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Conserved domains on  [gi|329663747|ref|NP_001192320|]
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autophagy-related protein 16-1 isoform 1 [Mus musculus]

Protein Classification

WD repeat ATG16 family protein( domain architecture ID 12095058)

WD repeat ATG16 (autophagy-related 16) family protein similar to human ATG16L1 that plays an essential role in autophagy; it interacts with ATG12-ATG5 to mediate the conjugation of phosphatidylethanolamine to LC3, and thus, controls the elongation of the nascent autophagosomal membrane

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
217-620 3.39e-59

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 203.60  E-value: 3.39e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747 217 QARLQKELAEAAKEPLPVEQDDDIEVIVDETSDHTEETSPVRAVSRAATKRLSQPAGGLLDSITNIFGLSESPLLGHHSS 296
Cdd:COG2319    1 ALSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747 297 DAARRRSvssipvPQDIMDTHPASGKDVRVPTTAS----YVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWEAFGDKC 372
Cdd:COG2319   81 VLSVAFS------PDGRLLASASADGTVRLWDLATglllRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKL 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747 373 EfkGSLSGSNAGITSIEFDSAGAYLLAASNDFASRIWTVDDYRLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWD 452
Cdd:COG2319  155 L--RTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWD 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747 453 LRSKVCIKTV-FAGSSCNDIVCT--EQCVMSGHFDKKIRFWDIRSESVVREME-LLGKITALDLNPERTELLSCSRDDLL 528
Cdd:COG2319  233 LATGKLLRTLtGHSGSVRSVAFSpdGRLLASGSADGTVRLWDLATGELLRTLTgHSGGVNSVAFSPDGKLLASGSDDGTV 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747 529 KVIDLRTNAVKQTFSAPgfkcGSDWTRVVFSPDGSYVAAGSAEGSLYVWSVLTGKVEKVLsKQHSSSINAVAWAPSGLHV 608
Cdd:COG2319  313 RLWDLATGKLLRTLTGH----TGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTL-TGHTGAVTSVAFSPDGRTL 387

                        410
                 ....*....|..
gi 329663747 609 VSVDKGSRAVLW 620
Cdd:COG2319  388 ASGSADGTVRLW 399
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 31-206 5.39e-55

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: 184.75  E-value: 5.39e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747   31 AFEEIILQYTKLLEKSDLHSVLTQKLQAEKHDMPNRHEISPGHDGAWNDSQLQEMAQLRIKHQEELTELHKKRGELAQLV 110
Cdd:pfam08614   1 AFLELIDAYNRLLDRTALLEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQLREELAELYRSRGELAQRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747  111 IDLNNQMQQKDKEIQMNEAKISEYLQTISDLETNCLDLRTKLQDLEVANQTLKDEYDALQITFTALEEKLRKTTEENQEL 190
Cdd:pfam08614  81 VDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQDELVALQLQLNMAEEKLRKLEKENREL 160

                         170
                  ....*....|....*.
gi 329663747  191 VTRWMAEKAQEANRLN 206
Cdd:pfam08614 161 VERWMKRKGQEAEAMN 176
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
217-620 3.39e-59

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 203.60  E-value: 3.39e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747 217 QARLQKELAEAAKEPLPVEQDDDIEVIVDETSDHTEETSPVRAVSRAATKRLSQPAGGLLDSITNIFGLSESPLLGHHSS 296
Cdd:COG2319    1 ALSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747 297 DAARRRSvssipvPQDIMDTHPASGKDVRVPTTAS----YVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWEAFGDKC 372
Cdd:COG2319   81 VLSVAFS------PDGRLLASASADGTVRLWDLATglllRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKL 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747 373 EfkGSLSGSNAGITSIEFDSAGAYLLAASNDFASRIWTVDDYRLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWD 452
Cdd:COG2319  155 L--RTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWD 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747 453 LRSKVCIKTV-FAGSSCNDIVCT--EQCVMSGHFDKKIRFWDIRSESVVREME-LLGKITALDLNPERTELLSCSRDDLL 528
Cdd:COG2319  233 LATGKLLRTLtGHSGSVRSVAFSpdGRLLASGSADGTVRLWDLATGELLRTLTgHSGGVNSVAFSPDGKLLASGSDDGTV 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747 529 KVIDLRTNAVKQTFSAPgfkcGSDWTRVVFSPDGSYVAAGSAEGSLYVWSVLTGKVEKVLsKQHSSSINAVAWAPSGLHV 608
Cdd:COG2319  313 RLWDLATGKLLRTLTGH----TGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTL-TGHTGAVTSVAFSPDGRTL 387

                        410
                 ....*....|..
gi 329663747 609 VSVDKGSRAVLW 620
Cdd:COG2319  388 ASGSADGTVRLW 399
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 333-621 4.14e-57

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 194.09  E-value: 4.14e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747 333 VFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWEAFGDKCEFkgSLSGSNAGITSIEFDSAGAYLLAASNDFASRIWTVD 412
Cdd:cd00200    4 TLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLR--TLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747 413 DYRLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTvFAG----------SSCNDIVCteqcvmSGH 482
Cdd:cd00200   82 TGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTT-LRGhtdwvnsvafSPDGTFVA------SSS 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747 483 FDKKIRFWDIRSESVVREMEL-LGKITALDLNPERTELLSCSRDDLLKVIDLRTNAVKQTFSAPgfkcgSDW-TRVVFSP 560
Cdd:cd00200  155 QDGTIKLWDLRTGKCVATLTGhTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGH-----ENGvNSVAFSP 229

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 329663747 561 DGSYVAAGSAEGSLYVWSVLTGKVEKVLSkQHSSSINAVAWAPSGLHVVSVDKGSRAVLWA 621
Cdd:cd00200  230 DGYLLASGSEDGTIRVWDLRTGECVQTLS-GHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 31-206 5.39e-55

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: 184.75  E-value: 5.39e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747   31 AFEEIILQYTKLLEKSDLHSVLTQKLQAEKHDMPNRHEISPGHDGAWNDSQLQEMAQLRIKHQEELTELHKKRGELAQLV 110
Cdd:pfam08614   1 AFLELIDAYNRLLDRTALLEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQLREELAELYRSRGELAQRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747  111 IDLNNQMQQKDKEIQMNEAKISEYLQTISDLETNCLDLRTKLQDLEVANQTLKDEYDALQITFTALEEKLRKTTEENQEL 190
Cdd:pfam08614  81 VDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQDELVALQLQLNMAEEKLRKLEKENREL 160

                         170
                  ....*....|....*.
gi 329663747  191 VTRWMAEKAQEANRLN 206
Cdd:pfam08614 161 VERWMKRKGQEAEAMN 176
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 119-209 3.70e-30

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: 113.81  E-value: 3.70e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747 119 QKDKEIQMNEAKISEYLQTISDLETNCLDLRTKLQDLEVANQTLKDEYDALQITFTALEEKLRKTTEENQELVTRWMAEK 198
Cdd:cd22887    1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEENDELVERWMAKK 80

                         90
                 ....*....|.
gi 329663747 199 AQEANRLNAEN 209
Cdd:cd22887   81 QQEADKMNEAN 91
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
79-264 9.71e-09

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 57.60  E-value: 9.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747  79 DSQLQEMAQLRIKHQEELTELHKKRGELAQL---VIDLNNQMQQKDKEIQMNEAKISEYLQTISDLETNCLDLRTKLQDL 155
Cdd:COG4372   41 DKLQEELEQLREELEQAREELEQLEEELEQArseLEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEEL 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747 156 EVANQTLKDEYDALQITFTALEEKLRKTTEENQELVTRwMAEKAQEANRLNAENEKDSRRR-QARLQKELAEAAKEPLPV 234
Cdd:COG4372  121 QKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ-LESLQEELAALEQELQALSEAEaEQALDELLKEANRNAEKE 199

                        170       180       190
                 ....*....|....*....|....*....|
gi 329663747 235 EQDDDIEVIVDETSDHTEETSPVRAVSRAA 264
Cdd:COG4372  200 EELAEAEKLIESLPRELAEELLEAKDSLEA 229
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 332-366 8.23e-08

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 48.46  E-value: 8.23e-08
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 329663747   332 YVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWE 366
Cdd:smart00320   6 KTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
332-366 2.25e-07

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 47.34  E-value: 2.25e-07
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 329663747  332 YVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWE 366
Cdd:pfam00400   5 KTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 79-230 2.28e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.83  E-value: 2.28e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747    79 DSQLQEMAQLRIKH-------QEELTELHKKRGELAQLVID-------LNNQMQQKDKEIQMNEAKISEYLQTISDLETN 144
Cdd:TIGR02168  245 QEELKEAEEELEELtaelqelEEKLEELRLEVSELEEEIEElqkelyaLANEISRLEQQKQILRERLANLERQLEELEAQ 324

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747   145 CLDLRTKLQDLEVANQTLKDEYDALQITFTALEEKLRKTTEENQELVTRWmAEKAQEANRLNAEnEKDSRRRQARLQKEL 224
Cdd:TIGR02168  325 LEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRL-EELEEQLETLRSK-VAQLELQIASLNNEI 402


                   ....*.
gi 329663747   225 AEAAKE 230
Cdd:TIGR02168  403 ERLEAR 408
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 341-577 6.37e-06

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 49.31  E-value: 6.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747 341 VNAVQFSPGSRLLATGGMDRRVKLWEAF-----GDKCEFKGSLSGSNAGITSIEFDSAGAYLLAASN-DFASRIWTVDDY 414
Cdd:PLN00181 486 VCAIGFDRDGEFFATAGVNKKIKIFECEsiikdGRDIHYPVVELASRSKLSGICWNSYIKSQVASSNfEGVVQVWDVARS 565

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747 415 RLRHTLTGHSGKVLSAKFL-LDNARIVSGSHDRTLKLWDLRSKVCIKTVfagSSCNDIVCTE------QCVMSGHFDKKI 487
Cdd:PLN00181 566 QLVTEMKEHEKRVWSIDYSsADPTLLASGSDDGSVKLWSINQGVSIGTI---KTKANICCVQfpsesgRSLAFGSADHKV 642

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747 488 RFWDIRSE-----SVVREMELLGKITALDlnpeRTELLSCSRDDLLKVIDLRTNA--VKQT--FSAPGFKCGSDWTRVVF 558
Cdd:PLN00181 643 YYYDLRNPklplcTMIGHSKTVSYVRFVD----SSTLVSSSTDNTLKLWDLSMSIsgINETplHSFMGHTNVKNFVGLSV 718

                        250
                 ....*....|....*....
gi 329663747 559 SpDGsYVAAGSAEGSLYVW 577
Cdd:PLN00181 719 S-DG-YIATGSETNEVFVY 735
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
46-230 2.49e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 44.26  E-value: 2.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747  46 SDLHSVLTQKLQAEKHDMPNRHEispghdgawndsqlQEMAQLR--IKHQEELTELHKKRGELAQLVIDLNNQMQQkdkE 123
Cdd:PRK02224 190 DQLKAQIEEKEEKDLHERLNGLE--------------SELAELDeeIERYEEQREQARETRDEADEVLEEHEERRE---E 252

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747 124 IQMNEAKISEYLQTISDLETNCLDLRTKLQDLEVANQTLKDEYDAL--QITFTALE----EKLRKTTEENQELVTRWMAE 197
Cdd:PRK02224 253 LETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLlaEAGLDDADaeavEARREELEDRDEELRDRLEE 332

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 329663747 198 KAQEANRLN------AENEKDSRRRQARLQKELAEAAKE 230
Cdd:PRK02224 333 CRVAAQAHNeeaeslREDADDLEERAEELREEAAELESE 371
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
217-620 3.39e-59

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 203.60  E-value: 3.39e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747 217 QARLQKELAEAAKEPLPVEQDDDIEVIVDETSDHTEETSPVRAVSRAATKRLSQPAGGLLDSITNIFGLSESPLLGHHSS 296
Cdd:COG2319    1 ALSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747 297 DAARRRSvssipvPQDIMDTHPASGKDVRVPTTAS----YVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWEAFGDKC 372
Cdd:COG2319   81 VLSVAFS------PDGRLLASASADGTVRLWDLATglllRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKL 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747 373 EfkGSLSGSNAGITSIEFDSAGAYLLAASNDFASRIWTVDDYRLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWD 452
Cdd:COG2319  155 L--RTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWD 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747 453 LRSKVCIKTV-FAGSSCNDIVCT--EQCVMSGHFDKKIRFWDIRSESVVREME-LLGKITALDLNPERTELLSCSRDDLL 528
Cdd:COG2319  233 LATGKLLRTLtGHSGSVRSVAFSpdGRLLASGSADGTVRLWDLATGELLRTLTgHSGGVNSVAFSPDGKLLASGSDDGTV 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747 529 KVIDLRTNAVKQTFSAPgfkcGSDWTRVVFSPDGSYVAAGSAEGSLYVWSVLTGKVEKVLsKQHSSSINAVAWAPSGLHV 608
Cdd:COG2319  313 RLWDLATGKLLRTLTGH----TGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTL-TGHTGAVTSVAFSPDGRTL 387

                        410
                 ....*....|..
gi 329663747 609 VSVDKGSRAVLW 620
Cdd:COG2319  388 ASGSADGTVRLW 399
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 333-621 4.14e-57

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 194.09  E-value: 4.14e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747 333 VFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWEAFGDKCEFkgSLSGSNAGITSIEFDSAGAYLLAASNDFASRIWTVD 412
Cdd:cd00200    4 TLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLR--TLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747 413 DYRLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTvFAG----------SSCNDIVCteqcvmSGH 482
Cdd:cd00200   82 TGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTT-LRGhtdwvnsvafSPDGTFVA------SSS 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747 483 FDKKIRFWDIRSESVVREMEL-LGKITALDLNPERTELLSCSRDDLLKVIDLRTNAVKQTFSAPgfkcgSDW-TRVVFSP 560
Cdd:cd00200  155 QDGTIKLWDLRTGKCVATLTGhTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGH-----ENGvNSVAFSP 229

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 329663747 561 DGSYVAAGSAEGSLYVWSVLTGKVEKVLSkQHSSSINAVAWAPSGLHVVSVDKGSRAVLWA 621
Cdd:cd00200  230 DGYLLASGSEDGTIRVWDLRTGECVQTLS-GHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 31-206 5.39e-55

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: 184.75  E-value: 5.39e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747   31 AFEEIILQYTKLLEKSDLHSVLTQKLQAEKHDMPNRHEISPGHDGAWNDSQLQEMAQLRIKHQEELTELHKKRGELAQLV 110
Cdd:pfam08614   1 AFLELIDAYNRLLDRTALLEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQLREELAELYRSRGELAQRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747  111 IDLNNQMQQKDKEIQMNEAKISEYLQTISDLETNCLDLRTKLQDLEVANQTLKDEYDALQITFTALEEKLRKTTEENQEL 190
Cdd:pfam08614  81 VDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQDELVALQLQLNMAEEKLRKLEKENREL 160

                         170
                  ....*....|....*.
gi 329663747  191 VTRWMAEKAQEANRLN 206
Cdd:pfam08614 161 VERWMKRKGQEAEAMN 176
WD40 COG2319
WD40 repeat [General function prediction only];
332-579 1.89e-47

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 171.63  E-value: 1.89e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747 332 YVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWEAFGDKCEFkgSLSGSNAGITSIEFDSAGAYLLAASNDFASRIWTV 411
Cdd:COG2319  156 RTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLR--TLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDL 233

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747 412 DDYRLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTvFAGSSC--NDIVCT--EQCVMSGHFDKKI 487
Cdd:COG2319  234 ATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRT-LTGHSGgvNSVAFSpdGKLLASGSDDGTV 312

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747 488 RFWDIRSESVVREME-LLGKITALDLNPERTELLSCSRDDLLKVIDLRTNAVKQTFSAPgfkcgSDW-TRVVFSPDGSYV 565
Cdd:COG2319  313 RLWDLATGKLLRTLTgHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGH-----TGAvTSVAFSPDGRTL 387

                        250
                 ....*....|....
gi 329663747 566 AAGSAEGSLYVWSV 579
Cdd:COG2319  388 ASGSADGTVRLWDL 401
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 332-578 1.85e-37

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 140.93  E-value: 1.85e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747 332 YVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWEAFGDKCEFkgSLSGSNAGITSIEFDSAGAYLLAASNDFASRIWTV 411
Cdd:cd00200   87 RTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLT--TLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDL 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747 412 DDYRLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTvfagsscndivcteqcvMSGHfdkkirfwd 491
Cdd:cd00200  165 RTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGT-----------------LRGH--------- 218

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747 492 irsesvvremelLGKITALDLNPERTELLSCSRDDLLKVIDLRTNAVKQTFSAPGFKCGSdwtrVVFSPDGSYVAAGSAE 571
Cdd:cd00200  219 ------------ENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTS----LAWSPDGKRLASGSAD 282


                 ....*..
gi 329663747 572 GSLYVWS 578
Cdd:cd00200  283 GTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
333-535 1.48e-36

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 141.20  E-value: 1.48e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747 333 VFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWEAFGDKCEFkgSLSGSNAGITSIEFDSAGAYLLAASNDFASRIWTVD 412
Cdd:COG2319  199 TLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLR--TLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLA 276

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747 413 DYRLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTvFAG--SSCNDIVCT--EQCVMSGHFDKKIR 488
Cdd:COG2319  277 TGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRT-LTGhtGAVRSVAFSpdGKTLASGSDDGTVR 355

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 329663747 489 FWDIRSESVVREME-LLGKITALDLNPERTELLSCSRDDLLKVIDLRT 535
Cdd:COG2319  356 LWDLATGELLRTLTgHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 416-610 8.96e-34

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 130.53  E-value: 8.96e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747 416 LRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTV----FAGSSCNDIVCTEQCVmSGHFDKKIRFWD 491
Cdd:cd00200    1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLkghtGPVRDVAASADGTYLA-SGSSDKTIRLWD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747 492 IRSESVVREMEL-LGKITALDLNPERTELLSCSRDDLLKVIDLRTNAVKQTFSAPgfkcgSDWTR-VVFSPDGSYVAAGS 569
Cdd:cd00200   80 LETGECVRTLTGhTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGH-----TDWVNsVAFSPDGTFVASSS 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 329663747 570 AEGSLYVWSVLTGKVEKVLsKQHSSSINAVAWAPSGLHVVS 610
Cdd:cd00200  155 QDGTIKLWDLRTGKCVATL-TGHTGEVNSVAFSPDGEKLLS 194
WD40 COG2319
WD40 repeat [General function prediction only];
332-494 8.08e-32

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 127.72  E-value: 8.08e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747 332 YVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWEAFGDKCefKGSLSGSNAGITSIEFDSAGAYLLAASNDFASRIWTV 411
Cdd:COG2319  240 RTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGEL--LRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDL 317

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747 412 DDYRLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTvFAGSScnDIVCT------EQCVMSGHFDK 485
Cdd:COG2319  318 ATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRT-LTGHT--GAVTSvafspdGRTLASGSADG 394


                 ....*....
gi 329663747 486 KIRFWDIRS 494
Cdd:COG2319  395 TVRLWDLAT 403
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 119-209 3.70e-30

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: 113.81  E-value: 3.70e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747 119 QKDKEIQMNEAKISEYLQTISDLETNCLDLRTKLQDLEVANQTLKDEYDALQITFTALEEKLRKTTEENQELVTRWMAEK 198
Cdd:cd22887    1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEENDELVERWMAKK 80

                         90
                 ....*....|.
gi 329663747 199 AQEANRLNAEN 209
Cdd:cd22887   81 QQEADKMNEAN 91
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
79-264 9.71e-09

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 57.60  E-value: 9.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747  79 DSQLQEMAQLRIKHQEELTELHKKRGELAQL---VIDLNNQMQQKDKEIQMNEAKISEYLQTISDLETNCLDLRTKLQDL 155
Cdd:COG4372   41 DKLQEELEQLREELEQAREELEQLEEELEQArseLEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEEL 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747 156 EVANQTLKDEYDALQITFTALEEKLRKTTEENQELVTRwMAEKAQEANRLNAENEKDSRRR-QARLQKELAEAAKEPLPV 234
Cdd:COG4372  121 QKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ-LESLQEELAALEQELQALSEAEaEQALDELLKEANRNAEKE 199

                        170       180       190
                 ....*....|....*....|....*....|
gi 329663747 235 EQDDDIEVIVDETSDHTEETSPVRAVSRAA 264
Cdd:COG4372  200 EELAEAEKLIESLPRELAEELLEAKDSLEA 229
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
88-238 2.63e-08

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 57.08  E-value: 2.63e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747  88 LRIKHQEELTELHKKRGELAQLVIDlnnQMQQKDKEIQMNEAKISEYLQTISDLETncldLRTKLQDLEVANQTLKDEYD 167
Cdd:COG4717   47 LLERLEKEADELFKPQGRKPELNLK---ELKELEEELKEAEEKEEEYAELQEELEE----LEEELEELEAELEELREELE 119

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 329663747 168 AL--QITFTALEEKLRKTTEENQELVTRWMAEKAQEANRLNAENEKDSRRRQ-ARLQKELAEAAKEPLPVEQDD 238
Cdd:COG4717  120 KLekLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAElAELQEELEELLEQLSLATEEE 193
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 332-366 8.23e-08

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 48.46  E-value: 8.23e-08
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 329663747   332 YVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWE 366
Cdd:smart00320   6 KTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 415-452 1.45e-07

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 48.08  E-value: 1.45e-07
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 329663747   415 RLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWD 452
Cdd:smart00320   3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 81-270 1.91e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.56  E-value: 1.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747  81 QLQEMAQLRIKHQEELTELHKKRGELAQlvidlnnQMQQKDKEIQMNEAKISEYLQTISDLETNCLDLRTKLQDLEVANQ 160
Cdd:COG1196  275 ELEELELELEEAQAEEYELLAELARLEQ-------DIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELE 347

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747 161 TLKDEYDALQITFTALEEKLRKTTEENQELVTRWMAEKAQEANRLNAENEKDSRRRQARLQKELAEAAKEPLPVEQDDDI 240
Cdd:COG1196  348 EAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE 427

                        170       180       190
                 ....*....|....*....|....*....|
gi 329663747 241 EVIVDETSDHTEETSPVRAVSRAATKRLSQ 270
Cdd:COG1196  428 EALAELEEEEEEEEEALEEAAEEEAELEEE 457
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
374-582 2.12e-07

DNA-binding beta-propeller fold protein YncE [General function prediction only];


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 52.39  E-value: 2.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747 374 FKGSLSGSNAGITSIEFDSAGAYLLAASNDFASRIWTVDDYRLRHTLTGHSGKVLSAKFLLDNARI-VSGSHDRTLKLWD 452
Cdd:COG3391   17 ALAALAVAVAALGLGGGGPLLAAASGGVVGAAVGGGGVALLAGLGLGAAAVADADGADAGADGRRLyVANSGSGRVSVID 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747 453 LRSKVCIKTVFAGSSCNDIVCTE---QCVMSGHFDKKIRFWDIRSESVVREMELLGKITALDLNPERTELLSCSRDD--- 526
Cdd:COG3391   97 LATGKVVATIPVGGGPRGLAVDPdggRLYVADSGNGRVSVIDTATGKVVATIPVGAGPHGIAVDPDGKRLYVANSGSntv 176

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 329663747 527 --LLKVIDLRTNAVKQTFSApgfkcGSDWTRVVFSPDGS--YVA------AGSAEGSLYVWSVLTG 582
Cdd:COG3391  177 svIVSVIDTATGKVVATIPV-----GGGPVGVAVSPDGRrlYVAnrgsntSNGGSNTVSVIDLATL 237
WD40 pfam00400
WD domain, G-beta repeat;
332-366 2.25e-07

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 47.34  E-value: 2.25e-07
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 329663747  332 YVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWE 366
Cdd:pfam00400   5 KTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 pfam00400
WD domain, G-beta repeat;
415-452 4.21e-07

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 46.57  E-value: 4.21e-07
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 329663747  415 RLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWD 452
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 79-230 5.07e-07

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 51.08  E-value: 5.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747  79 DSQLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQQKDKEIQMNEAKISEYLQTISDLEtncldlrTKLQdlEVA 158
Cdd:COG1579   16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE-------EQLG--NVR 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 329663747 159 NQtlkDEYDALQITFTALEEKLRKTTEENQELVTRwmAEKAQ----EANRLNAENEKDSRRRQARLQKELAEAAKE 230
Cdd:COG1579   87 NN---KEYEALQKEIESLKRRISDLEDEILELMER--IEELEeelaELEAELAELEAELEEKKAELDEELAELEAE 157
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 79-230 2.28e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.83  E-value: 2.28e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747    79 DSQLQEMAQLRIKH-------QEELTELHKKRGELAQLVID-------LNNQMQQKDKEIQMNEAKISEYLQTISDLETN 144
Cdd:TIGR02168  245 QEELKEAEEELEELtaelqelEEKLEELRLEVSELEEEIEElqkelyaLANEISRLEQQKQILRERLANLERQLEELEAQ 324

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747   145 CLDLRTKLQDLEVANQTLKDEYDALQITFTALEEKLRKTTEENQELVTRWmAEKAQEANRLNAEnEKDSRRRQARLQKEL 224
Cdd:TIGR02168  325 LEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRL-EELEEQLETLRSK-VAQLELQIASLNNEI 402


                   ....*.
gi 329663747   225 AEAAKE 230
Cdd:TIGR02168  403 ERLEAR 408
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 80-284 3.71e-06

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 49.38  E-value: 3.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747  80 SQLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQQKDKEIQMNEAKISEYLQTISDLE----------------- 142
Cdd:COG4942   41 KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKeelaellralyrlgrqp 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747 143 --------TNCLDLRTKLQDLEVANQTLKDEYDALQITFTALEEKLRKTTEENQELVTRwMAEKAQEANRLNAEnEKDSR 214
Cdd:COG4942  121 plalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL-LAELEEERAALEAL-KAERQ 198

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 329663747 215 RRQARLQKELAEAAKEPLPVEQDDD-----IEVIVDETSDHTEETSPVRAVsrAATKRLSQPAGGlldSITNIFG 284
Cdd:COG4942  199 KLLARLEKELAELAAELAELQQEAEelealIARLEAEAAAAAERTPAAGFA--ALKGKLPWPVSG---RVVRRFG 268
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 78-226 4.64e-06

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 49.63  E-value: 4.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747   78 NDSQLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQQK---DKEIQMNEAKISEYLQTISDLETNCLDLRTKLQD 154
Cdd:TIGR04523 379 NQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKellEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKN 458

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 329663747  155 LEVANQTLKDEYDALQITFTALEEKLRKTTEEnqelvtrwMAEKAQEANRLNAENeKDSRRRQARLQKELAE 226
Cdd:TIGR04523 459 LDNTRESLETQLKVLSRSINKIKQNLEQKQKE--------LKSKEKELKKLNEEK-KELEEKVKDLTKKISS 521
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 341-577 6.37e-06

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 49.31  E-value: 6.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747 341 VNAVQFSPGSRLLATGGMDRRVKLWEAF-----GDKCEFKGSLSGSNAGITSIEFDSAGAYLLAASN-DFASRIWTVDDY 414
Cdd:PLN00181 486 VCAIGFDRDGEFFATAGVNKKIKIFECEsiikdGRDIHYPVVELASRSKLSGICWNSYIKSQVASSNfEGVVQVWDVARS 565

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747 415 RLRHTLTGHSGKVLSAKFL-LDNARIVSGSHDRTLKLWDLRSKVCIKTVfagSSCNDIVCTE------QCVMSGHFDKKI 487
Cdd:PLN00181 566 QLVTEMKEHEKRVWSIDYSsADPTLLASGSDDGSVKLWSINQGVSIGTI---KTKANICCVQfpsesgRSLAFGSADHKV 642

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747 488 RFWDIRSE-----SVVREMELLGKITALDlnpeRTELLSCSRDDLLKVIDLRTNA--VKQT--FSAPGFKCGSDWTRVVF 558
Cdd:PLN00181 643 YYYDLRNPklplcTMIGHSKTVSYVRFVD----SSTLVSSSTDNTLKLWDLSMSIsgINETplHSFMGHTNVKNFVGLSV 718

                        250
                 ....*....|....*....
gi 329663747 559 SpDGsYVAAGSAEGSLYVW 577
Cdd:PLN00181 719 S-DG-YIATGSETNEVFVY 735
WD40 COG2319
WD40 repeat [General function prediction only];
251-367 7.36e-06

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 48.75  E-value: 7.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747 251 TEETSPVRAVSRAAT-KRLsqpAGGLLDSITNIFGLSESPLLGHHSSDAARRRSVSSIPVPQDImdthpASG---KDVRV 326
Cdd:COG2319  285 TGHSGGVNSVAFSPDgKLL---ASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTL-----ASGsddGTVRL 356

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 329663747 327 ----PTTASYVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWEA 367
Cdd:COG2319  357 wdlaTGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDL 401
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
93-241 1.26e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 48.37  E-value: 1.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747   93 QEELTELHKKRGELAQLVIDLNNQMQQKDkEIQMNEAKISEYLQTISD---LETNCLDLRTKLQDLEVAN---QTLKDEY 166
Cdd:COG4913   616 EAELAELEEELAEAEERLEALEAELDALQ-ERREALQRLAEYSWDEIDvasAEREIAELEAELERLDASSddlAALEEQL 694

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 329663747  167 DALQITFTALEEKLRKTTEENQELVTRW---MAEKAQEANRLNAENEKDSRRRQARLQKELAEAAKEPLPVEQDDDIE 241
Cdd:COG4913   695 EELEAELEELEEELDELKGEIGRLEKELeqaEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLE 772
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 337-453 1.39e-05

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 48.16  E-value: 1.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747 337 HDGEVNAVQFSPGS-RLLATGGMDRRVKLWEAfgDKCEFKGSLSgSNAGITSIEFDSAGAYLLAasndFASRIWTVDDYR 415
Cdd:PLN00181 574 HEKRVWSIDYSSADpTLLASGSDDGSVKLWSI--NQGVSIGTIK-TKANICCVQFPSESGRSLA----FGSADHKVYYYD 646

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 329663747 416 LRH------TLTGHSGKVLSAKFLlDNARIVSGSHDRTLKLWDL 453
Cdd:PLN00181 647 LRNpklplcTMIGHSKTVSYVRFV-DSSTLVSSSTDNTLKLWDL 689
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 81-226 1.83e-05

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 47.71  E-value: 1.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747   81 QLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQQ------------KDKEIQMNEAKISEYLQTISDLETNCLDL 148
Cdd:TIGR04523 268 QLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQdwnkelkselknQEKKLEEIQNQISQNNKIISQLNEQISQL 347

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747  149 RTKLQDLEVANQTLKDEydalqitftaLEEK---LRKTTEENQelvtrwmaEKAQEANRLnaENEKDSRRRQARLQKELA 225
Cdd:TIGR04523 348 KKELTNSESENSEKQRE----------LEEKqneIEKLKKENQ--------SYKQEIKNL--ESQINDLESKIQNQEKLN 407


                  .
gi 329663747  226 E 226
Cdd:TIGR04523 408 Q 408
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 79-189 1.93e-05

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 47.71  E-value: 1.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747   79 DSQLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQQKDKEIQMNEAKISEYLQTISDLETNCLDLRTKLQDLEVA 158
Cdd:TIGR04523 327 QNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKL 406

                          90       100       110
                  ....*....|....*....|....*....|....
gi 329663747  159 NQTLKDEYDALQITFTALE---EKLRKTTEENQE 189
Cdd:TIGR04523 407 NQQKDEQIKKLQQEKELLEkeiERLKETIIKNNS 440
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 55-230 2.35e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.74  E-value: 2.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747    55 KLQAEKHDMpnRHEISPGHDGAWNDSQLQEMAQLRIKHQE-ELTELHKKRGELAQLVIDLNNQMQQKDKEIQMNEAKISE 133
Cdd:TIGR02168  716 QLRKELEEL--SRQISALRKDLARLEAEVEQLEERIAQLSkELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ 793

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747   134 YLQTISDLETNCLDLRTKLQDL--EVANQT-----LKDEYDALQITFTALEEKLRKTTEEnQELVTRWMAEKAQEANRLN 206
Cdd:TIGR02168  794 LKEELKALREALDELRAELTLLneEAANLRerlesLERRIAATERRLEDLEEQIEELSED-IESLAAEIEELEELIEELE 872

                          170       180       190
                   ....*....|....*....|....*....|
gi 329663747   207 AE-----NEKDSRRRQ-ARLQKELAEAAKE 230
Cdd:TIGR02168  873 SEleallNERASLEEAlALLRSELEELSEE 902
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
48-230 3.02e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.07  E-value: 3.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747  48 LHSVLTQKLQAEKHDMPNRHeispGHDGAWNDSQLQEMaqlrikhQEELTELHKKRGELAQLVidlnNQMQQKDKEIQMN 127
Cdd:COG4717   43 IRAMLLERLEKEADELFKPQ----GRKPELNLKELKEL-------EEELKEAEEKEEEYAELQ----EELEELEEELEEL 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747 128 EAKISEYLQTISDLET--NCLDLRTKLQDLEVANQTLKDEYDALQITFTALEEKLRKTTEENQELvTRWMAEKAQEANRL 205
Cdd:COG4717  108 EAELEELREELEKLEKllQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAEL-AELQEELEELLEQL 186

                        170       180
                 ....*....|....*....|....*...
gi 329663747 206 NAENE---KDSRRRQARLQKELAEAAKE 230
Cdd:COG4717  187 SLATEeelQDLAEELEELQQRLAELEEE 214
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 80-230 3.87e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.85  E-value: 3.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747  80 SQLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQQKDKEIQMNEAKISEYLQTISDLETNCLDLRTKLQDLEVAN 159
Cdd:COG1196  295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 329663747 160 QTLKDEYDALQITFTALEEKLRKTTEENQELVTRwMAEKAQEANRLNAENEKDSRRRQARLQKELAEAAKE 230
Cdd:COG1196  375 AEAEEELEELAEELLEALRAAAELAAQLEELEEA-EEALLERLERLEEELEELEEALAELEEEEEEEEEAL 444
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
79-253 4.30e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.83  E-value: 4.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747   79 DSQLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQQKD-KEIQMNEAKISEYLQTISDLETNCLDLRTKLQDLEV 157
Cdd:COG4913   294 EAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGL 373

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747  158 ANQTLKDEYDALQITFTALEEKLRKTTEENQELVTRWMAEKaqeanrlnaeneKDSRRRQARLQKELA--EAAKEPLPVE 235
Cdd:COG4913   374 PLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAAL------------RDLRRELRELEAEIAslERRKSNIPAR 441

                         170
                  ....*....|....*...
gi 329663747  236 QDDDIEVIVDETSDHTEE 253
Cdd:COG4913   442 LLALRDALAEALGLDEAE 459
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 83-252 4.32e-05

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 46.55  E-value: 4.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747   83 QEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQQKD-----KEIQMNEAKISEYLQTISDLETNCLDLRTKLQDLEV 157
Cdd:TIGR04523 517 KKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKkenleKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEK 596

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747  158 ANQTLKDEYDALQITFTALEEKLRKTTEENQELvtrwmaekaqEANRLNAENEKDSRRRQARLQKELAEAAKEPLP--VE 235
Cdd:TIGR04523 597 EKKDLIKEIEEKEKKISSLEKELEKAKKENEKL----------SSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPeiIK 666

                         170
                  ....*....|....*..
gi 329663747  236 QDDDIEVIVDETSDHTE 252
Cdd:TIGR04523 667 KIKESKTKIDDIIELMK 683
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 81-274 4.59e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 4.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747  81 QLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQQKDKEIQMNEAKISEYLQTISDLETNCLDLRTKLQDLEVANQ 160
Cdd:COG1196  317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747 161 TLKDEYDALQITFTALEEKLRKTTEENQELVTrwmAEKAQEANRLNAENEKDSRRRQARLQKELAEAAKEPL--PVEQDD 238
Cdd:COG1196  397 ELAAQLEELEEAEEALLERLERLEEELEELEE---ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLaeLLEEAA 473

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 329663747 239 DIEVIVDETSDHTEETSPVRAVSRAATKRLSQPAGG 274
Cdd:COG1196  474 LLEAALAELLEELAEAAARLLLLLEAEADYEGFLEG 509
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 83-221 1.05e-04

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 45.55  E-value: 1.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747    83 QEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQQKDKEIQMNEAKISE-------YLQTISDLETNCLDLRTKLQD- 154
Cdd:pfam01576  204 QELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEetaqknnALKKIRELEAQISELQEDLESe 283

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 329663747   155 ------LEVANQTLKDEYDALQitfTALEEKLrKTTEENQELVTRwmaeKAQEANRLNAENEKDSRRRQARLQ 221
Cdd:pfam01576  284 raarnkAEKQRRDLGEELEALK---TELEDTL-DTTAAQQELRSK----REQEVTELKKALEEETRSHEAQLQ 348
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 101-270 1.05e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 44.75  E-value: 1.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747 101 KKRGELAQLVIDLNNQMQQKDKEIQMNEAKISEYLQTISDLETNCLDLRTKLQDLEVANQTLKDEYDALQITFTALEEKL 180
Cdd:COG4942   20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747 181 RKTTEENQELVTRW--MAEKAQEANRLNAENEKDSRRRQARLQ------KELAEAAKeplpvEQDDDIEVIVDETSDHTE 252
Cdd:COG4942  100 EAQKEELAELLRALyrLGRQPPLALLLSPEDFLDAVRRLQYLKylaparREQAEELR-----ADLAELAALRAELEAERA 174

                        170
                 ....*....|....*...
gi 329663747 253 ETSPVRAVSRAATKRLSQ 270
Cdd:COG4942  175 ELEALLAELEEERAALEA 192
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 79-249 1.08e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 45.44  E-value: 1.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747    79 DSQLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQQK-DKEIQMNEAKISEYLQTISDLETNCLDLRTKLQDLEV 157
Cdd:TIGR02169  243 ERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEE 322

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747   158 ANQTLKDEYDALQITFTALEEKLR-------KTTEENQELVTRwMAEKAQEANRLNAENeKDSRRRQARLQKELAEAAKE 230
Cdd:TIGR02169  323 RLAKLEAEIDKLLAEIEELEREIEeerkrrdKLTEEYAELKEE-LEDLRAELEEVDKEF-AETRDELKDYREKLEKLKRE 400

                          170       180
                   ....*....|....*....|.
gi 329663747   231 --PLPVEQDDDIEVIVDETSD 249
Cdd:TIGR02169  401 inELKRELDRLQEELQRLSEE 421
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 82-238 1.20e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 45.44  E-value: 1.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747    82 LQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQQKDKEIQMNEAKISEYLQTISDLETncldlrtKLQDLEVANQT 161
Cdd:TIGR02169  683 LEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEE-------DLSSLEQEIEN 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747   162 LKDEYDALQITFTALEEKLRKTTEENQELVTRWMAEKAQEANRLNAENEKDSRRRQARLQ------------KELAEAAK 229
Cdd:TIGR02169  756 VKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLReieqklnrltleKEYLEKEI 835


                   ....*....
gi 329663747   230 EPLPVEQDD 238
Cdd:TIGR02169  836 QELQEQRID 844
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 83-230 1.49e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.93  E-value: 1.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747  83 QEMAQLRIKH-QEELTELHKKRGELAQLVIDLNNQMQQKDKEIQMNEAKISEYLQTISDLETNCLDLRTKLQDLEVANQT 161
Cdd:COG1196  227 AELLLLKLRElEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIAR 306

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 329663747 162 LKDEYDALQITFTALEEKLRKTTEENQELVTR---WMAEKAQEANRLNAENEKDSRRRQARLQKELAEAAKE 230
Cdd:COG1196  307 LEERRRELEERLEELEEELAELEEELEELEEEleeLEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 81-237 1.60e-04

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: 45.05  E-value: 1.60e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747    81 QLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQQKDKEIQMNEAKISEYLQTISDLETNCLDLRTKLQ----DLE 156
Cdd:TIGR02168  324 QLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAslnnEIE 403

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747   157 VANQTLKDEYDALQITFTALEEKLRKTTEENQELVTRWMAEKAQEANRLNAENEkDSRRRQARLQKELAEAAKEPLPVEQ 236
Cdd:TIGR02168  404 RLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELE-RLEEALEELREELEEAEQALDAAER 482


                   .
gi 329663747   237 D 237
Cdd:TIGR02168  483 E 483
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
46-230 2.49e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 44.26  E-value: 2.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747  46 SDLHSVLTQKLQAEKHDMPNRHEispghdgawndsqlQEMAQLR--IKHQEELTELHKKRGELAQLVIDLNNQMQQkdkE 123
Cdd:PRK02224 190 DQLKAQIEEKEEKDLHERLNGLE--------------SELAELDeeIERYEEQREQARETRDEADEVLEEHEERRE---E 252

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747 124 IQMNEAKISEYLQTISDLETNCLDLRTKLQDLEVANQTLKDEYDAL--QITFTALE----EKLRKTTEENQELVTRWMAE 197
Cdd:PRK02224 253 LETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLlaEAGLDDADaeavEARREELEDRDEELRDRLEE 332

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 329663747 198 KAQEANRLN------AENEKDSRRRQARLQKELAEAAKE 230
Cdd:PRK02224 333 CRVAAQAHNeeaeslREDADDLEERAEELREEAAELESE 371
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 76-230 2.59e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.60  E-value: 2.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747  76 AWNDSQLQEMAQLRiKHQEELTELHKKRGELAQLVIDLNNQMQQKDKEIQMNEAKISEYLQTISDLETNCLDLRTKLQDL 155
Cdd:COG4942   17 AQADAAAEAEAELE-QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747 156 EVANQTLKDEY----DALQITFTALEEKLRKTTEENQELVTRWMAEKA-QEANRLNAENEKDSRRRQARLQKELAEAAKE 230
Cdd:COG4942   96 RAELEAQKEELaellRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYlAPARREQAEELRADLAELAALRAELEAERAE 175
46 PHA02562
endonuclease subunit; Provisional
 80-244 5.49e-04

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 43.08  E-value: 5.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747  80 SQLQEMAQLRIKHQEELTELHKKrgeLAQLVIDLNNQMQQKDKEIQMNE---------AKISEYLQTISDLETNCLDLRT 150
Cdd:PHA02562 237 EELTDELLNLVMDIEDPSAALNK---LNTAAAKIKSKIEQFQKVIKMYEkggvcptctQQISEGPDRITKIKDKLKELQH 313

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747 151 KLQDLEVANQTLK---DEYDALQITFTALEEKLRKtteENQELVT-RWMAEKAQEA-NRLNAENeKDSRRRQARLQKELA 225
Cdd:PHA02562 314 SLEKLDTAIDELEeimDEFNEQSKKLLELKNKIST---NKQSLITlVDKAKKVKAAiEELQAEF-VDNAEELAKLQDELD 389

                        170
                 ....*....|....*....
gi 329663747 226 EAAKEPLPVEQDDDIEVIV 244
Cdd:PHA02562 390 KIVKTKSELVKEKYHRGIV 408
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 80-230 5.90e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.13  E-value: 5.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747    80 SQLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQQKDKEIQMNEAKISEYLQTISDLETNclDLRTKLQDLEVAN 159
Cdd:TIGR02169  723 KEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEAR--LSHSRIPEIQAEL 800

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 329663747   160 QTLKDEYDALQITFTALEEKLRKTTEENQELvtRWMAEKAQEANRLNAENEKDSRRRQARLQKELAEAAKE 230
Cdd:TIGR02169  801 SKLEEEVSRIEARLREIEQKLNRLTLEKEYL--EKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE 869
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 79-193 9.51e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 42.36  E-value: 9.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747    79 DSQLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQQKDKEIQMNEAKISEYLQ-------------TISDLETNC 145
Cdd:TIGR02169  881 ESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDpkgedeeipeeelSLEDVQAEL 960

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 329663747   146 LDLRTKLQDLEVANQTLKDEYDALQITFTALEEKLRKTTEENQELVTR 193
Cdd:TIGR02169  961 QRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILER 1008
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
80-249 9.91e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.81  E-value: 9.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747  80 SQLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQQKDKEIQMNEAKISEYLQTISDLETNCLDLRTKLQDLEVAN 159
Cdd:COG4372   87 EQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEEL 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747 160 QTLKDEYDALQITFTALEEKLRKTTEENQELVTRWMAEKAQEANRLNAENEKDSRRRQARLQKELAEAAKEPLPVEQDDD 239
Cdd:COG4372  167 AALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEE 246

                        170
                 ....*....|
gi 329663747 240 IEVIVDETSD 249
Cdd:COG4372  247 DKEELLEEVI 256
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
80-208 1.01e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 41.43  E-value: 1.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747  80 SQLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQQKDKEIQMNEAK---ISEYLQTISDLE----TNCLD----- 147
Cdd:COG1340   57 EEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAggsIDKLRKEIERLEwrqqTEVLSpeeek 136

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 329663747 148 --------LRTKLQDLEVAN------QTLKDEYDALQITFTALEEKLRKTTEENQELVTRwMAEKAQEANRLNAE 208
Cdd:COG1340  137 elvekikeLEKELEKAKKALekneklKELRAELKELRKEAEEIHKKIKELAEEAQELHEE-MIELYKEADELRKE 210
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 79-230 1.55e-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: 41.54  E-value: 1.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747   79 DSQLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQQKDKEIQMNEAKISEYLQTISDLEtncLDLRTKLQDLEVA 158
Cdd:TIGR04523 411 DEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLS---RSINKIKQNLEQK 487

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747  159 NQTLK---DEYDALQITFTALEEKLRKTTEENQELVTRW------MAEKAQEANRLNAE-NEKDSRRRQARLQKELAEAA 228
Cdd:TIGR04523 488 QKELKskeKELKKLNEEKKELEEKVKDLTKKISSLKEKIekleseKKEKESKISDLEDElNKDDFELKKENLEKEIDEKN 567


                  ..
gi 329663747  229 KE 230
Cdd:TIGR04523 568 KE 569
TolB COG0823
Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, ...
 530-620 1.60e-03

Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 440585 [Multi-domain]  Cd Length: 158  Bit Score: 39.66  E-value: 1.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747 530 VIDLRTNAVKQ-TFSapgfkcGSDWTRVVFSPDGSYVAAGSAEGS---LYVWSVLTGKVEKVLSKQHSSSinavaWAPSG 605
Cdd:COG0823   59 VVDADGGEPRRlTFG------GGYNASPSWSPDGKRLAFVSRSDGrfdIYVLDLDGGAPRRLTDGPGSPS-----WSPDG 127

                         90
                 ....*....|....*.
gi 329663747 606 LHVV-SVDKGSRAVLW 620
Cdd:COG0823  128 RRIVfSSDRGGRPDLY 143
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 79-229 1.64e-03

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


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 41.65  E-value: 1.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747   79 DSQLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQQKDKEIQ-------MNEAKISEYLQTISDLETNCLDLRT- 150
Cdd:pfam05557  89 NKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEelqerldLLKAKASEAEQLRQNLEKQQSSLAEa 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747  151 --KLQDLEVANQtlKDEYDAL--------QITFTALEEKLRKTTEENQELvtrwmaEKAQEANRLNAENEKDSRRRQARL 220
Cdd:pfam05557 169 eqRIKELEFEIQ--SQEQDSEivknskseLARIPELEKELERLREHNKHL------NENIENKLLLKEEVEDLKRKLERE 240


                  ....*....
gi 329663747  221 QKELAEAAK 229
Cdd:pfam05557 241 EKYREEAAT 249
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 331-366 1.97e-03

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 40.40  E-value: 1.97e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 329663747 331 SYVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWE 366
Cdd:cd00200  254 VQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 91-226 2.08e-03

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 41.25  E-value: 2.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747   91 KHQEELTELHKKRGELAQLVIDLNNQMQQ-----KDKEIQMNEAKISEYLQTISDLEtncldlrtKLQDLEVANQ----T 161
Cdd:pfam05483 166 RSAEKTKKYEYEREETRQVYMDLNNNIEKmilafEELRVQAENARLEMHFKLKEDHE--------KIQHLEEEYKkeinD 237

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 329663747  162 LKDEYDALQITFTALEEKLRKTTEENQElvTRWMAEKAQEANRLNAENEKDSRRRQARLQKELAE 226
Cdd:pfam05483 238 KEKQVSLLLIQITEKENKMKDLTFLLEE--SRDKANQLEEKTKLQDENLKELIEKKDHLTKELED 300
COG4946 COG4946
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown] ...
 557-623 2.21e-03

Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown];


Pssm-ID: 443973 [Multi-domain]  Cd Length: 1072  Bit Score: 41.18  E-value: 2.21e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 329663747  557 VFSPDGSYVAAGSAEGSLYVWSVLTGKVEKVLSKQHSSSINAVAWAPsglhvvsvDkgSRAVLWAQP 623
Cdd:COG4946   395 VWSPDGKKIAFTDNRGRLWVVDLASGKVRKVDTDGYGDGISDLAWSP--------D--SKWLAYSKP 451
TolB COG0823
Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, ...
 530-609 2.38e-03

Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 440585 [Multi-domain]  Cd Length: 158  Bit Score: 38.88  E-value: 2.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747 530 VIDLRTNAVKQTFSAPGFKCGSDWtrvvfSPDGSYVAAGSAEGS---LYVWSVLTGKVEKVLSKQHSSSinAVAWAPSGL 606
Cdd:COG0823   15 VVDLDGGEPRRLTNSPGIDTSPAW-----SPDGRRIAFTSDRGGgpqIYVVDADGGEPRRLTFGGGYNA--SPSWSPDGK 87


                 ...
gi 329663747 607 HVV 609
Cdd:COG0823   88 RLA 90
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
93-243 2.52e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.66  E-value: 2.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747  93 QEELTELHKKRGELAQLvidlNNQMQQKDKEIQMNEAKISEYLQTISDLETNCLDLRTKLQDLEVANQTLKDEYDALQIT 172
Cdd:COG4372   34 RKALFELDKLQEELEQL----REELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEE 109

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 329663747 173 FTALEEKLRKTTEENQELVTRWMAEKAQEANRLNAENEKDSR-----RRQARLQKELAEAAKEPLPVEQDDDIEVI 243
Cdd:COG4372  110 AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEElkeleEQLESLQEELAALEQELQALSEAEAEQAL 185
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 93-230 2.60e-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: 2.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747   93 QEELTELHKKRGELAQLVIDLNNQMQQKDKEIQMNEAKISEYLQTISDLETNCLDLRT-KLQDLevaNQTLKDEYDALQI 171
Cdd:TIGR04523 245 TTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNqKEQDW---NKELKSELKNQEK 321

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 329663747  172 TFTALEEKLRKTTEENQELvTRWMAEKAQEANRLNAENEKdsrrrqarLQKELAEAAKE 230
Cdd:TIGR04523 322 KLEEIQNQISQNNKIISQL-NEQISQLKKELTNSESENSE--------KQRELEEKQNE 371
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
82-238 2.67e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 2.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747   82 LQEMAQLRiKHQEELTELHKKRGELAQLViDLNNQMQQKDKEIQMNEakiseYLQTISDLETNcldlRTKLQDLEVANQT 161
Cdd:COG4913   231 VEHFDDLE-RAHEALEDAREQIELLEPIR-ELAERYAAARERLAELE-----YLRAALRLWFA----QRRLELLEAELEE 299

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747  162 LKDEYDALQITFTALEEKLRKTTEENQELVTRWMAEKAQEANRL-----NAENEKDSRRRQARLQKELAEAAKEPLPVEQ 236
Cdd:COG4913   300 LRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLereieRLERELEERERRRARLEALLAALGLPLPASA 379


                  ..
gi 329663747  237 DD 238
Cdd:COG4913   380 EE 381
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 43-215 3.22e-03

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: 40.82  E-value: 3.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747    43 LEKSDLHSVLtQKLQAEKHDMPNRHeispghdgAWNDSQLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQQKDK 122
Cdd:TIGR02169  784 LEARLSHSRI-PEIQAELSKLEEEV--------SRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEK 854

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747   123 EIQMNEAKISEYLQTISDLETNCLDLRTKLQDLEVANQTLKDEYDALQITFTALEEKLRKTTEENQELvtrwmAEKAQEA 202
Cdd:TIGR02169  855 EIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSEL-----KAKLEAL 929

                          170
                   ....*....|...
gi 329663747   203 NRLNAENEKDSRR 215
Cdd:TIGR02169  930 EEELSEIEDPKGE 942
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 147-243 3.25e-03

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 40.45  E-value: 3.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747 147 DLRTKLQDLEVANQTLKDEYD-ALQITFTALEEKLRKTTEENQELVTRWMAEKA--QEANRLNAENEKDSRRRQArLQKE 223
Cdd:COG0542  415 ELERRLEQLEIEKEALKKEQDeASFERLAELRDELAELEEELEALKARWEAEKEliEEIQELKEELEQRYGKIPE-LEKE 493

                         90       100
                 ....*....|....*....|....*...
gi 329663747 224 LAEA-----AKEPLPVEQ--DDDI-EVI 243
Cdd:COG0542  494 LAELeeelaELAPLLREEvtEEDIaEVV 521
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 76-358 3.49e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.20  E-value: 3.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747  76 AWNDSQLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQQKDKEIQMNEAKISEYLQTISDLETNCLDLRTKLQD- 154
Cdd:COG3883   12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEr 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747 155 -------------LEV----------------------ANQTLKDEYDALQITFTALEEKLRKTTEENQELVTRwMAEKA 199
Cdd:COG3883   92 aralyrsggsvsyLDVllgsesfsdfldrlsalskiadADADLLEELKADKAELEAKKAELEAKLAELEALKAE-LEAAK 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747 200 QEANRLNAENEK-------DSRRRQARLQKELAEAAKEPLPVEQDDDIEVIVDETSDHTEETSPVRAVSRAATKRLSQPA 272
Cdd:COG3883  171 AELEAQQAEQEAllaqlsaEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAG 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747 273 GGLLDSITNIFGLSESPLLGHHSSDAARRRSVSSIPVPQDImdTHPASGKDVRVPTTASYVFDAHDGEVNAVQFSPGSRL 352
Cdd:COG3883  251 AAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGG--GGGGGGAASGGSGGGSGGAGGVGSGGGAGAVVGGASA 328


                 ....*.
gi 329663747 353 LATGGM 358
Cdd:COG3883  329 GGGGGS 334
PRK12704 PRK12704
phosphodiesterase; Provisional
 90-230 4.40e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.15  E-value: 4.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747  90 IKHQEELT---ELHKKRGELAQLVIDLNNQMQQKDKEIQMNEAKISEYLQTISDLEtncldlrTKLQDLEVANQTLKDEY 166
Cdd:PRK12704  54 IKKEALLEakeEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKRE-------EELEKKEKELEQKQQEL 126

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 329663747 167 DALQitftalEEKLRKTTEENQELvTRWMAEKAQEA-NRLNAENEKDSRRRQARLQKELAEAAKE 230
Cdd:PRK12704 127 EKKE------EELEELIEEQLQEL-ERISGLTAEEAkEILLEKVEEEARHEAAVLIKEIEEEAKE 184
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
120-230 5.99e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 39.84  E-value: 5.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747 120 KDKEIQMNEAKISEYLQTISDLETNCLDLRTKLQDLEVANQTLKDEYDALQITFTALEEKLRKT-TEENQELvtrwmaEK 198
Cdd:COG2433  390 LPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEArSEERREI------RK 463

                         90       100       110
                 ....*....|....*....|....*....|..
gi 329663747 199 AQEANRLNAENEkdsrrrqaRLQKELAEAAKE 230
Cdd:COG2433  464 DREISRLDREIE--------RLERELEEERER 487
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 112-350 6.15e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.43  E-value: 6.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747 112 DLNNQMQQKDKEIQMNEAKISEYLQTISDLETNCLDLRTKLQDLEVANQTLKDEYDALQitftaleeklrKTTEENQELV 191
Cdd:COG3883  116 DFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE-----------AQQAEQEALL 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747 192 TRWMAEKAQEANRLNA-ENEKDSRRRQARLQKELAEAAKEPLPVEQDDDIEVIVDETSDHTEETSPVRAVSRAATKRLSQ 270
Cdd:COG3883  185 AQLSAEEAAAEAQLAElEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGA 264

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747 271 PAGGLLDSITNIFGLSESPLLGHHSSDAARRRSVSSIPVPQDIMDTHPASGKDVRVPTTASYVFDAHDGEVNAVQFSPGS 350
Cdd:COG3883  265 AGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAVVGGASAGGGGGSGGGGGSSGGG 344
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
31-188 6.76e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.37  E-value: 6.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747  31 AFEEIILQYTKLLEKSDLHSVLTQKLQAEKhdmPNRHEISPGHDGAWNDSQLQEMAQLRIKHQEELTELHKKRGELaqlv 110
Cdd:COG4717  386 ELRAALEQAEEYQELKEELEELEEQLEELL---GELEELLEALDEEELEEELEELEEELEELEEELEELREELAEL---- 458

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 329663747 111 idlnnqmqqkdkEIQMNEAKISEYLQtisdletnclDLRTKLQDLEVANQTLKDEYDALQITFTALEEKLRKTTEENQ 188
Cdd:COG4717  459 ------------EAELEQLEEDGELA----------ELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERL 514
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 581-620 7.04e-03

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 34.60  E-value: 7.04e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 329663747   581 TGKVEKVLsKQHSSSINAVAWAPSGLHVVSVDKGSRAVLW 620
Cdd:smart00320   1 SGELLKTL-KGHTGPVTSVAFSPDGKYLASGSDDGTIKLW 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 554-578 7.11e-03

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 34.60  E-value: 7.11e-03
                           10        20
                   ....*....|....*....|....*
gi 329663747   554 TRVVFSPDGSYVAAGSAEGSLYVWS 578
Cdd:smart00320  16 TSVAFSPDGKYLASGSDDGTIKLWD 40
Ge1_WD40 pfam16529
WD40 region of Ge1, enhancer of mRNA-decapping protein; Ge1_WD40 is the N-terminal region of ...
 381-462 7.72e-03

WD40 region of Ge1, enhancer of mRNA-decapping protein; Ge1_WD40 is the N-terminal region of Ge-1 or enhancer of mRNA-decapping proteins. WD40-repeat regions are involved in protein-protein interactions.


Pssm-ID: 465162 [Multi-domain]  Cd Length: 328  Bit Score: 38.98  E-value: 7.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663747  381 SNAGITSIEFDSAGAYLLAASNDFASRIWTV-----DDYRLRHTLTGHSGKVLSAKFLLDNAR----------IVSGS-H 444
Cdd:pfam16529 185 EHSLLVDAAFSPDGTALATASLDGEVKFFQIylfdnRNPRCLHEWKPHDGKPLSSLFFLDNHKkppevqfwrfAITGAdN 264

                          90
                  ....*....|....*...
gi 329663747  445 DRTLKLWDLRSKVCIKTV 462
Cdd:pfam16529 265 NSELKLWSCESWTCLQTI 282
 
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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