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Conserved domains on  [gi|24762736|ref|NP_726482|]
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epidermal growth factor receptor pathway substrate clone 15, isoform B [Drosophila melanogaster]

Protein Classification

EH domain-containing protein( domain architecture ID 11506103)

EH domain-containing protein

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 ...
307-402 1.29e-33

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: 124.70  E-value: 1.29e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736     307 DWVVTPADLKRFEEIFRQSDLDKDGLVSGLEVKDIFIKSGIPQRSLADIWALCDTNQSGKLTVEQFALAMWFVERKQRGV 386
Cdd:smart00027    1 PWAISPEDKAKYEQIFRSLDKNQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGY 80
                            90
                    ....*....|....*.
gi 24762736     387 DPPHVLNANMVPPSMR 402
Cdd:smart00027   81 PIPASLPPSLIPPSKR 96
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
126-215 7.75e-30

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: 113.91  E-value: 7.75e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736     126 DWSIGVIDRLKYEQLFESLHPS-NGMLPGNKVKGVLMDSKLPMSILGTIWDLADQDKDGNLDMHEFVVAMHLVYQTLQKR 204
Cdd:smart00027    1 PWAISPEDKAKYEQIFRSLDKNqDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGY 80
                            90
                    ....*....|.
gi 24762736     205 TIPSVLPPELR 215
Cdd:smart00027   81 PIPASLPPSLI 91
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
16-82 2.09e-19

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: 83.04  E-value: 2.09e-19
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24762736   16 YEAYYKLIDPKGTGAIEAMTAAKFLKKSGLSDVVLSRIWDLSDPSGKGFLDKPGFFVALKLVSLSQA 82
Cdd:cd00052    1 YDQIFRSLDPDGDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
430-629 4.86e-15

Uncharacterized protein, contains DUF3084 domain [Function unknown];


:

Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 78.41  E-value: 4.86e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  430 EIEELARERRVLETEIAQKEADVRIKNGEVRSLQSELDTLTATLKQLENQRGEAQKRLDDLQAQVTKIRDQCHMQEVTIN 509
Cdd:COG4372   39 ELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELE 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  510 EQEGELNAKRSELQKLKDEEASLQKEYDSNNRELSKLTNHLQATQLQISSVRSMVTQLLETQRQMTDALLICRAAMENQN 589
Cdd:COG4372  119 ELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEK 198
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 24762736  590 AELVSEYQLKIEPDFDEARKTLTKEVQLPKDDPFEENNSG 629
Cdd:COG4372  199 EEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSAL 238
 
Name Accession Description Interval E-value
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
307-402 1.29e-33

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: 124.70  E-value: 1.29e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736     307 DWVVTPADLKRFEEIFRQSDLDKDGLVSGLEVKDIFIKSGIPQRSLADIWALCDTNQSGKLTVEQFALAMWFVERKQRGV 386
Cdd:smart00027    1 PWAISPEDKAKYEQIFRSLDKNQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGY 80
                            90
                    ....*....|....*.
gi 24762736     387 DPPHVLNANMVPPSMR 402
Cdd:smart00027   81 PIPASLPPSLIPPSKR 96
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
126-215 7.75e-30

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: 113.91  E-value: 7.75e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736     126 DWSIGVIDRLKYEQLFESLHPS-NGMLPGNKVKGVLMDSKLPMSILGTIWDLADQDKDGNLDMHEFVVAMHLVYQTLQKR 204
Cdd:smart00027    1 PWAISPEDKAKYEQIFRSLDKNqDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGY 80
                            90
                    ....*....|.
gi 24762736     205 TIPSVLPPELR 215
Cdd:smart00027   81 PIPASLPPSLI 91
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
137-202 6.11e-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: 98.83  E-value: 6.11e-25
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24762736  137 YEQLFESLHPSN-GMLPGNKVKGVLMDSKLPMSILGTIWDLADQDKDGNLDMHEFVVAMHLVYQTLQ 202
Cdd:cd00052    1 YDQIFRSLDPDGdGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
318-384 1.49e-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: 94.98  E-value: 1.49e-23
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24762736  318 FEEIFRQSDLDKDGLVSGLEVKDIFIKSGIPQRSLADIWALCDTNQSGKLTVEQFALAMWFVERKQR 384
Cdd:cd00052    1 YDQIFRSLDPDGDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
16-82 2.09e-19

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: 83.04  E-value: 2.09e-19
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24762736   16 YEAYYKLIDPKGTGAIEAMTAAKFLKKSGLSDVVLSRIWDLSDPSGKGFLDKPGFFVALKLVSLSQA 82
Cdd:cd00052    1 YDQIFRSLDPDGDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
EF-hand_4 pfam12763
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ...
136-211 2.59e-18

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: 81.27  E-value: 2.59e-18
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24762736    136 KYEQLFESLHPSNGMLPGNKVKGVLMDSKLPMSILGTIWDLADQDKDGNLDMHEFVVAMHLVYQTLQK--RTIPSVLP 211
Cdd:pfam12763   11 KYWEIFSGLKPENNKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLIFDLVNGniADVPDELP 88
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
16-84 1.14e-16

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: 76.55  E-value: 1.14e-16
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24762736      16 YEAYYKLIDPKGTGAIEAMTAAKFLKKSGLSDVVLSRIWDLSDPSGKGFLDKPGFFVALKLVSLSQAGQ 84
Cdd:smart00027   12 YEQIFRSLDKNQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGY 80
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
430-629 4.86e-15

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 78.41  E-value: 4.86e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  430 EIEELARERRVLETEIAQKEADVRIKNGEVRSLQSELDTLTATLKQLENQRGEAQKRLDDLQAQVTKIRDQCHMQEVTIN 509
Cdd:COG4372   39 ELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELE 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  510 EQEGELNAKRSELQKLKDEEASLQKEYDSNNRELSKLTNHLQATQLQISSVRSMVTQLLETQRQMTDALLICRAAMENQN 589
Cdd:COG4372  119 ELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEK 198
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 24762736  590 AELVSEYQLKIEPDFDEARKTLTKEVQLPKDDPFEENNSG 629
Cdd:COG4372  199 EEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSAL 238
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
423-592 2.48e-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: 78.17  E-value: 2.48e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    423 ELEMISKEIEELARERRVLETEIAQKEADVRIKNGEVRSLQSELDTLTATLKQLENQRGEAQKRLDDLQAQVTKIRDQCH 502
Cdd:TIGR02168  699 ALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELA 778
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    503 MQEVTINEQEGELNAKRSELQKLKDEEASLQKEYDSNNRELSKLTNHLQATQLQISSVRSMVTQLLETQRQMTDALLICR 582
Cdd:TIGR02168  779 EAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLA 858
                          170
                   ....*....|
gi 24762736    583 AAMENQNAEL 592
Cdd:TIGR02168  859 AEIEELEELI 868
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
423-614 2.73e-10

Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.


Pssm-ID: 437057 [Multi-domain]  Cd Length: 401  Bit Score: 63.93  E-value: 2.73e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    423 ELEMISKEIEELARERRVLETEIAQKEADVRIKNGEVRSLQSELDTLTATLKQLENQRGEAQKRLDDLQAQVTKIRDQCH 502
Cdd:pfam19220   70 ELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEALERQLAAETEQNRALEEENKALREEAQ 149
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    503 MQEVTINEQEGELNAKRSELQKLKDEEASLQKEYDSNNRELSKLTNHLQATQlqissvrsmvtQLLETQRQMTDALlicr 582
Cdd:pfam19220  150 AAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAELE-----------TQLDATRARLRAL---- 214
                          170       180       190
                   ....*....|....*....|....*....|..
gi 24762736    583 aamENQNAELVSEYQlKIEPDFDEARKTLTKE 614
Cdd:pfam19220  215 ---EGQLAAEQAERE-RAEAQLEEAVEAHRAE 242
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
423-570 2.95e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 55.07  E-value: 2.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736   423 ELEMISKEIEELARERRVLETEIAQKEADVRI----------KNGEVRSLQSELDTLTATLKQLENQRGEAQKRLDDLQA 492
Cdd:PRK03918  201 ELEEVLREINEISSELPELREELEKLEKEVKEleelkeeieeLEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEE 280
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24762736   493 QVTKIRDqchmqevtINEQEGELNAKRSELQKLKDEEASLQKeydsnnrELSKLTNHLQATQLQISSVRSMVTQLLET 570
Cdd:PRK03918  281 KVKELKE--------LKEKAEEYIKLSEFYEEYLDELREIEK-------RLSRLEEEINGIEERIKELEEKEERLEEL 343
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
423-492 1.44e-06

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: 47.56  E-value: 1.44e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  423 ELEMISKEIEELARERRVLETEIAQKEADVRIKNGEVRSLQSELDTLtatlkQLENqrGEAQKRLDDLQA 492
Cdd:cd22887    5 ELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIAL-----QIEN--NLLEEKLRKLQE 67
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
317-376 2.72e-05

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 45.17  E-value: 2.72e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  317 RFEEIFRQSDLDKDGLVSGLEVKDIFIKSGIPQRSLADIWALCDTNQSGKLTVEQFALAM 376
Cdd:COG5126   70 FARAAFDLLDTDGDGKISADEFRRLLTALGVSEEEADELFARLDTDGDGKISFEEFVAAV 129
EF-hand_4 pfam12763
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ...
312-406 4.31e-05

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: 43.90  E-value: 4.31e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    312 PADLKRFEEIFrQSDLDKDGLVSGLEVKDIFIKSGIPQRSLADIWALCDTNQSGKLTVEQFALAMWFVERKQRGV--DPP 389
Cdd:pfam12763    6 EWEIKKYWEIF-SGLKPENNKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLIFDLVNGNiaDVP 84
                           90
                   ....*....|....*..
gi 24762736    390 HVLNANMVPPSMRATVA 406
Cdd:pfam12763   85 DELPDWLVPGSKAHLIQ 101
EF-hand_4 pfam12763
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ...
24-77 1.45e-04

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: 42.36  E-value: 1.45e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 24762736     24 DPKGTGAieamTAAKFLKKSGLSDVVLSRIWDLSDPSGKGFLDKPGFFVALKLV 77
Cdd:pfam12763   23 NNKLTGD----QVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLI 72
SPEC smart00150
Spectrin repeats;
432-528 9.80e-04

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 39.62  E-value: 9.80e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736     432 EELARERRVLETEIAQKEADVRIKN-----GEVRSLQSELDTLTATLKQLENqrgeaqkRLDDLQAQVTKIRDQCHMQEV 506
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDlgkdlESVEALLKKHEAFEAELEAHEE-------RVEALNELGEQLIEEGHPDAE 73
                            90       100
                    ....*....|....*....|..
gi 24762736     507 TINEQEGELNAKRSELQKLKDE 528
Cdd:smart00150   74 EIEERLEELNERWEELKELAEE 95
 
Name Accession Description Interval E-value
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
307-402 1.29e-33

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: 124.70  E-value: 1.29e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736     307 DWVVTPADLKRFEEIFRQSDLDKDGLVSGLEVKDIFIKSGIPQRSLADIWALCDTNQSGKLTVEQFALAMWFVERKQRGV 386
Cdd:smart00027    1 PWAISPEDKAKYEQIFRSLDKNQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGY 80
                            90
                    ....*....|....*.
gi 24762736     387 DPPHVLNANMVPPSMR 402
Cdd:smart00027   81 PIPASLPPSLIPPSKR 96
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
126-215 7.75e-30

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: 113.91  E-value: 7.75e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736     126 DWSIGVIDRLKYEQLFESLHPS-NGMLPGNKVKGVLMDSKLPMSILGTIWDLADQDKDGNLDMHEFVVAMHLVYQTLQKR 204
Cdd:smart00027    1 PWAISPEDKAKYEQIFRSLDKNqDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGY 80
                            90
                    ....*....|.
gi 24762736     205 TIPSVLPPELR 215
Cdd:smart00027   81 PIPASLPPSLI 91
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
137-202 6.11e-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: 98.83  E-value: 6.11e-25
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24762736  137 YEQLFESLHPSN-GMLPGNKVKGVLMDSKLPMSILGTIWDLADQDKDGNLDMHEFVVAMHLVYQTLQ 202
Cdd:cd00052    1 YDQIFRSLDPDGdGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
318-384 1.49e-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: 94.98  E-value: 1.49e-23
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24762736  318 FEEIFRQSDLDKDGLVSGLEVKDIFIKSGIPQRSLADIWALCDTNQSGKLTVEQFALAMWFVERKQR 384
Cdd:cd00052    1 YDQIFRSLDPDGDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
16-82 2.09e-19

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: 83.04  E-value: 2.09e-19
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24762736   16 YEAYYKLIDPKGTGAIEAMTAAKFLKKSGLSDVVLSRIWDLSDPSGKGFLDKPGFFVALKLVSLSQA 82
Cdd:cd00052    1 YDQIFRSLDPDGDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
EF-hand_4 pfam12763
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ...
136-211 2.59e-18

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: 81.27  E-value: 2.59e-18
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24762736    136 KYEQLFESLHPSNGMLPGNKVKGVLMDSKLPMSILGTIWDLADQDKDGNLDMHEFVVAMHLVYQTLQK--RTIPSVLP 211
Cdd:pfam12763   11 KYWEIFSGLKPENNKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLIFDLVNGniADVPDELP 88
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
16-84 1.14e-16

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: 76.55  E-value: 1.14e-16
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24762736      16 YEAYYKLIDPKGTGAIEAMTAAKFLKKSGLSDVVLSRIWDLSDPSGKGFLDKPGFFVALKLVSLSQAGQ 84
Cdd:smart00027   12 YEQIFRSLDKNQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGY 80
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
430-629 4.86e-15

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 78.41  E-value: 4.86e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  430 EIEELARERRVLETEIAQKEADVRIKNGEVRSLQSELDTLTATLKQLENQRGEAQKRLDDLQAQVTKIRDQCHMQEVTIN 509
Cdd:COG4372   39 ELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELE 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  510 EQEGELNAKRSELQKLKDEEASLQKEYDSNNRELSKLTNHLQATQLQISSVRSMVTQLLETQRQMTDALLICRAAMENQN 589
Cdd:COG4372  119 ELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEK 198
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 24762736  590 AELVSEYQLKIEPDFDEARKTLTKEVQLPKDDPFEENNSG 629
Cdd:COG4372  199 EEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSAL 238
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
423-592 2.48e-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: 78.17  E-value: 2.48e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    423 ELEMISKEIEELARERRVLETEIAQKEADVRIKNGEVRSLQSELDTLTATLKQLENQRGEAQKRLDDLQAQVTKIRDQCH 502
Cdd:TIGR02168  699 ALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELA 778
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    503 MQEVTINEQEGELNAKRSELQKLKDEEASLQKEYDSNNRELSKLTNHLQATQLQISSVRSMVTQLLETQRQMTDALLICR 582
Cdd:TIGR02168  779 EAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLA 858
                          170
                   ....*....|
gi 24762736    583 AAMENQNAEL 592
Cdd:TIGR02168  859 AEIEELEELI 868
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
423-626 1.07e-13

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 74.17  E-value: 1.07e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  423 ELEMISKEIEELARERRVLETEIAQKEADVRIKNGEVRSLQSELDTLTATLKQLENQRGEAQKRLDDLQAQVTKIRDQCH 502
Cdd:COG4372   53 ELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRK 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  503 MQEVTINEQEGELNAKRSELQKLKDEEASLQKEYDSNNRELSKLTNhlQATQLQISSVRSMVTQLLETQRQMTDALLIcR 582
Cdd:COG4372  133 QLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSE--AEAEQALDELLKEANRNAEKEEELAEAEKL-I 209
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 24762736  583 AAMENQNAELVSEYQLKIEPDFDEARKTLTKEVQLPKDDPFEEN 626
Cdd:COG4372  210 ESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLE 253
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
423-616 1.44e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 75.74  E-value: 1.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  423 ELEMISKEIEELARERRVLETEIAQKEADVRIKNGEVRSLQSELDTLTATLKQLENQRGEAQKRLDDLQAQVTKIRDQCH 502
Cdd:COG1196  275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  503 MQEVTINEQEGELNAKRSELQKLKDEEASLQKEYDSNNRELSKLTNHLQATQLQISSVRSMVTQLLETQRQMTDALLICR 582
Cdd:COG1196  355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
                        170       180       190
                 ....*....|....*....|....*....|....
gi 24762736  583 AAMENQNAELVSEYQLKIEpdFDEARKTLTKEVQ 616
Cdd:COG1196  435 EEEEEEEEALEEAAEEEAE--LEEEEEALLELLA 466
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
427-620 1.91e-13

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 73.40  E-value: 1.91e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  427 ISKEIEELARERRVLETEIAQKEADVRIKNGEVRSLQSELDTLTATLKQLENQRGEAQKRLDDLQAQVTKIRDQchmqev 506
Cdd:COG4372   29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEE------ 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  507 tINEQEGELNAKRSELQKLKDEEASLQKEYDSNNRELSKLTNHLQATQLQISSVRSmvtQLLETQRQMtdallicRAAME 586
Cdd:COG4372  103 -LESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEE---QLESLQEEL-------AALEQ 171
                        170       180       190
                 ....*....|....*....|....*....|....
gi 24762736  587 NQNAELVSEYQLKIEPDFDEARKTLTKEVQLPKD 620
Cdd:COG4372  172 ELQALSEAEAEQALDELLKEANRNAEKEEELAEA 205
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
423-617 9.02e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 73.05  E-value: 9.02e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  423 ELEMISKEIEELARERRVLETEIAQKEADVRIKNGEVRSLQSELDTLTATLKQLENQRGEAQKRLDDLQAQVTKIRDQCH 502
Cdd:COG1196  261 ELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELE 340
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  503 MQEVTINEQEGELNAKRSELQKLKDEEASLQKEYDSNNRELSKLTNHLQATQLQISSVRSMVTQLLETQRQMTDALLICR 582
Cdd:COG1196  341 ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLE 420
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 24762736  583 AAMENQNAELvSEYQLKIEPDFDEARKTLTKEVQL 617
Cdd:COG1196  421 EELEELEEAL-AELEEEEEEEEEALEEAAEEEAEL 454
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
423-615 1.39e-12

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: 72.41  E-value: 1.39e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    423 ELEMISKEIEELARERRVLETEIAQKEADVRIK-NGEVRSLQSELDTLTATLKQLENQRGEAQKRLDDLQAQVTKIRDQC 501
Cdd:TIGR02169  252 ELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEI 331
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    502 HMQEVTINEQEGELNAKRSELQKLKDEEASLQKEYDSNNRELSKLTNHLQATQLQISSVR---SMVTQ----LLETQRQM 574
Cdd:TIGR02169  332 DKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYReklEKLKReineLKRELDRL 411
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 24762736    575 TDALLICRAAMENQNAELVSEYQLKIEpdFDEARKTLTKEV 615
Cdd:TIGR02169  412 QEELQRLSEELADLNAAIAGIEAKINE--LEEEKEDKALEI 450
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
423-614 1.73e-12

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 72.40  E-value: 1.73e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    423 ELEMISKEIEELARERRVLETEIAQKEADVRIKNGEVRSLQSELDTLTATLKQLENQRGEAQKRLDDLQAQVTKIRDQCH 502
Cdd:TIGR02168  247 ELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLE 326
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    503 MQEVTINEQEGELNAKRSELQKLKDEEASLQKEYDSNNRELSKLTNHLQATQLQISSVRSMVTQLLETQRQMTDALLICR 582
Cdd:TIGR02168  327 ELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLE 406
                          170       180       190
                   ....*....|....*....|....*....|....
gi 24762736    583 AAME--NQNAELVSEYQLKIEPDFDEARKTLTKE 614
Cdd:TIGR02168  407 ARLErlEDRRERLQQEIEELLKKLEEAELKELQA 440
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
362-580 3.68e-12

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 70.57  E-value: 3.68e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  362 NQSGKLTVEQFALAMwFVER---------KQRGVDPPHVLNANMvppSMRATVAGVDLQPQEVKPTYSnpELEMISKEIE 432
Cdd:COG4717   32 NEAGKSTLLAFIRAM-LLERlekeadelfKPQGRKPELNLKELK---ELEEELKEAEEKEEEYAELQE--ELEELEEELE 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  433 ELARERRVLETEIAQKEADVRIKN--GEVRSLQSELDTLTATLKQLENQ---RGEAQKRLDDLQAQVTKIRDQCHmqevt 507
Cdd:COG4717  106 ELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEERleeLRELEEELEELEAELAELQEELE----- 180
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24762736  508 iNEQEGELNAKRSELQKLKDEEASLQKEYDSNNRELSKLTNHLQATQLQISSVRS--MVTQLLETQRQMTDALLI 580
Cdd:COG4717  181 -ELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENelEAAALEERLKEARLLLLI 254
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
423-595 5.06e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 70.74  E-value: 5.06e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  423 ELEMISKEIEELARERRVLETEIAQKEADVRIKNGEVRSLQSELDTLTATLKQLENQRGEAQKRLDDLQAQVTKIRDQCH 502
Cdd:COG1196  226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA 305
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  503 MQEVTINEQEGELNAKRSELQKLKDEEASLQKEYDSNNRELSKLTNHLQATQLQISSVRSMVTQLLETQRQMTDALLICR 582
Cdd:COG1196  306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
                        170
                 ....*....|...
gi 24762736  583 AAMENQNAELVSE 595
Cdd:COG1196  386 EELLEALRAAAEL 398
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
423-597 5.31e-12

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 66.87  E-value: 5.31e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  423 ELEMISKEIEELARERRVLETEIAQKEADVRIKNGEVRSLQSELDTLTATLKQLENQRGEAQKRLDDLQAQVTKIRDQCH 502
Cdd:COG1579   11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKE 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  503 MQEVT--INEQEGELNAKRSELQKLKDEEASLQKEYDSNNRELSKLTNHLQATQLQISSvrsmvtQLLETQRQMtDALLI 580
Cdd:COG1579   91 YEALQkeIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDE------ELAELEAEL-EELEA 163
                        170
                 ....*....|....*...
gi 24762736  581 CRAAMENQ-NAELVSEYQ 597
Cdd:COG1579  164 EREELAAKiPPELLALYE 181
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
423-592 5.60e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 70.35  E-value: 5.60e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  423 ELEMISKEIEELARERRVLETEIAQKEADVRIKNGEVRSLQSELDTLTATLKQLENQRGEAQKRLDDLQAQVTKIRDQCH 502
Cdd:COG1196  247 ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELA 326
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  503 MQEVTINEQEGELNAKRSELQKLKDEEASLQKEYDSNNRELSKLTNHLQATQLQISSVRSMVTQLLETQRQMTDALLICR 582
Cdd:COG1196  327 ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE 406
                        170
                 ....*....|
gi 24762736  583 AAMENQNAEL 592
Cdd:COG1196  407 EAEEALLERL 416
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
425-612 6.96e-12

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 70.05  E-value: 6.96e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  425 EMISKEIEELARERRVLETEIAQKEADV---RIKNGEVrSLQSELDTLTATLKQLENQRGEAQKRLDDLQAQVTKIRDQC 501
Cdd:COG3206  171 EEARKALEFLEEQLPELRKELEEAEAALeefRQKNGLV-DLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQL 249
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  502 HMQEVTINE--QEGELNAKRSELQKLKDEEASLQKEYDSNNRELSKLTNHLQATQLQISSVRSMVTQLLETQRQmtdALL 579
Cdd:COG3206  250 GSGPDALPEllQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELE---ALQ 326
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 24762736  580 ICRAAMENQNAELVSEYQ---------LKIEPDFDEARKTLT 612
Cdd:COG3206  327 AREASLQAQLAQLEARLAelpeleaelRRLEREVEVARELYE 368
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
423-601 1.53e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 69.20  E-value: 1.53e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  423 ELEmisKEIEELARERRV------LETEIAQKEADVRIKngEVRSLQSELDTLTATLKQLENQRGEAQKRLDDLQAQVTK 496
Cdd:COG1196  197 ELE---RQLEPLERQAEKaeryreLKEELKELEAELLLL--KLRELEAELEELEAELEELEAELEELEAELAELEAELEE 271
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  497 IRDQCHMQEVTINEQEGELNAKRSELQKLKDEEASLQKEYDSNNRELSKLTNHLQATQLQISSVRSMVTQLLETQRQMTD 576
Cdd:COG1196  272 LRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE 351
                        170       180
                 ....*....|....*....|....*
gi 24762736  577 ALLICRAAMENQNAELVSEYQLKIE 601
Cdd:COG1196  352 ELEEAEAELAEAEEALLEAEAELAE 376
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
451-616 4.42e-11

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 66.08  E-value: 4.42e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  451 DVRIKNGEVRSLQSEldTLTATLKQLEnqrgEAQKRLDDLQAQVTKIRDQchmqevtINEQEGELNAKRSELQKLKDEEA 530
Cdd:COG4372   17 GLRPKTGILIAALSE--QLRKALFELD----KLQEELEQLREELEQAREE-------LEQLEEELEQARSELEQLEEELE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  531 SLQKEYDSNNRELSKLTNHLQATQLQISSVRSMVTQlLETQRQmtdALLICRAAMENQNAELVSEYQLKiepdfDEARKT 610
Cdd:COG4372   84 ELNEQLQAAQAELAQAQEELESLQEEAEELQEELEE-LQKERQ---DLEQQRKQLEAQIAELQSEIAER-----EEELKE 154

                 ....*.
gi 24762736  611 LTKEVQ 616
Cdd:COG4372  155 LEEQLE 160
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
424-635 6.78e-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: 67.00  E-value: 6.78e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    424 LEMISKEIE----------ELARERRVLETEIaqKEADVRIKNGEVRSLQSELDTLTATLKQLENQRGEAQKRLDDLQAQ 493
Cdd:TIGR02168  191 LEDILNELErqlkslerqaEKAERYKELKAEL--RELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEK 268
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    494 VTKIRDQCHMQEVTINEQEGELNAKRSELQKL-------KDEEASLQKEYDSNNRELSKLTNHLQATQLQISSVRSMVTQ 566
Cdd:TIGR02168  269 LEELRLEVSELEEEIEELQKELYALANEISRLeqqkqilRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEE 348
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24762736    567 LLEtqrqmtdalliCRAAMENQNAELVSEYQlkiepDFDEARKTLTKEVQLPKDDPFEENNSGAANQAT 635
Cdd:TIGR02168  349 LKE-----------ELESLEAELEELEAELE-----ELESRLEELEEQLETLRSKVAQLELQIASLNNE 401
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
428-584 7.16e-11

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 66.86  E-value: 7.16e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  428 SKEIEELARERRVLETEIAQKEADVRIKNGEVRSLQSELDTLTA--------TLKQLENQRGEAQKRLDDLQAQVTKIRD 499
Cdd:COG4913  287 QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAqirgnggdRLEQLEREIERLERELEERERRRARLEA 366
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  500 QCHMQEVTINEQEGELNAKRSE----LQKLKDEEASLQKEYDSNNRELSKLTNHLQATQLQISSVRSMVTQLLETQRQMT 575
Cdd:COG4913  367 LLAALGLPLPASAEEFAALRAEaaalLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALR 446

                 ....*....
gi 24762736  576 DAllICRAA 584
Cdd:COG4913  447 DA--LAEAL 453
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
414-613 1.25e-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: 66.24  E-value: 1.25e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    414 EVKPTYSNPELEmISKEIEELARERRVLETEIAQKEADVRIKNGEVRSLQSELDTLTATLKQLENQRGEAQKRLDDLQAQ 493
Cdd:TIGR02169  280 KIKDLGEEEQLR-VKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEE 358
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    494 VTKIRDQCHMQEVTINEQEGELNAKRSELQKLKDEEASLQKEYDSNNRELSKLTNHLQATQLQISSVRSMVT----QLLE 569
Cdd:TIGR02169  359 YAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAgieaKINE 438
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 24762736    570 TQRQMTDALLICRAAMEN--QNAELVSEYQ---LKIEPDFDEARKTLTK 613
Cdd:TIGR02169  439 LEEEKEDKALEIKKQEWKleQLAADLSKYEqelYDLKEEYDRVEKELSK 487
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
423-614 2.73e-10

Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.


Pssm-ID: 437057 [Multi-domain]  Cd Length: 401  Bit Score: 63.93  E-value: 2.73e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    423 ELEMISKEIEELARERRVLETEIAQKEADVRIKNGEVRSLQSELDTLTATLKQLENQRGEAQKRLDDLQAQVTKIRDQCH 502
Cdd:pfam19220   70 ELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEALERQLAAETEQNRALEEENKALREEAQ 149
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    503 MQEVTINEQEGELNAKRSELQKLKDEEASLQKEYDSNNRELSKLTNHLQATQlqissvrsmvtQLLETQRQMTDALlicr 582
Cdd:pfam19220  150 AAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAELE-----------TQLDATRARLRAL---- 214
                          170       180       190
                   ....*....|....*....|....*....|..
gi 24762736    583 aamENQNAELVSEYQlKIEPDFDEARKTLTKE 614
Cdd:pfam19220  215 ---EGQLAAEQAERE-RAEAQLEEAVEAHRAE 242
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
420-537 3.89e-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: 61.48  E-value: 3.89e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  420 SNPELEMISKEIEELARERRVLETEIAQkeadvrikngevrsLQSELDTLTATLKQLENQRGEAQKRLDDLQAQVTKIRD 499
Cdd:COG1579   87 NNKEYEALQKEIESLKRRISDLEDEILE--------------LMERIEELEEELAELEAELAELEAELEEKKAELDEELA 152
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 24762736  500 QchmqevtINEQEGELNAKRSELqkLKDEEASLQKEYD 537
Cdd:COG1579  153 E-------LEAELEELEAEREEL--AAKIPPELLALYE 181
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
423-611 5.75e-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: 62.86  E-value: 5.75e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  423 ELEMISKEIEELARERRVLETEIAQKEADVRIKNGEVRSLQSELDTLTATLKQLENQRGEAQKRLDDLQAQVTK------ 496
Cdd:COG4942   35 EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEllraly 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  497 --------------------IRDQCHMQEVT--INEQEGELNAKRSELQKLKDEEASLQKEYDSNNRELSKLTNHLQATQ 554
Cdd:COG4942  115 rlgrqpplalllspedfldaVRRLQYLKYLApaRREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALK 194
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24762736  555 LQISSVRSMVTQLLETQRQMTDALLICRAAMENQNAELVSEYQLKIE----PDFDEARKTL 611
Cdd:COG4942  195 AERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAErtpaAGFAALKGKL 255
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
429-617 5.80e-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: 62.86  E-value: 5.80e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  429 KEIEELARERRVLETEIAQKEADVRIKNGEVRSLQSELDTLTATLKQLENQRGEAQKRLDDLQAQVTKIRDQCHMQEVTI 508
Cdd:COG4942   27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  509 NEQEGEL--NAKRSELQKLKDEEASLQKE-----YDSNNRELSKLTNHLQATQLQISSVRSMVTQLLETQRQMTDALLIC 581
Cdd:COG4942  107 AELLRALyrLGRQPPLALLLSPEDFLDAVrrlqyLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEE 186
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 24762736  582 RAAME---NQNAELVSEYQLKIEPDFDEARKTLTKEVQL 617
Cdd:COG4942  187 RAALEalkAERQKLLARLEKELAELAAELAELQQEAEEL 225
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
420-624 7.50e-10

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 62.23  E-value: 7.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  420 SNPELEMISKEIEELARERRVLETEIAQKEADVRIKNGEVRSLQSEldtltatLKQLENQRGEAQKRLDDLQAQVTKIrd 499
Cdd:COG4372   71 ARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEE-------LEELQKERQDLEQQRKQLEAQIAEL-- 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  500 qchmqEVTINEQEGELNAKRSELQKLKDEEASLQKEYdsNNRELSKLTNHLQATQLQISSVRSMVTQLLETQRQMTDALL 579
Cdd:COG4372  142 -----QSEIAEREEELKELEEQLESLQEELAALEQEL--QALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPR 214
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 24762736  580 ICRAAMENQNAELVSEYQLKIEPDFDEARKTLTKEVQLPKDDPFE 624
Cdd:COG4372  215 ELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKE 259
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
417-715 9.84e-10

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 62.15  E-value: 9.84e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  417 PTYSNPELEMISKEIEELARERRVLETEIAQKEADVRIKNGEVRSLQSELDTLTATLKQLENQRGEAQKRLDDLQAQVTK 496
Cdd:COG3883   11 PAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  497 -IRDQcHMQEVTINEQEGELNAKrsELQKLKDEEASLQKEYDSNNRELskltNHLQATQLQISSVRSMVTQLLETQRQMT 575
Cdd:COG3883   91 rARAL-YRSGGSVSYLDVLLGSE--SFSDFLDRLSALSKIADADADLL----EELKADKAELEAKKAELEAKLAELEALK 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  576 DALLICRAAMENQNAELVSEYQlKIEPDFDEARKTLTKEVQLPKDDPFEENNSGAANQATNGFGSDPFSGQPVNKPAIST 655
Cdd:COG3883  164 AELEAAKAELEAQQAEQEALLA-QLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 242
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  656 GFDDSFNMSSGFDSGFDAFGQSGAGSAFGQTQRDPFGSDAFAANKSNAITPEPGKDDFGS 715
Cdd:COG3883  243 AASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGG 302
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
423-616 1.02e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.03  E-value: 1.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  423 ELEMISKEIEELARERRVLETEIAQKEADVRIKNGEVRSLQSELDTLTATLKQLENQRGEAQKRLDDLQAQVTKIRDQch 502
Cdd:COG1196  317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA-- 394
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  503 mqevtINEQEGELNAKRSELQKLKDEEASLQKEYDSNNRELSKLTNHLQATQLQISSVRSMVTQLLETQRQMTDALLICR 582
Cdd:COG1196  395 -----AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
                        170       180       190
                 ....*....|....*....|....*....|....
gi 24762736  583 AAMENQNAELVSEYQLKIEpdfDEARKTLTKEVQ 616
Cdd:COG1196  470 EEAALLEAALAELLEELAE---AAARLLLLLEAE 500
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
414-618 1.07e-09

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: 63.21  E-value: 1.07e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    414 EVKPTYSnpELEMISKEIEELARERRVLETEIAQKEADVRIkngEVRSLQSELDTLTATLKQLENQRGEAQKRLDDLQAQ 493
Cdd:pfam15921  661 EVKTSRN--ELNSLSEDYEVLKRNFRNKSEEMETTTNKLKM---QLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQ 735
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    494 VTKIRDQCHMQEVTINEQEGELNAKRSELQKLKDEEASLQKEYDSNNRELSKLTNHLQATQLQISSVRSMVTQLLETQRQ 573
Cdd:pfam15921  736 ITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDK 815
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 24762736    574 MTDALLICRAAMENQNAELVseyQLKIEPDFDearktlTKEVQLP 618
Cdd:pfam15921  816 ASLQFAECQDIIQRQEQESV---RLKLQHTLD------VKELQGP 851
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
423-616 1.43e-09

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 62.35  E-value: 1.43e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    423 ELEMISKE-------IEELARERRVLETEIAQKEADVRIKNGEVRSLQSELDTLTATLKQLENQRGEAQKRLDDLQAQVT 495
Cdd:TIGR04523  371 EIEKLKKEnqsykqeIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDS 450
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    496 KIRDQCHMQEVTINEQEGELNAKRSELQKLKDEEASLQKEYDSNNRELSKLTNHLQATQLQISSVRSMVTQLLETQRQMT 575
Cdd:TIGR04523  451 VKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLE 530
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 24762736    576 DAllicRAAMENQNAELVSEyqlKIEPDFDEARKTLTKEVQ 616
Cdd:TIGR04523  531 SE----KKEKESKISDLEDE---LNKDDFELKKENLEKEID 564
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
429-616 1.73e-09

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 62.24  E-value: 1.73e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  429 KEIEELARERRVLETEIAQkeADVRIKNGEVRSLQSELDTLTATLKQLENQRGEAQKRLDDLQAQVTKIRDQchmqevtI 508
Cdd:COG4913  262 ERYAAARERLAELEYLRAA--LRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQ-------I 332
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  509 NEQEGElnakrsELQKLKDEEASLQKEYDSNNRELSKLTNHLQATQLQISSVRSMVTQLLETQRQMTDALLICRAAMENQ 588
Cdd:COG4913  333 RGNGGD------RLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEA 406
                        170       180
                 ....*....|....*....|....*...
gi 24762736  589 NAELVSEYQlkiepDFDEARKTLTKEVQ 616
Cdd:COG4913  407 LAEAEAALR-----DLRRELRELEAEIA 429
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
414-615 2.27e-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: 62.01  E-value: 2.27e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    414 EVKPTYSNPELEMISKEIEELARERRVLETEIAQKEADVRIKNGEVRSLQSELDTLTATLKQLENQRGEAQKRLDDLQAQ 493
Cdd:TIGR02169  666 ILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEED 745
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    494 VTKIRDQCHMQEVTINEQEGELNAKRSELQKLKDEEASL------------QKEYDSNNRELSKLTNHLQATQLQISSvR 561
Cdd:TIGR02169  746 LSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLearlshsripeiQAELSKLEEEVSRIEARLREIEQKLNR-L 824
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24762736    562 SMVTQLLETQRQMTDALLI--------CRAAMENQNAEL------VSEYQLKIEpDFDEARKTLTKEV 615
Cdd:TIGR02169  825 TLEKEYLEKEIQELQEQRIdlkeqiksIEKEIENLNGKKeeleeeLEELEAALR-DLESRLGDLKKER 891
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
416-592 3.48e-09

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 60.94  E-value: 3.48e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  416 KPTYSNPELEMisKEIEELARERRVLETeiaqkeadvriKNGEVRSLQSELDTLTATLKQLENQRGEAQKRLDDLQAQVt 495
Cdd:COG4717   60 KPQGRKPELNL--KELKELEEELKEAEE-----------KEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL- 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  496 kirdQCHMQEVTINEQEGELNAKRSELQKLKDEEA---SLQKEYDSNNRELSKLTNHLQ--------ATQLQISSVRSMV 564
Cdd:COG4717  126 ----QLLPLYQELEALEAELAELPERLEELEERLEelrELEEELEELEAELAELQEELEelleqlslATEEELQDLAEEL 201
                        170       180
                 ....*....|....*....|....*...
gi 24762736  565 TQLLETQRQMTDALLICRAAMENQNAEL 592
Cdd:COG4717  202 EELQQRLAELEEELEEAQEELEELEEEL 229
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
418-558 4.41e-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: 4.41e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    418 TYSNPELEMISKEIEELARERRVLETEIAQKEADvrIKNgeVRSLQSELDTLTATLKQLENQRGEAQKRLDDLQAQVTKI 497
Cdd:TIGR04523  155 EKLNNKYNDLKKQKEELENELNLLEKEKLNIQKN--IDK--IKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQL 230
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24762736    498 RDQCHMQEVTINEQEGELNAKRSELQKLKDEEASL-------QKEYDSNNRELSKLTNHLQATQLQIS 558
Cdd:TIGR04523  231 KDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIkkqlsekQKELEQNNKKIKELEKQLNQLKSEIS 298
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
425-613 6.07e-09

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 58.77  E-value: 6.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  425 EMISKEIEELARERRVLETEIAQKEADVRIKNGEVRSLQSELDTLTATLKQLENQRGEAQKRLDDLQAQVTKIRDQchmq 504
Cdd:COG1340    4 DELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEE---- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  505 evtINEQEGELNAKRSELQKLKDEEASLQK---EYDSNNRELSKLTNHLQATQLQISSVRsmvtQLLETQRQMTDALLIC 581
Cdd:COG1340   80 ---RDELNEKLNELREELDELRKELAELNKaggSIDKLRKEIERLEWRQQTEVLSPEEEK----ELVEKIKELEKELEKA 152
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 24762736  582 RAAME--NQNAELVSEY-QLKIEpdFDEARKTLTK 613
Cdd:COG1340  153 KKALEknEKLKELRAELkELRKE--AEEIHKKIKE 185
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
428-559 6.46e-09

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 60.42  E-value: 6.46e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  428 SKEIEELARERRVLETEIAQKEADVRIKNGEVRSLQSELDTLTATLKQlenqrgEAQKRLDDLQAQVTKIRdqchMQEVT 507
Cdd:COG3206  262 SPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQ------EAQRILASLEAELEALQ----AREAS 331
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 24762736  508 INEQEGELNAKRSELQKLKDEEASLQKEYDSNNRELSKLTNHLQATQLQISS 559
Cdd:COG3206  332 LQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEAL 383
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
381-614 1.17e-08

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: 58.28  E-value: 1.17e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    381 RKQRGVDPPHVLNA--NMVPPSMRATVAGVDLQPQEVKPTYSNPELEMISKEIEELARERRVLETEIAQKEADVRIKNGE 458
Cdd:pfam15905   30 RKQKAAESQPNLNNskDASTPATARKVKSLELKKKSQKNLKESKDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAK 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    459 VRSLQSELDTLTATLKQLENQRGE----------------AQKRLDDLQAQVTKIRDQ--CHMQEVTINEQEGE------ 514
Cdd:pfam15905  110 LNAAVREKTSLSASVASLEKQLLEltrvnellkakfsedgTQKKMSSLSMELMKLRNKleAKMKEVMAKQEGMEgklqvt 189
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    515 ---LNAKRSELQKLKDEEASLQKEYDSNNRELSKLTNH---LQATQLQISSVRSMVTQLLETQRQMTDALLICRAAMEnQ 588
Cdd:pfam15905  190 qknLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYiteLSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLE-E 268
                          250       260
                   ....*....|....*....|....*.
gi 24762736    589 NAELVSEyQLKiepDFDEARKTLTKE 614
Cdd:pfam15905  269 KEQELSK-QIK---DLNEKCKLLESE 290
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
425-559 1.20e-08

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 59.70  E-value: 1.20e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    425 EMISKEIEELARERRVLETEIAQKEAdvrikngEVRSLQSELDTLTATLKQLENQRGEAQKRLDDLQAQVTKIRDQCHMQ 504
Cdd:TIGR02169  850 KSIEKEIENLNGKKEELEEELEELEA-------ALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSEL 922
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 24762736    505 EVTINEQEGELnakrSELQKLKDEEaslqKEYDSNNRELSKLTNHLQATQLQISS 559
Cdd:TIGR02169  923 KAKLEALEEEL----SEIEDPKGED----EEIPEEELSLEDVQAELQRVEEEIRA 969
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
430-550 1.47e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 59.54  E-value: 1.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  430 EIEELARERRVLETEIAQKEADvrikNGEVRSLQSELDTLTATLKQLENQRGEAQKRLDDLQAQVTKIRDQC-------- 501
Cdd:COG4913  662 DVASAEREIAELEAELERLDAS----SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELdelqdrle 737
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 24762736  502 HMQEVTINEQEGELNAKRSEL---QKLKDEEASLQKEYDSNNRELSKLTNHL 550
Cdd:COG4913  738 AAEDLARLELRALLEERFAAAlgdAVERELRENLEERIDALRARLNRAEEEL 789
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
422-601 2.32e-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: 58.91  E-value: 2.32e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    422 PELEMISKEIEELARERRVLETEIAQKEADVRIKNGEVRSLQSELDTLTAT-------LKQLEnqrgeaqKRLDDLQAQV 494
Cdd:TIGR02168  351 EELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEierlearLERLE-------DRRERLQQEI 423
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    495 TKIRDQchMQEVTINEQEGELNAKRSELQKLKDEEASLQKEYDSNNRELSKLTNHLQATQLQISSVRSMVTQLLETQRQM 574
Cdd:TIGR02168  424 EELLKK--LEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENL 501
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 24762736    575 TDALLICRAAMENQN---------AELVS---EYQLKIE 601
Cdd:TIGR02168  502 EGFSEGVKALLKNQSglsgilgvlSELISvdeGYEAAIE 540
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
430-554 3.38e-08

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 57.86  E-value: 3.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  430 EIEELARERRVLETEIAQKEADVRIKNGEVRSLQSELD--TLTATLKQLENQRGEAQKRLDDLQAQVTKIRDQchMQEVt 507
Cdd:COG4717  389 AALEQAEEYQELKEELEELEEQLEELLGELEELLEALDeeELEEELEELEEELEELEEELEELREELAELEAE--LEQL- 465
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 24762736  508 inEQEGELNAKRSELQKLKDEEASLQKEYDSNNRELSKLTNHLQATQ 554
Cdd:COG4717  466 --EEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYR 510
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
423-613 4.12e-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: 57.76  E-value: 4.12e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    423 ELEMISKEIEELARerrvletEIAQKEADVRIKNGEVRSLQSELDTLTATLKQLENQRGEAQKRLDDLQAQVTKIRDQch 502
Cdd:TIGR02168  832 RIAATERRLEDLEE-------QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEE-- 902
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    503 mqevtINEQEGELNAKRSELQKLKDEEASLQkeydsnnrelskltNHLQATQLQISSVRSMVTQLLETqrqmtdallicr 582
Cdd:TIGR02168  903 -----LRELESKRSELRRELEELREKLAQLE--------------LRLEGLEVRIDNLQERLSEEYSL------------ 951
                          170       180       190
                   ....*....|....*....|....*....|.
gi 24762736    583 aamenqNAELVSEYQLKIEPDFDEARKTLTK 613
Cdd:TIGR02168  952 ------TLEEAEALENKIEDDEEEARRRLKR 976
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
423-571 4.28e-08

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 57.72  E-value: 4.28e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    423 ELEMISKEIEELARERRVLETEIA----QKEADVrIKNgevrsLQSELDTLTATLKQLENQRGEAQKRLDDLQAQVTKIR 498
Cdd:TIGR04523  275 ELEQNNKKIKELEKQLNQLKSEISdlnnQKEQDW-NKE-----LKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLK 348
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24762736    499 DQCHMQEVTINEQEGELNAKRSELQKLKdeeaslqKEYDSNNRELSKLTNHLQATQLQISSVRSmVTQLLETQ 571
Cdd:TIGR04523  349 KELTNSESENSEKQRELEEKQNEIEKLK-------KENQSYKQEIKNLESQINDLESKIQNQEK-LNQQKDEQ 413
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
429-620 5.25e-08

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 57.34  E-value: 5.25e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    429 KEIEELARERRVLETEIAQKEADVRIKNGEVRSLQSELDTLTATLKQLENQRGEAQKRLDDLQAQVTKIRDQCHMQEVTI 508
Cdd:TIGR04523  454 LIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEK 533
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    509 NEQEGELNAKRSELQKLKDE--EASLQKEYDSNNRELSKL---TNHLQATQLQ---------------ISSVRSMVTQLL 568
Cdd:TIGR04523  534 KEKESKISDLEDELNKDDFElkKENLEKEIDEKNKEIEELkqtQKSLKKKQEEkqelidqkekekkdlIKEIEEKEKKIS 613
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 24762736    569 ETQRQMTDAllicraamENQNAELVSeyqlkIEPDFDEARKTLTKEVQLPKD 620
Cdd:TIGR04523  614 SLEKELEKA--------KKENEKLSS-----IIKNIKSKKNKLKQEVKQIKE 652
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
413-562 8.25e-08

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 56.57  E-value: 8.25e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    413 QEVKptYSNPELEMISKEIEELARERRVLETEIAQKEADVRIKN---------GEVRSLQSELDTLTATLKQLENQRGEA 483
Cdd:TIGR04523  510 EKVK--DLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDfelkkenleKEIDEKNKEIEELKQTQKSLKKKQEEK 587
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24762736    484 QKRLDDLQAQVTKIRDQCHMQEVTINEQEGELNAKRSELQKLKDEEASLQKEYDsnnrelsKLTNHLQATQLQISSVRS 562
Cdd:TIGR04523  588 QELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKN-------KLKQEVKQIKETIKEIRN 659
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
431-616 1.30e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 56.08  E-value: 1.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  431 IEELARERRVLETEIAQKEADVRIKNGEVRSLQSELDTLTATLKQLENQR--GEAQKRLDDLQAQVTkirdqchmqevti 508
Cdd:COG4913  612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvASAEREIAELEAELE------------- 678
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  509 neqegELNAKRSELQKLKDEEASLQKEYDSNNRELSKLTNHLQATQLQISSVRSMVTQLLETQRQMTDallicrAAMENQ 588
Cdd:COG4913  679 -----RLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAED------LARLEL 747
                        170       180
                 ....*....|....*....|....*....
gi 24762736  589 NAELVSEY-QLKIEPDFDEARKTLTKEVQ 616
Cdd:COG4913  748 RALLEERFaAALGDAVERELRENLEERID 776
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
425-595 1.81e-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: 55.80  E-value: 1.81e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    425 EMISK---EIEELARERRVLETEIAQKEADVRIKNGEVRSLQSELDTLTATLKQLENQRGEAQKRLDDlQAQVTKIRDqc 501
Cdd:TIGR04523  335 KIISQlneQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQN-QEKLNQQKD-- 411
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    502 hmQEVTINEQEGELNAKR------------SELQKLKDEEASLQKEYDSNNRELSKLTNHLQATQLQISSVRS---MVTQ 566
Cdd:TIGR04523  412 --EQIKKLQQEKELLEKEierlketiiknnSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQnleQKQK 489
                          170       180
                   ....*....|....*....|....*....
gi 24762736    567 LLETQRQMTDALLICRAAMENQNAELVSE 595
Cdd:TIGR04523  490 ELKSKEKELKKLNEEKKELEEKVKDLTKK 518
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
420-609 1.97e-07

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 54.15  E-value: 1.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  420 SNPELEMISKEIEELARERRVLETEIAQKEADVRI-------KNGEVRSLQSEL-------DTLTATLKQLENQRGEAQK 485
Cdd:COG1340    6 LSSSLEELEEKIEELREEIEELKEKRDELNEELKElaekrdeLNAQVKELREEAqelrekrDELNEKVKELKEERDELNE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  486 RLDDLQAQVTKIRDQchMQEvtINEQEGELNAKRSELQKL----------KDEE-------ASLQKEYD------SNNRE 542
Cdd:COG1340   86 KLNELREELDELRKE--LAE--LNKAGGSIDKLRKEIERLewrqqtevlsPEEEkelvekiKELEKELEkakkalEKNEK 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24762736  543 LSKLTNHLQATQLQISSVRSMVTQLLETQRQMTDALLICRAAMENQNAEL------VSEYQLKIEP---DFDEARK 609
Cdd:COG1340  162 LKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEAdelhkeIVEAQEKADElheEIIELQK 237
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
401-592 2.04e-07

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: 55.51  E-value: 2.04e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    401 MRATVAGVDLQPQEVKPTYSNpELEMISKE----IEELARERRVLETEIAQKEADVRiknGEVRSLQSELDTLTatlKQL 476
Cdd:pfam15921  236 LKGRIFPVEDQLEALKSESQN-KIELLLQQhqdrIEQLISEHEVEITGLTEKASSAR---SQANSIQSQLEIIQ---EQA 308
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    477 ENQRGEAQKRLDDLQAQVTKIRDQC----HMQEVTINEQEGELNAKRSELQKLKDEEASLQKEYDSNNRELSKLTNHLQA 552
Cdd:pfam15921  309 RNQNSMYMRQLSDLESTVSQLRSELreakRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHK 388
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 24762736    553 TQLQISSVRSMVTQLLEtqRQMTDALLI--CRAAMENQNAEL 592
Cdd:pfam15921  389 REKELSLEKEQNKRLWD--RDTGNSITIdhLRRELDDRNMEV 428
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
423-592 2.39e-07

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: 54.90  E-value: 2.39e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    423 ELEMISKEI----EELARERRVLETEIAQKEADVRIKNGEVRSL-------QSELDTLTATLKQLENQRGEAQKRLDDLQ 491
Cdd:pfam07888   98 ELEEKYKELsassEELSEEKDALLAQRAAHEARIRELEEDIKTLtqrvlerETELERMKERAKKAGAQRKEEEAERKQLQ 177
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    492 AQVTKIRDQCHMQEVTINEQEGELNAKRSELQKLKDEEASLQKEYDSNNR----------ELSKLTNHLQATQLQI---- 557
Cdd:pfam07888  178 AKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRkeaenealleELRSLQERLNASERKVeglg 257
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 24762736    558 SSVRSMVTQLLETQRQMTDALLICrAAMENQNAEL 592
Cdd:pfam07888  258 EELSSMAAQRDRTQAELHQARLQA-AQLTLQLADA 291
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
423-570 2.95e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 55.07  E-value: 2.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736   423 ELEMISKEIEELARERRVLETEIAQKEADVRI----------KNGEVRSLQSELDTLTATLKQLENQRGEAQKRLDDLQA 492
Cdd:PRK03918  201 ELEEVLREINEISSELPELREELEKLEKEVKEleelkeeieeLEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEE 280
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24762736   493 QVTKIRDqchmqevtINEQEGELNAKRSELQKLKDEEASLQKeydsnnrELSKLTNHLQATQLQISSVRSMVTQLLET 570
Cdd:PRK03918  281 KVKELKE--------LKEKAEEYIKLSEFYEEYLDELREIEK-------RLSRLEEEINGIEERIKELEEKEERLEEL 343
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
424-638 3.73e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 54.92  E-value: 3.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  424 LEMISKEIEELARERRVLETEIAQKEA-----------------------DVRIKNGEVRSLQSELDTLTAT---LKQLE 477
Cdd:COG4913  612 LAALEAELAELEEELAEAEERLEALEAeldalqerrealqrlaeyswdeiDVASAEREIAELEAELERLDASsddLAALE 691
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  478 NQRGEAQKRLDDLQAQVTKIRDQchmqevtINEQEGELNAKRSELQKLKDEEASLQKEYDSNNRELskLTNHLQAtQLQI 557
Cdd:COG4913  692 EQLEELEAELEELEEELDELKGE-------IGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL--LEERFAA-ALGD 761
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  558 SSVRSMVTQLLETQRQMTDALLICRAAMENQNAELVSEYQLKIE---------PDFDEARKTLtKEVQLPKddpFEENNS 628
Cdd:COG4913  762 AVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETAdldadleslPEYLALLDRL-EEDGLPE---YEERFK 837
                        250
                 ....*....|
gi 24762736  629 GAANQATNGF 638
Cdd:COG4913  838 ELLNENSIEF 847
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
425-598 3.87e-07

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: 54.74  E-value: 3.87e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    425 EMISKEIEELARERRVLE----------TEIAQKEADVRIKNGEVRSLQSELDTLTATLKQLENQrGE----AQKRLDDL 490
Cdd:pfam15921  475 EMLRKVVEELTAKKMTLEssertvsdltASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNE-GDhlrnVQTECEAL 553
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    491 QAQVTK-------IRDQCH--MQ------------EVTINEQEGELNAKRSELQKLKdeeaSLQKEYDSNNRELSKLTNH 549
Cdd:pfam15921  554 KLQMAEkdkvieiLRQQIEnmTQlvgqhgrtagamQVEKAQLEKEINDRRLELQEFK----ILKDKKDAKIRELEARVSD 629
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 24762736    550 LQATQLQISSVRSMVTQLLETQRQMTDALL----ICRAAMENqnaeLVSEYQL 598
Cdd:pfam15921  630 LELEKVKLVNAGSERLRAVKDIKQERDQLLnevkTSRNELNS----LSEDYEV 678
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
423-578 4.46e-07

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: 54.44  E-value: 4.46e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    423 ELEMISKEIEELARERRVLETEIAQKEAdvrikngEVRSLQSELDTLTATLKQLENQRGEAQKRLDDLQA--------QV 494
Cdd:pfam10174  545 NAEEAVRTNPEINDRIRLLEQEVARYKE-------ESGKAQAEVERLLGILREVENEKNDKDKKIAELESltlrqmkeQN 617
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    495 TKIRDQCHMQEVTINEQEGELNAKRSELQKLKDEEASLQKEYDSNnrELSKLTNHLQATQLQISSVRSMVTQ-------- 566
Cdd:pfam10174  618 KKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELMG--ALEKTRQELDATKARLSSTQQSLAEkdghltnl 695
                          170
                   ....*....|..
gi 24762736    567 LLETQRQMTDAL 578
Cdd:pfam10174  696 RAERRKQLEEIL 707
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
423-601 5.62e-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: 54.30  E-value: 5.62e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    423 ELEMISKEIEELARERRVLETEIAQKEADVRIK---------------------NGEVRSLQSELDTLTATLKQLENQRG 481
Cdd:TIGR02169  351 RRDKLTEEYAELKEELEDLRAELEEVDKEFAETrdelkdyrekleklkreinelKRELDRLQEELQRLSEELADLNAAIA 430
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    482 EAQKRLDDLQAQVTKIRDQchmqevtINEQEGELNAKRSELQKLKDEEASLQKEYDSNNRELSKLtnhlqatQLQISSVR 561
Cdd:TIGR02169  431 GIEAKINELEEEKEDKALE-------IKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKL-------QRELAEAE 496
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 24762736    562 SMVTQLLETQRQMTDALLICRAAME---NQNAELVS---EYQLKIE 601
Cdd:TIGR02169  497 AQARASEERVRGGRAVEEVLKASIQgvhGTVAQLGSvgeRYATAIE 542
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
423-601 6.84e-07

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 53.89  E-value: 6.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736   423 ELEMISKEIEELARErrvLETEIAQKEADVRIKNGEVRSLQSELDTLTATLKQLENQRGEAQKRLDDLQAQVTKIRDQCH 502
Cdd:PRK02224  353 DLEERAEELREEAAE---LESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREA 429
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736   503 MQEVTINE-----QEGE-----------------------LNAKRSELQKLKDEEASLQKEYDSNNRELSKLTNhLQATQ 554
Cdd:PRK02224  430 ELEATLRTarervEEAEalleagkcpecgqpvegsphvetIEEDRERVEELEAELEDLEEEVEEVEERLERAED-LVEAE 508
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 24762736   555 LQISSV---RSMVTQLLETQRQMTDALLICRAAMENQNAELVSEYQLKIE 601
Cdd:PRK02224  509 DRIERLeerREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKRE 558
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
425-615 7.29e-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: 53.49  E-value: 7.29e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    425 EMISKEIEELAR-ERRVLETEIAQKEADVRIKN--GEVRSLQSELDTLTATLKQLENQRGEAQKRLDDLQAQVTKIRDQC 501
Cdd:TIGR04523  117 EQKNKLEVELNKlEKQKKENKKNIDKFLTEIKKkeKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKL 196
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    502 HMQEVTI------NEQEGELNakrSELQKLKDEEASLQKEYDSNNRELSKLTNHLQATQLQISSVRS----MVTQLLETQ 571
Cdd:TIGR04523  197 LKLELLLsnlkkkIQKNKSLE---SQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDeqnkIKKQLSEKQ 273
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 24762736    572 RQM--TDALLIcraAMENQnaelVSEYQLKIEPDFDEARKTLTKEV 615
Cdd:TIGR04523  274 KELeqNNKKIK---ELEKQ----LNQLKSEISDLNNQKEQDWNKEL 312
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
423-492 1.44e-06

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: 47.56  E-value: 1.44e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  423 ELEMISKEIEELARERRVLETEIAQKEADVRIKNGEVRSLQSELDTLtatlkQLENqrGEAQKRLDDLQA 492
Cdd:cd22887    5 ELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIAL-----QIEN--NLLEEKLRKLQE 67
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
429-621 1.53e-06

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: 52.87  E-value: 1.53e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    429 KEIEELARERRVL-----ETEIAQKEAD-------VRIKNGE---------VRSLQSELDTLTATLKQLENQRGEAQKRL 487
Cdd:pfam01576  384 SENAELQAELRTLqqakqDSEHKRKKLEgqlqelqARLSESErqraelaekLSKLQSELESVSSLLNEAEGKNIKLSKDV 463
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    488 DDLQAQVTKIrdqchmQEVTINEQEGELNAKrSELQKLKDEEASLQKEYDSNNRELSKLTNHLQATQLQISSVRSMVTQL 567
Cdd:pfam01576  464 SSLESQLQDT------QELLQEETRQKLNLS-TRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEED 536
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 24762736    568 LETqrqmTDALLICRAAMENQNAELVSEYQLKIEPdFDEARKTLTKeVQLPKDD 621
Cdd:pfam01576  537 AGT----LEALEEGKKRLQRELEALTQQLEEKAAA-YDKLEKTKNR-LQQELDD 584
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
423-534 1.60e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 52.76  E-value: 1.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736   423 ELEMISKEIEELARERRVLETEIAQK-----EADVRIKNGEVRSLQSELDTLTATLKQLENQRGEAQKRLDDLQAQVTKI 497
Cdd:PRK03918  627 ELDKAFEELAETEKRLEELRKELEELekkysEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEER 706
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 24762736   498 RDQCHMQEVtINEQEGELNAKRSELQKLKD--EEASLQK 534
Cdd:PRK03918  707 EKAKKELEK-LEKALERVEELREKVKKYKAllKERALSK 744
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
438-616 1.81e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 52.08  E-value: 1.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  438 RRVLETEIAQKEADVRIKNGEVRSLQ-SELDTLTATLKQLENQRGE---AQKRLDDLQAQvtkirdqchmqevtINEQEG 513
Cdd:COG4717   44 RAMLLERLEKEADELFKPQGRKPELNlKELKELEEELKEAEEKEEEyaeLQEELEELEEE--------------LEELEA 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  514 ELNAKRSELQKLKDEEA--SLQKEYDSNNRELSKLTNHLQATQLQISSVRSMVTQL-------LETQRQMTDALLICRAA 584
Cdd:COG4717  110 ELEELREELEKLEKLLQllPLYQELEALEAELAELPERLEELEERLEELRELEEELeeleaelAELQEELEELLEQLSLA 189
                        170       180       190
                 ....*....|....*....|....*....|..
gi 24762736  585 MENQNAELVSEYQlkiepDFDEARKTLTKEVQ 616
Cdd:COG4717  190 TEEELQDLAEELE-----ELQQRLAELEEELE 216
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
423-552 1.86e-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: 52.37  E-value: 1.86e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    423 ELEMISKEIEELARERRVLETEIAQKEADVRIKNGEVRSLQSELDTLTATL-------KQLENQRGEAQKRLDDLQAQVT 495
Cdd:TIGR02168  853 DIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELreleskrSELRRELEELREKLAQLELRLE 932
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 24762736    496 KIrdqchmqEVTINEQEGELNAKRS-ELQKLKDEEASLQKEYDSNNRELSKLTNHLQA 552
Cdd:TIGR02168  933 GL-------EVRIDNLQERLSEEYSlTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
409-616 2.28e-06

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: 52.10  E-value: 2.28e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    409 DLQPQEVKPTYSNpELEMISKEIEELARERRVLETEIAQKEAdvrikngEVRSLQSELDTLTATLKQLENQRGEAQKRLD 488
Cdd:pfam01576  344 EAQLQEMRQKHTQ-ALEELTEQLEQAKRNKANLEKAKQALES-------ENAELQAELRTLQQAKQDSEHKRKKLEGQLQ 415
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    489 DLQAQVTKirdqchmqevtINEQEGELNAKRSELQKLKDEEASLQKEYDSNN----RELSKLTNHLQATQ---------- 554
Cdd:pfam01576  416 ELQARLSE-----------SERQRAELAEKLSKLQSELESVSSLLNEAEGKNiklsKDVSSLESQLQDTQellqeetrqk 484
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24762736    555 LQISS-VRSM---VTQLLETQRQMTDAllicRAAMENQ----NAELvSEYQLKIEPD------FDEARKTLTKEVQ 616
Cdd:pfam01576  485 LNLSTrLRQLedeRNSLQEQLEEEEEA----KRNVERQlstlQAQL-SDMKKKLEEDagtleaLEEGKKRLQRELE 555
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
423-621 2.37e-06

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: 52.36  E-value: 2.37e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    423 ELEMISKEIEELARERRVLETEIAQKEADVRIKNGEVRSLQSELDTLTATLKQLENQRGEAQKRL----------DDLQA 492
Cdd:TIGR00606  710 KLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLgtimpeeesaKVCLT 789
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    493 QVTkIRDQCHMQ----EVTINEQEGELNAKRSEL--QKLKDEEASLQKEYDSNNRELSKLTNHLQATQLQISSVRSMVTQ 566
Cdd:TIGR00606  790 DVT-IMERFQMElkdvERKIAQQAAKLQGSDLDRtvQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNE 868
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 24762736    567 LLETQRQMTDALLIcRAAMENQNAELVSEYQLKIEpDFDEARKTLTKEVQLPKDD 621
Cdd:TIGR00606  869 LKSEKLQIGTNLQR-RQQFEEQLVELSTEVQSLIR-EIKDAKEQDSPLETFLEKD 921
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
428-577 2.40e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 51.99  E-value: 2.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736   428 SKEIEELARErrvLETEIAQKEADVRIKNGEVRSLQSELDTLTATLKQLENQRGEaqkrLDDLQAQVTKIRDQCHMQEVT 507
Cdd:PRK03918  188 TENIEELIKE---KEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEE----IEELEKELESLEGSKRKLEEK 260
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24762736   508 INEQEGELNAKRSELQKLKDEEASLQ------KEYDSNNRELSKLTNHLQATQLQISSVRSmvtQLLETQRQMTDA 577
Cdd:PRK03918  261 IRELEERIEELKKEIEELEEKVKELKelkekaEEYIKLSEFYEEYLDELREIEKRLSRLEE---EINGIEERIKEL 333
BAR_SNX cd07596
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ...
401-579 2.54e-06

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153280 [Multi-domain]  Cd Length: 218  Bit Score: 49.66  E-value: 2.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  401 MRATVAGVDLQPQEVKPTYSN--PELEMISKEIEELARERRVLETEIAQKEADVRIKNgeVRSLQSELDTLTATL----- 473
Cdd:cd07596   23 LSKQAQRLVKRRRELGSALGEfgKALIKLAKCEEEVGGELGEALSKLGKAAEELSSLS--EAQANQELVKLLEPLkeylr 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  474 -----KQLENQRGEAQKRLDDLQAQVTKIRDQCHMQEVTINEQEGELNAKRSELQKLKDEEASLQKEYD----SNNRELS 544
Cdd:cd07596  101 ycqavKETLDDRADALLTLQSLKKDLASKKAQLEKLKAAPGIKPAKVEELEEELEEAESALEEARKRYEeiseRLKEELK 180
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 24762736  545 KLTNHLQAtqlqisSVRSMVTQLLETQRQMTDALL 579
Cdd:cd07596  181 RFHEERAR------DLKAALKEFARLQVQYAEKIA 209
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
413-545 2.95e-06

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 50.68  E-value: 2.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  413 QEVKPTysNPELEM-ISKEIEELARERRVLETEIAQKEaDVRIKNGEVRSLQSELDTLTATLKQLENQRGEA-------- 483
Cdd:COG1340  125 QQTEVL--SPEEEKeLVEKIKELEKELEKAKKALEKNE-KLKELRAELKELRKEAEEIHKKIKELAEEAQELheemiely 201
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24762736  484 ------QKRLDDLQAQVTKIRDQchmqevtINEQEGELNAKRSELQKLKDEEASLQKEYDSNNRELSK 545
Cdd:COG1340  202 keadelRKEADELHKEIVEAQEK-------ADELHEEIIELQKELRELRKELKKLRKKQRALKREKEK 262
Filament pfam00038
Intermediate filament protein;
434-601 3.07e-06

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 50.69  E-value: 3.07e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    434 LARERRVLETEIAQKEADV-----RIKN---GEVRSLQSELDTLTATLKQLENQRGEAQKRLDDLQAQVTK---IRDQCH 502
Cdd:pfam00038   23 LEQQNKLLETKISELRQKKgaepsRLYSlyeKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDelnLRTSAE 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    503 MQEVTINEQEGELNAKRSELQK----LKDEEASLQKEYDSnnrELSKLTNHLQATQLQIS--SVRSM-VTQLLETQRQMT 575
Cdd:pfam00038  103 NDLVGLRKDLDEATLARVDLEAkiesLKEELAFLKKNHEE---EVRELQAQVSDTQVNVEmdAARKLdLTSALAEIRAQY 179
                          170       180
                   ....*....|....*....|....*.
gi 24762736    576 DALlicrAAMENQNAElvSEYQLKIE 601
Cdd:pfam00038  180 EEI----AAKNREEAE--EWYQSKLE 199
CEP63 pfam17045
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ...
422-629 3.86e-06

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: 49.82  E-value: 3.86e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    422 PELE--------MISKEIEELARERRVLETeiaqkeadvRIKNGEvrslqSELDTLTATLKQLENQRGEAQKRLDDLQAQ 493
Cdd:pfam17045    6 AELQelmkqidiMVAHKKSEWEGQTRALET---------RLDIRE-----EELLSARNTLERKHKEIGLLRQQLEELEKG 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    494 vtkirdqchMQEVTInEQEGELNAKRSELQKLKDEEASLQKEYDSNNRELSKLtnhlqatQLQISSVRSMVTQLLETQRQ 573
Cdd:pfam17045   72 ---------KQELVA-KYEQQLQKLQEELSKLKRSYEKLQRKQLKEAREEAKS-------REEDRSELSRLNGKLEEFRQ 134
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 24762736    574 MTdallicrAAMENQnaELVSEYQLKiepDFDEARKTLTKEVQLPKDDPFEENNSG 629
Cdd:pfam17045  135 KS-------LEWEQQ--RLQYQQQVA---SLEAQRKALAEQSSLIQSAAYQVQLEG 178
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
420-578 5.52e-06

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 49.52  E-value: 5.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  420 SNPELEMISKEIEELarERRvLETEIAQKEADVRIKNgEVRSLQSELDTLTATLKQLENQRgEAQKRLDDLQAQVTKIRD 499
Cdd:COG1340  107 AGGSIDKLRKEIERL--EWR-QQTEVLSPEEEKELVE-KIKELEKELEKAKKALEKNEKLK-ELRAELKELRKEAEEIHK 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  500 QchMQEVT--INEQEGELNAKRSELQKLKDEEASLQKEYDSNNRELSKLTNHLQATQLQISSVRsmvtQLLETQRQMTDA 577
Cdd:COG1340  182 K--IKELAeeAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELR----KELKKLRKKQRA 255

                 .
gi 24762736  578 L 578
Cdd:COG1340  256 L 256
46 PHA02562
endonuclease subunit; Provisional
421-568 7.96e-06

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 50.01  E-value: 7.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736   421 NPELEMISKEIEELARERRVLETEIA---------QKEADVRIKNGE--------------VRSLQSELDTLTATLKQLE 477
Cdd:PHA02562  240 TDELLNLVMDIEDPSAALNKLNTAAAkikskieqfQKVIKMYEKGGVcptctqqisegpdrITKIKDKLKELQHSLEKLD 319
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736   478 NQRGEAQKRLDDLQAQVTKIRDqchMQEvTINEQEGELNAKRSELQKLKDEEASLQKEYDSNNRELSKLTNHLQATQLQI 557
Cdd:PHA02562  320 TAIDELEEIMDEFNEQSKKLLE---LKN-KISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTK 395
                         170
                  ....*....|....*..
gi 24762736   558 SSV------RSMVTQLL 568
Cdd:PHA02562  396 SELvkekyhRGIVTDLL 412
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
423-551 1.23e-05

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: 48.10  E-value: 1.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    423 ELEMISKE----IEELARERRVLETEIAQKEADVRIKNGEVRSLQSELDTLTATLKQLENQRGEAQKRLDDLQAQvtkIR 498
Cdd:pfam00261  103 EAKEIAEEadrkYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSLEASEEKASEREDKYEEQ---IR 179
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24762736    499 DqchmqeVTINEQEGELNAKRSE-----LQKLKD---EEASLQKE-YDSNNRELSKLTNHLQ 551
Cdd:pfam00261  180 F------LTEKLKEAETRAEFAErsvqkLEKEVDrleDELEAEKEkYKAISEELDQTLAELN 235
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
428-621 1.60e-05

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: 49.44  E-value: 1.60e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    428 SKEIEELARERRVLETEIAQKEADVRIKNGEVRSLQSELDTLTATLKQLENQRGEAQKRLDDLQAQ-------------- 493
Cdd:pfam10174  365 TKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDssntdtalttleea 444
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    494 -------VTKIRDQchmQEVTINEQEGELNAKRSELQKLKDEEASLQKEYDSNNRELSKLTNHlqATQLQISSVR--SMV 564
Cdd:pfam10174  445 lsekeriIERLKEQ---REREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEH--ASSLASSGLKkdSKL 519
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 24762736    565 TQL-LETQRQMTDALLICRAAMENQNAELVSeyqlKIEPDFDEARKTLTKEVQLPKDD 621
Cdd:pfam10174  520 KSLeIAVEQKKEECSKLENQLKKAHNAEEAV----RTNPEINDRIRLLEQEVARYKEE 573
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
426-616 2.04e-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: 49.02  E-value: 2.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    426 MISKEIEELARE---RRVLETEIAQKEADVRIKNGEVRSLQSELDTLTATLKQLENQRGEAQKRLDDLQAQVT----KIR 498
Cdd:pfam01576  188 MISDLEERLKKEekgRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNnalkKIR 267
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    499 D-QCHMQEVTIN-EQE---------------GELNAKRSELQKLKDEEASLQKEYDSNNRELSKLTNHLQ----ATQLQI 557
Cdd:pfam01576  268 ElEAQISELQEDlESEraarnkaekqrrdlgEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEeetrSHEAQL 347
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24762736    558 SSVRSMVTQLLET-QRQMTDA------LLICRAAMENQNAELVSEYQL--KIEPDFDEARKTLTKEVQ 616
Cdd:pfam01576  348 QEMRQKHTQALEElTEQLEQAkrnkanLEKAKQALESENAELQAELRTlqQAKQDSEHKRKKLEGQLQ 415
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
317-376 2.72e-05

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 45.17  E-value: 2.72e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  317 RFEEIFRQSDLDKDGLVSGLEVKDIFIKSGIPQRSLADIWALCDTNQSGKLTVEQFALAM 376
Cdd:COG5126   70 FARAAFDLLDTDGDGKISADEFRRLLTALGVSEEEADELFARLDTDGDGKISFEEFVAAV 129
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
469-574 2.79e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 47.84  E-value: 2.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  469 LTATLKQLENQRGEAQKRLDDLQAQVTKIRDQCHMQEVTINEQEGELNAKRSELQKLKDEEASLQKEYDSNNRELSKLTN 548
Cdd:COG4942   11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
                         90       100
                 ....*....|....*....|....*.
gi 24762736  549 HLQATQLQISSVRSMVTQLLETQRQM 574
Cdd:COG4942   91 EIAELRAELEAQKEELAELLRALYRL 116
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
423-621 3.21e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.59  E-value: 3.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  423 ELEMISKEIEELARERRVLETE-------IAQKEADVRIKNGEVRSLQSELDTLTATLKQLENQRG-----EAQKRLDDL 490
Cdd:COG4372  109 EAEELQEELEELQKERQDLEQQrkqleaqIAELQSEIAEREEELKELEEQLESLQEELAALEQELQalseaEAEQALDEL 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  491 QAQ----VTKIRDQC-----HMQEVTINEQEGELNAKRSELQKLKDEEASLQKEYDSNNRELSKLTNHLQATQLQISSVR 561
Cdd:COG4372  189 LKEanrnAEKEEELAeaeklIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAIL 268
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  562 SMVTQLLETQRQMTDALLICRAAMENQNAELVSEYQLKIEPDFDEARKTLTKEVQLPKDD 621
Cdd:COG4372  269 VEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKL 328
DUF4515 pfam14988
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ...
429-578 3.27e-05

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


Pssm-ID: 405647 [Multi-domain]  Cd Length: 206  Bit Score: 46.30  E-value: 3.27e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    429 KEIEELARERRVLETEIAQKEADVRIKNGEVRSLQSELDTLTATLKQLENQRGEAQKRLDDLQAQVTKIR-------DQC 501
Cdd:pfam14988   29 QECEEIERRRQELASRYTQQTAELQTQLLQKEKEQASLKKELQALRPFAKLKESQEREIQDLEEEKEKVRaetaekdREA 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    502 HMQ---EVTINEQE---------GELNAK--RSELQKLKDEEASLQKEYDSN----NRELSK-LTNHLQATQ-LQ-ISSV 560
Cdd:pfam14988  109 HLQflkEKALLEKQlqelrilelGERATRelKRKAQALKLAAKQALSEFCRSikreNRQLQKeLLQLIQETQaLEaIKSK 188
                          170
                   ....*....|....*...
gi 24762736    561 RSMVTQLLETQRQMTDAL 578
Cdd:pfam14988  189 LENRKQRLKEEQWYLEAL 206
ADIP pfam11559
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ...
445-550 3.38e-05

Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.


Pssm-ID: 463295 [Multi-domain]  Cd Length: 151  Bit Score: 45.38  E-value: 3.38e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    445 IAQKEADVRIK---NGEVRSLQSELDTLTATLKQLENQRGEAQKRLDDLQAQVTKIRDQchmqevtINEQEGELNAKRSE 521
Cdd:pfam11559   44 LQQRDRDLEFReslNETIRTLEAEIERLQSKIERLKTQLEDLERELALLQAKERQLEKK-------LKTLEQKLKNEKEE 116
                           90       100       110
                   ....*....|....*....|....*....|...
gi 24762736    522 LQKLK----DEEASLQKEYDSNNRELSKLTNHL 550
Cdd:pfam11559  117 LQRLKnalqQIKTQFAHEVKKRDREIEKLKERL 149
COG5022 COG5022
Myosin heavy chain [General function prediction only];
423-632 3.64e-05

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 48.15  E-value: 3.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  423 ELEMISKEIEELAReRRVLETEIAQKEAD-------------VRIKNGEVRSLQSELDTLT---ATLKQLENQRG----- 481
Cdd:COG5022  868 TIYLQSAQRVELAE-RQLQELKIDVKSISslklvnleleseiIELKKSLSSDLIENLEFKTeliARLKKLLNNIDleegp 946
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  482 ----EAQKRLDDLQAQVTKIRDQCHMQEVTIN---EQEGELNAKRSELQKLKDEEASLQKEYDSNNRELSKLT------N 548
Cdd:COG5022  947 sieyVKLPELNKLHEVESKLKETSEEYEDLLKkstILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKelpvevA 1026
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  549 HLQATQLQISSVRSMVTQLLETQRQMTDALLicraaMENQNAELVSEYQLKIEPDFD--------EARKTLTKEVQLPKD 620
Cdd:COG5022 1027 ELQSASKIISSESTELSILKPLQKLKGLLLL-----ENNQLQARYKALKLRRENSLLddkqlyqlESTENLLKTINVKDL 1101
                        250
                 ....*....|..
gi 24762736  621 DPFEENNSGAAN 632
Cdd:COG5022 1102 EVTNRNLVKPAN 1113
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
448-576 3.75e-05

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 46.28  E-value: 3.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  448 KEADVRIKNGEVRSLQSELDTLTATLKQLENQRGEAQKRLDDLQAQVTKIRDQCHMQEVTINEQEGELNAKRSELQKLKD 527
Cdd:cd00176   17 SEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLEELNQRWEELRELAE 96
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 24762736  528 E-EASLQKEYD--SNNRELSKLTNHLQATQLQISSvRSMVTQLLETQRQMTD 576
Cdd:cd00176   97 ErRQRLEEALDlqQFFRDADDLEQWLEEKEAALAS-EDLGKDLESVEELLKK 147
EF-hand_4 pfam12763
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ...
312-406 4.31e-05

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: 43.90  E-value: 4.31e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    312 PADLKRFEEIFrQSDLDKDGLVSGLEVKDIFIKSGIPQRSLADIWALCDTNQSGKLTVEQFALAMWFVERKQRGV--DPP 389
Cdd:pfam12763    6 EWEIKKYWEIF-SGLKPENNKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLIFDLVNGNiaDVP 84
                           90
                   ....*....|....*..
gi 24762736    390 HVLNANMVPPSMRATVA 406
Cdd:pfam12763   85 DELPDWLVPGSKAHLIQ 101
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
422-551 5.60e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 47.73  E-value: 5.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736   422 PELEMISKEIEELARERRVLETEIAQKEADVRIKNGEVRSLQSELDTLTATLKQLENQRGEAQKRLDDLQAQVTKIRDQC 501
Cdd:PRK02224  307 ADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEI 386
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 24762736   502 HMQEVTINEQEGELNAKRSELQKLKDEEASLQKEYDSNNRELSKLTNHLQ 551
Cdd:PRK02224  387 EELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLR 436
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
460-578 6.17e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 47.32  E-value: 6.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  460 RSLQSELDTLTATLKQLENQRGEAQKRLDDLQAQVTKIRDQchMQEVTINEQEGELNAK----RSELQKLKDEEASLQKE 535
Cdd:COG3206  164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQK--NGLVDLSEEAKLLLQQlselESQLAEARAELAEAEAR 241
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 24762736  536 YDSNNRELSKLTNHLQATqLQISSVRSMVTQLLETQRQMTDAL 578
Cdd:COG3206  242 LAALRAQLGSGPDALPEL-LQSPVIQQLRAQLAELEAELAELS 283
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
409-601 7.26e-05

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: 47.12  E-value: 7.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    409 DLQpQEVKPTYSNPELEMIS-----KEIEELARERRVLETEIAQKEADVRIKNGEVRSLQSELDTLT---ATLKQ----L 476
Cdd:pfam10174  251 DLE-DEVQMLKTNGLLHTEDreeeiKQMEVYKSHSKFMKNKIDQLKQELSKKESELLALQTKLETLTnqnSDCKQhievL 329
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    477 ENQRGEAQKRLDDLQAQVTKIRdqchmqeVTINEQEGELNAKRSELQKLKDEEASLQKE-------YDSNNRE---LSKL 546
Cdd:pfam10174  330 KESLTAKEQRAAILQTEVDALR-------LRLEEKESFLNKKTKQLQDLTEEKSTLAGEirdlkdmLDVKERKinvLQKK 402
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    547 TNHLQaTQL-----QISSVRSMVtQLLETQRQMTDALLicrAAMEnqnaELVSEYQLKIE 601
Cdd:pfam10174  403 IENLQ-EQLrdkdkQLAGLKERV-KSLQTDSSNTDTAL---TTLE----EALSEKERIIE 453
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
423-526 7.41e-05

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 46.06  E-value: 7.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  423 ELEMISKEIEELARERRVLETEIAQ--KEADvRIKnGEVRSLQSELDTLTATLKQLENQRGEAQKRLDDLQAQVTKIRDQ 500
Cdd:COG1340  175 EAEEIHKKIKELAEEAQELHEEMIElyKEAD-ELR-KEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKK 252
                         90       100
                 ....*....|....*....|....*..
gi 24762736  501 CHMQEVTinEQEGELNAKRSE-LQKLK 526
Cdd:COG1340  253 QRALKRE--KEKEELEEKAEEiFEKLK 277
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
475-547 9.21e-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: 42.55  E-value: 9.21e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24762736  475 QLENQRGEAQKRLDDLQAQVTKIRDQChmqevtiNEQEGELNAKRSELQKLKDEEASLQKEYDSNNRELSKLT 547
Cdd:cd22887    1 ELESELQELEKRLAELEAELASLEEEI-------KDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQ 66
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
434-615 9.60e-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: 9.60e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    434 LARERRVLETEIAQKE-------ADVRIKNGEVRSLQSELDTLTATL--------------KQLENQRGEAQKRLDDLQA 492
Cdd:pfam01576  880 LQDEKRRLEARIAQLEeeleeeqSNTELLNDRLRKSTLQVEQLTTELaaerstsqksesarQQLERQNKELKAKLQEMEG 959
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    493 QV-TKIRDQCHMQEVTINEQEGELNAKRSELQ-----------KLKdeEASLQKEYDSNNRELSKltnhlqaTQLQISSV 560
Cdd:pfam01576  960 TVkSKFKSSIAALEAKIAQLEEQLEQESRERQaanklvrrtekKLK--EVLLQVEDERRHADQYK-------DQAEKGNS 1030
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 24762736    561 RsmVTQLletQRQMTDallicrAAMENQNAelvSEYQLKIEPDFDEARK---TLTKEV 615
Cdd:pfam01576 1031 R--MKQL---KRQLEE------AEEEASRA---NAARRKLQRELDDATEsneSMNREV 1074
PRK01156 PRK01156
chromosome segregation protein; Provisional
400-606 1.04e-04

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 46.82  E-value: 1.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736   400 SMRATVAGVDLQPQEVKPtySNPELEMISKEIEELARERRVLETEIAQKEADVRIKNGEVRSLQSELDTLTA---TLKQL 476
Cdd:PRK01156  177 MLRAEISNIDYLEEKLKS--SNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSledMKNRY 254
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736   477 ENQRGEAQKRLDDLQAQVTK----------------------IRDQCHMQEVTINEQE------GELNA------KRSEL 522
Cdd:PRK01156  255 ESEIKTAESDLSMELEKNNYykeleerhmkiindpvyknrnyINDYFKYKNDIENKKQilsnidAEINKyhaiikKLSVL 334
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736   523 QKLKDEEASLQKEYDSNNRELSKLTNHLQATQLQISSVRSMVTQLLE---TQRQMTDALLICRAAMENQNAELVSEYQlK 599
Cdd:PRK01156  335 QKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEyskNIERMSAFISEILKIQEIDPDAIKKELN-E 413

                  ....*..
gi 24762736   600 IEPDFDE 606
Cdd:PRK01156  414 INVKLQD 420
Taxilin pfam09728
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ...
423-638 1.18e-04

Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.


Pssm-ID: 462861 [Multi-domain]  Cd Length: 302  Bit Score: 45.71  E-value: 1.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    423 ELEMISKEIEELARERRVLETE--IAQKEADVRIKngEVRSLQSELDTLTATLKQLENQRGEAQKRLDDLQA---QVTKI 497
Cdd:pfam09728   19 KLAALCKKYAELLEEMKRLQKDlkKLKKKQDQLQK--EKDQLQSELSKAILAKSKLEKLCRELQKQNKKLKEeskKLAKE 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    498 RDQCHMQ-----EVTINEQEGELNAKRSELQKLKDEEASLQKeydsnnrELSKLTNHLQATQLQISSvrsmVTQLLETQR 572
Cdd:pfam09728   97 EEEKRKElsekfQSTLKDIQDKMEEKSEKNNKLREENEELRE-------KLKSLIEQYELRELHFEK----LLKTKELEV 165
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24762736    573 QMTDALLIC------RAAMENQNAElVSEYQLKIEpdfdEARKTLTK-----EVQLPKDDPFEE--NNSgaaNQATNGF 638
Cdd:pfam09728  166 QLAEAKLQQateeeeKKAQEKEVAK-ARELKAQVQ----TLSETEKElreqlNLYVEKFEEFQDtlNKS---NEVFTTF 236
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
465-592 1.20e-04

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 45.81  E-value: 1.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  465 ELDT--LTATLKQLENQRGEAQKRLDDLQAQVTkirdqchmQEVTINEQEGELNAKRSELQKLKDEEASLQK-------- 534
Cdd:COG1566   75 RLDPtdLQAALAQAEAQLAAAEAQLARLEAELG--------AEAEIAAAEAQLAAAQAQLDLAQRELERYQAlykkgavs 146
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24762736  535 --EYDSNNRELSKLTNHLQATQLQISSVRSMV---TQLLETQRQMTDAllicRAAMENQNAEL 592
Cdd:COG1566  147 qqELDEARAALDAAQAQLEAAQAQLAQAQAGLreeEELAAAQAQVAQA----EAALAQAELNL 205
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
432-585 1.34e-04

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 46.59  E-value: 1.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736   432 EELARERRVLETEIAQKEADVRiknGEVRSLQSELdtltatlkqlenqrgeAQKRLDDLQAQVTKIRDQCHMQEvtinEQ 511
Cdd:PRK10929  181 ESAALKALVDELELAQLSANNR---QELARLRSEL----------------AKKRSQQLDAYLQALRNQLNSQR----QR 237
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24762736   512 EGELNAKRSELqkLKDEEASLQKEYDSN---NRELSKLTNHlQATQL-QISSvrsmvtqlleTQRQMTDALLICRAAM 585
Cdd:PRK10929  238 EAERALESTEL--LAEQSGDLPKSIVAQfkiNRELSQALNQ-QAQRMdLIAS----------QQRQAASQTLQVRQAL 302
EF-hand_4 pfam12763
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ...
24-77 1.45e-04

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: 42.36  E-value: 1.45e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 24762736     24 DPKGTGAieamTAAKFLKKSGLSDVVLSRIWDLSDPSGKGFLDKPGFFVALKLV 77
Cdd:pfam12763   23 NNKLTGD----QVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLI 72
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
423-614 1.86e-04

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 45.81  E-value: 1.86e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    423 ELEMISKEIEELARERRvletEIAQKEADVRIKNGEVrSLQSELDTLTATLKQLENQRGEAQKRLDDLQ----------- 491
Cdd:TIGR00606  320 ELVDCQRELEKLNKERR----LLNQEKTELLVEQGRL-QLQADRHQEHIRARDSLIQSLATRLELDGFErgpfserqikn 394
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    492 AQVTKIR---DQCHMQEVTINEQEGELNAKRSELQKLKDEEASLQKEYDSNNRELSKLTNHLQATQLQISSVRSMVTQLL 568
Cdd:TIGR00606  395 FHTLVIErqeDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRIL 474
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 24762736    569 ETQRQMTDALLICRAAMENQNAE--LVSEYQLKIEP-DFDEARKTLTKE 614
Cdd:TIGR00606  475 ELDQELRKAERELSKAEKNSLTEtlKKEVKSLQNEKaDLDRKLRKLDQE 523
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
421-578 2.11e-04

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


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 44.05  E-value: 2.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  421 NPElEMISKEIEELARERRVLETEIAQkeadvrikngevrslqseldtLTATLKQLENQRGEAQKRLDDLQAQVtkirdq 500
Cdd:COG1842   23 DPE-KMLDQAIRDMEEDLVEARQALAQ---------------------VIANQKRLERQLEELEAEAEKWEEKA------ 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  501 chmqEVTINEQEGELnAKR--SELQKLKDEEASLQKEYDSNNRELSKLTNHLQATQLQISSVRSMVTQLL------ETQR 572
Cdd:COG1842   75 ----RLALEKGREDL-AREalERKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKarakaaKAQE 149

                 ....*.
gi 24762736  573 QMTDAL 578
Cdd:COG1842  150 KVNEAL 155
ADIP pfam11559
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ...
423-527 2.52e-04

Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.


Pssm-ID: 463295 [Multi-domain]  Cd Length: 151  Bit Score: 42.69  E-value: 2.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    423 ELEMISKEIEELARERRVLETEIAQKEADvrikngeVRSLQSELDTLTATLKqleNQRGEAQKRLDDLQAqvtkIRDQCh 502
Cdd:pfam11559   67 EIERLQSKIERLKTQLEDLERELALLQAK-------ERQLEKKLKTLEQKLK---NEKEELQRLKNALQQ----IKTQF- 131
                           90       100
                   ....*....|....*....|....*
gi 24762736    503 MQEVTINEQegelnakrsELQKLKD 527
Cdd:pfam11559  132 AHEVKKRDR---------EIEKLKE 147
mukB PRK04863
chromosome partition protein MukB;
429-612 3.41e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 44.95  E-value: 3.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736   429 KEIEELARERRVLET---EIAQKEADVRikngEVRSLQSELDTLTATLKQLeNQR------GEAQKRLDDLQAQVTKIRD 499
Cdd:PRK04863  918 NALAQLEPIVSVLQSdpeQFEQLKQDYQ----QAQQTQRDAKQQAFALTEV-VQRrahfsyEDAAEMLAKNSDLNEKLRQ 992
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736   500 QCHMQEVTINEQEGELNAKRSELQKLKDEEASLQKEYDSNNRELSKLTNHLQATQLQI--------SSVRSMVTQLLETQ 571
Cdd:PRK04863  993 RLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPAdsgaeeraRARRDELHARLSAN 1072
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 24762736   572 RQMTDALL----ICRAAMENQNAELVseyqlKIEPDFDEARKTLT 612
Cdd:PRK04863 1073 RSRRNQLEkqltFCEAEMDNLTKKLR-----KLERDYHEMREQVV 1112
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
424-620 3.42e-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: 45.21  E-value: 3.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    424 LEMISKEIEELARERRVLETEI--AQKEADVRIKNgevrsLQSELDTLTATLKQ-LENQRGEAQKRL----DDLQAQVTK 496
Cdd:pfam12128  349 LPSWQSELENLEERLKALTGKHqdVTAKYNRRRSK-----IKEQNNRDIAGIKDkLAKIREARDRQLavaeDDLQALESE 423
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    497 IRDQCHMQEVTINEQEGELNAKRSELqKLKDEEASLQKEYDSNNRELSKLTNHLQATQLQ----ISSVRSMVTQLLETQR 572
Cdd:pfam12128  424 LREQLEAGKLEFNEEEYRLKSRLGEL-KLRLNQATATPELLLQLENFDERIERAREEQEAanaeVERLQSELRQARKRRD 502
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 24762736    573 QMTDALLICRAAMENQNAELvSEYQLKIEPDFDEARKTLTKEVQLPKD 620
Cdd:pfam12128  503 QASEALRQASRRLEERQSAL-DELELQLFPQAGTLLHFLRKEAPDWEQ 549
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
444-617 3.70e-04

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: 44.68  E-value: 3.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    444 EIAQK----EADVRIKNGEVRSLQSELDTLTATLKQLENQRGE---AQKRLDDLQAQVTKIRDQ--------------CH 502
Cdd:pfam05622   11 ELAQRchelDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSgtpGGKKYLLLQKQLEQLQEEnfrletarddyrikCE 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    503 MQEvtinEQEGELNAKRSELQKLKDEEASLQKEYD----SNNReLSKLtnhlqatQLQISSVRSMVTQLLETQRQMTdal 578
Cdd:pfam05622   91 ELE----KEVLELQHRNEELTSLAEEAQALKDEMDilreSSDK-VKKL-------EATVETYKKKLEDLGDLRRQVK--- 155
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 24762736    579 licraAMENQNAELVSEyQLKIEpdfDEARKTLTKEVQL 617
Cdd:pfam05622  156 -----LLEERNAEYMQR-TLQLE---EELKKANALRGQL 185
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
422-619 3.88e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.67  E-value: 3.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736   422 PELEMISKEIEELARER---RVLETEIAQKEADVRIKNGEVRSLQSELDTLTATLKQLENQRGEAQKRLDDLQAQVTKIR 498
Cdd:PRK03918  286 KELKEKAEEYIKLSEFYeeyLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYE 365
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736   499 dqchmqevtineqegELNAKRSELQKLKDEEASLQKEydSNNRELSKLTNHLQATQLQISSVRSMVTQLLETQRQMTDAL 578
Cdd:PRK03918  366 ---------------EAKAKKEELERLKKRLTGLTPE--KLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAI 428
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 24762736   579 L----------ICRAAM-ENQNAELVSEYQLKIEPDFDEARKTLTKEVQLPK 619
Cdd:PRK03918  429 EelkkakgkcpVCGRELtEEHRKELLEEYTAELKRIEKELKEIEEKERKLRK 480
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
420-549 4.03e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.91  E-value: 4.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  420 SNPELEMISKEIEELARERRVLETEIAQKEADVRIKNGEVRSLQSELDTLTATLKQLEN-----QRGEAQKRLDDL--QA 492
Cdd:COG4913  683 SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDlarleLRALLEERFAAAlgDA 762
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24762736  493 QVTKIRDQchmQEVTINEQEGELNAKRSELQKL--------KDEEASLQKEYDSNN---RELSKLTNH 549
Cdd:COG4913  763 VERELREN---LEERIDALRARLNRAEEELERAmrafnrewPAETADLDADLESLPeylALLDRLEED 827
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
417-534 5.39e-04

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: 44.29  E-value: 5.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    417 PTYSNPELEMISKEIEE----LARERRVLEteiAQKEADVRIKNGEvrsLQSELDTLTATLKQLENQRGEAQKRLDDLQA 492
Cdd:pfam05622  266 DPGDNLAAEIMPAEIREklirLQHENKMLR---LGQEGSYRERLTE---LQQLLEDANRRKNELETQNRLANQRILELQQ 339
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 24762736    493 QVTKIrdQCHMQEV-TINEQEGELNAKRSE-LQKLKDEEASLQK 534
Cdd:pfam05622  340 QVEEL--QKALQEQgSKAEDSSLLKQKLEEhLEKLHEAQSELQK 381
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
423-493 5.58e-04

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: 41.09  E-value: 5.58e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    423 ELEMI--SKEIEELARERrvleTEIAQKEAdvrikngEVRSLQSELDTLTATL-----------KQLENQRGEAQKRLDD 489
Cdd:pfam07926   46 ERELVlhAEDIKALQALR----EELNELKA-------EIAELKAEAESAKAELeeseesweeqkKELEKELSELEKRIED 114

                   ....
gi 24762736    490 LQAQ 493
Cdd:pfam07926  115 LNEQ 118
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
447-543 5.78e-04

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


Pssm-ID: 439196 [Multi-domain]  Cd Length: 91  Bit Score: 40.24  E-value: 5.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  447 QKEADVRIKNGEVRSLQSELDTLTATLKQLENQrgeaqkrLDDLQAQVTKIRDQchMQEVTIneqegELNAKRSELQKLK 526
Cdd:cd22887    1 ELESELQELEKRLAELEAELASLEEEIKDLEEE-------LKEKNKANEILNDE--LIALQI-----ENNLLEEKLRKLQ 66
                         90       100
                 ....*....|....*....|....*
gi 24762736  527 DEEASL--------QKEYDSNNREL 543
Cdd:cd22887   67 EENDELverwmakkQQEADKMNEAN 91
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
427-712 5.88e-04

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


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 44.18  E-value: 5.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  427 ISKEIEELARERrvlETEIAQKEADvrIKNGEvRSLQSELDTLTATLKQL--ENQRGEAQKRLDDLQAQVTKIRDQCHMQ 504
Cdd:COG5185  323 AEQELEESKRET---ETGIQNLTAE--IEQGQ-ESLTENLEAIKEEIENIvgEVELSKSSEELDSFKDTIESTKESLDEI 396
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  505 EVTINEQEGELNAKRSELQKLKDEEAslqKEYdsnNRELSKLTNHLQATQlqissvRSMVTQLLETQRQMTDALLICRAA 584
Cdd:COG5185  397 PQNQRGYAQEILATLEDTLKAADRQI---EEL---QRQIEQATSSNEEVS------KLLNELISELNKVMREADEESQSR 464
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  585 MENQNAELVSEYQLKIEpDFDEARKTLTKEVQLPKDDpfEENNSGAANQATNGFGSDPFSGQPvnkpaistgfddSFNMS 664
Cdd:COG5185  465 LEEAYDEINRSVRSKKE-DLNEELTQIESRVSTLKAT--LEKLRAKLERQLEGVRSKLDQVAE------------SLKDF 529
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 24762736  665 SGFDSGFDAFGQSGAGSAFGQTQRDPFGSDAFAANKSNAITPEPGKDD 712
Cdd:COG5185  530 MRARGYAHILALENLIPASELIQASNAKTDGQAANLRTAVIDELTQYL 577
WEMBL pfam05701
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ...
430-586 6.13e-04

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: 43.86  E-value: 6.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    430 EIEE------LARERRVL--ETEIAQKEADVRIKNGEVRS---LQSELDT-----------LTA----TLKQLENQRGEA 483
Cdd:pfam05701  205 EAEEhrigaaLAREQDKLnwEKELKQAEEELQRLNQQLLSakdLKSKLETasallldlkaeLAAymesKLKEEADGEGNE 284
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    484 QKRLDDLQAQVTKIRDQchMQEVTINEQEGELNAK---------RSELQKLKDEEASLQKEYDSNNRELSKLTNHLQATQ 554
Cdd:pfam05701  285 KKTSTSIQAALASAKKE--LEEVKANIEKAKDEVNclrvaaaslRSELEKEKAELASLRQREGMASIAVSSLEAELNRTK 362
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 24762736    555 LQISSVRS--------MVT---QLLETQRQMTDALLICRAAME 586
Cdd:pfam05701  363 SEIALVQAkekearekMVElpkQLQQAAQEAEEAKSLAQAARE 405
UPF0242 pfam06785
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ...
410-525 6.52e-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: 42.12  E-value: 6.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    410 LQPQEVKPTYSNPE-LEMISKEIEELARERRVLETEIAQKEADVRIKNGEVRSLQSELDtltATLKQLENQRGEAQKRLD 488
Cdd:pfam06785   70 LEEKEAKLTELDAEgFKILEETLEELQSEEERLEEELSQKEEELRRLTEENQQLQIQLQ---QISQDFAEFRLESEEQLA 146
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 24762736    489 DLQAQVTKIRDqchmqevTINEQEGELNAKRSELQKL 525
Cdd:pfam06785  147 EKQLLINEYQQ-------TIEEQRSVLEKRQDQIENL 176
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
470-578 7.16e-04

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


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 43.13  E-value: 7.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  470 TATLKQLENQRGEAQKRLDDLQAQVTKIRDQChmQEV----------------TINEQEGELNAK---------RSELQK 524
Cdd:cd22656  106 ATDDEELEEAKKTIKALLDDLLKEAKKYQDKA--AKVvdkltdfenqtekdqtALETLEKALKDLltdeggaiaRKEIKD 183
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24762736  525 LKDEEASLQKEY--------DSNNRELSKLTNHLQATQLQISSVRSMVTQLLETQRQMTDAL 578
Cdd:cd22656  184 LQKELEKLNEEYaaklkakiDELKALIADDEAKLAAALRLIADLTAADTDLDNLLALIGPAI 245
PRK12704 PRK12704
phosphodiesterase; Provisional
423-562 7.34e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 43.61  E-value: 7.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736   423 ELEMISKEI-----EELARERRVLETEIAQKEADvrIKNGEVRSLQSEldtltatlKQLENQRGEAQKRLDDLQAQvtki 497
Cdd:PRK12704   50 EAEAIKKEAlleakEEIHKLRNEFEKELRERRNE--LQKLEKRLLQKE--------ENLDRKLELLEKREEELEKK---- 115
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24762736   498 rdqchmqEVTINEQEGELNAKRSELQKLKDEE-ASLQkeydsnnrELSKLTNHlQATQLQISSVRS 562
Cdd:PRK12704  116 -------EKELEQKQQELEKKEEELEELIEEQlQELE--------RISGLTAE-EAKEILLEKVEE 165
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
429-533 7.68e-04

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 40.38  E-value: 7.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    429 KEIEELARERRVLETEIAQKEADVriKNGEVRSLQSELDTLTATLKQLENQRGEAQKRLDDLQAQVTKIRDQCHMQEVTI 508
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALL--SSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEI 78
                           90       100
                   ....*....|....*....|....*.
gi 24762736    509 NEQEGELNAKRSELQKL-KDEEASLQ 533
Cdd:pfam00435   79 QERLEELNERWEQLLELaAERKQKLE 104
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
483-579 8.84e-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: 8.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  483 AQKRLDDLQAQVTKIRDQchmqevtINEQEGELNAKRSELQKLKDEEASLQKEYDSNNRELSKLTNHLQATQLQISSVRS 562
Cdd:COG4942   18 QADAAAEAEAELEQLQQE-------IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
                         90       100
                 ....*....|....*....|
gi 24762736  563 MVTQL---LETQRQMTDALL 579
Cdd:COG4942   91 EIAELraeLEAQKEELAELL 110
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
423-648 9.60e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.49  E-value: 9.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736   423 ELEMISKEIEELA-------RERRVLETEIAQKEAdvrikngEVRSLQSELDTLTATLkQLENQRGEA-QKRLDDLQAQV 494
Cdd:PRK02224  252 ELETLEAEIEDLRetiaeteREREELAEEVRDLRE-------RLEELEEERDDLLAEA-GLDDADAEAvEARREELEDRD 323
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736   495 TKIRDqchmqevTINEQEGELNAKRSELQKLKDEEASLQKEYDSNNRELSKLTNHLQATQLQISSVRSMVTQLLEtqrQM 574
Cdd:PRK02224  324 EELRD-------RLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEE---EI 393
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24762736   575 TDAllicRAAMENQNAEL--VSEYQLKIEPDFDEAR---KTLTKEVQlpkddpfEENNSGAANQATNGFGSDPFSGQPV 648
Cdd:PRK02224  394 EEL----RERFGDAPVDLgnAEDFLEELREERDELRereAELEATLR-------TARERVEEAEALLEAGKCPECGQPV 461
SPEC smart00150
Spectrin repeats;
432-528 9.80e-04

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 39.62  E-value: 9.80e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736     432 EELARERRVLETEIAQKEADVRIKN-----GEVRSLQSELDTLTATLKQLENqrgeaqkRLDDLQAQVTKIRDQCHMQEV 506
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDlgkdlESVEALLKKHEAFEAELEAHEE-------RVEALNELGEQLIEEGHPDAE 73
                            90       100
                    ....*....|....*....|..
gi 24762736     507 TINEQEGELNAKRSELQKLKDE 528
Cdd:smart00150   74 EIEERLEELNERWEELKELAEE 95
CCDC22 pfam05667
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
423-544 1.07e-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: 43.09  E-value: 1.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    423 ELEMISKEIEELARERRVLETEIAQKEADVRIK--------NGE--VRSLQSELDTLTATLKQLE--------------- 477
Cdd:pfam05667  357 EIKKLESSIKQVEEELEELKEQNEELEKQYKVKkktldllpDAEenIAKLQALVDASAQRLVELAgqwekhrvplieeyr 436
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24762736    478 -------NQRGEAQKRLDDLQaqvtKIRDQchMQEVtineqegelnakrSELQKLKDEE-ASLQKEYDSNNRELS 544
Cdd:pfam05667  437 alkeaksNKEDESQRKLEEIK----ELREK--IKEV-------------AEEAKQKEELyKQLVAEYERLPKDVS 492
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
424-526 1.09e-03

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 43.15  E-value: 1.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  424 LEMISK--EIEELARERRVLETEI--AQKEADVRIKNgEVRSLQSELDTLTATLKQLEnQRGEAQKrldDLQAQVTKIRD 499
Cdd:COG0542  404 MEIDSKpeELDELERRLEQLEIEKeaLKKEQDEASFE-RLAELRDELAELEEELEALK-ARWEAEK---ELIEEIQELKE 478
                         90       100
                 ....*....|....*....|....*..
gi 24762736  500 QCHMQEVTINEQEGELNAKRSELQKLK 526
Cdd:COG0542  479 ELEQRYGKIPELEKELAELEEELAELA 505
MscS_porin pfam12795
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...
429-574 1.14e-03

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


Pssm-ID: 432790 [Multi-domain]  Cd Length: 238  Bit Score: 41.90  E-value: 1.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    429 KEIEELARErrvLETEIAQKEADVRIKNGEvRSL----------QSELDTLTATLKQLENQRGEAQKRLDDLQAQVTKIR 498
Cdd:pfam12795   51 AELRELRQE---LAALQAKAEAAPKEILAS-LSLeeleqrllqtSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEAR 126
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    499 DQchMQEVTIN----------EQEGELNAKRSELQKLKDEEASLQKEYDSNN--RELSK-----LTNHLQATQLQISSVR 561
Cdd:pfam12795  127 QR--LQQIRNRlngpappgepLSEAQRWALQAELAALKAQIDMLEQELLSNNnrQDLLKarrdlLTLRIQRLEQQLQALQ 204
                          170
                   ....*....|....*
gi 24762736    562 SMVTQ--LLETQRQM 574
Cdd:pfam12795  205 ELLNEkrLQEAEQAV 219
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
317-376 1.24e-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: 38.30  E-value: 1.24e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24762736  317 RFEEIFRQSDLDKDGLVSGLEVKDIFIKSGIPQRS--LADIWALCDTNQSGKLTVEQFALAM 376
Cdd:cd00051    1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEeeIDEMIREVDKDGDGKIDFEEFLELM 62
KpsE COG3524
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
472-606 1.31e-03

Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442746 [Multi-domain]  Cd Length: 370  Bit Score: 42.53  E-value: 1.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  472 TLKQLENQRGEAQKRLDDLQAQVTKIRD---------QCHMQEVTINEQEGELNAKRSELQKLKdeeaslqkeydSNNRE 542
Cdd:COG3524  178 AVRFAEEEVERAEERLRDAREALLAFRNrngildpeaTAEALLQLIATLEGQLAELEAELAALR-----------SYLSP 246
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24762736  543 lskltNHLQATQLQiSSVRSMVTQLLETQRQMTDallicrAAMENQNAELVSEYQ-LKIEPDFDE 606
Cdd:COG3524  247 -----NSPQVRQLR-RRIAALEKQIAAERARLTG------ASGGDSLASLLAEYErLELEREFAE 299
mukB PRK04863
chromosome partition protein MukB;
429-612 1.61e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 43.02  E-value: 1.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736   429 KEIEELARERRVLETEIAQKEADVRikngEVRSLQSELDTLTAT-------------LKQLENQRGEAQKRLDDLQA--- 492
Cdd:PRK04863  786 KRIEQLRAEREELAERYATLSFDVQ----KLQRLHQAFSRFIGShlavafeadpeaeLRQLNRRRVELERALADHESqeq 861
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736   493 ----QVTKIRDQC-----HMQEVTINEQEG---ELNAKRSELQKLKDEEASLQKeYDSNNRELSKLTNHLQATQLQISSV 560
Cdd:PRK04863  862 qqrsQLEQAKEGLsalnrLLPRLNLLADETladRVEEIREQLDEAEEAKRFVQQ-HGNALAQLEPIVSVLQSDPEQFEQL 940
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24762736   561 RSMVTQLLETQR---QMTDAL--LICRAA---------MENQNAELVSEYQLKI---EPDFDEARKTLT 612
Cdd:PRK04863  941 KQDYQQAQQTQRdakQQAFALteVVQRRAhfsyedaaeMLAKNSDLNEKLRQRLeqaEQERTRAREQLR 1009
Filament pfam00038
Intermediate filament protein;
418-536 1.63e-03

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 42.21  E-value: 1.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    418 TYSNPELEMISKEI----EELA-RERRVLE------TEIAQKEADvriKNGE---------------VRSLQSELDTLTA 471
Cdd:pfam00038  162 AARKLDLTSALAEIraqyEEIAaKNREEAEewyqskLEELQQAAA---RNGDalrsakeeitelrrtIQSLEIELQSLKK 238
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24762736    472 TLKQLENQRGEAQKRlddLQAQVTKIRDQchmqevtineqegeLNAKRSELQKLKDEEASLQKEY 536
Cdd:pfam00038  239 QKASLERQLAETEER---YELQLADYQEL--------------ISELEAELQETRQEMARQLREY 286
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
430-608 1.75e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.72  E-value: 1.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736   430 EIEELARERRVLETEIAQKEADVrikngevrslqseldtltATLKQLEnqrgEAQKRLDDLQAQVTKIRDQCHMQEVTIN 509
Cdd:PRK02224  476 RVEELEAELEDLEEEVEEVEERL------------------ERAEDLV----EAEDRIERLEERREDLEELIAERRETIE 533
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736   510 EQEGELNAKRSELQKLKDE----EASLQK---EYDSNNRELSKLTNHLQATQLQISSVRSMVTQL---------LETQRQ 573
Cdd:PRK02224  534 EKRERAEELRERAAELEAEaeekREAAAEaeeEAEEAREEVAELNSKLAELKERIESLERIRTLLaaiadaedeIERLRE 613
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 24762736   574 MTDALlicrAAMENQNAELVSEYQLKI---EPDFDEAR 608
Cdd:PRK02224  614 KREAL----AELNDERRERLAEKRERKrelEAEFDEAR 647
CENP-F_leu_zip pfam10473
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ...
423-556 1.78e-03

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: 39.97  E-value: 1.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    423 ELEMISKEIEELarerrVLETEIAQKEadvrikngeVRSLQSELDTLTATLKQLENQRGEAQKRLDDLQAQVTKirdqch 502
Cdd:pfam10473   32 ELEMSEENQELA-----ILEAENSKAE---------VETLKAEIEEMAQNLRDLELDLVTLRSEKENLTKELQK------ 91
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 24762736    503 MQEvTINEQEGELNAKRSELQKLKDEEASLQKEYDSNNRELSkltnhlqaTQLQ 556
Cdd:pfam10473   92 KQE-RVSELESLNSSLENLLEEKEQEKVQMKEESKTAVEMLQ--------TQLK 136
MPS2 pfam17060
Monopolar spindle protein 2; Is a fungal transmembrane protein which is part of the component ...
461-588 1.86e-03

Monopolar spindle protein 2; Is a fungal transmembrane protein which is part of the component of the spindle pole body (SPB) required for the insertion of the nascent SPB into the nuclear envelope and for the proper execution of spindle pole body (SPB) duplication. It seems that Mps2-Spc24 interaction may contribute to the localization of Spc24 and other kinetochore components to the inner plaque of the SPB.


Pssm-ID: 407228 [Multi-domain]  Cd Length: 340  Bit Score: 41.88  E-value: 1.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    461 SLQSELDTLTATLKQ--LENQRGEAQ--------KRLDDLQAQVTKIRDQCHMQEVTINEQEGELNAKRSELQKLKDEEA 530
Cdd:pfam17060  113 SPRSEADSLGTPIKVdlLRNLKPQESpetprrinRKYKSLELRVESMKDELEFKDETIMEKDRELTELTSTISKLKDKYD 192
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24762736    531 SLQKEYD-SNNRELSKLTNHLQAT---QLQISSVRSMVTQLLETQRQMTDALLICRAAMENQ 588
Cdd:pfam17060  193 FLSREFEfYKQHHEHGGNNSIKTAtkhEFIISELKRKLQEQNRLIRILQEQIQFDPGALHDN 254
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
430-546 2.06e-03

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: 40.30  E-value: 2.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    430 EIEELARERRVLETEIAQKEADVRIKNGEVRSLQSELDTLTATLKQLEnqrgeaqkrlddlqaqvTKIRDqchmqevtin 509
Cdd:pfam08614   65 ELAELYRSRGELAQRLVDLNEELQELEKKLREDERRLAALEAERAQLE-----------------EKLKD---------- 117
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 24762736    510 eQEGELNAKRSELQKLKDEEASLQKEYDSNNRELSKL 546
Cdd:pfam08614  118 -REEELREKRKLNQDLQDELVALQLQLNMAEEKLRKL 153
CDC37_N smart01071
Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of ...
435-546 2.59e-03

Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of numerous eukaryotic protein kinases. This domain corresponds to the N terminal domain which binds predominantly to protein kinases.and is found N terminal to the Hsp (Heat shocked protein) 90-binding domain. Expression of a construct consisting of only the N-terminal domain of Saccharomyces pombe Cdc37 results in cellular viability. This indicates that interactions with the cochaperone Hsp90 may not be essential for Cdc37 function.


Pssm-ID: 198139 [Multi-domain]  Cd Length: 154  Bit Score: 39.71  E-value: 2.59e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736     435 ARERRVLEteIAQKEADVRIKNGevrsLQSELDTLTATLK--QLENQRGEAQKRLDDLQAQVTKirdqchMQEVTINEQE 512
Cdd:smart01071   40 ARVERMEE--IKNLKYELIMNDH----LNKRIDKLLKGLReeELSPETPTYNEMLAELQDQLKK------ELEEANGDSE 107
                            90       100       110
                    ....*....|....*....|....*....|....
gi 24762736     513 GELNAKRSELQKLKDEEASLQKEYDSNNRELSKL 546
Cdd:smart01071  108 GLLEELKKHRDKLKKEQKELRKKLDELEKEEKKK 141
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
458-598 2.60e-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: 2.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    458 EVRSLQSELDTLTATLKQLENQrgeAQKRLDDLQAQvTKIrdqchMQEVTIN-EQEGELNAK-RSELQKLKDEEASLQKE 535
Cdd:pfam07926    2 ELSSLQSEIKRLKEEAADAEAQ---LQKLQEDLEKQ-AEI-----AREAQQNyERELVLHAEdIKALQALREELNELKAE 72
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24762736    536 YDSNNRELSKLTNHLQatQLQISsvrsmvtqlLETQRQMtdaLLICRAAMENQNAELVSEYQL 598
Cdd:pfam07926   73 IAELKAEAESAKAELE--ESEES---------WEEQKKE---LEKELSELEKRIEDLNEQNKL 121
CCCAP pfam15964
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ...
423-574 2.94e-03

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


Pssm-ID: 435040 [Multi-domain]  Cd Length: 703  Bit Score: 41.82  E-value: 2.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    423 ELEMISKEIE-ELA--RERRVLETEIAQKEAdvrikNGEVRSLQSELDTLTATLKQLENQRGEAQKRLDDLQAQVTKIRD 499
Cdd:pfam15964  364 ELERQKERLEkELAsqQEKRAQEKEALRKEM-----KKEREELGATMLALSQNVAQLEAQVEKVTREKNSLVSQLEEAQK 438
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    500 QCHMQEVTINEQEGELNAKRSELQKLKDEEASLQKEYDSN-NR--------------ELSKLTNHLQATQLQISSVRS-- 562
Cdd:pfam15964  439 QLASQEMDVTKVCGEMRYQLNQTKMKKDEAEKEHREYRTKtGRqleikdqeieklglELSESKQRLEQAQQDAARAREec 518
                          170
                   ....*....|....
gi 24762736    563 -MVTQLL-ETQRQM 574
Cdd:pfam15964  519 lKLTELLgESEHQL 532
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
420-546 2.97e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.85  E-value: 2.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  420 SNPELEMISKEIEELARERRVLETEIAQKEADVRIKNGEVRSLQSELDTLTATLKQLENQRGEAQKRLDDLQAQVTKIRD 499
Cdd:COG1196  656 GSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAERE 735
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 24762736  500 QCHMQEVtinEQEGELNAKRSELQKLKDEEASLQKEYDSNNRELSKL 546
Cdd:COG1196  736 ELLEELL---EEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
RNase_Y_N pfam12072
RNase Y N-terminal region;
482-573 3.34e-03

RNase Y N-terminal region;


Pssm-ID: 463456 [Multi-domain]  Cd Length: 201  Bit Score: 40.25  E-value: 3.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    482 EAQKRLDDLQAQ--VTKIRdqchmqevtiNEQEGELNAKRSELQKLkdEEASLQKE---------YDSNNRELSKLTNHL 550
Cdd:pfam12072   48 ETKKKEALLEAKeeIHKLR----------AEAERELKERRNELQRQ--ERRLLQKEetldrkdesLEKKEESLEKKEKEL 115
                           90       100
                   ....*....|....*....|...
gi 24762736    551 QATQLQISSVRSMVTQLLETQRQ 573
Cdd:pfam12072  116 EAQQQQLEEKEEELEELIEEQRQ 138
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
423-613 3.40e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.59  E-value: 3.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736   423 ELEMISKEIEELARERRVLETEIAQKEADVRIKNGevrsLQSELDTLTATLKQLENQRGEAQKRLDDLQAQVTKirdqch 502
Cdd:PRK03918  519 ELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEE----LKKKLAELEKKLDELEEELAELLKELEELGFESVE------ 588
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736   503 MQEVTINEQEG------ELNAKRSELQKLKDEEASLQKEYDSNNRELSKLTNHLQATQLQISSVRSMVTQllETQRQMTD 576
Cdd:PRK03918  589 ELEERLKELEPfyneylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE--EEYEELRE 666
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 24762736   577 ALLICRAAMENQNAELVSeyqlkIEPDFDEARKTLTK 613
Cdd:PRK03918  667 EYLELSRELAGLRAELEE-----LEKRREEIKKTLEK 698
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
458-558 3.94e-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: 38.32  E-value: 3.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    458 EVRSLQSELDTLTATLKQLENQrgeAQKRLDDLQAQVTKIRDQCHMQEVTINEQEgelnAKRSELQKLKDEEASLQKEYD 537
Cdd:pfam13863    7 EMFLVQLALDAKREEIERLEEL---LKQREEELEKKEQELKEDLIKFDKFLKEND----AKRRRALKKAEEETKLKKEKE 79
                           90       100
                   ....*....|....*....|.
gi 24762736    538 snnRELSKLTNHLQATQLQIS 558
Cdd:pfam13863   80 ---KEIKKLTAQIEELKSEIS 97
Prefoldin_2 pfam01920
Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996.
462-556 4.17e-03

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


Pssm-ID: 396482 [Multi-domain]  Cd Length: 102  Bit Score: 37.97  E-value: 4.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    462 LQSELDTLTATLKQLENQRGEAQKRLDDLQ--AQVTKIRDQCH--MQEVTINEQEGELNAKRSELQKlkdEEASLQKEYD 537
Cdd:pfam01920    7 LQQQLQLLAQQIKQLETQLKELELALEELEllDEDTKVYKLIGdvLVKQDKEEVKEQLEERKETLEK---EIKTLEKQLE 83
                           90
                   ....*....|....*....
gi 24762736    538 SNNRELSKLTNHLQATQLQ 556
Cdd:pfam01920   84 KLEKELEELKEELYKKFGQ 102
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
461-575 4.67e-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: 40.77  E-value: 4.67e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736     461 SLQSELDTLTATLKQLENQRGEAQKRLDDLQAQVTKIRDQchmqEVTINE-QEGELNAKRSELQKLKDEEASLQKEYDSN 539
Cdd:smart00787  155 GLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQL----EDELEDcDPTELDRAKEKLKKLLQEIMIKVKKLEEL 230
                            90       100       110
                    ....*....|....*....|....*....|....*....
gi 24762736     540 NRELSKLTNHLQATQLQISSVR---SMVTQLLETQRQMT 575
Cdd:smart00787  231 EEELQELESKIEDLTNKKSELNteiAEAEKKLEQCRGFT 269
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
423-552 4.77e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 4.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736   423 ELEMISKE-IEELARERRVLETEIAQKEADVRIKNGEVRSLQ---SELDTLTATLKQLENQRGEAQKRL--------DDL 490
Cdd:PRK03918  511 KLKKYNLEeLEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEelkKKLAELEKKLDELEEELAELLKELeelgfesvEEL 590
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24762736   491 QAQVTKIRdQCHMQEVTINEQEGELNAKRSELQKLKDEEASLQKEYDSNNRELSKLTNHLQA 552
Cdd:PRK03918  591 EERLKELE-PFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEE 651
DD_cGKI cd12083
Dimerization/Docking domain of Cyclic GMP-dependent Protein Kinase I; Cyclic GMP-dependent ...
428-467 5.60e-03

Dimerization/Docking domain of Cyclic GMP-dependent Protein Kinase I; Cyclic GMP-dependent Protein Kinase I (PKG1 or cGKI) is a Serine/Threonine Kinase (STK), catalyzing the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. cGKI exists as two splice variants, cGKI-alpha and cGKI-beta. They contain an N-terminal regulatory domain containing a dimerization/docking region and an autoinhibitory pseudosubstrate region, two cGMP-binding domains, and a C-terminal catalytic domain. Binding of cGMP to both binding sites releases the inhibition of the catalytic center by the pseudosubstrate region, allowing autophosphorylation and activation of the kinase. cGKI is a soluble protein expressed in all smooth muscles, platelets, cerebellum, and kidney. It is also expressed at lower concentrations in other tissues. It is involved in the regulation of smooth muscle tone, smooth cell proliferation, and platelet activation. The dimerization/docking (D/D) domain is a leucine/isoleucine zipper that mediates both homodimerization and interaction with isotype-specific G-kinase-anchoring proteins (GKAPs). The D/D domain of the two variants (alpha and beta) differ, allowing their targeting to different subcellular compartments and intracellular substrates.


Pssm-ID: 213373 [Multi-domain]  Cd Length: 48  Bit Score: 36.01  E-value: 5.60e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 24762736  428 SKEIEELARERRVLETEIAQKEADVRIKNGEVRSLQSELD 467
Cdd:cd12083    1 SGLLEEKTEELRKKDERIRELEQELQEKDEEIQELRSQLD 40
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
429-535 6.03e-03

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 40.63  E-value: 6.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736  429 KEIEELARERRVLETEIAQKEADVRIKNGEVRsLQSELDTLTATlKQLENQRGEAQKRLdDLQAQVTKIRDQCHMQEVTI 508
Cdd:COG2268  223 AEEAELEQEREIETARIAEAEAELAKKKAEER-REAETARAEAE-AAYEIAEANAEREV-QRQLEIAEREREIELQEKEA 299
                         90       100       110
                 ....*....|....*....|....*....|.
gi 24762736  509 NEQEGELNA---KRSELQKLKDE-EASLQKE 535
Cdd:COG2268  300 EREEAELEAdvrKPAEAEKQAAEaEAEAEAE 330
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
436-528 6.10e-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: 38.39  E-value: 6.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    436 RERRVLETEIAQKEADVRIKNGEVRSLQSELDTLTA---------------------TLKQLENQRGEAQKRLDDLQAQV 494
Cdd:pfam07926    1 AELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEiareaqqnyerelvlhaedikALQALREELNELKAEIAELKAEA 80
                           90       100       110
                   ....*....|....*....|....*....|....
gi 24762736    495 TKIRDQCHMQEVTINEQEGELNAKRSELQKLKDE 528
Cdd:pfam07926   81 ESAKAELEESEESWEEQKKELEKELSELEKRIED 114
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
423-621 6.81e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 40.77  E-value: 6.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    423 ELEMISKEIEELARERRVLETEIAQKEAdvRIKNgevrsLQSELDTLTATLKQLENQRGEAQKRLDDLQAQVTKIRDqch 502
Cdd:TIGR04523   41 KLKTIKNELKNKEKELKNLDKNLNKDEE--KINN-----SNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINS--- 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    503 mqevtineqegELNAKRSELQKLKDEEASLQKEYDSNNR--------------ELSKLTNHLQATQLQISSVRSMVTQL- 567
Cdd:TIGR04523  111 -----------EIKNDKEQKNKLEVELNKLEKQKKENKKnidkflteikkkekELEKLNNKYNDLKKQKEELENELNLLe 179
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24762736    568 ---LETQRQMTDA---------LLICRAAMENQNAELVSEYQlkiepDFDEARKTLTKEVQLPKDD 621
Cdd:TIGR04523  180 kekLNIQKNIDKIknkllklelLLSNLKKKIQKNKSLESQIS-----ELKKQNNQLKDNIEKKQQE 240
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
435-574 6.85e-03

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


Pssm-ID: 464776 [Multi-domain]  Cd Length: 193  Bit Score: 39.12  E-value: 6.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736    435 ARERRV--LETEIA---QKEADVRIKNGEVRSLQSELDtltATLKQLENQRGEAQKRLDDLQAQVTKIRDQCHMQEVTIN 509
Cdd:pfam15619    8 ARLHKIkeLQNELAelqSKLEELRKENRLLKRLQKRQE---KALGKYEGTESELPQLIARHNEEVRVLRERLRRLQEKER 84
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24762736    510 EQEGELNAKRSELQKLKDEEASLQK-EYDSNNRELSKLTNHLQATQLQISSVRSMVTQLletQRQM 574
Cdd:pfam15619   85 DLERKLKEKEAELLRLRDQLKRLEKlSEDKNLAEREELQKKLEQLEAKLEDKDEKIQDL---ERKL 147
PRK12705 PRK12705
hypothetical protein; Provisional
423-609 7.17e-03

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 40.46  E-value: 7.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736   423 ELEMISKEIEELARERRVlETEIAQKEADVRIKNG---EVRSLQSELDTLTATLKQLENQRGEAQKRLDDLQAQVTKird 499
Cdd:PRK12705   34 EAERILQEAQKEAEEKLE-AALLEAKELLLRERNQqrqEARREREELQREEERLVQKEEQLDARAEKLDNLENQLEE--- 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736   500 qchmQEVTINEQEGELNAKRSELqKLKDEEASLQKEYDSNNRELSKLTNHL--QATQLqissVRSMVTQLLETQRQmtDA 577
Cdd:PRK12705  110 ----REKALSARELELEELEKQL-DNELYRVAGLTPEQARKLLLKLLDAELeeEKAQR----VKKIEEEADLEAER--KA 178
                         170       180       190
                  ....*....|....*....|....*....|..
gi 24762736   578 LLICRAAMENQNAELVSEYQLKIEPDFDEARK 609
Cdd:PRK12705  179 QNILAQAMQRIASETASDLSVSVVPIPSDAMK 210
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
372-512 9.19e-03

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 40.32  E-value: 9.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736   372 FALAMWFVE--RKQRGVDPPHvlnanMVPPSmratvagvdlQPQEVKPTYSNpELEMISKEIEELARERRVLETEIAQKE 449
Cdd:PRK11448  113 FRLAVWFHRtyGKDWDFKPGP-----FVPPE----------DPENLLHALQQ-EVLTLKQQLELQAREKAQSQALAEAQQ 176
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24762736   450 ADVRIKNGEVRSLQSELDTLTATLKQLENQRGEAQKrldDLQAQVTKIRDQChMQEVTINEQE 512
Cdd:PRK11448  177 QELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQ---ERKQKRKEITDQA-AKRLELSEEE 235
46 PHA02562
endonuclease subunit; Provisional
423-567 9.28e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 40.00  E-value: 9.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762736   423 ELEMISKEIEELARERRVLETEIAQKEADVRIKNGEVRSLQSELDTLTATLKQLENQrGEA---QKRLDDLQAQVTKIRD 499
Cdd:PHA02562  228 EAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKG-GVCptcTQQISEGPDRITKIKD 306
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24762736   500 QCHmqevTINEQEGELNAKRSELQKLKDEEASLQKEYDSNNRELSKLTNHLQATQLQISSVRSMVTQL 567
Cdd:PHA02562  307 KLK----ELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEEL 370
 
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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