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Conserved domains on  [gi|564369545|ref|XP_006245481|]
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autophagy-related protein 16-1 isoform X1 [Rattus norvegicus]

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 1.64e-59

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 204.37  E-value: 1.64e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545 217 QARLQKELAEAAKEPLPVEQDDDIEVIVDETSDHTEETSPVRAISRAATKRLSQPAGGLLDSITNIFGLSESPLLGHHSS 296
Cdd:COG2319    1 ALSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545 297 DAARRRSvssipvPQDVVDTHPASGKDVRVPTTAS----YVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWEAFGDKC 372
Cdd:COG2319   81 VLSVAFS------PDGRLLASASADGTVRLWDLATglllRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKL 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545 373 EfkGSLSGSNAGITSIEFDSAGAYLLAASNDFASRIWTVDDYRLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWD 452
Cdd:COG2319  155 L--RTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWD 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545 453 LRSKVCIKTV-FAGSSCNDIVCT--EQCVMSGHFDKKIRFWDIRSESVVREME-LLGKITALDLNPERTELLSCSRDDLL 528
Cdd:COG2319  233 LATGKLLRTLtGHSGSVRSVAFSpdGRLLASGSADGTVRLWDLATGELLRTLTgHSGGVNSVAFSPDGKLLASGSDDGTV 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545 529 KIIDLRTNAIKQSFSAPgfkcGSDWTRVVFSPDGSYVAAGSADGSLYVWSVLTGKVEKVLsKQHSSSINAVAWAPSGLHV 608
Cdd:COG2319  313 RLWDLATGKLLRTLTGH----TGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTL-TGHTGAVTSVAFSPDGRTL 387

                        410
                 ....*....|..
gi 564369545 609 VSVDKGSRAVLW 620
Cdd:COG2319  388 ASGSADGTVRLW 399
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 31-206 1.88e-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: 185.91  E-value: 1.88e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545   31 AFEEIILQYTKLLEKSDLHSVLTQKLQAEKHDVPNRHEISPGHDGAWNDSQLQEMAQLKMKHQEELTELHKKRGELAQLV 110
Cdd:pfam08614   1 AFLELIDAYNRLLDRTALLEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQLREELAELYRSRGELAQRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545  111 IDLNNQMQQKDKEIQTNEAKIAECLQTISDLEADCLDLRTKLQDLEVANQTLKDEYDALQITFTALEEKLRKTTEENQEL 190
Cdd:pfam08614  81 VDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQDELVALQLQLNMAEEKLRKLEKENREL 160

                         170
                  ....*....|....*.
gi 564369545  191 VTRWMAEKAQEANRLN 206
Cdd:pfam08614 161 VERWMKRKGQEAEAMN 176
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
217-620 1.64e-59

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 204.37  E-value: 1.64e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545 217 QARLQKELAEAAKEPLPVEQDDDIEVIVDETSDHTEETSPVRAISRAATKRLSQPAGGLLDSITNIFGLSESPLLGHHSS 296
Cdd:COG2319    1 ALSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545 297 DAARRRSvssipvPQDVVDTHPASGKDVRVPTTAS----YVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWEAFGDKC 372
Cdd:COG2319   81 VLSVAFS------PDGRLLASASADGTVRLWDLATglllRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKL 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545 373 EfkGSLSGSNAGITSIEFDSAGAYLLAASNDFASRIWTVDDYRLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWD 452
Cdd:COG2319  155 L--RTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWD 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545 453 LRSKVCIKTV-FAGSSCNDIVCT--EQCVMSGHFDKKIRFWDIRSESVVREME-LLGKITALDLNPERTELLSCSRDDLL 528
Cdd:COG2319  233 LATGKLLRTLtGHSGSVRSVAFSpdGRLLASGSADGTVRLWDLATGELLRTLTgHSGGVNSVAFSPDGKLLASGSDDGTV 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545 529 KIIDLRTNAIKQSFSAPgfkcGSDWTRVVFSPDGSYVAAGSADGSLYVWSVLTGKVEKVLsKQHSSSINAVAWAPSGLHV 608
Cdd:COG2319  313 RLWDLATGKLLRTLTGH----TGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTL-TGHTGAVTSVAFSPDGRTL 387

                        410
                 ....*....|..
gi 564369545 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 6.89e-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: 193.71  E-value: 6.89e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545 333 VFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWEAFGDKCEFkgSLSGSNAGITSIEFDSAGAYLLAASNDFASRIWTVD 412
Cdd:cd00200    4 TLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLR--TLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545 413 DYRLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTvFAG----------SSCNDIVCteqcvmSGH 482
Cdd:cd00200   82 TGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTT-LRGhtdwvnsvafSPDGTFVA------SSS 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545 483 FDKKIRFWDIRSESVVREMEL-LGKITALDLNPERTELLSCSRDDLLKIIDLRTNAIKQSFSAPgfkcgSDW-TRVVFSP 560
Cdd:cd00200  155 QDGTIKLWDLRTGKCVATLTGhTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGH-----ENGvNSVAFSP 229

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564369545 561 DGSYVAAGSADGSLYVWSVLTGKVEKVLSkQHSSSINAVAWAPSGLHVVSVDKGSRAVLWA 621
Cdd:cd00200  230 DGYLLASGSEDGTIRVWDLRTGECVQTLS-GHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 31-206 1.88e-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: 185.91  E-value: 1.88e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545   31 AFEEIILQYTKLLEKSDLHSVLTQKLQAEKHDVPNRHEISPGHDGAWNDSQLQEMAQLKMKHQEELTELHKKRGELAQLV 110
Cdd:pfam08614   1 AFLELIDAYNRLLDRTALLEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQLREELAELYRSRGELAQRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545  111 IDLNNQMQQKDKEIQTNEAKIAECLQTISDLEADCLDLRTKLQDLEVANQTLKDEYDALQITFTALEEKLRKTTEENQEL 190
Cdd:pfam08614  81 VDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQDELVALQLQLNMAEEKLRKLEKENREL 160

                         170
                  ....*....|....*.
gi 564369545  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 2.07e-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: 114.20  E-value: 2.07e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545 119 QKDKEIQTNEAKIAECLQTISDLEADCLDLRTKLQDLEVANQTLKDEYDALQITFTALEEKLRKTTEENQELVTRWMAEK 198
Cdd:cd22887    1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEENDELVERWMAKK 80

                         90
                 ....*....|.
gi 564369545 199 AQEANRLNAEN 209
Cdd:cd22887   81 QQEADKMNEAN 91
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
83-264 1.15e-09

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 60.69  E-value: 1.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545  83 QEMAQLKMKHQEELTELHKKRGELAQLvidlNNQMQQKDKEIQTNEAKIAECLQTISDLEADCLDLRTKLQDLEVANQTL 162
Cdd:COG4372   52 EELEQAREELEQLEEELEQARSELEQL----EEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDL 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545 163 KDEYDALQITFTALEEKLRKTTEENQELVTRwMAEKAQEANRLNAENEKDSRRR-QARLQKELAEAAKEPLPVEQDDDIE 241
Cdd:COG4372  128 EQQRKQLEAQIAELQSEIAEREEELKELEEQ-LESLQEELAALEQELQALSEAEaEQALDELLKEANRNAEKEEELAEAE 206

                        170       180
                 ....*....|....*....|...
gi 564369545 242 VIVDETSDHTEETSPVRAISRAA 264
Cdd:COG4372  207 KLIESLPRELAEELLEAKDSLEA 229
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 332-366 9.92e-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: 9.92e-08
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 564369545   332 YVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWE 366
Cdd:smart00320   6 KTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
332-366 2.58e-07

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 47.34  E-value: 2.58e-07
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 564369545  332 YVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWE 366
Cdd:pfam00400   5 KTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 114-266 7.98e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 52.37  E-value: 7.98e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545   114 NNQMQQKDKEIQTNEAKIAECLQTISDLEADCLDLRTKLQDLEVANQTLKDEYDALQITFTALEEKLRKTTEEnQELVTR 193
Cdd:TIGR02168  669 NSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE-VEQLEE 747

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564369545   194 WMAEKAQEANRLNAE-NEKDSRRRQARLQKELAEAAKEPLPVEQDDDIEVIVDETSDHTEETSPVRAISRAATK 266
Cdd:TIGR02168  748 RIAQLSKELTELEAEiEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAAN 821
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 341-577 3.43e-06

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 50.09  E-value: 3.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545 341 VNAVQFSPGSRLLATGGMDRRVKLWEAF-----GDKCEFKGSLSGSNAGITSIEFDSAGAYLLAASN-DFASRIWTVDDY 414
Cdd:PLN00181 486 VCAIGFDRDGEFFATAGVNKKIKIFECEsiikdGRDIHYPVVELASRSKLSGICWNSYIKSQVASSNfEGVVQVWDVARS 565

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545 415 RLRHTLTGHSGKVLSAKFL-LDNARIVSGSHDRTLKLWDLRSKVCIKTVfagSSCNDIVCTE------QCVMSGHFDKKI 487
Cdd:PLN00181 566 QLVTEMKEHEKRVWSIDYSsADPTLLASGSDDGSVKLWSINQGVSIGTI---KTKANICCVQfpsesgRSLAFGSADHKV 642

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545 488 RFWDIRSE-----SVVREMELLGKITALDlnpeRTELLSCSRDDLLKIIDLRTNA--IKQS--FSAPGFKCGSDWTRVVF 558
Cdd:PLN00181 643 YYYDLRNPklplcTMIGHSKTVSYVRFVD----SSTLVSSSTDNTLKLWDLSMSIsgINETplHSFMGHTNVKNFVGLSV 718

                        250
                 ....*....|....*....
gi 564369545 559 SpDGsYVAAGSADGSLYVW 577
Cdd:PLN00181 719 S-DG-YIATGSETNEVFVY 735
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
46-230 1.81e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 44.65  E-value: 1.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545  46 SDLHSVLTQKLQAEKHDVPNRHEispghdgawndsqlQEMAQLK--MKHQEELTELHKKRGELAQLVIDLNNQMQQkdkE 123
Cdd:PRK02224 190 DQLKAQIEEKEEKDLHERLNGLE--------------SELAELDeeIERYEEQREQARETRDEADEVLEEHEERRE---E 252

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545 124 IQTNEAKIAECLQTISDLEADCLDLRTKLQDLEVANQTLKDEYDAL--QITFTALE----EKLRKTTEENQELVTRWMAE 197
Cdd:PRK02224 253 LETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLlaEAGLDDADaeavEARREELEDRDEELRDRLEE 332

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 564369545 198 KAQEANRLN------AENEKDSRRRQARLQKELAEAAKE 230
Cdd:PRK02224 333 CRVAAQAHNeeaeslREDADDLEERAEELREEAAELESE 371
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 39-170 4.81e-04

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


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 42.70  E-value: 4.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545    39 YTKLLEKSDLHSVLTQKLQAEKHDVPNRHEISPGHDGAWNDSQLQEMAQLKMKHQEELTELHKKRGELAQLvidlNNQMQ 118
Cdd:smart00787 160 YKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRAKEKLKKLLQEIMIKVKKLEEL----EEELQ 235

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 564369545   119 QKDKEIQTNEAKIAECLQTISDLEADCLDLRtKLQDLEVAnqTLKDEYDALQ 170
Cdd:smart00787 236 ELESKIEDLTNKKSELNTEIAEAEKKLEQCR-GFTFKEIE--KLKEQLKLLQ 284
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
217-620 1.64e-59

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 204.37  E-value: 1.64e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545 217 QARLQKELAEAAKEPLPVEQDDDIEVIVDETSDHTEETSPVRAISRAATKRLSQPAGGLLDSITNIFGLSESPLLGHHSS 296
Cdd:COG2319    1 ALSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545 297 DAARRRSvssipvPQDVVDTHPASGKDVRVPTTAS----YVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWEAFGDKC 372
Cdd:COG2319   81 VLSVAFS------PDGRLLASASADGTVRLWDLATglllRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKL 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545 373 EfkGSLSGSNAGITSIEFDSAGAYLLAASNDFASRIWTVDDYRLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWD 452
Cdd:COG2319  155 L--RTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWD 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545 453 LRSKVCIKTV-FAGSSCNDIVCT--EQCVMSGHFDKKIRFWDIRSESVVREME-LLGKITALDLNPERTELLSCSRDDLL 528
Cdd:COG2319  233 LATGKLLRTLtGHSGSVRSVAFSpdGRLLASGSADGTVRLWDLATGELLRTLTgHSGGVNSVAFSPDGKLLASGSDDGTV 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545 529 KIIDLRTNAIKQSFSAPgfkcGSDWTRVVFSPDGSYVAAGSADGSLYVWSVLTGKVEKVLsKQHSSSINAVAWAPSGLHV 608
Cdd:COG2319  313 RLWDLATGKLLRTLTGH----TGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTL-TGHTGAVTSVAFSPDGRTL 387

                        410
                 ....*....|..
gi 564369545 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 6.89e-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: 193.71  E-value: 6.89e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545 333 VFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWEAFGDKCEFkgSLSGSNAGITSIEFDSAGAYLLAASNDFASRIWTVD 412
Cdd:cd00200    4 TLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLR--TLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545 413 DYRLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTvFAG----------SSCNDIVCteqcvmSGH 482
Cdd:cd00200   82 TGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTT-LRGhtdwvnsvafSPDGTFVA------SSS 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545 483 FDKKIRFWDIRSESVVREMEL-LGKITALDLNPERTELLSCSRDDLLKIIDLRTNAIKQSFSAPgfkcgSDW-TRVVFSP 560
Cdd:cd00200  155 QDGTIKLWDLRTGKCVATLTGhTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGH-----ENGvNSVAFSP 229

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564369545 561 DGSYVAAGSADGSLYVWSVLTGKVEKVLSkQHSSSINAVAWAPSGLHVVSVDKGSRAVLWA 621
Cdd:cd00200  230 DGYLLASGSEDGTIRVWDLRTGECVQTLS-GHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 31-206 1.88e-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: 185.91  E-value: 1.88e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545   31 AFEEIILQYTKLLEKSDLHSVLTQKLQAEKHDVPNRHEISPGHDGAWNDSQLQEMAQLKMKHQEELTELHKKRGELAQLV 110
Cdd:pfam08614   1 AFLELIDAYNRLLDRTALLEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQLREELAELYRSRGELAQRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545  111 IDLNNQMQQKDKEIQTNEAKIAECLQTISDLEADCLDLRTKLQDLEVANQTLKDEYDALQITFTALEEKLRKTTEENQEL 190
Cdd:pfam08614  81 VDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQDELVALQLQLNMAEEKLRKLEKENREL 160

                         170
                  ....*....|....*.
gi 564369545  191 VTRWMAEKAQEANRLN 206
Cdd:pfam08614 161 VERWMKRKGQEAEAMN 176
WD40 COG2319
WD40 repeat [General function prediction only];
332-579 1.62e-47

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 172.02  E-value: 1.62e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545 332 YVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWEAFGDKCEFkgSLSGSNAGITSIEFDSAGAYLLAASNDFASRIWTV 411
Cdd:COG2319  156 RTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLR--TLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDL 233

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545 412 DDYRLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTVFAGSSC-NDIVCT--EQCVMSGHFDKKIR 488
Cdd:COG2319  234 ATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGvNSVAFSpdGKLLASGSDDGTVR 313

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545 489 FWDIRSESVVREME-LLGKITALDLNPERTELLSCSRDDLLKIIDLRTNAIKQSFSAPgfkcgSDW-TRVVFSPDGSYVA 566
Cdd:COG2319  314 LWDLATGKLLRTLTgHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGH-----TGAvTSVAFSPDGRTLA 388

                        250
                 ....*....|...
gi 564369545 567 AGSADGSLYVWSV 579
Cdd:COG2319  389 SGSADGTVRLWDL 401
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 332-578 3.16e-38

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: 142.86  E-value: 3.16e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545 332 YVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWEAFGDKCEFkgSLSGSNAGITSIEFDSAGAYLLAASNDFASRIWTV 411
Cdd:cd00200   87 RTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLT--TLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDL 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545 412 DDYRLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTvfagsscndivcteqcvMSGHfdkkirfwd 491
Cdd:cd00200  165 RTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGT-----------------LRGH--------- 218

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545 492 irsesvvremelLGKITALDLNPERTELLSCSRDDLLKIIDLRTNAIKQSFSAPGFKCGSdwtrVVFSPDGSYVAAGSAD 571
Cdd:cd00200  219 ------------ENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTS----LAWSPDGKRLASGSAD 282


                 ....*..
gi 564369545 572 GSLYVWS 578
Cdd:cd00200  283 GTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
333-535 2.68e-36

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 140.43  E-value: 2.68e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545 333 VFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWEAFGDKCEFkgSLSGSNAGITSIEFDSAGAYLLAASNDFASRIWTVD 412
Cdd:COG2319  199 TLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLR--TLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLA 276

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545 413 DYRLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTvFAG--SSCNDIVCT--EQCVMSGHFDKKIR 488
Cdd:COG2319  277 TGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRT-LTGhtGAVRSVAFSpdGKTLASGSDDGTVR 355

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 564369545 489 FWDIRSESVVREME-LLGKITALDLNPERTELLSCSRDDLLKIIDLRT 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 1.22e-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: 132.84  E-value: 1.22e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545 416 LRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTV----FAGSSCNDIVCTEQCVmSGHFDKKIRFWD 491
Cdd:cd00200    1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLkghtGPVRDVAASADGTYLA-SGSSDKTIRLWD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545 492 IRSESVVREMEL-LGKITALDLNPERTELLSCSRDDLLKIIDLRTNAIKQSFSAPgfkcgSDWTR-VVFSPDGSYVAAGS 569
Cdd:cd00200   80 LETGECVRTLTGhTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGH-----TDWVNsVAFSPDGTFVASSS 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 564369545 570 ADGSLYVWSVLTGKVEKVLsKQHSSSINAVAWAPSGLHVVS 610
Cdd:cd00200  155 QDGTIKLWDLRTGKCVATL-TGHTGEVNSVAFSPDGEKLLS 194
WD40 COG2319
WD40 repeat [General function prediction only];
332-494 1.64e-31

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 126.95  E-value: 1.64e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545 332 YVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWEAFGDKCefKGSLSGSNAGITSIEFDSAGAYLLAASNDFASRIWTV 411
Cdd:COG2319  240 RTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGEL--LRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDL 317

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545 412 DDYRLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTvFAGSScnDIVCT------EQCVMSGHFDK 485
Cdd:COG2319  318 ATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRT-LTGHT--GAVTSvafspdGRTLASGSADG 394


                 ....*....
gi 564369545 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 2.07e-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: 114.20  E-value: 2.07e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545 119 QKDKEIQTNEAKIAECLQTISDLEADCLDLRTKLQDLEVANQTLKDEYDALQITFTALEEKLRKTTEENQELVTRWMAEK 198
Cdd:cd22887    1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEENDELVERWMAKK 80

                         90
                 ....*....|.
gi 564369545 199 AQEANRLNAEN 209
Cdd:cd22887   81 QQEADKMNEAN 91
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
83-264 1.15e-09

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 60.69  E-value: 1.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545  83 QEMAQLKMKHQEELTELHKKRGELAQLvidlNNQMQQKDKEIQTNEAKIAECLQTISDLEADCLDLRTKLQDLEVANQTL 162
Cdd:COG4372   52 EELEQAREELEQLEEELEQARSELEQL----EEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDL 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545 163 KDEYDALQITFTALEEKLRKTTEENQELVTRwMAEKAQEANRLNAENEKDSRRR-QARLQKELAEAAKEPLPVEQDDDIE 241
Cdd:COG4372  128 EQQRKQLEAQIAELQSEIAEREEELKELEEQ-LESLQEELAALEQELQALSEAEaEQALDELLKEANRNAEKEEELAEAE 206

                        170       180
                 ....*....|....*....|...
gi 564369545 242 VIVDETSDHTEETSPVRAISRAA 264
Cdd:COG4372  207 KLIESLPRELAEELLEAKDSLEA 229
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 81-253 4.15e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.48  E-value: 4.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545  81 QLQEMAQLKMKHQEELTELHKKRGEL-------AQLVIDLNNQMQQKDKEIQTNEAKIAECLQTISDLEADCLDLRTKLQ 153
Cdd:COG1196  275 ELEELELELEEAQAEEYELLAELARLeqdiarlEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545 154 DLEVANQTLKDEYDALQITFTALEEKLRKTTEENQELVTRWMAEKAQEANRlnAENEKDSRRRQARLQKELAEAAKEPLP 233
Cdd:COG1196  355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL--EEAEEALLERLERLEEELEELEEALAE 432

                        170       180
                 ....*....|....*....|
gi 564369545 234 VEQDDDIEVIVDETSDHTEE 253
Cdd:COG1196  433 LEEEEEEEEEALEEAAEEEA 452
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 79-230 7.71e-08

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: 53.78  E-value: 7.71e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545  79 DSQLQEMAQLKMKHQEELTELHKKRGELAQLVIDLNNQMQQKDKEIQTNEAKIAECLQTISDLEAdcldlrtKLQdlEVA 158
Cdd:COG1579   16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE-------QLG--NVR 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564369545 159 NQtlkDEYDALQITFTALEEKLRKTTEENQELVTRwmAEKAQ----EANRLNAENEKDSRRRQARLQKELAEAAKE 230
Cdd:COG1579   87 NN---KEYEALQKEIESLKRRISDLEDEILELMER--IEELEeelaELEAELAELEAELEEKKAELDEELAELEAE 157
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 332-366 9.92e-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: 9.92e-08
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 564369545   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 1.72e-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: 47.69  E-value: 1.72e-07
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 564369545   415 RLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWD 452
Cdd:smart00320   3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
93-238 2.01e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 54.00  E-value: 2.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545  93 QEELTELHKKRGELAQLVIDlnnQMQQKDKEIQTNEAKIAECLQTISDLEAdcldLRTKLQDLEVANQTLKDEYDAL--Q 170
Cdd:COG4717   52 EKEADELFKPQGRKPELNLK---ELKELEEELKEAEEKEEEYAELQEELEE----LEEELEELEAELEELREELEKLekL 124

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564369545 171 ITFTALEEKLRKTTEENQELVTRWMAEKAQEANRLNAENEKDSRRRQ-ARLQKELAEAAKEPLPVEQDD 238
Cdd:COG4717  125 LQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAElAELQEELEELLEQLSLATEEE 193
WD40 pfam00400
WD domain, G-beta repeat;
332-366 2.58e-07

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 47.34  E-value: 2.58e-07
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 564369545  332 YVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWE 366
Cdd:pfam00400   5 KTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 80-284 4.75e-07

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 52.46  E-value: 4.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545  80 SQLQEMAQLKMKHQEELTELHKKRGELAQLVIDLNNQMQQKDKEIQTNEAKIAECLQTISDLEA---------------- 143
Cdd:COG4942   41 KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEelaellralyrlgrqp 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545 144 ---------DCLDLRTKLQDLEVANQTLKDEYDALQITFTALEEKLRKTTEENQELVTRwMAEKAQEANRLNAEnEKDSR 214
Cdd:COG4942  121 plalllspeDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL-LAELEEERAALEAL-KAERQ 198

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564369545 215 RRQARLQKELAEAAKEPLPVEQDDD-----IEVIVDETSDHTEETSPVRAIsrAATKRLSQPAGGlldSITNIFG 284
Cdd:COG4942  199 KLLARLEKELAELAAELAELQQEAEelealIARLEAEAAAAAERTPAAGFA--ALKGKLPWPVSG---RVVRRFG 268
WD40 pfam00400
WD domain, G-beta repeat;
415-452 4.83e-07

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 46.57  E-value: 4.83e-07
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 564369545  415 RLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWD 452
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 114-266 7.98e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 52.37  E-value: 7.98e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545   114 NNQMQQKDKEIQTNEAKIAECLQTISDLEADCLDLRTKLQDLEVANQTLKDEYDALQITFTALEEKLRKTTEEnQELVTR 193
Cdd:TIGR02168  669 NSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE-VEQLEE 747

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564369545   194 WMAEKAQEANRLNAE-NEKDSRRRQARLQKELAEAAKEPLPVEQDDDIEVIVDETSDHTEETSPVRAISRAATK 266
Cdd:TIGR02168  748 RIAQLSKELTELEAEiEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAAN 821
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
374-582 1.12e-06

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


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 50.08  E-value: 1.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545 374 FKGSLSGSNAGITSIEFDSAGAYLLAASNDFASRIWTVDDYRLRHTLTGHSGKVLSAKFLLDNARI-VSGSHDRTLKLWD 452
Cdd:COG3391   17 ALAALAVAVAALGLGGGGPLLAAASGGVVGAAVGGGGVALLAGLGLGAAAVADADGADAGADGRRLyVANSGSGRVSVID 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545 453 LRSKVCIKTVFAGSSCNDIVCTE---QCVMSGHFDKKIRFWDIRSESVVREMELLGKITALDLNPERTELLSCSRDD--- 526
Cdd:COG3391   97 LATGKVVATIPVGGGPRGLAVDPdggRLYVADSGNGRVSVIDTATGKVVATIPVGAGPHGIAVDPDGKRLYVANSGSntv 176

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564369545 527 --LLKIIDLRTNAIKQSFSApgfkcGSDWTRVVFSPDGS--YVA------AGSADGSLYVWSVLTG 582
Cdd:COG3391  177 svIVSVIDTATGKVVATIPV-----GGGPVGVAVSPDGRrlYVAnrgsntSNGGSNTVSVIDLATL 237
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 86-230 1.48e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.60  E-value: 1.48e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545    86 AQLKMKhQEELTELHKKRGELAQLVID-------LNNQMQQKDKEIQTNEAKIAECLQTISDLEADCLDLRTKLQDLEVA 158
Cdd:TIGR02168  260 AELQEL-EEKLEELRLEVSELEEEIEElqkelyaLANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEE 338

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564369545   159 NQTLKDEYDALQITFTALEEKLRKTTEENQELVTRWmAEKAQEANRLNAEnEKDSRRRQARLQKELAEAAKE 230
Cdd:TIGR02168  339 LAELEEKLEELKEELESLEAELEELEAELEELESRL-EELEEQLETLRSK-VAQLELQIASLNNEIERLEAR 408
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 83-230 2.66e-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: 2.66e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545    83 QEMAQLkmkhQEELTELHKKRGELAQLVIDLNNQMQQKDKEIQTNEAKIAEclqtisdLEADCLDLRTKLQDLEVANQTL 162
Cdd:TIGR02168  747 ERIAQL----SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ-------LKEELKALREALDELRAELTLL 815

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564369545   163 KDEYDALQITFTALEEKLRKTTEENQELVTRWmAEKAQEANRLNAENEkDSRRRQARLQKELAEAAKE 230
Cdd:TIGR02168  816 NEEAANLRERLESLERRIAATERRLEDLEEQI-EELSEDIESLAAEIE-ELEELIEELESELEALLNE 881
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 83-226 2.99e-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: 50.40  E-value: 2.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545   83 QEMAQLKMKHQEELTELHKKRGELAQ---LVIDLNNQMQQ--------------------------KDKEIQTNEAKIAE 133
Cdd:TIGR04523 253 TQLNQLKDEQNKIKKQLSEKQKELEQnnkKIKELEKQLNQlkseisdlnnqkeqdwnkelkselknQEKKLEEIQNQISQ 332

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545  134 CLQTISDLEADCLDLRTKLQDLEVANQTLKDEydalqitftaLEEK---LRKTTEENQelvtrwmaEKAQEANRLnaENE 210
Cdd:TIGR04523 333 NNKIISQLNEQISQLKKELTNSESENSEKQRE----------LEEKqneIEKLKKENQ--------SYKQEIKNL--ESQ 392

                         170
                  ....*....|....*.
gi 564369545  211 KDSRRRQARLQKELAE 226
Cdd:TIGR04523 393 INDLESKIQNQEKLNQ 408
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 341-577 3.43e-06

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 50.09  E-value: 3.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545 341 VNAVQFSPGSRLLATGGMDRRVKLWEAF-----GDKCEFKGSLSGSNAGITSIEFDSAGAYLLAASN-DFASRIWTVDDY 414
Cdd:PLN00181 486 VCAIGFDRDGEFFATAGVNKKIKIFECEsiikdGRDIHYPVVELASRSKLSGICWNSYIKSQVASSNfEGVVQVWDVARS 565

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545 415 RLRHTLTGHSGKVLSAKFL-LDNARIVSGSHDRTLKLWDLRSKVCIKTVfagSSCNDIVCTE------QCVMSGHFDKKI 487
Cdd:PLN00181 566 QLVTEMKEHEKRVWSIDYSsADPTLLASGSDDGSVKLWSINQGVSIGTI---KTKANICCVQfpsesgRSLAFGSADHKV 642

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545 488 RFWDIRSE-----SVVREMELLGKITALDlnpeRTELLSCSRDDLLKIIDLRTNA--IKQS--FSAPGFKCGSDWTRVVF 558
Cdd:PLN00181 643 YYYDLRNPklplcTMIGHSKTVSYVRFVD----SSTLVSSSTDNTLKLWDLSMSIsgINETplHSFMGHTNVKNFVGLSV 718

                        250
                 ....*....|....*....
gi 564369545 559 SpDGsYVAAGSADGSLYVW 577
Cdd:PLN00181 719 S-DG-YIATGSETNEVFVY 735
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
48-292 4.10e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.77  E-value: 4.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545  48 LHSVLTQKLQAEKHDVPNRHeispGHDGAWNDSQLQEMaqlkmkhQEELTELHKKRGELAQLVidlnNQMQQKDKEIQTN 127
Cdd:COG4717   43 IRAMLLERLEKEADELFKPQ----GRKPELNLKELKEL-------EEELKEAEEKEEEYAELQ----EELEELEEELEEL 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545 128 EAKIAECLQTISDLEA--DCLDLRTKLQDLEVANQTLKDEYDALQITFTALEEKLRKTTEENQELvTRWMAEKAQEANRL 205
Cdd:COG4717  108 EAELEELREELEKLEKllQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAEL-AELQEELEELLEQL 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545 206 NAENE---KDSRRRQARLQKELAEAAKEPLPVEQD-DDIEVIVDETSDHTEETSPVRAISRAATKRLSQPAGGLLDSITN 281
Cdd:COG4717  187 SLATEeelQDLAEELEELQQRLAELEEELEEAQEElEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGG 266

                        250
                 ....*....|.
gi 564369545 282 IFGLSESPLLG 292
Cdd:COG4717  267 SLLSLILTIAG 277
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 83-221 4.42e-06

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 50.17  E-value: 4.42e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545    83 QEMAQLKMKHQEELTELHKKRGELAQLVIDLNNQMQQKDKEIQTNEAKIAE-------CLQTISDLEADCLDLRTKLQD- 154
Cdd:pfam01576  204 QELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEetaqknnALKKIRELEAQISELQEDLESe 283

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564369545   155 ------LEVANQTLKDEYDALQitfTALEEKLrKTTEENQELVTRwmaeKAQEANRLNAENEKDSRRRQARLQ 221
Cdd:pfam01576  284 raarnkAEKQRRDLGEELEALK---TELEDTL-DTTAAQQELRSK----REQEVTELKKALEEETRSHEAQLQ 348
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 83-230 5.37e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.55  E-value: 5.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545  83 QEMAQLKMKH-QEELTELHKKRGELAQLVIDLNNQMQQKDKEIQTNEAKIAECLQTISDLEADCLDLRTKLQDLEVANQT 161
Cdd:COG1196  227 AELLLLKLRElEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIAR 306

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564369545 162 LKDEYDALQITFTALEEKLRKTTEENQELVTR---WMAEKAQEANRLNAENEKDSRRRQARLQKELAEAAKE 230
Cdd:COG1196  307 LEERRRELEERLEELEEELAELEEELEELEEEleeLEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 80-226 6.21e-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: 49.25  E-value: 6.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545   80 SQLQEMAQLKMKHQEELTELHKKRGELAQLVIDLNNQMQQKDKEIQTNEAKIAECLQTISDLEADCLDLRTKLQDLEVAN 159
Cdd:TIGR04523 370 NEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQD 449

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564369545  160 QTLKDEYDALQITFTALEEKLR------KTTEENQELVTRWMAEKAQEANRLNAENeKDSRRRQARLQKELAE 226
Cdd:TIGR04523 450 SVKELIIKNLDNTRESLETQLKvlsrsiNKIKQNLEQKQKELKSKEKELKKLNEEK-KELEEKVKDLTKKISS 521
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 31-249 8.35e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 49.30  E-value: 8.35e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545    31 AFEEIILQYTKLLEKSDLHSVLTQKLQAEKHDV----------PNRHEISPGhdgawnDSQLQEMAQLKMKHQEELTELH 100
Cdd:TIGR02169  191 LIIDEKRQQLERLRREREKAERYQALLKEKREYegyellkekeALERQKEAI------ERQLASLEEELEKLTEEISELE 264

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545   101 KKRGELAQLVIDLNNQMQQK-DKEIQTNEAKIAECLQTISDLEADCLDLRTKLQDLEVANQTLKDEYDALQITFTALEEK 179
Cdd:TIGR02169  265 KRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELERE 344

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564369545   180 LR-------KTTEENQELVTRwMAEKAQEANRLNAENeKDSRRRQARLQKELAEAAKE--PLPVEQDDDIEVIVDETSD 249
Cdd:TIGR02169  345 IEeerkrrdKLTEEYAELKEE-LEDLRAELEEVDKEF-AETRDELKDYREKLEKLKREinELKRELDRLQEELQRLSEE 421
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 81-237 1.37e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 48.51  E-value: 1.37e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545    81 QLQEMAQLKMKHQEELTELHKKRGEL--------------AQLVIDLNNQMQQKDKEIQTNEAKIAECLQTISDLEADCL 146
Cdd:TIGR02168  324 QLEELESKLDELAEELAELEEKLEELkeelesleaeleelEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIE 403

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545   147 DLRTKLQDLEVANQTLKDEydalqitftaLEEKLRKTTEENQELVTRWMAEKAQEANRLNAENEkDSRRRQARLQKELAE 226
Cdd:TIGR02168  404 RLEARLERLEDRRERLQQE----------IEELLKKLEEAELKELQAELEELEEELEELQEELE-RLEEALEELREELEE 472

                          170
                   ....*....|.
gi 564369545   227 AAKEPLPVEQD 237
Cdd:TIGR02168  473 AEQALDAAERE 483
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 564369545 337 HDGEVNAVQFSPGS-RLLATGGMDRRVKLWEAfgDKCEFKGSLSgSNAGITSIEFDSAGAYLLAasndFASRIWTVDDYR 415
Cdd:PLN00181 574 HEKRVWSIDYSSADpTLLASGSDDGSVKLWSI--NQGVSIGTIK-TKANICCVQFPSESGRSLA----FGSADHKVYYYD 646

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 564369545 416 LRH------TLTGHSGKVLSAKFLlDNARIVSGSHDRTLKLWDL 453
Cdd:PLN00181 647 LRNpklplcTMIGHSKTVSYVRFV-DSSTLVSSSTDNTLKLWDL 689
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
79-253 1.89e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.99  E-value: 1.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545   79 DSQLQEMAQLKMKHQEELTELHKKRGELAQLVIDLNNQMQQKD-KEIQTNEAKIAECLQTISDLEADCLDLRTKLQDLEV 157
Cdd:COG4913   294 EAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGL 373

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545  158 ANQTLKDEYDALQITFTALEEKLRKTTEENQELVTRWMAEKaqeanrlnaeneKDSRRRQARLQKELA--EAAKEPLPVE 235
Cdd:COG4913   374 PLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAAL------------RDLRRELRELEAEIAslERRKSNIPAR 441

                         170
                  ....*....|....*...
gi 564369545  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 2.67e-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: 47.32  E-value: 2.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545   83 QEMAQLKMKHQEELTELHKKRGELAQLVIDLNNQMQQKD-----KEIQTNEAKIAECLQTISDLEADCLDLRTKLQDLEV 157
Cdd:TIGR04523 517 KKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKkenleKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEK 596

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545  158 ANQTLKDEYDALQITFTALEEKLRKTTEENQELvtrwmaekaqEANRLNAENEKDSRRRQARLQKELAEAAKEPLP--VE 235
Cdd:TIGR04523 597 EKKDLIKEIEEKEKKISSLEKELEKAKKENEKL----------SSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPeiIK 666

                         170
                  ....*....|....*..
gi 564369545  236 QDDDIEVIVDETSDHTE 252
Cdd:TIGR04523 667 KIKESKTKIDDIIELMK 683
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 84-232 3.52e-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: 3.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545  84 EMAQLKMKHQEELTELHKKRGELAQL---VIDLNNQMQQKDKEIQTNEAKIAECLQTISDLEADCLDLRTKLQDLEVANQ 160
Cdd:COG1196  268 ELEELRLELEELELELEEAQAEEYELlaeLARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELE 347

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545 161 TLKDEYDALQITFTALEEKLRKTTEENQELVTRWMAEKAQEANRLNAENEK------------DSRRRQARLQKELAE-- 226
Cdd:COG1196  348 EAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELaaqleeleeaeeALLERLERLEEELEEle 427

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 564369545 227 --------------------------------AAKEPL 232
Cdd:COG1196  428 ealaeleeeeeeeeealeeaaeeeaeleeeeeALLELL 465
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 81-238 4.30e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.98  E-value: 4.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545    81 QLQEMAQLKMKHQEELTELHKKRGELAQLVIDLNNQMQQKDKEIQTNEAKIAECLQTISDLEADCLDLRTKLQDLEVANQ 160
Cdd:TIGR02169  675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIE 754

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545   161 TLKDEYDALQITFTALEEKLRKTTEENQELVTRWMAEKAQEANRLNAENEKDSRRRQARLQ------------KELAEAA 228
Cdd:TIGR02169  755 NVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLReieqklnrltleKEYLEKE 834

                          170
                   ....*....|
gi 564369545   229 KEPLPVEQDD 238
Cdd:TIGR02169  835 IQELQEQRID 844
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 78-253 6.01e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.20  E-value: 6.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545    78 NDSQLQEmaqLKMKHQEELTELHKKRGELAQL---VIDLNNQMQQKDKEIQTNEAKIAECLQTISDLEADCLDLRTKLQD 154
Cdd:TIGR02168  801 LREALDE---LRAELTLLNEEAANLRERLESLerrIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEA 877

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545   155 L-------EVANQTLKDEYDALQITFTALEEKLRKTTEENQELvtrwMAEKAQEANRLN-AENEKDSRRRQARLQKELAE 226
Cdd:TIGR02168  878 LlneraslEEALALLRSELEELSEELRELESKRSELRRELEEL----REKLAQLELRLEgLEVRIDNLQERLSEEYSLTL 953

                          170       180
                   ....*....|....*....|....*..
gi 564369545   227 AAKEPLPVEQDDDIEVIVDETSDHTEE 253
Cdd:TIGR02168  954 EEAEALENKIEDDEEEARRRLKRLENK 980
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 101-270 8.60e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 45.14  E-value: 8.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545 101 KKRGELAQLVIDLNNQMQQKDKEIQTNEAKIAECLQTISDLEADCLDLRTKLQDLEVANQTLKDEYDALQITFTALEEKL 180
Cdd:COG4942   20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545 181 RKTTEENQELVTRW--MAEKAQEANRLNAENEKDSRRRQARLQ------KELAEAAKeplpvEQDDDIEVIVDETSDHTE 252
Cdd:COG4942  100 EAQKEELAELLRALyrLGRQPPLALLLSPEDFLDAVRRLQYLKylaparREQAEELR-----ADLAELAALRAELEAERA 174

                        170
                 ....*....|....*...
gi 564369545 253 ETSPVRAISRAATKRLSQ 270
Cdd:COG4942  175 ELEALLAELEEERAALEA 192
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 54-211 9.97e-05

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 45.81  E-value: 9.97e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545    54 QKLQAEKHDVPNRHE-ISPGHDGAWNDSQLQEMAQLKMKHQEELTELHKKRGELAQLVIDLNNQ---MQQKDKEIQTNEA 129
Cdd:TIGR00606  795 ERFQMELKDVERKIAqQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQiqhLKSKTNELKSEKL 874

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545   130 KIAECLQTISDLEADCLDLRTKLQDLEVANQTLKDEydalqitFTALEEKLRKTTEENQELVTRWMAEKAQEANRLNAEN 209
Cdd:TIGR00606  875 QIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQ-------DSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIK 947


                   ..
gi 564369545   210 EK 211
Cdd:TIGR00606  948 EK 949
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 43-215 1.24e-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: 1.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545    43 LEKSDLHSVLtQKLQAEKHDVPNRHeispghdgAWNDSQLQEMAQLKMKHQEELTELHKKRGELAQLVIDLNNQMQQKDK 122
Cdd:TIGR02169  784 LEARLSHSRI-PEIQAELSKLEEEV--------SRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEK 854

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545   123 EIQTNEAKIAECLQTISDLEADCLDLRTKLQDLEVANQTLKDEYDALQITFTALEEKLRKTTEENQELvtrwmAEKAQEA 202
Cdd:TIGR02169  855 EIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSEL-----KAKLEAL 929

                          170
                   ....*....|...
gi 564369545   203 NRLNAENEKDSRR 215
Cdd:TIGR02169  930 EEELSEIEDPKGE 942
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
46-230 1.81e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 44.65  E-value: 1.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545  46 SDLHSVLTQKLQAEKHDVPNRHEispghdgawndsqlQEMAQLK--MKHQEELTELHKKRGELAQLVIDLNNQMQQkdkE 123
Cdd:PRK02224 190 DQLKAQIEEKEEKDLHERLNGLE--------------SELAELDeeIERYEEQREQARETRDEADEVLEEHEERRE---E 252

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545 124 IQTNEAKIAECLQTISDLEADCLDLRTKLQDLEVANQTLKDEYDAL--QITFTALE----EKLRKTTEENQELVTRWMAE 197
Cdd:PRK02224 253 LETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLlaEAGLDDADaeavEARREELEDRDEELRDRLEE 332

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 564369545 198 KAQEANRLN------AENEKDSRRRQARLQKELAEAAKE 230
Cdd:PRK02224 333 CRVAAQAHNeeaeslREDADDLEERAEELREEAAELESE 371
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 76-321 2.09e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.05  E-value: 2.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545  76 AWNDSQLQEMAQLKMKHQEELTELHKKRGELAQLVIDLNNQMQQKDKEIQTNEAKIAECLQTISDLEADCLDLRTKLQD- 154
Cdd:COG3883   12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEr 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545 155 -------------LEV----------------------ANQTLKDEYDALQITFTALEEKLRKTTEENQELVTRwMAEKA 199
Cdd:COG3883   92 aralyrsggsvsyLDVllgsesfsdfldrlsalskiadADADLLEELKADKAELEAKKAELEAKLAELEALKAE-LEAAK 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545 200 QEANRLNAENEK-------DSRRRQARLQKELAEAAKEPLPVEQDDDIEVIVDETSDHTEETSPVRAISRAATKRLSQPA 272
Cdd:COG3883  171 AELEAQQAEQEAllaqlsaEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAG 250

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 564369545 273 GGLLDSITNIFGLSESPLLGHHSSDAARRRSVSSIPVPQDVVDTHPASG 321
Cdd:COG3883  251 AAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAA 299
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 42-232 2.65e-04

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


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 43.73  E-value: 2.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545   42 LLEKSDLHsvltQKLQAEKHDVPNRHEISPGHDGAWnDSQLQEMAQLKMKHQEELTELHKKRGELAQLVIDLNNQMQQKD 121
Cdd:pfam07888  40 LQERAELL----QAQEAANRQREKEKERYKRDREQW-ERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELS 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545  122 KEIQTNEAKIAECLQTISDLEADCLDLRTKLQDLEVANQTLKD--------------EYDALQITFTALEEKLRKTTEEN 187
Cdd:pfam07888 115 EEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKErakkagaqrkeeeaERKQLQAKLQQTEEELRSLSKEF 194

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 564369545  188 QELvTRWMAEKAQEANRLNAENEKDSRRRQARLQKELA-EAAKEPL 232
Cdd:pfam07888 195 QEL-RNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAEnEALLEEL 239
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
93-270 2.67e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.14  E-value: 2.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545   93 QEELTELHKKRGELAQLVIDLNNQMQQKDKEIQTNEAKiAECLQTISDLEADCLDLRTKLQDLEVANQTLkDEYDALQIT 172
Cdd:COG4913   609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQER-REALQRLAEYSWDEIDVASAEREIAELEAEL-ERLDASSDD 686

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545  173 FTALEEKLRKTTEENQELVTRWmaEKAQEANRLNAENEKDSRRRQARLQKELAEAAKEPLPVEQDDdieviVDETSDHTE 252
Cdd:COG4913   687 LAALEEQLEELEAELEELEEEL--DELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL-----LEERFAAAL 759

                         170
                  ....*....|....*...
gi 564369545  253 ETSPVRAISRAATKRLSQ 270
Cdd:COG4913   760 GDAVERELRENLEERIDA 777
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
81-230 2.81e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.14  E-value: 2.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545   81 QLQEMAQLKMKHQEELTELHKKRGELAQLVID--------LNNQMQQKDKEIQTNEAKIAECLQTISDLEADCLDLR--- 149
Cdd:COG4913   253 LLEPIRELAERYAAARERLAELEYLRAALRLWfaqrrlelLEAELEELRAELARLEAELERLEARLDALREELDELEaqi 332

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545  150 ------------TKLQDLEVANQTLKDEYDALQITFTALEEKLRKTTEENQELVTRWMAEKAQEANRLNAENEK--DSRR 215
Cdd:COG4913   333 rgnggdrleqleREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEAlaEAEA 412

                         170
                  ....*....|....*
gi 564369545  216 RQARLQKELAEAAKE 230
Cdd:COG4913   413 ALRDLRRELRELEAE 427
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 554-578 3.17e-04

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: 38.45  E-value: 3.17e-04
                           10        20
                   ....*....|....*....|....*
gi 564369545   554 TRVVFSPDGSYVAAGSADGSLYVWS 578
Cdd:smart00320  16 TSVAFSPDGKYLASGSDDGTIKLWD 40
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 80-227 4.02e-04

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: 43.58  E-value: 4.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545   80 SQLQ-EMAQLKMKHQEELTELHKKRGELAQLV---IDLNNQMQQKDKEIQTNEAKIAECLQ--------TISDLEADCLD 147
Cdd:pfam05557  12 SQLQnEKKQMELEHKRARIELEKKASALKRQLdreSDRNQELQKRIRLLEKREAEAEEALReqaelnrlKKKYLEALNKK 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545  148 LRTKLQDLEVANQT---LKDEYDALQITFTALEEKLRKTTEENQELVTR--WMAEKAQEANRLNAENEKDsrrrqarlQK 222
Cdd:pfam05557  92 LNEKESQLADAREViscLKNELSELRRQIQRAELELQSTNSELEELQERldLLKAKASEAEQLRQNLEKQ--------QS 163


                  ....*
gi 564369545  223 ELAEA 227
Cdd:pfam05557 164 SLAEA 168
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 80-230 4.05e-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: 43.52  E-value: 4.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545    80 SQLQEMAQLKMKHQEELTELHKKRGELAQLVIDLNNQMQQKDKEIQTNEAKIAECLQTISDLEADclDLRTKLQDLEVAN 159
Cdd:TIGR02169  723 KEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEAR--LSHSRIPEIQAEL 800

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564369545   160 QTLKDEYDALQITFTALEEKLRKTTEENQELvtRWMAEKAQEANRLNAENEKDSRRRQARLQKELAEAAKE 230
Cdd:TIGR02169  801 SKLEEEVSRIEARLREIEQKLNRLTLEKEYL--EKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE 869
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 79-270 4.17e-04

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 43.29  E-value: 4.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545  79 DSQLQEMAQLK------------MKHQEELTELHKKRGELAQLVIDLNN--------------QMQQK---------DKE 123
Cdd:PRK04778 178 EEEFSQFVELTesgdyveareilDQLEEELAALEQIMEEIPELLKELQTelpdqlqelkagyrELVEEgyhldhldiEKE 257

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545 124 IQTNEAKIAECLQTISDLEadcldlrtkLQDLEVANQTLKDEYDALQITFTAlEEKLRKTTEENQELVTRwMAEKAQEAN 203
Cdd:PRK04778 258 IQDLKEQIDENLALLEELD---------LDEAEEKNEEIQERIDQLYDILER-EVKARKYVEKNSDTLPD-FLEHAKEQN 326

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564369545 204 R-LNAE----------NEKDSRRRQArLQKELAEAakeplpveqDDDIEVIVDETSDHTEETSPVRAISRAATKRLSQ 270
Cdd:PRK04778 327 KeLKEEidrvkqsytlNESELESVRQ-LEKQLESL---------EKQYDEITERIAEQEIAYSELQEELEEILKQLEE 394
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 79-189 4.19e-04

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 43.47  E-value: 4.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545   79 DSQLQEMAQLKMKHQEELTELHKKRGELAQLVIDLNNQMQQKDKEIQTNEAKIAECLQTISDLEADCLDLRTKLQDLEVA 158
Cdd:TIGR04523 327 QNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKL 406

                          90       100       110
                  ....*....|....*....|....*....|....
gi 564369545  159 NQTLKDEYDALQITFTALE---EKLRKTTEENQE 189
Cdd:TIGR04523 407 NQQKDEQIKKLQQEKELLEkeiERLKETIIKNNS 440
COG4946 COG4946
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown] ...
 557-623 4.33e-04

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


Pssm-ID: 443973 [Multi-domain]  Cd Length: 1072  Bit Score: 43.49  E-value: 4.33e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564369545  557 VFSPDGSYVAAGSADGSLYVWSVLTGKVEKVLSKQHSSSINAVAWAPsglhvvsvDkgSRAVLWAQP 623
Cdd:COG4946   395 VWSPDGKKIAFTDNRGRLWVVDLASGKVRKVDTDGYGDGISDLAWSP--------D--SKWLAYSKP 451
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 39-170 4.81e-04

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


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 42.70  E-value: 4.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545    39 YTKLLEKSDLHSVLTQKLQAEKHDVPNRHEISPGHDGAWNDSQLQEMAQLKMKHQEELTELHKKRGELAQLvidlNNQMQ 118
Cdd:smart00787 160 YKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRAKEKLKKLLQEIMIKVKKLEEL----EEELQ 235

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 564369545   119 QKDKEIQTNEAKIAECLQTISDLEADCLDLRtKLQDLEVAnqTLKDEYDALQ 170
Cdd:smart00787 236 ELESKIEDLTNKKSELNTEIAEAEKKLEQCR-GFTFKEIE--KLKEQLKLLQ 284
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 79-230 5.01e-04

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 43.09  E-value: 5.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545   79 DSQLQEMAQLKMKHQEELTELHKKRGELAQLVID---LNNQMQQKDKEIQTNEAKIAECLQTISDLEADCLDLRTKLQDL 155
Cdd:TIGR04523 464 ESLETQLKVLSRSINKIKQNLEQKQKELKSKEKElkkLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDL 543

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545  156 E---------VANQTLKDEYDALQITFTALEE---KLRKTTEENQELVtrwmAEKAQEANRLNAENEKDSrRRQARLQKE 223
Cdd:TIGR04523 544 EdelnkddfeLKKENLEKEIDEKNKEIEELKQtqkSLKKKQEEKQELI----DQKEKEKKDLIKEIEEKE-KKISSLEKE 618


                  ....*..
gi 564369545  224 LAEAAKE 230
Cdd:TIGR04523 619 LEKAKKE 625
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
80-262 5.29e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.58  E-value: 5.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545  80 SQLQEMAQLKMKHQEELTELHKKRGELAQLVIDLNNQMQQKDKEIQTNEAKIAECLQTISDLEADCLDLRTKLQDLEVAN 159
Cdd:COG4372   87 EQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEEL 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545 160 QTLKDEYDALQITFTALEEKLRKTTEENQELVTRWMAEKAQEANRLNAENEKDSRRRQARLQKELAEAAKEPLPVEQDDD 239
Cdd:COG4372  167 AALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEE 246

                        170       180
                 ....*....|....*....|...
gi 564369545 240 IEVIVDETSDHTEETSPVRAISR 262
Cdd:COG4372  247 DKEELLEEVILKEIEELELAILV 269
WD40 pfam00400
WD domain, G-beta repeat;
554-578 5.85e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 37.71  E-value: 5.85e-04
                          10        20
                  ....*....|....*....|....*
gi 564369545  554 TRVVFSPDGSYVAAGSADGSLYVWS 578
Cdd:pfam00400  15 TSLAFSPDGKLLASGSDDGTVKVWD 39
PTZ00420 PTZ00420
coronin; Provisional
 385-542 6.13e-04

coronin; Provisional


Pssm-ID: 240412 [Multi-domain]  Cd Length: 568  Bit Score: 42.63  E-value: 6.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545 385 ITSIEFDSAGaylLAASNDFASRIWTVDD------YRLRHT--------LTGHSGKVLSAKFLLDNARIV-SGSHDRTLK 449
Cdd:PTZ00420  24 ICSRVIDSCG---IACSSGFVAVPWEVEGggligaIRLENQmrkppvikLKGHTSSILDLQFNPCFSEILaSGSEDLTIR 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545 450 LWDLRSKvciktvfaGSSCNDIVcTEQCVMSGH---------------------FDKKIRFWDIRSESVVREMELLGKIT 508
Cdd:PTZ00420 101 VWEIPHN--------DESVKEIK-DPQCILKGHkkkisiidwnpmnyyimcssgFDSFVNIWDIENEKRAFQINMPKKLS 171

                        170       180       190
                 ....*....|....*....|....*....|....
gi 564369545 509 ALDLNPERTELLSCSRDDLLKIIDLRTNAIKQSF 542
Cdd:PTZ00420 172 SLKWNIKGNLLSGTCVGKHMHIIDPRKQEIASSF 205
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 86-270 7.57e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.06  E-value: 7.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545  86 AQLKMKHQEELTELHKKRGELAQLVIDLNNQMQQKDKEIQTNEAKIAECLQTISDLEADCLDLRTKLQDLEVANQTLKDE 165
Cdd:COG4942   19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545 166 YDALQitfTALEEKLRK--TTEENQELVTRWMAEKAQEANR----LNAENEKDsRRRQARLQKELAE-AAKEPLPVEQDD 238
Cdd:COG4942   99 LEAQK---EELAELLRAlyRLGRQPPLALLLSPEDFLDAVRrlqyLKYLAPAR-REQAEELRADLAElAALRAELEAERA 174

                        170       180       190
                 ....*....|....*....|....*....|..
gi 564369545 239 DIEVIVDETSDHTEETSPVRAISRAATKRLSQ 270
Cdd:COG4942  175 ELEALLAELEEERAALEALKAERQKLLARLEK 206
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
93-243 8.18e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.20  E-value: 8.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545  93 QEELTELHKKRGELAQLvidlNNQMQQKDKEIQTNEAKIAECLQTISDLEADCLDLRTKLQDLEVANQTLKDEYDALQIT 172
Cdd:COG4372   34 RKALFELDKLQEELEQL----REELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEE 109

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564369545 173 FTALEEKLRKTTEENQELVTRWMAEKAQEANRLNAENEKDSR-----RRQARLQKELAEAAKEPLPVEQDDDIEVI 243
Cdd:COG4372  110 AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEElkeleEQLESLQEELAALEQELQALSEAEAEQAL 185
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
81-188 9.07e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 9.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545  81 QLQEMAQLKMKHQEELTELHKKRGELAQLV---------IDLNNQMQQKDKEIQTNEAKIAECLQTISDLEADCL--DLR 149
Cdd:COG4717  396 EYQELKEELEELEEQLEELLGELEELLEALdeeeleeelEELEEELEELEEELEELREELAELEAELEQLEEDGElaELL 475

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 564369545 150 TKLQDLEVANQTLKDEYDALQITFTALEEKLRKTTEENQ 188
Cdd:COG4717  476 QELEELKAELRELAEEWAALKLALELLEEAREEYREERL 514
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 80-230 9.13e-04

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 42.31  E-value: 9.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545   80 SQLQEMAQLKMKHQEELT-ELHKKRGELAQLV---IDLNNQMQQKDKEIQTNEAKiaeclqtISDLEADCLDLRTKLQDL 155
Cdd:TIGR04523 228 NQLKDNIEKKQQEINEKTtEISNTQTQLNQLKdeqNKIKKQLSEKQKELEQNNKK-------IKELEKQLNQLKSEISDL 300

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545  156 -----EVANQTLKDEYDALQITFTALEEKLRKTTEENQELvTRWMAEKAQEANRLNAENEKdsrrrqarLQKELAEAAKE 230
Cdd:TIGR04523 301 nnqkeQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQL-NEQISQLKKELTNSESENSE--------KQRELEEKQNE 371
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 79-212 1.64e-03

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


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 40.82  E-value: 1.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545  79 DSQLQEMAQLKMKHQEELTElhKKRGELAQLVIDLNNQMQqkdKEIQTNEAKIAECLQTISDLEADCLDLRTKLQDLEVA 158
Cdd:cd22656   90 DSYYAEILELIDDLADATDD--EELEEAKKTIKALLDDLL---KEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKA 164

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 564369545 159 NQTLKDEYDALqITFTALEEKLRKTTEENQELVTRwMAEKAQEANRLNAENEKD 212
Cdd:cd22656  165 LKDLLTDEGGA-IARKEIKDLQKELEKLNEEYAAK-LKAKIDELKALIADDEAK 216
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
83-230 2.05e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.16  E-value: 2.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545  83 QEMAQLKMKH-----QEELTELHKKRGELAQLVIDLNNQMQQKDKEIQTNEAKIAECLQTISDLEADCL--DLRTKLQDL 155
Cdd:COG3206  196 AALEEFRQKNglvdlSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPViqQLRAQLAEL 275

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564369545 156 EVanqtlkdEYDALQITFTALEEKLRKTTEENQELvtrwMAEKAQEANRL--NAENEKDS-RRRQARLQKELAEAAKE 230
Cdd:COG3206  276 EA-------ELAELSARYTPNHPDVIALRAQIAAL----RAQLQQEAQRIlaSLEAELEAlQAREASLQAQLAQLEAR 342
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 331-366 2.23e-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: 2.23e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 564369545 331 SYVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWE 366
Cdd:cd00200  254 VQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
82-238 2.27e-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: 2.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545   82 LQEMAQLkMKHQEELTELHKKRGELAQLViDLNNQMQQKDKEIQTNEAkiaecLQTISDLEADcldlRTKLQDLEVANQT 161
Cdd:COG4913   231 VEHFDDL-ERAHEALEDAREQIELLEPIR-ELAERYAAARERLAELEY-----LRAALRLWFA----QRRLELLEAELEE 299

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545  162 LKDEYDALQITFTALEEKLRKTTEENQELVTRWMAEKAQEANRL-----NAENEKDSRRRQARLQKELAEAAKEPLPVEQ 236
Cdd:COG4913   300 LRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLereieRLERELEERERRRARLEALLAALGLPLPASA 379


                  ..
gi 564369545  237 DD 238
Cdd:COG4913   380 EE 381
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 79-193 2.33e-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: 41.21  E-value: 2.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545    79 DSQLQEMAQLKMKHQEELTELHKKRGELAQLVIDLNNQMQQKDKEIQTNEAKIAE-------------CLQTISDLEADC 145
Cdd:TIGR02169  881 ESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEiedpkgedeeipeEELSLEDVQAEL 960

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 564369545   146 LDLRTKLQDLEVANQTLKDEYDALQITFTALEEKLRKTTEENQELVTR 193
Cdd:TIGR02169  961 QRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILER 1008
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
90-230 2.52e-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: 2.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545   90 MKHQEELTELHKKRGELAQLVIDLNN--QMQQKDKEIQTNEAKIAECLQTISDLEADCLDLRTKLQDLEVANQTLKDEYD 167
Cdd:COG4913   583 VKGNGTRHEKDDRRRIRSRYVLGFDNraKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEID 662

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564369545  168 --ALQITFTALEEKLRKTTEENQEL--VTRWMAEKAQEANRLNAEnEKDSRRRQARLQKELAEAAKE 230
Cdd:COG4913   663 vaSAEREIAELEAELERLDASSDDLaaLEEQLEELEAELEELEEE-LDELKGEIGRLEKELEQAEEE 728
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
79-253 2.92e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.27  E-value: 2.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545  79 DSQLQEMAQLKMKHQEELTELHKKRGELAQLVIDLNNQMQQKDKEIQTNEAKIAECLQTISDLEADCLDLRTKLQDLEVA 158
Cdd:COG4372   72 RSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEE 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545 159 NQTLKDEYDALQITFTALEEKLRKTTEENQElvtRWMAEKAQEANRlNAENEKDSRRRQARLQKELAEAAKEPLPVEQDD 238
Cdd:COG4372  152 LKELEEQLESLQEELAALEQELQALSEAEAE---QALDELLKEANR-NAEKEEELAEAEKLIESLPRELAEELLEAKDSL 227

                        170
                 ....*....|....*
gi 564369545 239 DIEVIVDETSDHTEE 253
Cdd:COG4372  228 EAKLGLALSALLDAL 242
TolB COG0823
Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, ...
 550-620 2.99e-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: 2.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545 550 GSDWTRV----------VFSPDGSYVA-AGSADGSLYVWSV-LTGKVEKVLSKqhssSINAVAWAPSGLHVV-SVDKGSR 616
Cdd:COG0823   64 GGEPRRLtfgggynaspSWSPDGKRLAfVSRSDGRFDIYVLdLDGGAPRRLTD----GPGSPSWSPDGRRIVfSSDRGGR 139


                 ....
gi 564369545 617 AVLW 620
Cdd:COG0823  140 PDLY 143
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 147-243 3.31e-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: 3.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545 147 DLRTKLQDLEVANQTLKDEYD-ALQITFTALEEKLRKTTEENQELVTRWMAEKA--QEANRLNAENEKDSRRRQArLQKE 223
Cdd:COG0542  415 ELERRLEQLEIEKEALKKEQDeASFERLAELRDELAELEEELEALKARWEAEKEliEEIQELKEELEQRYGKIPE-LEKE 493

                         90       100
                 ....*....|....*....|....*...
gi 564369545 224 LAEA-----AKEPLPVEQ--DDDI-EVI 243
Cdd:COG0542  494 LAELeeelaELAPLLREEvtEEDIaEVV 521
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
82-230 3.47e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 39.89  E-value: 3.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545  82 LQEMAQLKMKHQEELTELHKKRGELAqlviDLNNQMQQKDKEIQTNEAKIAECLQtisdlEADcldlrtklqdlevanqT 161
Cdd:COG1340  152 AKKALEKNEKLKELRAELKELRKEAE----EIHKKIKELAEEAQELHEEMIELYK-----EAD----------------E 206

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564369545 162 LKDEYDALQITFTALEEKLRKTTEENQELVTRwMAEKAQEANRLNAENEKDSRRRQARLQKELAEAAKE 230
Cdd:COG1340  207 LRKEADELHKEIVEAQEKADELHEEIIELQKE-LRELRKELKKLRKKQRALKREKEKEELEEKAEEIFE 274
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 87-208 3.61e-03

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


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 39.79  E-value: 3.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545   87 QLKMKHQEELTELHKKRGELAQL---VIDLNNQMQQKDKEIQTNEAKIAECLQTISDLEADCLDLR-------TKLQDLE 156
Cdd:pfam15905 181 GMEGKLQVTQKNLEHSKGKVAQLeekLVSTEKEKIEEKSETEKLLEYITELSCVSEQVEKYKLDIAqleellkEKNDEIE 260

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 564369545  157 VANQTLKDEYDALQITFTALEEKLRKTTEENQELVTRwmaEKAQEANrLNAE 208
Cdd:pfam15905 261 SLKQSLEEKEQELSKQIKDLNEKCKLLESEKEELLRE---YEEKEQT-LNAE 308
TolB COG0823
Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, ...
 530-609 3.64e-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: 38.50  E-value: 3.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545 530 IIDLRTNAIKQSFSAPGFKCGSDWtrvvfSPDGSYVAAGSADGS---LYVWSVLTGKVEKVLSKQHSSSinAVAWAPSGL 606
Cdd:COG0823   15 VVDLDGGEPRRLTNSPGIDTSPAW-----SPDGRRIAFTSDRGGgpqIYVVDADGGEPRRLTFGGGYNA--SPSWSPDGK 87


                 ...
gi 564369545 607 HVV 609
Cdd:COG0823   88 RLA 90
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 54-230 4.10e-03

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 40.42  E-value: 4.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545    54 QKLQAEKHDVPNRHEISpghdgawndsqlQEMAQLKMKH-QEELTELHKKRGELAQLVID-LNNQMQQKDKEIQTNEAKI 131
Cdd:TIGR00606  919 EKDQQEKEELISSKETS------------NKKAQDKVNDiKEKVKNIHGYMKDIENKIQDgKDDYLKQKETELNTVNAQL 986

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545   132 AECLQTISDLEAdclDLRTKLQDLEVANQT---LKDeydalQITFTALEEKLRKTTEE--------NQELVTRWMAE--K 198
Cdd:TIGR00606  987 EECEKHQEKINE---DMRLMRQDIDTQKIQerwLQD-----NLTLRKRENELKEVEEElkqhlkemGQMQVLQMKQEhqK 1058

                          170       180       190
                   ....*....|....*....|....*....|..
gi 564369545   199 AQEANRLNAENEKDSRRRQARLQKELAEAAKE 230
Cdd:TIGR00606 1059 LEENIDLIKRNHVLALGRQKGYEKEIKHFKKE 1090
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 80-187 4.30e-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: 40.00  E-value: 4.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545   80 SQLQEMAQLKMKHQEELTELHKKRGELAQLVIDLNNQMQQKDKEIQTNEAKIaecLQTISDLEADCLDLRTKLQDLEVAN 159
Cdd:TIGR04523 204 SNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQL---NQLKDEQNKIKKQLSEKQKELEQNN 280

                          90       100
                  ....*....|....*....|....*...
gi 564369545  160 QTLKDEYDALQITFTALEEkLRKTTEEN 187
Cdd:TIGR04523 281 KKIKELEKQLNQLKSEISD-LNNQKEQD 307
46 PHA02562
endonuclease subunit; Provisional
 79-244 5.10e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 40.00  E-value: 5.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545  79 DSQLQEMAQLKMKH---QEELTELHKKRGE-------LAQLVIDLNNQMQQKDKEIQ--TNEAKIAECLQTISDLEADCL 146
Cdd:PHA02562 223 DELVEEAKTIKAEIeelTDELLNLVMDIEDpsaalnkLNTAAAKIKSKIEQFQKVIKmyEKGGVCPTCTQQISEGPDRIT 302

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545 147 DLRTK-------LQDLEVANQTLK---DEYDALQITFTALEEKLRKtteENQELVT-RWMAEKAQEA-NRLNAENeKDSR 214
Cdd:PHA02562 303 KIKDKlkelqhsLEKLDTAIDELEeimDEFNEQSKKLLELKNKIST---NKQSLITlVDKAKKVKAAiEELQAEF-VDNA 378

                        170       180       190
                 ....*....|....*....|....*....|
gi 564369545 215 RRQARLQKELAEAAKEPLPVEQDDDIEVIV 244
Cdd:PHA02562 379 EELAKLQDELDKIVKTKSELVKEKYHRGIV 408
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 112-362 5.44e-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: 5.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545 112 DLNNQMQQKDKEIQTNEAKIAECLQTISDLEADCLDLRTKLQDLEVANQTLKDEYDALQitftaleeklrKTTEENQELV 191
Cdd:COG3883  116 DFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE-----------AQQAEQEALL 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545 192 TRWMAEKAQEANRLNAENEKDSRRRQARLQKELAEAAKEPLPVEQDDDIEVIVDETSDHTEETSPVRAISRAATKRLSQP 271
Cdd:COG3883  185 AQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGA 264

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545 272 AGGLLDSITNIFGLSESPLLGHHSSDAARRRSVSSIPVPQDVVDTHPASGKDVRVPTTASYVFDAHDGEVNAVQFSPGSR 351
Cdd:COG3883  265 AGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAVVGGASAGGGGGSGGGGGSSGGG 344

                        250
                 ....*....|.
gi 564369545 352 LLATGGMDRRV 362
Cdd:COG3883  345 SGGGGGGGGGG 355
PTZ00332 PTZ00332
paraflagellar rod protein; Provisional
 10-226 6.37e-03

paraflagellar rod protein; Provisional


Pssm-ID: 240364 [Multi-domain]  Cd Length: 589  Bit Score: 39.56  E-value: 6.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545  10 FPRWKRHIAE-ELRRRDRLQRQAFEEIILQYTKLLEKS----DLH---SVLTQKLQAEK-HDVPNRHeispghdgawnDS 80
Cdd:PTZ00332 341 FEEVKRRIEEnDREEKRRVEYQQFLEVAGQHKKLLELTvyncDLAlrcTGLVEELVSEGcAAVKARH-----------DK 409

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545  81 QLQEMAQLKMK-HQEELTELHKKRGELAQLVIDLNNQMQQKDKEIQTNEAKIAECLQTI-------SDLEADCLDLRtkl 152
Cdd:PTZ00332 410 TNQDLAALRLQvHKEHLEYFRMLYLTLGSLIYKKEKRLEEIDRNIRTTHIQLEFCVETFdpnakkhADMKKELYKLR--- 486

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545 153 QDLEVANQTLKDEYDALQITFTALEEKLRKT--------TEENQELVTRW--MAE-----KAQEANRLNAENEKDSRRRQ 217
Cdd:PTZ00332 487 QGVEEELAMLKEKQAQALEMFKESEEALDAAgiefvhpvDENNEEVLTRRskMVEyrshlAKQEEVKIAAEREEIKRARL 566


                 ....*....
gi 564369545 218 ARLQKELAE 226
Cdd:PTZ00332 567 LRSQGYRGE 575
Prefoldin_2 pfam01920
Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996.
 93-190 6.39e-03

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


Pssm-ID: 396482 [Multi-domain]  Cd Length: 102  Bit Score: 36.43  E-value: 6.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545   93 QEELTELHKKRGELAQlvidlnnqmQQKDKEIQTNEAKIAecLQTISDLEADcldlrTK----------LQDLEVANQTL 162
Cdd:pfam01920   1 INKFQQLQQQLQLLAQ---------QIKQLETQLKELELA--LEELELLDED-----TKvykligdvlvKQDKEEVKEQL 64

                          90       100
                  ....*....|....*....|....*...
gi 564369545  163 KDEYDALQITFTALEEKLRKTTEENQEL 190
Cdd:pfam01920  65 EERKETLEKEIKTLEKQLEKLEKELEEL 92
Ge1_WD40 pfam16529
WD40 region of Ge1, enhancer of mRNA-decapping protein; Ge1_WD40 is the N-terminal region of ...
 381-462 7.99e-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: 7.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545  381 SNAGITSIEFDSAGAYLLAASNDFASRIWTV-----DDYRLRHTLTGHSGKVLSAKFLLDNAR----------IVSGS-H 444
Cdd:pfam16529 185 EHSLLVDAAFSPDGTALATASLDGEVKFFQIylfdnRNPRCLHEWKPHDGKPLSSLFFLDNHKkppevqfwrfAITGAdN 264

                          90
                  ....*....|....*...
gi 564369545  445 DRTLKLWDLRSKVCIKTV 462
Cdd:pfam16529 265 NSELKLWSCESWTCLQTI 282
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
97-230 8.09e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.12  E-value: 8.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545  97 TELHKKRGELAQLVIDLNNQMQQKDKEIQTNeakiaecLQTISDLEADCLDLRTKLQDLEVANQTLKDEYDALQITFTAL 176
Cdd:COG4372    6 EKVGKARLSLFGLRPKTGILIAALSEQLRKA-------LFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQL 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 564369545 177 EEKLRKTTEENQELVTRwMAEKAQEANRLNAENEKdSRRRQARLQKELAEAAKE 230
Cdd:COG4372   79 EEELEELNEQLQAAQAE-LAQAQEELESLQEEAEE-LQEELEELQKERQDLEQQ 130
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 581-620 8.17e-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: 8.17e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 564369545   581 TGKVEKVLsKQHSSSINAVAWAPSGLHVVSVDKGSRAVLW 620
Cdd:smart00320   1 SGELLKTL-KGHTGPVTSVAFSPDGKYLASGSDDGTIKLW 39
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
81-246 8.82e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.98  E-value: 8.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545  81 QLQEMAQLKMKHQEELTELHKKRG-------ELAQLVIDLNNQMQQKDKEIQT--NEAKIAECLQTISDLEADCldlrtK 151
Cdd:COG4717  306 ELQALPALEELEEEELEELLAALGlppdlspEELLELLDRIEELQELLREAEEleEELQLEELEQEIAALLAEA-----G 380

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545 152 LQDLE--VANQTLKDEYDALQITFTALEEKLRKTTEENQELVTRWMAEKAQEANRLNAENEKDSRRRQARLQKELAEAAK 229
Cdd:COG4717  381 VEDEEelRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEA 460

                        170
                 ....*....|....*..
gi 564369545 230 EPLPVEQDDDIEVIVDE 246
Cdd:COG4717  461 ELEQLEEDGELAELLQE 477
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
78-186 9.61e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.13  E-value: 9.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564369545   78 NDSQLQEMAQLKMKHQEELTELHKKRGELAQLVIDLNNQMQQKDKEIQTNEAKIAECLQTISDLEADCLDLRtkLQDLEV 157
Cdd:COG4913   683 SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEER--FAAALG 760

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 564369545  158 ANQT------LKDEYDALQITFTALEEKLRKTTEE 186
Cdd:COG4913   761 DAVErelrenLEERIDALRARLNRAEEELERAMRA 795
 
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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