVQR-ESLnlQKLQAQKQQVQELLDELDEQ 440
Cdd:PRK03918  231 KELEELKEEIEELEKELESLEGSkrkleekIRELEERIEELKKEIEELEEKVKElKEL--KEKAEEYIKLSEFYEEYLDE 308
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 441 KAQLEEQLKEVRkkcaEEAQLISSLKAEITSQESQIstyeEELSKAREElsrLQQETAQLEESV---ESGKAQLEPLQQH 517
Cdd:PRK03918  309 LREIEKRLSRLE----EEINGIEERIKELEEKEERL----EELKKKLKE---LEKRLEELEERHelyEEAKAKKEELERL 377
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
381-500 3.21e-05

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: 44.65  E-value: 3.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 381 LQREKNNVEQDLKE------KEDTVRQRTTEAQDLQDEVQReslnlqklqaqkqqvqelLDEldEQKAQLEEQLKEVRKK 454
Cdd:pfam05672  25 EQREREEQERLEKEeeerlrKEELRRRAEEERARREEEARR------------------LEE--ERRREEEERQRKAEEE 84
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1958776456 455 CAEEAQlisslkAEITSQESQISTYEEELSKAREELSRLQQETAQL 500
Cdd:pfam05672  85 AEEREQ------REQEEQERLQKQKEEAEAKAREEAERQRQEREKI 124
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
433-533 3.33e-05

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: 45.67  E-value: 3.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 433 LLDELDEQKaQLEEQLKEVRKKCAEEAQLISSLKAEITSQEsqistyeEELSKAREELSRLQQETAQLE---ESVESGKA 509
Cdd:pfam13851  21 TRNNLELIK-SLKEEIAELKKKEERNEKLMSEIQQENKRLT-------EPLQKAQEEVEELRKQLENYEkdkQSLKNLKA 92
                          90       100
                  ....*....|....*....|....
gi 1958776456 510 QLEPLQQHLQDSQQEISSMQMRLA 533
Cdd:pfam13851  93 RLKVLEKELKDLKWEHEVLEQRFE 116
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
439-546 3.70e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.60  E-value: 3.70e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  439 EQKAQLEEQLKEVRKKCAEEAQLISSLKAEITSQESQISTY---------EEELSKAREELSRLQQETAQLEESvesgKA 509
Cdd:COG4913    610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERREALqrlaeyswdEIDVASAEREIAELEAELERLDAS----SD 685
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1958776456  510 QLEPLQQHLQDSQQEISSMQMRLAMKDLETDNNQSNW 546
Cdd:COG4913    686 DLAALEEQLEELEAELEELEEELDELKGEIGRLEKEL 722
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
369-634 3.83e-05

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: 47.53  E-value: 3.83e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  369 KELDTLNNEIIDLQREKNNVEQDLKE---------KEDTVRQRttEAQDLQDEVQRESLNLQKLqaqkqqvqELLDELDE 439
Cdd:pfam12128  361 ERLKALTGKHQDVTAKYNRRRSKIKEqnnrdiagiKDKLAKIR--EARDRQLAVAEDDLQALES--------ELREQLEA 430
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  440 QKAQLEEQLKEVRKKCAEE------AQLISSLKAEITSQESQISTYEEELSKAREELSRLQQETAQLEESVESGKAQLEP 513
Cdd:pfam12128  431 GKLEFNEEEYRLKSRLGELklrlnqATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQ 510
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  514 LQQHLQDSQQEISSMQMRLAMKD---LETDNNQS-NWCSSPQSILVNGAADYCSLSTSSSETANLNEHAEGQNNLESEPI 589
Cdd:pfam12128  511 ASRRLEERQSALDELELQLFPQAgtlLHFLRKEApDWEQSIGKVISPELLHRTDLDPEVWDGSVGGELNLYGVKLDLKRI 590
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1958776456  590 -HPES-----SVRSSPEIAPSDVTDESEVVTAADIEKVSPRFDDDKHSKEE 634
Cdd:pfam12128  591 dVPEWaaseeELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREE 641
CENP-F_leu_zip pfam10473
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ...
438-531 4.06e-05

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


Pssm-ID: 463102 [Multi-domain]  Cd Length: 140  Bit Score: 44.21  E-value: 4.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 438 DEQKAQLEEQLKEVRKKCAEEAQLISSLKAEI-TSQESQ------ISTYEEELSKAREELSRLQQETAQLEESVESGKAQ 510
Cdd:pfam10473   2 EKKQLHVLEKLKESERKADSLKDKVENLERELeMSEENQelaileAENSKAEVETLKAEIEEMAQNLRDLELDLVTLRSE 81
                          90       100
                  ....*....|....*....|.
gi 1958776456 511 LEPLQQHLQDSQQEISSMQMR 531
Cdd:pfam10473  82 KENLTKELQKKQERVSELESL 102
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
368-524 4.20e-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: 47.35  E-value: 4.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  368 IKELDTLNNEI----IDLQREKNNVEQDLKEKEdTVRQRTTEAQDLQDEV------QRESLNLQKLQAQKQQVQELLD-- 435
Cdd:TIGR00606  743 EKEIPELRNKLqkvnRDIQRLKNDIEEQETLLG-TIMPEEESAKVCLTDVtimerfQMELKDVERKIAQQAAKLQGSDld 821
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  436 ----ELDEQKAQLEEQLK------EVRKKCAEEAQ-LISSLKA---EITSQESQISTYEEELSKAREELSRLQQETAQLE 501
Cdd:TIGR00606  822 rtvqQVNQEKQEKQHELDtvvskiELNRKLIQDQQeQIQHLKSktnELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLI 901
                          170       180
                   ....*....|....*....|...
gi 1958776456  502 ESVESGKAQLEPLQQHLQDSQQE 524
Cdd:TIGR00606  902 REIKDAKEQDSPLETFLEKDQQE 924
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
471-543 4.31e-05

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: 42.94  E-value: 4.31e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958776456 471 SQESQISTYEEELSKAREELSRLQQETAQLEESVEsgkaQLEPLQQHLQDsqqEISSMQMRLAM-----KDLETDNNQ 543
Cdd:cd22887     1 ELESELQELEKRLAELEAELASLEEEIKDLEEELK----EKNKANEILND---ELIALQIENNLleeklRKLQEENDE 71
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
435-533 4.82e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 46.93  E-value: 4.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 435 DELDEQKAQLEEQLKEVRKKcAEEAQL-ISSLKAE--ITSQESQISTYEEELSKAREELSRLQQETAQLEESVESGKAQL 511
Cdd:COG3206   171 EEARKALEFLEEQLPELRKE-LEEAEAaLEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQL 249
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1958776456 512 EPLQQH---------LQDSQQEISSMQMRLA 533
Cdd:COG3206   250 GSGPDAlpellqspvIQQLRAQLAELEAELA 280
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
434-545 5.07e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.98  E-value: 5.07e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  434 LDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAEITSQESQISTYEEELSKAREE-------LSRLQQETAQLEESVES 506
Cdd:TIGR02169  683 LEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERleeleedLSSLEQEIENVKSELKE 762
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1958776456  507 GKAQLEPLQQHLQDSQQEISSMQMRLAMKDLETDNNQSN 545
Cdd:TIGR02169  763 LEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELS 801
PRK12704 PRK12704
phosphodiesterase; Provisional
367-512 5.50e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 46.69  E-value: 5.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 367 AIKELDTLNNEIIDLQREKNnveQDLKEK-EDTVRQRTTEAQDLQDEV-QREslnlqklqaqkqqvqELLDELDEQKAQL 444
Cdd:PRK12704   47 AKKEAEAIKKEALLEAKEEI---HKLRNEfEKELRERRNELQKLEKRLlQKE---------------ENLDRKLELLEKR 108
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 445 EEQLKEVRKKCAEEAQLISSLKAEItsqESQISTYEEELskarEELSRLQQETA--QLEESVESgKAQLE 512
Cdd:PRK12704  109 EEELEKKEKELEQKQQELEKKEEEL---EELIEEQLQEL----ERISGLTAEEAkeILLEKVEE-EARHE 170
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
53-189 6.04e-05

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 43.63  E-value: 6.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  53 LGKIWDLADTDGKGVLNKQEFfIALRLVACAQnglevslsslnLAVPPPRFHDSSsplLTSGTSVAELPWAVKSEDKAKY 132
Cdd:COG5126     7 LDRRFDLLDADGDGVLERDDF-EALFRRLWAT-----------LFSEADTDGDGR---ISREEFVAGMESLFEATVEPFA 71
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958776456 133 DAIFDSLSP-VDGFLSGDKVKPVLLNSKLPVEILGRVWELSDIDHDGKLDRDEFAVAM 189
Cdd:COG5126    72 RAAFDLLDTdGDGKISADEFRRLLTALGVSEEEADELFARLDTDGDGKISFEEFVAAV 129
PRK09039 PRK09039
peptidoglycan -binding protein;
369-542 6.50e-05

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 46.11  E-value: 6.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 369 KELDTLNNEIIDLQrEKNNVEQDlkekedtvrqrttEAQDLQDEVQRESLNLQKLQAQKQQVQELLDELDEQKAQLEEQL 448
Cdd:PRK09039   53 SALDRLNSQIAELA-DLLSLERQ-------------GNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRA 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 449 KEVRKKCAEEAQLisslkaeitSQEsqistyeeelskAREELSRLQQETAQLeesvesgKAQLEPLQQHLQDSQQEISSM 528
Cdd:PRK09039  119 GELAQELDSEKQV---------SAR------------ALAQVELLNQQIAAL-------RRQLAALEAALDASEKRDRES 170
                         170
                  ....*....|....
gi 1958776456 529 QMRLAmkDLETDNN 542
Cdd:PRK09039  171 QAKIA--DLGRRLN 182
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
374-532 6.87e-05

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 46.71  E-value: 6.87e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  374 LNNEIIDLQREKNNVEQDLKEKEDTvRQR------TTEAQ--DLQDEV-----QRESLNLQKlqaqkQqvqelldeldeq 440
Cdd:pfam01576   94 LQNEKKKMQQHIQDLEEQLDEEEAA-RQKlqlekvTTEAKikKLEEDIllledQNSKLSKER-----K------------ 155
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  441 kaQLEEQLKEVRKKCAEEAQLISSLKAEITSQESQISTYEEEL---SKAREELS----RLQQETAQLEESVESGKAQLEP 513
Cdd:pfam01576  156 --LLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLkkeEKGRQELEkakrKLEGESTDLQEQIAELQAQIAE 233
                          170
                   ....*....|....*....
gi 1958776456  514 LQQHLQDSQQEISSMQMRL 532
Cdd:pfam01576  234 LRAQLAKKEEELQAALARL 252
Tektin pfam03148
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ...
369-530 9.67e-05

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: 45.62  E-value: 9.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 369 KELDTLNNEIIDLQREKNNVEQDLKEKED---------TVRQRTTEAqDL-QDEVQRESLNlqklqaqkqqVQELL---- 434
Cdd:pfam03148  64 KELEELDEEIELLLEEKRRLEKALEALEEplhiaqeclTLREKRQGI-DLvHDEVEKELLK----------EVELIegiq 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 435 DELDEQKAQLEEQL---KEVRKKCA------EEAQLI----------S---SLKAEITSQESQISTYEEELSKAREELSR 492
Cdd:pfam03148 133 ELLQRTLEQAWEQLrllRAARHKLEkdlsdkKEALEIdekclslnntSpniSYKPGPTRIPPNSSTPEEWEKFTQDNIER 212
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958776456 493 LQQE---TAQLEESVESGKAQ--------------------------LEPLQQHLQDSQQEISSMQM 530
Cdd:pfam03148 213 AEKEraaSAQLRELIDSILEQtandlraqadavnfalrkrieetedaKNKLEWQLKKTLQEIAELEK 279
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
368-502 1.03e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.83  E-value: 1.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 368 IKELDTLNNEIIDLQreknNVEQDLKEKEDTVRQRTTEAQDLQDEVQRESlnlqklqaqkQQVQELLDELDE-QKAQLEE 446
Cdd:PRK03918  594 LKELEPFYNEYLELK----DAEKELEREEKELKKLEEELDKAFEELAETE----------KRLEELRKELEElEKKYSEE 659
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958776456 447 QLKEVRKKCAEEAQLISSLKAEITSQESQISTYE----------EELSKAREELSRLQQETAQLEE 502
Cdd:PRK03918  660 EYEELREEYLELSRELAGLRAELEELEKRREEIKktleklkeelEEREKAKKELEKLEKALERVEE 725
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
434-533 1.10e-04

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: 43.79  E-value: 1.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 434 LDELDEQKAQLEEQL----KEVRKKCAEEAQ-LISSLKAEITSQESQISTYEEELSK--------AREELSRLQQE-TAQ 499
Cdd:pfam01442   6 LDELSTYAEELQEQLgpvaQELVDRLEKETEaLRERLQKDLEEVRAKLEPYLEELQAklgqnveeLRQRLEPYTEElRKR 85
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1958776456 500 LEESVESGKAQLEPLQQHLQDS-QQEISSMQMRLA 533
Cdd:pfam01442  86 LNADAEELQEKLAPYGEELRERlEQNVDALRARLA 120
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
433-543 1.13e-04

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: 43.77  E-value: 1.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 433 LLD---ELDEQKAQLEEQLKEVRKKC-AEEAQLISSLKAEITSQESQISTYEEELSKAR--------------EELSRLQ 494
Cdd:pfam08614  12 LLDrtaLLEAENAKLQSEPESVLPSTsSSKLSKASPQSASIQSLEQLLAQLREELAELYrsrgelaqrlvdlnEELQELE 91
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958776456 495 QET--------------AQLEESVESGKAQLEPLQQHLQDSQQEISSMQMRLAM-----KDLETDNNQ 543
Cdd:pfam08614  92 KKLrederrlaaleaerAQLEEKLKDREEELREKRKLNQDLQDELVALQLQLNMaeeklRKLEKENRE 159
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
369-527 1.18e-04

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 45.78  E-value: 1.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 369 KELDTLNNEIIDLQREKNNVEQDLKEKEDTVRQRTTE--AQDLQDEVQRESLNLQKLQAQKQQVQELLDELDEQKAQLEE 446
Cdd:TIGR04523 517 KKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFElkKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEK 596
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 447 QLKEVRKKCAEEAQLISSLKAEITSQESQISTYEEELSKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQDSQQEIS 526
Cdd:TIGR04523 597 EKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKID 676

                  .
gi 1958776456 527 S 527
Cdd:TIGR04523 677 D 677
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
434-500 1.37e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 45.21  E-value: 1.37e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958776456 434 LDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAEITSQESQISTYEEELSKAREELSRLQQETAQL 500
Cdd:COG3883    25 LSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
369-502 1.42e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.44  E-value: 1.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 369 KELDTLNNEIIDLQREKNNVEQDLKEKEDtVRQRTTEAQDLQ--------DEVQRESLNLQKLQAQKQqvqELLDELDEQ 440
Cdd:PRK03918  338 ERLEELKKKLKELEKRLEELEERHELYEE-AKAKKEELERLKkrltgltpEKLEKELEELEKAKEEIE---EEISKITAR 413
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 441 KAQLE----------EQLKEVRKKCA---------EEAQLISSLKAEITSQESQISTYEEELSKAREELSRLQQETAQLE 501
Cdd:PRK03918  414 IGELKkeikelkkaiEELKKAKGKCPvcgrelteeHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKES 493

                  .
gi 1958776456 502 E 502
Cdd:PRK03918  494 E 494
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
433-532 1.47e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.53  E-value: 1.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 433 LLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAEITSQESQISTYEEELSKAREELSRLQQETAQLEESVE--SGKAQ 510
Cdd:COG4717    47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEklEKLLQ 126
                          90       100
                  ....*....|....*....|..
gi 1958776456 511 LEPLQQHLQDSQQEISSMQMRL 532
Cdd:COG4717   127 LLPLYQELEALEAELAELPERL 148
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
338-518 1.48e-04

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


Pssm-ID: 430783 [Multi-domain]  Cd Length: 618  Bit Score: 45.52  E-value: 1.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 338 SLTPEMIPPSDKSSLQKNTIGSSPVAdfSAIKELDTLNNEIIDLQ-REKNNVEQDLKEKEDTVRQ------------RTT 404
Cdd:pfam09731 265 SIFPDIIPVLKEDNLLSNDDLNSLIA--HAHREIDQLSKKLAELKkREEKHIERALEKQKEELDKlaeelsarleevRAA 342
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 405 EAQDLQDEVQRE----------SLNLQKLQAQKQQVQELLDELDEQKAQLE-EQLKEVRKKCAEEAQLISSLKAEITSQE 473
Cdd:pfam09731 343 DEAQLRLEFEREreeiresyeeKLRTELERQAEAHEEHLKDVLVEQEIELQrEFLQDIKEKVEEERAGRLLKLNELLANL 422
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958776456 474 SQISTYEEELSKAREELSRLQQETA---QLEESVESGKA--QLEPLQQHL 518
Cdd:pfam09731 423 KGLEKATSSHSEVEDENRKAQQLWLaveALRSTLEDGSAdsRPRPLVREL 472
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
377-544 1.49e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 45.44  E-value: 1.49e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  377 EIID-------LQREKnnveQDLKEKEDTVRQRTTEAQDLQDEVQREslnlqklqaqkqqvqelLDELDEQKAQLEEQLK 449
Cdd:TIGR02169  157 KIIDeiagvaeFDRKK----EKALEELEEVEENIERLDLIIDEKRQQ-----------------LERLRREREKAERYQA 215
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  450 EVRKKCAEEAQLIS----SLKAEITSQESQISTYEEELSKAREELSRLQQETAQLE----------------------ES 503
Cdd:TIGR02169  216 LLKEKREYEGYELLkekeALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEqlleelnkkikdlgeeeqlrvkEK 295
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1958776456  504 VESGKAQLEPLQQHLQDSQQEISSMQMRLAMKDLETDNNQS 544
Cdd:TIGR02169  296 IGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLA 336
DUF4515 pfam14988
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ...
395-530 1.71e-04

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: 43.60  E-value: 1.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 395 KEDTVRQRTTEA---QDLQD--EVQRESlnlqklqaqkqqvQELLDELDEQKAQLEEQLKEVRKkcaEEAQLISSLKA-- 467
Cdd:pfam14988  11 KKTEEKQKKIEKlwnQYVQEceEIERRR-------------QELASRYTQQTAELQTQLLQKEK---EQASLKKELQAlr 74
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958776456 468 EIT----SQESQISTYEEELSKAREELSRLQQETaqleesvesgKAQLEPLQQHLQDSQQEISSMQM 530
Cdd:pfam14988  75 PFAklkeSQEREIQDLEEEKEKVRAETAEKDREA----------HLQFLKEKALLEKQLQELRILEL 131
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
371-523 1.75e-04

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: 43.02  E-value: 1.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 371 LDTLNNEIIDLQREKNNVEQDLKEKedtvrqRTTEAQDLQDEVQREslnlqklqaqkqqvqelldeLDEQKAQLEEQLKE 450
Cdd:pfam01442   6 LDELSTYAEELQEQLGPVAQELVDR------LEKETEALRERLQKD--------------------LEEVRAKLEPYLEE 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 451 VRKKCAEEAQLissLKAEItsqESQISTYEEELSKAREELSR----LQQETAQ-LEESVESGKAQLEP--------LQQH 517
Cdd:pfam01442  60 LQAKLGQNVEE---LRQRL---EPYTEELRKRLNADAEELQEklapYGEELRErLEQNVDALRARLAPyaeelrqkLAER 133

                  ....*.
gi 1958776456 518 LQDSQQ 523
Cdd:pfam01442 134 LEELKE 139
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
348-532 1.76e-04

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 45.10  E-value: 1.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 348 DKSSLQKNTIGSSPVADFSAIKELDTLNneiIDLQRE---KNNVEQDLKEKEDTVRQRTTEAQDLQDEVQRESLNLQKLQ 424
Cdd:pfam05483 275 EKTKLQDENLKELIEKKDHLTKELEDIK---MSLQRSmstQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVV 351
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 425 AQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAEITSQESQISTYEEELSKAREELSRLQQETAQLEESV 504
Cdd:pfam05483 352 TEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIA 431
                         170       180
                  ....*....|....*....|....*...
gi 1958776456 505 ESGKAQLEPLQQHLQDSQQEISSMQMRL 532
Cdd:pfam05483 432 EELKGKEQELIFLLQAREKEIHDLEIQL 459
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
365-545 1.90e-04

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


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 44.95  E-value: 1.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 365 FSAIKELD---TLNNEIIDLQREKNNVEQDLKEKEDTVRQRTTEAQDLQD--EVQRESLNLQKLQAQKQqVQELLDEL-- 437
Cdd:COG5185   335 ETGIQNLTaeiEQGQESLTENLEAIKEEIENIVGEVELSKSSEELDSFKDtiESTKESLDEIPQNQRGY-AQEILATLed 413
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 438 -----DEQKAQLEEQLKEVRKKCAEEAQLISSLKAEIT---------SQESQISTYEEELSKAREELSRLQQETAQLEES 503
Cdd:COG5185   414 tlkaaDRQIEELQRQIEQATSSNEEVSKLLNELISELNkvmreadeeSQSRLEEAYDEINRSVRSKKEDLNEELTQIESR 493
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1958776456 504 VESGKAQLEPLQQHLQDSQQEISSM--QMRLAMKDLETDNNQSN 545
Cdd:COG5185   494 VSTLKATLEKLRAKLERQLEGVRSKldQVAESLKDFMRARGYAH 537
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
440-529 2.02e-04

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 44.27  E-value: 2.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 440 QKAQLEEQLKEVrkkcaEEAQLISSLKAEITSQESQISTYEEELSKAREELSRL----------QQETAQLEESVESGKA 509
Cdd:COG1566    88 AEAQLAAAEAQL-----ARLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYqalykkgavsQQELDEARAALDAAQA 162
                          90       100
                  ....*....|....*....|
gi 1958776456 510 QLEPLQQHLQDSQQEISSMQ 529
Cdd:COG1566   163 QLEAAQAQLAQAQAGLREEE 182
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
372-576 2.10e-04

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


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 44.89  E-value: 2.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 372 DTLNNEIIDLQREKNNVEQDLKEKEDTVR-------QRTTEAQDLQDEVQRESLNLQKLQAQKQQVQELLDELDEQKAQL 444
Cdd:pfam07888 111 EELSEEKDALLAQRAAHEARIRELEEDIKtltqrvlERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSL 190
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 445 EEQLKEVRKKCAEEAQLISSLKAEITSQESQIST---YEEELSKAREELSRLQQETAQLEESVESGKAQLEPL------- 514
Cdd:pfam07888 191 SKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTahrKEAENEALLEELRSLQERLNASERKVEGLGEELSSMaaqrdrt 270
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958776456 515 -----QQHLQDSQQEISSMQMRLAMKDletdnNQSNWCSSPQSILVNGAADYCSLSTSSSETANLNE 576
Cdd:pfam07888 271 qaelhQARLQAAQLTLQLADASLALRE-----GRARWAQERETLQQSAEADKDRIEKLSAELQRLEE 332
DUF1090 pfam06476
Protein of unknown function (DUF1090); This family consists of several bacterial proteins of ...
440-488 2.18e-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: 2.18e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1958776456 440 QKAQLEEQLKEVRKKCAeEAQLISSLKAEITSQESQISTYEEELSKARE 488
Cdd:pfam06476  39 RVAGLEKALAEVRAHCT-DAGLRAERQQKVAEKREEVAEREAELAEAQA 86
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
369-532 2.23e-04

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 44.13  E-value: 2.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 369 KELDTLNNEIIDLQREKNNVEQ---DLKEKEDTVRQRT----TEAQDLQDEvqRESLNlqklqAQKQQVQELLDELDEQK 441
Cdd:COG1340    15 EKIEELREEIEELKEKRDELNEelkELAEKRDELNAQVkelrEEAQELREK--RDELN-----EKVKELKEERDELNEKL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 442 AQLEEQLKEVRKKCAEEAQL---ISSLKAEITSQESQISTyeEELSKAREElsRLQQETAQLEESVESGKAQLEpLQQHL 518
Cdd:COG1340    88 NELREELDELRKELAELNKAggsIDKLRKEIERLEWRQQT--EVLSPEEEK--ELVEKIKELEKELEKAKKALE-KNEKL 162
                         170
                  ....*....|....
gi 1958776456 519 QDSQQEISSMQMRL 532
Cdd:COG1340   163 KELRAELKELRKEA 176
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
374-538 2.27e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 44.82  E-value: 2.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 374 LNNEIID-----LQREKNNVEQ---DLKEKEDTVRQRTTEAQDLQDEVQReslnlqklqaqkqqvqeLLDELDEQKAQLE 445
Cdd:PRK00409  499 LPENIIEeakklIGEDKEKLNEliaSLEELERELEQKAEEAEALLKEAEK-----------------LKEELEEKKEKLQ 561
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 446 EQLKEVRKKCAEEAQ-LISSLKAEI---------------TSQESQISTYE-EELSKAREELSRLQQETAQLEESVESG- 507
Cdd:PRK00409  562 EEEDKLLEEAEKEAQqAIKEAKKEAdeiikelrqlqkggyASVKAHELIEArKRLNKANEKKEKKKKKQKEKQEELKVGd 641
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1958776456 508 KAQLEPLQQHLQ--------DSQQEISSMQMRLAMKDLE 538
Cdd:PRK00409  642 EVKYLSLGQKGEvlsipddkEAIVQAGIMKMKVPLSDLE 680
DUF3450 pfam11932
Protein of unknown function (DUF3450); This family of proteins are functionally ...
432-525 2.28e-04

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: 43.76  E-value: 2.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 432 ELLDELDEQKAQLEEQLKevrkkcaeeaqlisSLKAEITSQESQISTYEEELSKAREELSRLQQETAQLEEsvesGKAQL 511
Cdd:pfam11932  34 KKIDKWDDEKQELLAEYR--------------ALKAELESLEVYNRQLERLVASQEQEIASLERQIEEIER----TEREL 95
                          90
                  ....*....|....
gi 1958776456 512 EPLQQHLQDSQQEI 525
Cdd:pfam11932  96 VPLMLKMLDRLEQF 109
FapA pfam03961
Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta ...
436-509 2.40e-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: 43.83  E-value: 2.40e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958776456 436 ELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAEITSQ-----ESQISTYEEELSKAREELSRLQQETAQLEESVESGKA 509
Cdd:pfam03961 153 ELKEKLEELEKELEELEEELEKLKKRLKKLPKKARGQlppekREQLEKLLETKNKLSEELEELEEELKELKEELESLLG 231
Tektin pfam03148
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ...
376-540 2.65e-04

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: 44.08  E-value: 2.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 376 NEIIDL-QREKNNVEQdLKEKEDTVRQRTteAQDLQDevQRESLNlqklqaqkqqvqELLD----ELDEQKAQLEEQLKE 450
Cdd:pfam03148 207 QDNIERaEKERAASAQ-LRELIDSILEQT--ANDLRA--QADAVN------------FALRkrieETEDAKNKLEWQLKK 269
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 451 VRKKCAEEAQLISSLKAEITSQESQI----STYEEELSKAREEL------SRLQQETAQLEESVESgkaqlepLQQHLQD 520
Cdd:pfam03148 270 TLQEIAELEKNIEALEKAIRDKEAPLklaqTRLENRTYRPNVELcrdeaqYGLVDEVKELEETIEA-------LKQKLAE 342
                         170       180
                  ....*....|....*....|
gi 1958776456 521 SQQEISSMQMRLAmkDLETD 540
Cdd:pfam03148 343 AEASLQALERTRL--RLEED 360
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
368-524 2.90e-04

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 44.57  E-value: 2.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  368 IKELDTLNNEIidlQREKNNVEQDLKEKEDTVRQRTTEAQDLQDEV--------QRESLNLQKLQAQKQQVQELLDELDE 439
Cdd:TIGR00618  713 IEEYDREFNEI---ENASSSLGSDLAAREDALNQSLKELMHQARTVlkarteahFNNNEEVTAALQTGAELSHLAAEIQF 789
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  440 QKAQLEEQLKEVRKKCAEEAQLISSLKAEITSQESQISTYEEELSKAREELSRLQQE-TAQLEESVESGKAQLEPLQQHL 518
Cdd:TIGR00618  790 FNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEiTHQLLKYEECSKQLAQLTQEQA 869

                   ....*.
gi 1958776456  519 QDSQQE 524
Cdd:TIGR00618  870 KIIQLS 875
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
389-533 2.99e-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: 2.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 389 EQDLKEKEDTVRQRTTEAQDLQDEvqreslnlqklqaqkqqvqelLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAE 468
Cdd:COG3883    15 DPQIQAKQKELSELQAELEAAQAE---------------------LDALQAELEELNEEYNELQAELEALQAEIDKLQAE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 469 ITSQESQISTYEEELSK-AREE----------------------------LSRLQQETAQLEESVESGKAQLEPLQQHLQ 519
Cdd:COG3883    74 IAEAEAEIEERREELGErARALyrsggsvsyldvllgsesfsdfldrlsaLSKIADADADLLEELKADKAELEAKKAELE 153
                         170
                  ....*....|....
gi 1958776456 520 DSQQEISSMQMRLA 533
Cdd:COG3883   154 AKLAELEALKAELE 167
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
368-532 3.02e-04

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 44.24  E-value: 3.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 368 IKELDTLNNEIIDLQREKNNVEQDLKEKEDTVRQRTTEAQDLQDEVQ----RESLNLQKLQAQKQQVQELLDELDEQKAQ 443
Cdd:TIGR04523  39 EKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKdlndKLKKNKDKINKLNSDLSKINSEIKNDKEQ 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 444 ----------LEEQLKEVRKKCA--------EEAQL-------------ISSLKAEITSQESQISTYEEELSKAREELSR 492
Cdd:TIGR04523 119 knklevelnkLEKQKKENKKNIDkflteikkKEKELeklnnkyndlkkqKEELENELNLLEKEKLNIQKNIDKIKNKLLK 198
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958776456 493 -----------------LQQETAQLEESVESGKAQLEPLQQHLQDSQQEISSMQMRL 532
Cdd:TIGR04523 199 lelllsnlkkkiqknksLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQL 255
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
432-530 3.09e-04

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 44.56  E-value: 3.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  432 ELLDELDEQKAQLEEQLKEVrkkcAEEAQLISSLKAEITSQESQISTYEEELSKAREELSRLQQETAQleesvesgkAQL 511
Cdd:PRK11448   146 ALQQEVLTLKQQLELQAREK----AQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAE---------TSQ 212
                           90
                   ....*....|....*....
gi 1958776456  512 EPLQQHLQDSQQEISSMQM 530
Cdd:PRK11448   213 ERKQKRKEITDQAAKRLEL 231
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
370-543 5.06e-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: 43.67  E-value: 5.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  370 ELDTLNNEIIDLQREKNNVEQDLK----EKEDTVRQRTTEAQDLQDEVQRESLNLqklqaqkqqvqelLDELDEQKAQLE 445
Cdd:pfam12128  676 RKDSANERLNSLEAQLKQLDKKHQawleEQKEQKREARTEKQAYWQVVEGALDAQ-------------LALLKAAIAARR 742
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  446 EQLKEVRKKCAEE-----------AQLISSLKAEITSQESQIS-------------------------TYEEELSKAREE 489
Cdd:pfam12128  743 SGAKAELKALETWykrdlaslgvdPDVIAKLKREIRTLERKIEriavrrqevlryfdwyqetwlqrrpRLATQLSNIERA 822
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958776456  490 LSRLQQETAQLEESVESGKAQLEPLQQHLQDSQQEIS-------SMQMRLAMKDLETDNNQ 543
Cdd:pfam12128  823 ISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSenlrglrCEMSKLATLKEDANSEQ 883
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
476-544 5.23e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.35  E-value: 5.23e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958776456 476 ISTYEEELSKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQDSQQEISSMQMRLAMKDLETDNNQS 544
Cdd:COG4372    26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQA 94
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
368-512 5.35e-04

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 42.98  E-value: 5.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 368 IKELdtlnNEIIDLQREKNNVEQDLKEKEDTVRQRTTEAQDLQDEVQreslnlqklqaqkqQVQELLDELDEQKAQLEEQ 447
Cdd:COG1340   142 IKEL----EKELEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIK--------------ELAEEAQELHEEMIELYKE 203
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958776456 448 LKEVRKKcAEEA-QLISSLKAEITSQESQISTYEEELSKAREELSRLQQETAQLEESVESGKAQLE 512
Cdd:COG1340   204 ADELRKE-ADELhKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEK 268
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
369-530 5.39e-04

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


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 43.66  E-value: 5.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 369 KELDTLNNEIIDLQREKNN-------VEQDLKEKEdtvrqRTTEAqdLQDEVQREslnlqklqaqkqqVQELLDELDeqk 441
Cdd:pfam10174 415 KQLAGLKERVKSLQTDSSNtdtalttLEEALSEKE-----RIIER--LKEQRERE-------------DRERLEELE--- 471
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 442 aQLEEQLKEVRKKcaeeaqlISSLKAEITSQESQISTYEEELSKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQDS 521
Cdd:pfam10174 472 -SLKKENKDLKEK-------VSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKA 543

                  ....*....
gi 1958776456 522 QQEISSMQM 530
Cdd:pfam10174 544 HNAEEAVRT 552
Nnf1 pfam03980
Nnf1; NNF1 is an essential yeast gene that is necessary for chromosome segregation. It is ...
432-507 5.60e-04

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: 39.92  E-value: 5.60e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958776456 432 ELLDELDEqkaqLEEQLKEvRKKCAEEAQLISSLKAE--ITSQESqiSTYEEELSKAREELSRLQQETAQLEESVESG 507
Cdd:pfam03980  33 AKLNELDE----LIEEAKE-RREEGEGPAWRPSVPPEelIRAHLA--PYKQKQLEQLNARLQKLEAENAALAEEVQAQ 103
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
471-543 5.62e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.21  E-value: 5.62e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958776456 471 SQESQISTYEEELSKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQDSQQEISSMQMRLAMKDLETDNNQ 543
Cdd:COG4942    17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
345-500 5.86e-04

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: 41.46  E-value: 5.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 345 PPSDKSSLQKNTIGSSPVADFSAikELDTLNNEIIDLQREKNNVEQDLKEKEDTVrqrtteaQDLQDEVQRESlnlqklq 424
Cdd:pfam08614  35 PSTSSSKLSKASPQSASIQSLEQ--LLAQLREELAELYRSRGELAQRLVDLNEEL-------QELEKKLREDE------- 98
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958776456 425 aqkqqvqELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAEITSqeSQIstyeeELSKAREELSRLQQETAQL 500
Cdd:pfam08614  99 -------RRLAALEAERAQLEEKLKDREEELREKRKLNQDLQDELVA--LQL-----QLNMAEEKLRKLEKENREL 160
UPF0242 pfam06785
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ...
432-528 6.63e-04

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: 41.73  E-value: 6.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 432 ELLDELDEQKAQLEEQL----KEVRKKCAEEAQLISSLKAEITSQESQISTYEEELSKAREELSRLQQETAQLEESVESG 507
Cdd:pfam06785  90 ETLEELQSEEERLEEELsqkeEELRRLTEENQQLQIQLQQISQDFAEFRLESEEQLAEKQLLINEYQQTIEEQRSVLEKR 169
                          90       100
                  ....*....|....*....|.
gi 1958776456 508 KAQLEPLQQHLQDSQQEISSM 528
Cdd:pfam06785 170 QDQIENLESKVRDLNYEIKTL 190
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
385-539 6.67e-04

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: 41.97  E-value: 6.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 385 KNNVEQDLKEKEDTVRQRTTEAQDLQDEVQRESLNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEaqLISS 464
Cdd:pfam04012  10 RANIHEGLDKAEDPEKMLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGNEE--LARE 87
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958776456 465 LKAEITSQESQISTYEEELSKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQdSQQEISSMQMRLAMKDLET 539
Cdd:pfam04012  88 ALAEKKSLEKQAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKARLK-AAKAQEAVQTSLGSLSTSS 161
FliJ pfam02050
Flagellar FliJ protein;
434-529 7.01e-04

Flagellar FliJ protein;


Pssm-ID: 426581 [Multi-domain]  Cd Length: 123  Bit Score: 40.34  E-value: 7.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 434 LDELDEQKAQLEEQLKEVRKKCAEEA-----QLISSLKAEITSQESQISTYEEELSKAREELSRLQQEtaqlEESVE--S 506
Cdd:pfam02050  21 LEELQQYRAEYQQQLSGAGQGISAAElrnyqAFISQLDEAIAQQQQELAQAEAQVEKAREEWQEARQE----RKSLEklR 96
                          90       100
                  ....*....|....*....|....*...
gi 1958776456 507 GKAQLEplQQHLQDSQQ-----EISSMQ 529
Cdd:pfam02050  97 EREKKE--ERKEQNRREqkqldELAARL 122
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
380-532 7.36e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.11  E-value: 7.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 380 DLQREKNNVeqdLKEKEDTVRQRttEAQDLQDevqreSLNLQKLQAQKQQvqELLDELDEQKAQLEEQL---KEVRKKCA 456
Cdd:PRK02224  180 RVLSDQRGS---LDQLKAQIEEK--EEKDLHE-----RLNGLESELAELD--EEIERYEEQREQARETRdeaDEVLEEHE 247
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 457 EEAQLISSLKAEITSQESQISTYE-------EELSKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQDSQQEISSMQ 529
Cdd:PRK02224  248 ERREELETLEAEIEDLRETIAETErereelaEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELR 327

                  ...
gi 1958776456 530 MRL 532
Cdd:PRK02224  328 DRL 330
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
374-540 7.59e-04

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: 41.59  E-value: 7.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 374 LNNEIIDLQRE----KNNVEQDLKEK---EDTVRQRTTEAQDLQDEVQrESLNLQKLqaqkqqvqELLDELDEQKAQLEE 446
Cdd:pfam04012  27 LEQAIRDMQSElvkaRQALAQTIARQkqlERRLEQQTEQAKKLEEKAQ-AALTKGNE--------ELAREALAEKKSLEK 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 447 QLKEVRKKCAEEAQLISSLKAEITSQESQISTYEeelSKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQDSQQEIS 526
Cdd:pfam04012  98 QAEALETQLAQQRSAVEQLRKQLAALETKIQQLK---AKKNLLKARLKAAKAQEAVQTSLGSLSTSSATDSFERIEEKIE 174
                         170
                  ....*....|....*
gi 1958776456 527 SMQMRL-AMKDLETD 540
Cdd:pfam04012 175 EREARAdAAAELASA 189
Rcc_KIF21 cd22248
regulatory coiled-coil domain found in the kinesin-like KIF21 family; The KIF21 family ...
481-530 8.01e-04

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: 39.11  E-value: 8.01e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 481 EELSKAREELSR----------LQQETAQLEESVESGKAQLEPLQQHLQDSQQEIssMQM 530
Cdd:cd22248    20 EKLSKELEKLEKkreraldegkDESVLRDLEEEIDSLKANIDYVQENITECQSNI--MQM 77
mukB PRK04863
chromosome partition protein MukB;
369-541 8.44e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 43.02  E-value: 8.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  369 KELDTLNNEIIDLQREKNNVEQdLKEKEDTVRQRtteAQDLQDEVQR-ESLNLQKLQAQKQQVQELLDELDEQKAQLE-- 445
Cdd:PRK04863   925 PIVSVLQSDPEQFEQLKQDYQQ-AQQTQRDAKQQ---AFALTEVVQRrAHFSYEDAAEMLAKNSDLNEKLRQRLEQAEqe 1000
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  446 -----EQLKEVRKKCAEEAQLISSLKaeitsqeSQISTYEEELSKAREELSRLQ-QETAQLEESVESGKaqlEPLQQHLQ 519
Cdd:PRK04863  1001 rtrarEQLRQAQAQLAQYNQVLASLK-------SSYDAKRQMLQELKQELQDLGvPADSGAEERARARR---DELHARLS 1070
                          170       180
                   ....*....|....*....|..
gi 1958776456  520 DSQQEISSMQMRLAMKDLETDN 541
Cdd:PRK04863  1071 ANRSRRNQLEKQLTFCEAEMDN 1092
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
383-532 9.62e-04

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 43.03  E-value: 9.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  383 REKNNVEQDLkEKEDTVRQRTTEAQDLQDEV--QRESLNLQKLQAQKQQVqELLDELDEQKAQLEEQLKEVRKKCAEEAQ 460
Cdd:TIGR00618  163 KEKKELLMNL-FPLDQYTQLALMEFAKKKSLhgKAELLTLRSQLLTLCTP-CMPDTYHERKQVLEKELKHLREALQQTQQ 240
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958776456  461 LISSLKAEITSQESQiSTYEEELSKAREELSRLQQETAQLEESVES-----GKAQLEPLQQHLQDSQQEISSMQMRL 532
Cdd:TIGR00618  241 SHAYLTQKREAQEEQ-LKKQQLLKQLRARIEELRAQEAVLEETQERinrarKAAPLAAHIKAVTQIEQQAQRIHTEL 316
End3 pfam12761
Actin cytoskeleton-regulatory complex protein END3; Endocytosis is accomplished through the ...
350-494 1.02e-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: 41.13  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 350 SSLQKNTIG--SSPVADFSAIKELDtlnNEIIDLQREKNNVEQDLKEKEDTVRQRTTEAQDLQDE---VQREslnlqklq 424
Cdd:pfam12761  73 SYLSRLGVGgrSEKGTDFSATKGTD---WEEVRLKRELAELEEKLEKVEQAASKRRGGNRDESSKpalVKRE-------- 141
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958776456 425 aqkqqvqelLDELDEQKaqlEEQLKEVR--KKCAEEAQLiSSLKAEITSQESQISTYEEELSKAREELSRLQ 494
Cdd:pfam12761 142 ---------FEQLLDYK---ERQLRELEegSGKSKPINL-KSVREDIDTVEEQVDGLESHLSSRKQELQQLR 200
mukB PRK04863
chromosome partition protein MukB;
434-533 1.06e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 43.02  E-value: 1.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  434 LDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAEITSQESQISTYEEELSKAREELSRLQ-----QE------------ 496
Cdd:PRK04863   281 RRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQtalrqQEkieryqadleel 360
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1958776456  497 TAQLEES---VESGKAQLEPLQQHLQDSQQEISSMQMRLA 533
Cdd:PRK04863   361 EERLEEQnevVEEADEQQEENEARAEAAEEEVDELKSQLA 400
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
377-532 1.13e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.72  E-value: 1.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 377 EIIDLQREKNNVEQDLkEKEDTVRQRTTEAQDLQDEVQRESLNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVR---- 452
Cdd:PRK02224  573 EVAELNSKLAELKERI-ESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARieea 651
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 453 ---KKCAEEAQL-----ISSLKAEITSQESQISTYEEELskarEELSRLQQETAQLEESVESgkaqLEPlqqhLQDSQQE 524
Cdd:PRK02224  652 redKERAEEYLEqveekLDELREERDDLQAEIGAVENEL----EELEELRERREALENRVEA----LEA----LYDEAEE 719

                  ....*...
gi 1958776456 525 ISSMQMRL 532
Cdd:PRK02224  720 LESMYGDL 727
PRK11637 PRK11637
AmiB activator; Provisional
369-521 1.23e-03

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 41.99  E-value: 1.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 369 KELDTLNNEIIDLQREKNNVEQDLKEKEDTV-RQrtTEAQDLQ-----DEVQRES--------LNLQKLqaqkqqvqELL 434
Cdd:PRK11637  103 KQIDELNASIAKLEQQQAAQERLLAAQLDAAfRQ--GEHTGLQlilsgEESQRGErilayfgyLNQARQ--------ETI 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 435 DELDEQKAQLEEQLKEVRKKCAEEAQLIsslkaeiTSQESQistyEEELSKAREElsrlQQET-AQLEESVESGKAQLEP 513
Cdd:PRK11637  173 AELKQTREELAAQKAELEEKQSQQKTLL-------YEQQAQ----QQKLEQARNE----RKKTlTGLESSLQKDQQQLSE 237
                         170
                  ....*....|.
gi 1958776456 514 LQQH---LQDS 521
Cdd:PRK11637  238 LRANesrLRDS 248
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
446-535 1.26e-03

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


Pssm-ID: 284517 [Multi-domain]  Cd Length: 749  Bit Score: 42.43  E-value: 1.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 446 EQLKEVRKKCAEEAQLISSL-KAEITSQESQISTYEEELSKAREELsrlQQETAQLEESVESGKAQLEPLQQHLQDSQQE 524
Cdd:pfam07111 484 EQLREERNRLDAELQLSAHLiQQEVGRAREQGEAERQQLSEVAQQL---EQELQRAQESLASVGQQLEVARQGQQESTEE 560
                          90
                  ....*....|.
gi 1958776456 525 ISSMQMRLAMK 535
Cdd:pfam07111 561 AASLRQELTQQ 571
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
382-524 1.39e-03

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: 39.13  E-value: 1.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 382 QREKNNVEQDLKEKEDTVRQRtteAQDLQDEVQReslnlqklqaqkqqvqelldeldeqKAQLEEQLKEVRkkcaEEAQL 461
Cdd:pfam20492   5 EREKQELEERLKQYEEETKKA---QEELEESEET-------------------------AEELEEERRQAE----EEAER 52
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958776456 462 I----SSLKAEITSQESQISTYEEELSKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQDSQQE 524
Cdd:pfam20492  53 LeqkrQEAEEEKERLEESAEMEAEEKEQLEAELAEAQEEIARLEEEVERKEEEARRLQEELEEAREE 119
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
374-540 1.40e-03

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 42.40  E-value: 1.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 374 LNNEI---------IDLQREKNNVEQDLKEKEDTvrqrtTEAQDLQDEVQRE--------SLNLQKLQAQKQQVQEL--- 433
Cdd:pfam05483 188 LNNNIekmilafeeLRVQAENARLEMHFKLKEDH-----EKIQHLEEEYKKEindkekqvSLLLIQITEKENKMKDLtfl 262
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 434 LDELDEQKAQLEEQ-------LKEVRKKCAEEAQLISSLKAEITSQESQISTYEEELSKAREELSRLQQET-AQLEES-- 503
Cdd:pfam05483 263 LEESRDKANQLEEKtklqdenLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKeAQMEELnk 342
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958776456 504 -----------VESGKAQLEPL----QQHLQDSQQEISSMQMRLAMKDLETD 540
Cdd:pfam05483 343 akaahsfvvteFEATTCSLEELlrteQQRLEKNEDQLKIITMELQKKSSELE 394
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
361-546 1.48e-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: 42.41  E-value: 1.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  361 PVADfsaikELDTLNNEIID-----LQREKNNVEQ----------DLKEKEDTVRQRTTEAQDLQDEVQRESLNLQKLQA 425
Cdd:pfam15921  242 PVED-----QLEALKSESQNkiellLQQHQDRIEQliseheveitGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYM 316
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  426 QKqqvqelLDELDEQKAQLEEQLKEVRKkcaeeaqlisslkaeitSQESQISTYEEELSKAREELSRLQQETAQLeeSVE 505
Cdd:pfam15921  317 RQ------LSDLESTVSQLRSELREAKR-----------------MYEDKIEELEKQLVLANSELTEARTERDQF--SQE 371
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1958776456  506 SGKA--QLEPLQQHLQDSQQEISsmqmrlamkdLETDNNQSNW 546
Cdd:pfam15921  372 SGNLddQLQKLLADLHKREKELS----------LEKEQNKRLW 404
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
380-540 1.51e-03

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 42.34  E-value: 1.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  380 DLQREKNNVEQDLKEKEDTVRQRTTEAQDLQDEVQreSLNLQKLqaqkqqvqelldELDEQKAQLEEQLKEVRKKCAEE- 458
Cdd:TIGR00606  238 EIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIK--ALKSRKK------------QMEKDNSELELKMEKVFQGTDEQl 303
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  459 AQLISSLKAEITSQESQISTYEEELSKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQDSQQEISSMQMRLAMKDLE 538
Cdd:TIGR00606  304 NDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFE 383

                   ..
gi 1958776456  539 TD 540
Cdd:TIGR00606  384 RG 385
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
376-524 1.52e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 41.43  E-value: 1.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 376 NEIIDLQREKNNVEQDLKEKEDtVRQRTTEAQDLQDEVqreslnlqklqaqkqqvqellDELDEQKAQLEEQLKEVRKKC 455
Cdd:COG1340   140 EKIKELEKELEKAKKALEKNEK-LKELRAELKELRKEA---------------------EEIHKKIKELAEEAQELHEEM 197
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958776456 456 AEEAQLISSLKAEITSQESQISTYEEELSKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQDSQQE 524
Cdd:COG1340   198 IELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELE 266
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
369-521 1.53e-03

Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 41.91  E-value: 1.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 369 KELDTLNNEIIDLQREKNNVEQDLKEKEDTVRQRTTEAQDLQDEVQRESlnlqklqaqkQQVQELLDEldEQKAQLEEQL 448
Cdd:pfam05262 220 EELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADTSS----------PKEDKQVAE--NQKREIEKAQ 287
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958776456 449 KEVRKKcAEEAQLISSLKAEITSQESQISTYEEElSKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQDS 521
Cdd:pfam05262 288 IEIKKN-DEEALKAKDHKAFDLKQESKASEKEAE-DKELEAQKKREPVAEDLQKTKPQVEAQPTSLNEDAIDS 358
Kre28 pfam17097
Spindle pole body component; In Saccharomyces cerevisae Kre28 and Spc105 form a kinetochore ...
369-502 1.54e-03

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


Pssm-ID: 407241 [Multi-domain]  Cd Length: 360  Bit Score: 41.72  E-value: 1.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 369 KELDTLNNEIIDLQREKNNVEQDLKEKEDTVRQRTTEAQDLQDEVQreslnlqklqaqkqqvqELLDELDeqkaQLEEQL 448
Cdd:pfam17097 133 DTLTVLNQEIDQIKGDILQVAQEIADKQDQVNELCLETSNELDECW-----------------ELLNELE----RLRDQR 191
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958776456 449 KEVRKKCAEEAQLISSLKAEITSQESQISTYEEELSKAREELSRLQQETAQLEE 502
Cdd:pfam17097 192 ITVEEQTSNEKDTELDPVEETYEEWKSLQESLQQLEHLKEELDQLQKQKDSLEK 245
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
377-538 1.57e-03

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: 42.04  E-value: 1.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 377 EIIDLQREKNNVEQDLKEKEDTVRQRTTEAQDLQD-EVQRESLNLQK--LQAQKQQVQELLDELDEQKAQLEEQLKEV-- 451
Cdd:pfam05557  28 ARIELEKKASALKRQLDRESDRNQELQKRIRLLEKrEAEAEEALREQaeLNRLKKKYLEALNKKLNEKESQLADAREVis 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 452 --RKKCAEEAQLISSLKAEITSQESQISTYEEELSKAREELSRLQQETAQLEESVESGKAQ------LE-PLQQHLQDSq 522
Cdd:pfam05557 108 clKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAeqrikeLEfEIQSQEQDS- 186
                         170
                  ....*....|....*..
gi 1958776456 523 QEISSMQMRLA-MKDLE 538
Cdd:pfam05557 187 EIVKNSKSELArIPELE 203
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
370-473 1.66e-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: 1.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 370 ELDTLNNEIIDLQREKNNV--EQDLKEKEDTVRQRTTEAQdLQDEVQRESLNLQKLQAQKQQVQELLDELDEQKAQLEEQ 447
Cdd:COG0542   412 ELDELERRLEQLEIEKEALkkEQDEASFERLAELRDELAE-LEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPEL 490
                          90       100
                  ....*....|....*....|....*.
gi 1958776456 448 LKEVRKKCAEEAQLISSLKAEITSQE 473
Cdd:COG0542   491 EKELAELEEELAELAPLLREEVTEED 516
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
349-540 1.70e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 42.08  E-value: 1.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  349 KSSLQKNTIG-SSPVADFSAikELDTLNNEIIDLQREKNNVEQDLKE----KEDTVRQRTtEAQD----LQDEVqrESLN 419
Cdd:pfam01576  372 KANLEKAKQAlESENAELQA--ELRTLQQAKQDSEHKRKKLEGQLQElqarLSESERQRA-ELAEklskLQSEL--ESVS 446
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  420 LqklqaqkqqvqeLLDELDEQK-------AQLEEQLKEVRKKCAEEAQL-------ISSLKAEITSQESQISTYEEELSK 485
Cdd:pfam01576  447 S------------LLNEAEGKNiklskdvSSLESQLQDTQELLQEETRQklnlstrLRQLEDERNSLQEQLEEEEEAKRN 514
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958776456  486 AREELSRLQQETAQLEESVESGKAQLEPLQQHLQDSQQEISSMQMRLAMKDLETD 540
Cdd:pfam01576  515 VERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYD 569
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
389-523 1.75e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 41.43  E-value: 1.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 389 EQDLKEKEDTVRQRTTEAQDLQDEVQRESlnlqklqaqkQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAE 468
Cdd:COG1340    10 LEELEEKIEELREEIEELKEKRDELNEEL----------KELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEE 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958776456 469 itsqesqISTYEEELSKAREELSRLQQETAQLEESVESgKAQLEPLQQHLQDSQQ 523
Cdd:COG1340    80 -------RDELNEKLNELREELDELRKELAELNKAGGS-IDKLRKEIERLEWRQQ 126
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
432-538 1.89e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 41.05  E-value: 1.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 432 ELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAEITSQESQISTYEEELSKAREELSRLQQETAQLEESVESGKAQL 511
Cdd:COG1340    22 EEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKEL 101
                          90       100
                  ....*....|....*....|....*..
gi 1958776456 512 EPLQQhlqdSQQEISSMQMRLAmkDLE 538
Cdd:COG1340   102 AELNK----AGGSIDKLRKEIE--RLE 122
PRK09039 PRK09039
peptidoglycan -binding protein;
445-531 1.91e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 41.49  E-value: 1.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 445 EEQLKEVRKKCAEEAQLISSLKAEITSQESQISTYEEELSKAREELSRLQQETAQLEESVESGKAQLEPLQQHLqDSQQE 524
Cdd:PRK09039   52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQEL-DSEKQ 130

                  ....*..
gi 1958776456 525 ISSMQMR 531
Cdd:PRK09039  131 VSARALA 137
YscO-like pfam16789
YscO-like protein; This family of proteins is similar to the type III secretion protein YscO. ...
381-524 1.95e-03

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: 39.82  E-value: 1.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 381 LQREKNNVEQDLKEKEDTVRQRTTEAQDLQDEVQRESlnlqklqaqkqqVQELLDELDEQKAQLEEQLKEVRKKCAEeaq 460
Cdd:pfam16789  30 LEKEKEKLAELEAERDKVRKHKKAKMQQLRDEMDRGT------------TSDKILQMKRYIKVVKERLKQEEKKVQD--- 94
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958776456 461 lisslkaeitsQESQISTYEEELSKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQDSQQE 524
Cdd:pfam16789  95 -----------QKEQVRTAARNLEIAREELKKKRQEVEKLEKHKKEWVKEMKKEEEDQEEREQD 147
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
369-506 1.99e-03

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


Pssm-ID: 462316 [Multi-domain]  Cd Length: 129  Bit Score: 39.16  E-value: 1.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 369 KELDTLNNEIIDLQREKNNVEQDLKEKEDTVRQRTTEAQDLQDEVQRESLNLQKLQaqkqqvqELLDELDEQKAQLEEQL 448
Cdd:pfam07926   1 AELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQNYERELVLHAEDI-------KALQALREELNELKAEI 73
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958776456 449 KEVRKKcAEEAQliSSLKAEITSQESQISTYEEELSKAREELSRLQQETAQLEESVES 506
Cdd:pfam07926  74 AELKAE-AESAK--AELEESEESWEEQKKELEKELSELEKRIEDLNEQNKLLHDQLES 128
UPF0242 pfam06785
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ...
432-544 2.05e-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: 2.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 432 ELLDELDEQKAQLEEQLkevRKKCAEEAQLISSLKAEITSQESQISTYEEELSKAREELSRLQQETAQLEESVES----- 506
Cdd:pfam06785  58 EDALKEKFEKSFLEEKE---AKLTELDAEGFKILEETLEELQSEEERLEEELSQKEEELRRLTEENQQLQIQLQQisqdf 134
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1958776456 507 ------GKAQLEPLQQHLQDSQQEISSMQMRLAMKDLETDNNQS 544
Cdd:pfam06785 135 aefrleSEEQLAEKQLLINEYQQTIEEQRSVLEKRQDQIENLES 178
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
369-538 2.44e-03

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 41.06  E-value: 2.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 369 KELDTLNNEIID---LQREKNNVE-----QDLKEKEDTVRQRTTEAQDLQDEVQRESLNLQKLQAQKQQVQELLDELDEQ 440
Cdd:pfam13868 130 EEIDEFNEEQAEwkeLEKEEEREEderilEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAK 209
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 441 KAQlEEQLKEVRKKCAEEAQlissLKAEItsqesqistyEEELSKAREEL----SRLQQETAQLEEsvesgKAQLEPLQQ 516
Cdd:pfam13868 210 LYQ-EEQERKERQKEREEAE----KKARQ----------RQELQQAREEQielkERRLAEEAEREE-----EEFERMLRK 269
                         170       180
                  ....*....|....*....|....*
gi 1958776456 517 HLQDSQQEissmQM---RLAMKDLE 538
Cdd:pfam13868 270 QAEDEEIE----QEeaeKRRMKRLE 290
DUF4618 pfam15397
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins ...
326-525 2.47e-03

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: 40.71  E-value: 2.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 326 NQKLIKGI----DPPHSLTPEMippsdkssLQKNTI--GSSPVADFSAIKELDTLnneIIDLQREKNNVEQDLKEKEDTV 399
Cdd:pfam15397  22 NLELIKAIqdteDSTALKVRKL--------LQQYEKfgTIISILEYSNKKQLQQA---KAELQEWEEKEESKLNKLEQQL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 400 RQRTTEAQDLQDE----------------VQRESLnlqkLQAQKQQVQELLDELDEqkaqLEEQLKEVRKKCAEEAQLIs 463
Cdd:pfam15397  91 EQLNAKIQKTQEElnflstykdkeypvkaVQIANL----VRQLQQLKDSQQDELDE----LEEMRRMVLESLSRKIQKK- 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958776456 464 slKAEITSQ--ESQISTYEEEL-SKARE------ELSRLQQETAQLEESVESGKAQLEPLQQHLQDSQQEI 525
Cdd:pfam15397 162 --KEKILSSlaEKTLSPYQESLlQKTRDnqvmlkEIEQFREFIDELEEEIPKLKAEVQQLQAQRQEPREVI 230
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
434-535 2.61e-03

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 38.96  E-value: 2.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 434 LDELDEQKAQLEEQLKEVRKKCAE---EAQLISSlKAEITSQEsqisTYEEELSKAREELSRLqQETAQLEESVESGKAq 510
Cdd:cd06503    39 LEEAEKAKEEAEELLAEYEEKLAEaraEAQEIIE-EARKEAEK----IKEEILAEAKEEAERI-LEQAKAEIEQEKEKA- 111
                          90       100
                  ....*....|....*....|....*
gi 1958776456 511 leplqqhLQDSQQEISSMQMRLAMK 535
Cdd:cd06503   112 -------LAELRKEVADLAVEAAEK 129
mukB PRK04863
chromosome partition protein MukB;
371-531 2.63e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 41.48  E-value: 2.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  371 LDTLNNEIIDLQREKNNVEQDLKEKEDTVRQRTTEAQDLQ---DEVQREslnlqklqAQKQQVQELLDELDEQKA----- 442
Cdd:PRK04863   444 LEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRkiaGEVSRS--------EAWDVARELLRRLREQRHlaeql 515
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  443 -QLEEQLKEVRKKCAEEAQLISsLKAEITSQESQISTYEEELskaREELSRLQQETAQLEESVESGKAQLEPLQQHLQDS 521
Cdd:PRK04863   516 qQLRMRLSELEQRLRQQQRAER-LLAEFCKRLGKNLDDEDEL---EQLQEELEARLESLSESVSEARERRMALRQQLEQL 591
                          170
                   ....*....|
gi 1958776456  522 QQEISSMQMR 531
Cdd:PRK04863   592 QARIQRLAAR 601
growth_prot_Scy NF041483
polarized growth protein Scy;
393-516 2.84e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 41.35  E-value: 2.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  393 KEKEDTVRQRTTEAQDLQDEVQRESlnlqklqaqkqqvQELLDELDEQKAQL-EEQLKEVRKKCAEEAQLISSLKAEits 471
Cdd:NF041483   520 RQAEETLERTRAEAERLRAEAEEQA-------------EEVRAAAERAARELrEETERAIAARQAEAAEELTRLHTE--- 583
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1958776456  472 QESQISTYEEELSKAREELSRLQQETAQLEESVESGKAQ-LEPLQQ 516
Cdd:NF041483   584 AEERLTAAEEALADARAEAERIRREAAEETERLRTEAAErIRTLQA 629
UPF0242 pfam06785
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ...
353-495 2.93e-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: 39.80  E-value: 2.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 353 QKNTIGSSPVADFSAIKEldtlnnEIIDLQREKNNVEQDLKEKEDTVRQRTTEAQDLQDEVQRESlnlqklqaqkQQVQE 432
Cdd:pfam06785  73 KEAKLTELDAEGFKILEE------TLEELQSEEERLEEELSQKEEELRRLTEENQQLQIQLQQIS----------QDFAE 136
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958776456 433 LLDELDEQKAQLEEQLKEVRkkcaeeaQLISSLKAEITSQESQISTYEEELSKAREELSRLQQ 495
Cdd:pfam06785 137 FRLESEEQLAEKQLLINEYQ-------QTIEEQRSVLEKRQDQIENLESKVRDLNYEIKTLLQ 192
growth_prot_Scy NF041483
polarized growth protein Scy;
392-529 2.94e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 41.35  E-value: 2.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  392 LKEKEDTVRQRTT-EAQDLQDEVQRESlnlqklQAQKQQVQELLDEL----DEQKAQLEEQLKEVRKKCAEEAqliSSLK 466
Cdd:NF041483  1119 IRERAEELRDRITgEIEELHERARRES------AEQMKSAGERCDALvkaaEEQLAEAEAKAKELVSDANSEA---SKVR 1189
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958776456  467 -AEITSQESQISTYEEELSKAREELSRLQQET-AQLEESVESGKAQLEPLQQHLQDSQQEISSMQ 529
Cdd:NF041483  1190 iAAVKKAEGLLKEAEQKKAELVREAEKIKAEAeAEAKRTVEEGKRELDVLVRRREDINAEISRVQ 1254
CEP63 pfam17045
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ...
436-575 2.94e-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: 40.19  E-value: 2.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 436 ELDEQKAQLEEQLKEVRKKCA--EEAQlisSLKAEITSQesqistYEEELSKAREELSRLQ------------------- 494
Cdd:pfam17045  43 ELLSARNTLERKHKEIGLLRQqlEELE---KGKQELVAK------YEQQLQKLQEELSKLKrsyeklqrkqlkeareeak 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 495 -QETAQLEESVESGKAQ------LEPLQQHLQdSQQEISSMQ-MRLAMKDletdnnQSNWCSSpQSILVNGAADYCSLST 566
Cdd:pfam17045 114 sREEDRSELSRLNGKLEefrqksLEWEQQRLQ-YQQQVASLEaQRKALAE------QSSLIQS-AAYQVQLEGRKQCLEA 185

                  ....*....
gi 1958776456 567 SSSETANLN 575
Cdd:pfam17045 186 SQSEIQRLR 194
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
369-581 3.04e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 41.31  E-value: 3.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  369 KELDTLNNE----IIDLQREKNNVEQDLKEKEDTVRQRTTEAQDLQDEVQRESLNLQKLQAQKQQVQE----LLDELDEQ 440
Cdd:pfam01576  176 KSLSKLKNKheamISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEelqaALARLEEE 255
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  441 KAQLEEQLKEVRKKCAEEAQLISSLKAEITSQ---ESQISTYEEELSKAREEL--------------SRLQQETAQLEES 503
Cdd:pfam01576  256 TAQKNNALKKIRELEAQISELQEDLESERAARnkaEKQRRDLGEELEALKTELedtldttaaqqelrSKREQEVTELKKA 335
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  504 VES-GKAQLEPLQQHLQDSQQEISSMQMRLAmkdlETDNNQSNWCSSPQSI---LVNGAADYCSLSTSSSETANLNEHAE 579
Cdd:pfam01576  336 LEEeTRSHEAQLQEMRQKHTQALEELTEQLE----QAKRNKANLEKAKQALeseNAELQAELRTLQQAKQDSEHKRKKLE 411

                   ..
gi 1958776456  580 GQ 581
Cdd:pfam01576  412 GQ 413
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
312-514 3.10e-03

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 41.19  E-value: 3.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  312 KLSKDQFALAFHLIN-QKLIKGIDPPHSLTPEMIPP-SDKSSLQKNTIGSSpvadfsAIKELDTLNNEIIDLQR------ 383
Cdd:TIGR00606  448 ILEKKQEELKFVIKElQQLEGSSDRILELDQELRKAeRELSKAEKNSLTET------LKKEVKSLQNEKADLDRklrkld 521
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  384 ----EKNNVEQDLKEKEDTVRQRTTEAQDLQDEVQRESLNLQKLQAQKQQVQEL---LDELDEQKAQLEEQLKEVRKKCA 456
Cdd:TIGR00606  522 qemeQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLedwLHSKSKEINQTRDRLAKLNKELA 601
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958776456  457 EEAQLISSLKAEITSQESQISTYEEELSKA---REELSRLQqetaQLEESVESGKAQLEPL 514
Cdd:TIGR00606  602 SLEQNKNHINNELESKEEQLSSYEDKLFDVcgsQDEESDLE----RLKEEIEKSSKQRAML 658
STAT5_CCD cd16855
Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family ...
442-536 3.27e-03

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: 39.55  E-value: 3.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 442 AQLEEQLKEVRKKCAEEAQLISSLKAEitsQESQISTYEEeLSKAREELSRLQ-QETAQLEESVESGKAQLEPLQQHLQD 520
Cdd:cd16855     4 LEIRQQLEELRQRTQETENDLRNLQQK---QESFVIQYQE-SQKIQAQLQQLQqQPQNERIELEQQLQQQKEQLEQLLNA 79
                          90
                  ....*....|....*...
gi 1958776456 521 SQQEISSMQMRLA--MKD 536
Cdd:cd16855    80 KAQELLQLRMELAdkFKK 97
PRK12704 PRK12704
phosphodiesterase; Provisional
437-544 3.35e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.92  E-value: 3.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 437 LDEQKAQLEEQLKEVRKKCAEEAQL-ISSLKAEITSQESQIstyEEELSKAREELSRLQQETAQLEESVESGKAQLEPLQ 515
Cdd:PRK12704   33 IKEAEEEAKRILEEAKKEAEAIKKEaLLEAKEEIHKLRNEF---EKELRERRNELQKLEKRLLQKEENLDRKLELLEKRE 109
                          90       100
                  ....*....|....*....|....*....
gi 1958776456 516 QHLQDSQQEISSMQMRLAMKDLETDNNQS 544
Cdd:PRK12704  110 EELEKKEKELEQKQQELEKKEEELEELIE 138
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
369-535 3.44e-03

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 41.26  E-value: 3.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  369 KELDTLNNEIIDLQREKNNVEQDLKEKEDTVRQRTTEAQDLQDEVQRESLNLQKLQAQKQQVQELLD----ELDEQKAQ- 443
Cdd:pfam15921  349 KQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDhlrrELDDRNMEv 428
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  444 --LEEQLKEVRKKCaeEAQLISSLKA---------EITSQESQISTYEEELSKAREELSRLQQETAQLEESVESGKAQLE 512
Cdd:pfam15921  429 qrLEALLKAMKSEC--QGQMERQMAAiqgknesleKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQ 506
                          170       180
                   ....*....|....*....|...
gi 1958776456  513 PLQQHLQDSQQEISSMQMRLAMK 535
Cdd:pfam15921  507 EKERAIEATNAEITKLRSRVDLK 529
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
442-540 3.47e-03

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


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 40.98  E-value: 3.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  442 AQLEEQLKEVRKKCAEEAQLISSLKAEITSQESQISTYEEELSK-----------AREELSRL----QQETAQLEESVES 506
Cdd:pfam12128  596 AASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASReetfartalknARLDLRRLfdekQSEKDKKNKALAE 675
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1958776456  507 GK-----------AQLEPLQQHLQDSQQEI------SSMQMRLAMKDLETD 540
Cdd:pfam12128  676 RKdsanerlnsleAQLKQLDKKHQAWLEEQkeqkreARTEKQAYWQVVEGA 726
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
389-544 3.64e-03

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: 40.96  E-value: 3.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 389 EQDLKEKEDTVRQRTTEAQDLQDEVQRESLNLQklqaqkqqvqelldelDEQKAQLEE--QLKEVRKKCAEEAQLISSLK 466
Cdd:pfam10174 124 EHERQAKELFLLRKTLEEMELRIETQKQTLGAR----------------DESIKKLLEmlQSKGLPKKSGEEDWERTRRI 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 467 AEITSQ----ESQISTYEEELSKAREELSR---LQQETAQ---LEESVESGKAQLEPLQQHLQDSQQEI---------SS 527
Cdd:pfam10174 188 AEAEMQlghlEVLLDQKEKENIHLREELHRrnqLQPDPAKtkaLQTVIEMKDTKISSLERNIRDLEDEVqmlktngllHT 267
                         170
                  ....*....|....*..
gi 1958776456 528 MQMRLAMKDLETDNNQS 544
Cdd:pfam10174 268 EDREEEIKQMEVYKSHS 284
DUF4201 pfam13870
Domain of unknown function (DUF4201); This is a family of coiled-coil proteins from eukaryotes. ...
369-533 3.75e-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: 39.13  E-value: 3.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 369 KELDTLNNEIIDLQREKNNVEQDLKEKEDTvrqrtTEA------QDLQDEVQreslnlqklqaqkqqvqELLDELDEQKA 442
Cdd:pfam13870   6 NELSKLRLELITLKHTLAKIQEKLEQKEEL-----GEGltmidfLQLQIENQ-----------------ALNEKIEERNK 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 443 QLEE----------QLKEVRKKCAEEAQLISSLKAEITSQESQISTYEEELSKAREELSRLQQETAQLEESveSG----- 507
Cdd:pfam13870  64 ELKRlklkvtntvhALTHLKEKLHFLSAELSRLKKELRERQELLAKLRKELYRVKLERDKLRKQNKKLRQQ--GGllhvp 141
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1958776456 508 ---------KAQLEPLQQHLQDSQQEISSMQMRLA 533
Cdd:pfam13870 142 allhdydktKAEVEEKRKSVKKLRRKVKILEMRIK 176
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
467-533 4.48e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.13  E-value: 4.48e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958776456 467 AEITSQESQISTYEEELSKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQDSQQEISSMQMRLA 533
Cdd:COG4942    20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA 86
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
432-538 4.53e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 39.89  E-value: 4.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 432 ELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAEITSQESQISTYEEELSKAREELSRLQQETAQLEESVESGKAQL 511
Cdd:COG1340     8 SSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKL 87
                          90       100
                  ....*....|....*....|....*...
gi 1958776456 512 EPLQQHLQDSQQEISSM-QMRLAMKDLE 538
Cdd:COG1340    88 NELREELDELRKELAELnKAGGSIDKLR 115
Filament pfam00038
Intermediate filament protein;
369-533 4.89e-03

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 39.90  E-value: 4.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 369 KELDTLNNEIIDLqreKNNVEQDLKEkedtvrqrtteaqdLQDEVQRESLNLQKLQAQKQQVQELLDELDEQ-------- 440
Cdd:pfam00038 124 AKIESLKEELAFL---KKNHEEEVRE--------------LQAQVSDTQVNVEMDAARKLDLTSALAEIRAQyeeiaakn 186
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 441 KAQLEE----QLKEVRKKCAEEAQLISSLKAEITSQESQISTYEEELSKAREELSRLQqetAQLEESVESGKAQLEPLQQ 516
Cdd:pfam00038 187 REEAEEwyqsKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLE---RQLAETEERYELQLADYQE 263
                         170
                  ....*....|....*..
gi 1958776456 517 HLQDSQQEISSMQMRLA 533
Cdd:pfam00038 264 LISELEAELQETRQEMA 280
Leu_zip pfam15294
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ...
369-519 5.05e-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: 39.69  E-value: 5.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 369 KELDTLNNEIIDLQREKNNVEQDLKEKEDTVRQRTTEAQDLQDevqreslnlqklqaqkqqvqelLDELDEQKAQLEEQL 448
Cdd:pfam15294 147 ERLKTLESQATQALDEKSKLEKALKDLQKEQGAKKDVKSNLKE----------------------ISDLEEKMAALKSDL 204
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958776456 449 KevrKKCAEEAQLISSLKAEITSQESQISTYEEELSKAREELSRLQQETAQ---LEESVESGKAQLEPLQQHLQ 519
Cdd:pfam15294 205 E---KTLNASTALQKSLEEDLASTKHELLKVQEQLEMAEKELEKKFQQTAAyrnMKEMLTKKNEQIKELRKRLS 275
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
369-528 5.60e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 40.54  E-value: 5.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  369 KELDTLNNEIIDLQ-------REKNNVEQDLKEKEDTV--------------RQRTTEAQDLQDEVQRESLNLQKLQAQK 427
Cdd:pfam01576  833 KKLKNLEAELLQLQedlaaseRARRQAQQERDELADEIasgasgksalqdekRRLEARIAQLEEELEEEQSNTELLNDRL 912
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  428 QQVQELLDELDEQ--------------KAQLEEQLKEVRKKCAE-EAQLISSLKAEITSQESQISTYEEELSKAREE--- 489
Cdd:pfam01576  913 RKSTLQVEQLTTElaaerstsqksesaRQQLERQNKELKAKLQEmEGTVKSKFKSSIAALEAKIAQLEEQLEQESRErqa 992
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958776456  490 ------------------------------------LSRLQQETAQLEESVESGK---AQLEPLQQHLQDSQQEISSM 528
Cdd:pfam01576  993 anklvrrtekklkevllqvederrhadqykdqaekgNSRMKQLKRQLEEAEEEASranAARRKLQRELDDATESNESM 1070
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
381-531 6.00e-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: 40.11  E-value: 6.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 381 LQREKNNVEQDLKEKEDTvRQRttEAQDLQDEVQRESLNLQKLQAQKQQVQELL--DELDEQKAQ--------------- 443
Cdd:pfam17380 415 IQQQKVEMEQIRAEQEEA-RQR--EVRRLEEERAREMERVRLEEQERQQQVERLrqQEEERKRKKlelekekrdrkraee 491
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 444 -----LEEQLKEVRKKCAEEAQLISSLKAEItsQESQISTYEEELSKAREELSRLQQETA---QLEESVESG---KAQLE 512
Cdd:pfam17380 492 qrrkiLEKELEERKQAMIEEERKRKLLEKEM--EERQKAIYEEERRREAEEERRKQQEMEerrRIQEQMRKAteeRSRLE 569
                         170
                  ....*....|....*....
gi 1958776456 513 PLQQHLQDSQQEISSMQMR 531
Cdd:pfam17380 570 AMEREREMMRQIVESEKAR 588
mukB PRK04863
chromosome partition protein MukB;
439-529 6.08e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 40.33  E-value: 6.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  439 EQKAQLEEQLKEVRKKCAEEAQLISSLKAEITSQESQISTYEEELSKAREELSRLQQETAQLEESVESGKAQ-------- 510
Cdd:PRK04863   530 RQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARapawlaaq 609
                           90       100
                   ....*....|....*....|....*
gi 1958776456  511 --LEPLQQH----LQDSQQEISSMQ 529
Cdd:PRK04863   610 daLARLREQsgeeFEDSQDVTEYMQ 634
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
433-547 6.22e-03

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: 40.19  E-value: 6.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 433 LLDELDEQKAQLEEQLKEvRKKCAEEAQLISSLKAEITSQESQISTYEEELSKAREELSRL-----------QQETAQLe 501
Cdd:pfam10174 200 LLDQKEKENIHLREELHR-RNQLQPDPAKTKALQTVIEMKDTKISSLERNIRDLEDEVQMLktngllhtedrEEEIKQM- 277
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958776456 502 ESVESG----KAQLEPLQQHLQDSQQEISSMQMRlamkdLETDNNQSNWC 547
Cdd:pfam10174 278 EVYKSHskfmKNKIDQLKQELSKKESELLALQTK-----LETLTNQNSDC 322
Uso1_p115_C pfam04871
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ...
446-543 6.72e-03

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


Pssm-ID: 461461 [Multi-domain]  Cd Length: 121  Bit Score: 37.38  E-value: 6.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 446 EQLKEVRKKCAEEAQLISSLKAEITSQESQIstyeEELSKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQDSQQEI 525
Cdd:pfam04871   1 AKKSELESEASSLKNENTELKAELQELSKQY----NSLEQKESQAKELEAEVKKLEEALKKLKAELSEEKQKEKEKQSEL 76
                          90
                  ....*....|....*...
gi 1958776456 526 SSMQmrLAMKDLETDNNQ 543
Cdd:pfam04871  77 DDLL--LLLGDLEEKVEK 92
46 PHA02562
endonuclease subunit; Provisional
434-541 7.08e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 40.00  E-value: 7.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 434 LDELDEQKAQLEEQLKEVRkkcaEEAQLISSLKAEITSQESQISTYEEELSKAREELSRLQQETAQLEESVESGKAQLEP 513
Cdd:PHA02562  315 LEKLDTAIDELEEIMDEFN----EQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDK 390
                          90       100
                  ....*....|....*....|....*...
gi 1958776456 514 LQQHLQDSQQEIssmQMRLAMKDLETDN 541
Cdd:PHA02562  391 IVKTKSELVKEK---YHRGIVTDLLKDS 415
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
436-538 7.10e-03

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


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 40.32  E-value: 7.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  436 ELDEQKAQLEEQLKEVRKKCAEEAQLISSLKA---------EITSQESQISTYEEELS--------------KAREELSR 492
Cdd:COG3096    300 QLAEEQYRLVEMARELEELSARESDLEQDYQAasdhlnlvqTALRQQEKIERYQEDLEelterleeqeevveEAAEQLAE 379
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1958776456  493 LQQETAQLEESVESGKAQLEPLQQHLqDSQQEiSSMQMRLAMKDLE 538
Cdd:COG3096    380 AEARLEAAEEEVDSLKSQLADYQQAL-DVQQT-RAIQYQQAVQALE 423
CCDC22 pfam05667
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
369-554 7.11e-03

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: 40.01  E-value: 7.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 369 KELDTLNNEIIDLQREKNNVEQDLKEKEDTVRQRTteaqdlqdevqreslnlqklqaqkqqvqELLDELDEQKAQLEEQL 448
Cdd:pfam05667 335 EELEELQEQLEDLESSIQELEKEIKKLESSIKQVE----------------------------EELEELKEQNEELEKQY 386
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 449 KeVRKKCAEEAQL----ISSLKAEITSQESQISTYEEELSKAR----EELSRLQQETAQLEESVESGKAQLEPLQQHLQD 520
Cdd:pfam05667 387 K-VKKKTLDLLPDaeenIAKLQALVDASAQRLVELAGQWEKHRvpliEEYRALKEAKSNKEDESQRKLEEIKELREKIKE 465
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1958776456 521 SQQEISS---MQMRLaMKDLETDNNQSNWCSSPQSIL 554
Cdd:pfam05667 466 VAEEAKQkeeLYKQL-VAEYERLPKDVSRSAYTRRIL 501
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
432-523 7.26e-03

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: 39.23  E-value: 7.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  432 ELLDELDEQKAQLEEQLKEVRKKCAEEAQlisSLKAEITSQESQIstyEEELSKareeLSRLQQETAQLEESVESGKAQL 511
Cdd:smart00787 179 DRKDALEEELRQLKQLEDELEDCDPTELD---RAKEKLKKLLQEI---MIKVKK----LEELEEELQELESKIEDLTNKK 248
                           90
                   ....*....|..
gi 1958776456  512 EPLQQHLQDSQQ 523
Cdd:smart00787 249 SELNTEIAEAEK 260
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
435-525 7.35e-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: 7.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  435 DELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAEITSQESQISTYEEELSKAREELSRLQQETAQlEESVESGKAQLEPL 514
Cdd:COG3096    281 RELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTALRQ-QEKIERYQEDLEEL 359
                           90
                   ....*....|.
gi 1958776456  515 QQHLqDSQQEI 525
Cdd:COG3096    360 TERL-EEQEEV 369
ZapB pfam06005
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is ...
480-532 7.63e-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: 35.70  E-value: 7.63e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958776456 480 EEELSKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQDSQQEISSMQMRL 532
Cdd:pfam06005  10 ETKIQAAVDTIALLQMENEELKEENEELKEEANELEEENQQLKQERNQWQERI 62
Uso1_p115_C pfam04871
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ...
380-502 8.15e-03

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


Pssm-ID: 461461 [Multi-domain]  Cd Length: 121  Bit Score: 36.99  E-value: 8.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 380 DLQREKNNVEQDLKEKEDTVRQRTTEAQDLQDEvqreslnlqklqaqkqqvQELLDELDEQKAQLEEQLKEVRKKCAEEA 459
Cdd:pfam04871   5 ELESEASSLKNENTELKAELQELSKQYNSLEQK------------------ESQAKELEAEVKKLEEALKKLKAELSEEK 66
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1958776456 460 QLISSLKAEITSQESQISTYEEELSKAREELSRLQQETAQLEE 502
Cdd:pfam04871  67 QKEKEKQSELDDLLLLLGDLEEKVEKYKARLKELGEEVLSDDE 109
ZapB pfam06005
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is ...
473-528 8.42e-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: 35.70  E-value: 8.42e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958776456 473 ESQISTYEEELSKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQDSQQEISSM 528
Cdd:pfam06005  10 ETKIQAAVDTIALLQMENEELKEENEELKEEANELEEENQQLKQERNQWQERIRGL 65
PRK11637 PRK11637
AmiB activator; Provisional
365-503 8.66e-03

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 39.29  E-value: 8.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 365 FSAIKELDTLNNEIIDLQREKNNVEQDLKEKEDTVRQRtteaqdlqdEVQRESLnlqklqaqkqqvqelLDELDEQK--- 441
Cdd:PRK11637   29 LSAGVLLCAFSAHASDNRDQLKSIQQDIAAKEKSVRQQ---------QQQRASL---------------LAQLKKQEeai 84
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958776456 442 AQLEEQLKEVRKKCAEEAQLISSLKAEITSQESQISTYEEELSKAREELSRLQQETA-QL----EES 503
Cdd:PRK11637   85 SQASRKLRETQNTLNQLNKQIDELNASIAKLEQQQAAQERLLAAQLDAAFRQGEHTGlQLilsgEES 151
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
143-189 8.95e-03

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 35.60  E-value: 8.95e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1958776456 143 DGFLSGDKVKPVL--LNSKLPVEILGRVWELSDIDHDGKLDRDEFAVAM 189
Cdd:cd00051    14 DGTISADELKAALksLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELM 62
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
378-520 9.48e-03

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


Pssm-ID: 464003 [Multi-domain]  Cd Length: 119  Bit Score: 36.78  E-value: 9.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 378 IIDLQREKNNVEQDLKEKEDTVRQRTTEAQdlqdevQREslnlqklqaqkqqvqellDELDEQKAQLEEQLKEVRKKCAE 457
Cdd:pfam13863   1 LLEKKREMFLVQLALDAKREEIERLEELLK------QRE------------------EELEKKEQELKEDLIKFDKFLKE 56
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958776456 458 -EAQLISSLKaEITSQESQISTYEEELSKAREELSRLQQETAQLEESVEsgkaQLEPLQQHLQD 520
Cdd:pfam13863  57 nDAKRRRALK-KAEEETKLKKEKEKEIKKLTAQIEELKSEISKLEEKLE----EYKPYEDFLEK 115
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
434-502 9.84e-03

Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.


Pssm-ID: 459736 [Multi-domain]  Cd Length: 235  Bit Score: 38.47  E-value: 9.84e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958776456 434 LDELDEQKAQLEEQLKEVRKKcAEEAqlisslKAEITSQESQISTYEEELSKAREelsRLQQETAQLEE 502
Cdd:pfam00261  10 LDEAEERLKEAMKKLEEAEKR-AEKA------EAEVAALNRRIQLLEEELERTEE---RLAEALEKLEE 68
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
460-538 9.84e-03

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


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 38.35  E-value: 9.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 460 QLISSLKAEITSQESQISTYEEELSKAREELSRLQQETAQLEEsvesgkaQLEPLQQHLQDSQQEISSMQ-MRLAMKDLE 538
Cdd:pfam13851  26 ELIKSLKEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQE-------EVEELRKQLENYEKDKQSLKnLKARLKVLE 98
WEMBL pfam05701
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ...
433-538 9.88e-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: 39.24  E-value: 9.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456 433 LLDELDEQKAQLEEqlkeVRKKCAEEAQLISSLKAEITSQESQISTYEEELSKAREELSRLQQETAQLEESVESGKAQLE 512
Cdd:pfam05701 326 LRSELEKEKAELAS----LRQREGMASIAVSSLEAELNRTKSEIALVQAKEKEAREKMVELPKQLQQAAQEAEEAKSLAQ 401
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1958776456 513 PLQQHLQDSQQE-------ISSMQMRL--AMKDLE 538
Cdd:pfam05701 402 AAREELRKAKEEaeqakaaASTVESRLeaVLKEIE 436
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
394-524 9.88e-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: 39.55  E-value: 9.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  394 EKEDTVRQRTTEAQDLQDEVQ------------RESLNLQKLQAQKQQVQELLDELDEQKAQLE-------EQLKEVRKK 454
Cdd:COG3096    934 EQFEQLQADYLQAKEQQRRLKqqifalsevvqrRPHFSYEDAVGLLGENSDLNEKLRARLEQAEearrearEQLRQAQAQ 1013
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  455 CAEEAQLISSLKAEITSQESQISTYEEELS------------KAR-------EELSRLQQETAQLEESVESGKAQLEPLQ 515
Cdd:COG3096   1014 YSQYNQVLASLKSSRDAKQQTLQELEQELEelgvqadaeaeeRARirrdelhEELSQNRSRRSQLEKQLTRCEAEMDSLQ 1093

                   ....*....
gi 1958776456  516 QHLQDSQQE 524
Cdd:COG3096   1094 KRLRKAERD 1102
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
353-556 9.90e-03

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 39.64  E-value: 9.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  353 QKNTIgSSPVADFSA--IKEL----DTLNNEIIDLQREKN---NVEQDLKEKEDTVRQRTTEA----------QDLQDEV 413
Cdd:TIGR00606  124 EKVSL-SSKCAEIDRemISHLgvskAVLNNVIFCHQEDSNwplSEGKALKQKFDEIFSATRYIkaletlrqvrQTQGQKV 202
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776456  414 QRESLNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKaEITSQESQISTYEEELSKAREELSRL 493
Cdd:TIGR00606  203 QEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLK-EIEHNLSKIMKLDNEIKALKSRKKQM 281
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958776456  494 QQETAQLEES-VESGKAQLEPLQQHLQDSQQEISSMQMRLA--MKDLETDNNQSNWCSSPQSILVN 556
Cdd:TIGR00606  282 EKDNSELELKmEKVFQGTDEQLNDLYHNHQRTVREKERELVdcQRELEKLNKERRLLNQEKTELLV 347
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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