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Conserved domains on  [gi|124256478|ref|NP_060444|]
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autophagy-related protein 16-1 isoform 2 [Homo sapiens]

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];
199-585 3.99e-61

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 207.84  E-value: 3.99e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478 199 AQEANRLNAENEKDSRRRQARLQKELAEAAKEPLPVEQDDDIEVIVDETSDHTEETSPVRAISRAATRRSVSSFPV---- 274
Cdd:COG2319    7 AALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLsvaf 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478 275 -PQDNVDTHPGSGKEVRV----PATALCVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWEVFGEKCEfkGSLSGSNAG 349
Cdd:COG2319   87 sPDGRLLASASADGTVRLwdlaTGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLL--RTLTGHSGA 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478 350 ITSIEFDSAGSYLLAASNDFASRIWTVDDYRLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTV-F 428
Cdd:COG2319  165 VTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLtG 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478 429 AGSSCNDIVCT--EQCVMSGHFDKKIRFWDIRSESIVREME-LLGKITALDLNPERTELLSCSRDDLLKVIDLRTNAIKQ 505
Cdd:COG2319  245 HSGSVRSVAFSpdGRLLASGSADGTVRLWDLATGELLRTLTgHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLR 324

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478 506 TFSAPgfkcGSDWTRVVFSPDGSYVAAGSAEGSLYIWSVLTGKVEKVLsKQHSSSINAVAWSPSGSHVVSVDKGCKAVLW 585
Cdd:COG2319  325 TLTGH----TGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTL-TGHTGAVTSVAFSPDGRTLASGSADGTVRLW 399
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 31-206 9.56e-58

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: 191.30  E-value: 9.56e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478   31 AFEEIILQYNKLLEKSDLHSVLAQKLQAEKHDVPNRHEISPGHDGTWNDNQLQEMAQLRIKHQEELTELHKKRGELAQLV 110
Cdd:pfam08614   1 AFLELIDAYNRLLDRTALLEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQLREELAELYRSRGELAQRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478  111 IDLNNQMQRKDREMQMNEAKIAECLQTISDLETECLDLRTKLCDLERANQTLKDEYDALQITFTALEGKLRKTTEENQEL 190
Cdd:pfam08614  81 VDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQDELVALQLQLNMAEEKLRKLEKENREL 160

                         170
                  ....*....|....*.
gi 124256478  191 VTRWMAEKAQEANRLN 206
Cdd:pfam08614 161 VERWMKRKGQEAEAMN 176
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
199-585 3.99e-61

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 207.84  E-value: 3.99e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478 199 AQEANRLNAENEKDSRRRQARLQKELAEAAKEPLPVEQDDDIEVIVDETSDHTEETSPVRAISRAATRRSVSSFPV---- 274
Cdd:COG2319    7 AALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLsvaf 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478 275 -PQDNVDTHPGSGKEVRV----PATALCVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWEVFGEKCEfkGSLSGSNAG 349
Cdd:COG2319   87 sPDGRLLASASADGTVRLwdlaTGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLL--RTLTGHSGA 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478 350 ITSIEFDSAGSYLLAASNDFASRIWTVDDYRLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTV-F 428
Cdd:COG2319  165 VTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLtG 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478 429 AGSSCNDIVCT--EQCVMSGHFDKKIRFWDIRSESIVREME-LLGKITALDLNPERTELLSCSRDDLLKVIDLRTNAIKQ 505
Cdd:COG2319  245 HSGSVRSVAFSpdGRLLASGSADGTVRLWDLATGELLRTLTgHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLR 324

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478 506 TFSAPgfkcGSDWTRVVFSPDGSYVAAGSAEGSLYIWSVLTGKVEKVLsKQHSSSINAVAWSPSGSHVVSVDKGCKAVLW 585
Cdd:COG2319  325 TLTGH----TGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTL-TGHTGAVTSVAFSPDGRTLASGSADGTVRLW 399
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 296-586 8.85e-59

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: 197.94  E-value: 8.85e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478 296 LCVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWEVfgEKCEFKGSLSGSNAGITSIEFDSAGSYLLAASNDFASRIWT 375
Cdd:cd00200    2 RRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDL--ETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478 376 VDDYRLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTvFAG----------SSCNDIVCteqcvmS 445
Cdd:cd00200   80 LETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTT-LRGhtdwvnsvafSPDGTFVA------S 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478 446 GHFDKKIRFWDIRSESIVREMEL-LGKITALDLNPERTELLSCSRDDLLKVIDLRTNAIKQTFSAPgfkcgSDW-TRVVF 523
Cdd:cd00200  153 SSQDGTIKLWDLRTGKCVATLTGhTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGH-----ENGvNSVAF 227

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124256478 524 SPDGSYVAAGSAEGSLYIWSVLTGKVEKVLSkQHSSSINAVAWSPSGSHVVSVDKGCKAVLWA 586
Cdd:cd00200  228 SPDGYLLASGSEDGTIRVWDLRTGECVQTLS-GHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 31-206 9.56e-58

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: 191.30  E-value: 9.56e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478   31 AFEEIILQYNKLLEKSDLHSVLAQKLQAEKHDVPNRHEISPGHDGTWNDNQLQEMAQLRIKHQEELTELHKKRGELAQLV 110
Cdd:pfam08614   1 AFLELIDAYNRLLDRTALLEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQLREELAELYRSRGELAQRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478  111 IDLNNQMQRKDREMQMNEAKIAECLQTISDLETECLDLRTKLCDLERANQTLKDEYDALQITFTALEGKLRKTTEENQEL 190
Cdd:pfam08614  81 VDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQDELVALQLQLNMAEEKLRKLEKENREL 160

                         170
                  ....*....|....*.
gi 124256478  191 VTRWMAEKAQEANRLN 206
Cdd:pfam08614 161 VERWMKRKGQEAEAMN 176
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 120-209 2.09e-29

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: 111.50  E-value: 2.09e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478 120 KDREMQMNEAKIAECLQTISDLETECLDLRTKLCDLERANQTLKDEYDALQITFTALEGKLRKTTEENQELVTRWMAEKA 199
Cdd:cd22887    2 LESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEENDELVERWMAKKQ 81

                         90
                 ....*....|
gi 124256478 200 QEANRLNAEN 209
Cdd:cd22887   82 QEADKMNEAN 91
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 296-331 6.84e-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: 48.85  E-value: 6.84e-08
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 124256478   296 LCVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWE 331
Cdd:smart00320   5 LKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
79-264 1.17e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 54.14  E-value: 1.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478  79 DNQLQEMAQLRIKHQEELTELHKKRGELAQL---VIDLNNQMQRKDREMQMNEAKIAECLQTISDLETECLDLRTKLCDL 155
Cdd:COG4372   41 DKLQEELEQLREELEQAREELEQLEEELEQArseLEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEEL 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478 156 ERANQTLKDEYDALQITFTALEGKLRKTTEENQELVTRwMAEKAQEANRLNAENEKDSRRR-QARLQKELAEAAKEPLPV 234
Cdd:COG4372  121 QKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ-LESLQEELAALEQELQALSEAEaEQALDELLKEANRNAEKE 199

                        170       180       190
                 ....*....|....*....|....*....|
gi 124256478 235 EQDDDIEVIVDETSDHTEETSPVRAISRAA 264
Cdd:COG4372  200 EELAEAEKLIESLPRELAEELLEAKDSLEA 229
WD40 pfam00400
WD domain, G-beta repeat;
296-331 2.34e-07

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 47.34  E-value: 2.34e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 124256478  296 LCVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWE 331
Cdd:pfam00400   4 LKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 306-542 2.16e-06

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 50.86  E-value: 2.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478 306 VNAVQFSPGSRLLATGGMDRRVKLWEVF-----GEKCEFKGSLSGSNAGITSIEFDSAGSYLLAASN-DFASRIWTVDDY 379
Cdd:PLN00181 486 VCAIGFDRDGEFFATAGVNKKIKIFECEsiikdGRDIHYPVVELASRSKLSGICWNSYIKSQVASSNfEGVVQVWDVARS 565

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478 380 RLRHTLTGHSGKVLSAKFL-LDNARIVSGSHDRTLKLWDLRSKVCIKTVfagSSCNDIVCTE------QCVMSGHFDKKI 452
Cdd:PLN00181 566 QLVTEMKEHEKRVWSIDYSsADPTLLASGSDDGSVKLWSINQGVSIGTI---KTKANICCVQfpsesgRSLAFGSADHKV 642

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478 453 RFWDIRSESI-VREMELLGKITALDLNPERTELLSCSRDDLLKVIDLRTNA--IKQT--FSAPGFKCGSDWTRVVFSpDG 527
Cdd:PLN00181 643 YYYDLRNPKLpLCTMIGHSKTVSYVRFVDSSTLVSSSTDNTLKLWDLSMSIsgINETplHSFMGHTNVKNFVGLSVS-DG 721

                        250
                 ....*....|....*
gi 124256478 528 sYVAAGSAEGSLYIW 542
Cdd:PLN00181 722 -YIATGSETNEVFVY 735
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 83-230 2.55e-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: 2.55e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478    83 QEMAQLRIKHQeeltELHKKRGELAQLVIDLNNQMQRKDREMQMNEAKIAECLQTISDLETECLDLRTKLCDLERANQTL 162
Cdd:TIGR02168  267 EKLEELRLEVS----ELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAEL 342

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124256478   163 KDEYDALQITFTALEGKLRKTTEENQELVTRWmAEKAQEANRLNAEnEKDSRRRQARLQKELAEAAKE 230
Cdd:TIGR02168  343 EEKLEELKEELESLEAELEELEAELEELESRL-EELEEQLETLRSK-VAQLELQIASLNNEIERLEAR 408
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
46-230 2.82e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.88  E-value: 2.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478  46 SDLHSVLAQKLQAEKHDVPNRHEispghdgtwndnqlQEMAQLR--IKHQEELTELHKKRGELAQLVIDLNNQMQRkdrE 123
Cdd:PRK02224 190 DQLKAQIEEKEEKDLHERLNGLE--------------SELAELDeeIERYEEQREQARETRDEADEVLEEHEERRE---E 252

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478 124 MQMNEAKIAECLQTISDLETECLDLRTKLCDLERANQTLKDEYDAL--QITFTALEGK----LRKTTEENQELVTRWMAE 197
Cdd:PRK02224 253 LETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLlaEAGLDDADAEaveaRREELEDRDEELRDRLEE 332

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 124256478 198 KAQEANRLN------AENEKDSRRRQARLQKELAEAAKE 230
Cdd:PRK02224 333 CRVAAQAHNeeaeslREDADDLEERAEELREEAAELESE 371
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
199-585 3.99e-61

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 207.84  E-value: 3.99e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478 199 AQEANRLNAENEKDSRRRQARLQKELAEAAKEPLPVEQDDDIEVIVDETSDHTEETSPVRAISRAATRRSVSSFPV---- 274
Cdd:COG2319    7 AALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLsvaf 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478 275 -PQDNVDTHPGSGKEVRV----PATALCVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWEVFGEKCEfkGSLSGSNAG 349
Cdd:COG2319   87 sPDGRLLASASADGTVRLwdlaTGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLL--RTLTGHSGA 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478 350 ITSIEFDSAGSYLLAASNDFASRIWTVDDYRLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTV-F 428
Cdd:COG2319  165 VTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLtG 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478 429 AGSSCNDIVCT--EQCVMSGHFDKKIRFWDIRSESIVREME-LLGKITALDLNPERTELLSCSRDDLLKVIDLRTNAIKQ 505
Cdd:COG2319  245 HSGSVRSVAFSpdGRLLASGSADGTVRLWDLATGELLRTLTgHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLR 324

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478 506 TFSAPgfkcGSDWTRVVFSPDGSYVAAGSAEGSLYIWSVLTGKVEKVLsKQHSSSINAVAWSPSGSHVVSVDKGCKAVLW 585
Cdd:COG2319  325 TLTGH----TGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTL-TGHTGAVTSVAFSPDGRTLASGSADGTVRLW 399
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 296-586 8.85e-59

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: 197.94  E-value: 8.85e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478 296 LCVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWEVfgEKCEFKGSLSGSNAGITSIEFDSAGSYLLAASNDFASRIWT 375
Cdd:cd00200    2 RRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDL--ETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478 376 VDDYRLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTvFAG----------SSCNDIVCteqcvmS 445
Cdd:cd00200   80 LETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTT-LRGhtdwvnsvafSPDGTFVA------S 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478 446 GHFDKKIRFWDIRSESIVREMEL-LGKITALDLNPERTELLSCSRDDLLKVIDLRTNAIKQTFSAPgfkcgSDW-TRVVF 523
Cdd:cd00200  153 SSQDGTIKLWDLRTGKCVATLTGhTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGH-----ENGvNSVAF 227

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124256478 524 SPDGSYVAAGSAEGSLYIWSVLTGKVEKVLSkQHSSSINAVAWSPSGSHVVSVDKGCKAVLWA 586
Cdd:cd00200  228 SPDGYLLASGSEDGTIRVWDLRTGECVQTLS-GHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 31-206 9.56e-58

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: 191.30  E-value: 9.56e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478   31 AFEEIILQYNKLLEKSDLHSVLAQKLQAEKHDVPNRHEISPGHDGTWNDNQLQEMAQLRIKHQEELTELHKKRGELAQLV 110
Cdd:pfam08614   1 AFLELIDAYNRLLDRTALLEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQLREELAELYRSRGELAQRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478  111 IDLNNQMQRKDREMQMNEAKIAECLQTISDLETECLDLRTKLCDLERANQTLKDEYDALQITFTALEGKLRKTTEENQEL 190
Cdd:pfam08614  81 VDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQDELVALQLQLNMAEEKLRKLEKENREL 160

                         170
                  ....*....|....*.
gi 124256478  191 VTRWMAEKAQEANRLN 206
Cdd:pfam08614 161 VERWMKRKGQEAEAMN 176
WD40 COG2319
WD40 repeat [General function prediction only];
284-544 1.05e-49

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 177.03  E-value: 1.05e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478 284 GSGKEVRV----PATALCVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWEVFGEKCEFkgSLSGSNAGITSIEFDSAG 359
Cdd:COG2319  139 SADGTVRLwdlaTGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLR--TLTGHTGAVRSVAFSPDG 216

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478 360 SYLLAASNDFASRIWTVDDYRLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTvFAGSSC--NDIV 437
Cdd:COG2319  217 KLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRT-LTGHSGgvNSVA 295

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478 438 CT--EQCVMSGHFDKKIRFWDIRSESIVREME-LLGKITALDLNPERTELLSCSRDDLLKVIDLRTNAIKQTFSAPgfkc 514
Cdd:COG2319  296 FSpdGKLLASGSDDGTVRLWDLATGKLLRTLTgHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGH---- 371

                        250       260       270
                 ....*....|....*....|....*....|.
gi 124256478 515 gSDW-TRVVFSPDGSYVAAGSAEGSLYIWSV 544
Cdd:COG2319  372 -TGAvTSVAFSPDGRTLASGSADGTVRLWDL 401
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 381-585 1.49e-35

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: 135.16  E-value: 1.49e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478 381 LRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTV----FAGSSCNDIVCTEQCVmSGHFDKKIRFWD 456
Cdd:cd00200    1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLkghtGPVRDVAASADGTYLA-SGSSDKTIRLWD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478 457 IRSESIVREMEL-LGKITALDLNPERTELLSCSRDDLLKVIDLRTNAIKQTFSAPgfkcgSDWTR-VVFSPDGSYVAAGS 534
Cdd:cd00200   80 LETGECVRTLTGhTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGH-----TDWVNsVAFSPDGTFVASSS 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 124256478 535 AEGSLYIWSVLTGKVEKVLsKQHSSSINAVAWSPSGSHVV--SVDKGCKavLW 585
Cdd:cd00200  155 QDGTIKLWDLRTGKCVATL-TGHTGEVNSVAFSPDGEKLLssSSDGTIK--LW 204
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 120-209 2.09e-29

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: 111.50  E-value: 2.09e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478 120 KDREMQMNEAKIAECLQTISDLETECLDLRTKLCDLERANQTLKDEYDALQITFTALEGKLRKTTEENQELVTRWMAEKA 199
Cdd:cd22887    2 LESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEENDELVERWMAKKQ 81

                         90
                 ....*....|
gi 124256478 200 QEANRLNAEN 209
Cdd:cd22887   82 QEADKMNEAN 91
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 296-331 6.84e-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: 48.85  E-value: 6.84e-08
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 124256478   296 LCVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWE 331
Cdd:smart00320   5 LKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
79-264 1.17e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 54.14  E-value: 1.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478  79 DNQLQEMAQLRIKHQEELTELHKKRGELAQL---VIDLNNQMQRKDREMQMNEAKIAECLQTISDLETECLDLRTKLCDL 155
Cdd:COG4372   41 DKLQEELEQLREELEQAREELEQLEEELEQArseLEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEEL 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478 156 ERANQTLKDEYDALQITFTALEGKLRKTTEENQELVTRwMAEKAQEANRLNAENEKDSRRR-QARLQKELAEAAKEPLPV 234
Cdd:COG4372  121 QKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ-LESLQEELAALEQELQALSEAEaEQALDELLKEANRNAEKE 199

                        170       180       190
                 ....*....|....*....|....*....|
gi 124256478 235 EQDDDIEVIVDETSDHTEETSPVRAISRAA 264
Cdd:COG4372  200 EELAEAEKLIESLPRELAEELLEAKDSLEA 229
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 380-417 1.62e-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: 1.62e-07
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 124256478   380 RLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWD 417
Cdd:smart00320   3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
296-331 2.34e-07

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 47.34  E-value: 2.34e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 124256478  296 LCVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWE 331
Cdd:pfam00400   4 LKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 pfam00400
WD domain, G-beta repeat;
380-417 4.26e-07

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 46.57  E-value: 4.26e-07
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 124256478  380 RLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWD 417
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
88-238 1.65e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 50.92  E-value: 1.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478  88 LRIKHQEELTELHKKRGELAQLVIDLNNQMQRKDREMQMNEAKIAECLQTISDLETECLDLRTKLCDLERANQTLKDEYD 167
Cdd:COG4717   47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124256478 168 ALQitftaLEGKLRKTTEENQELVTRWMAEKAQEANRLNAENEKDSRRRQ-ARLQKELAEAAKEPLPVEQDD 238
Cdd:COG4717  127 LLP-----LYQELEALEAELAELPERLEELEERLEELRELEEELEELEAElAELQEELEELLEQLSLATEEE 193
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 306-542 2.16e-06

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 50.86  E-value: 2.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478 306 VNAVQFSPGSRLLATGGMDRRVKLWEVF-----GEKCEFKGSLSGSNAGITSIEFDSAGSYLLAASN-DFASRIWTVDDY 379
Cdd:PLN00181 486 VCAIGFDRDGEFFATAGVNKKIKIFECEsiikdGRDIHYPVVELASRSKLSGICWNSYIKSQVASSNfEGVVQVWDVARS 565

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478 380 RLRHTLTGHSGKVLSAKFL-LDNARIVSGSHDRTLKLWDLRSKVCIKTVfagSSCNDIVCTE------QCVMSGHFDKKI 452
Cdd:PLN00181 566 QLVTEMKEHEKRVWSIDYSsADPTLLASGSDDGSVKLWSINQGVSIGTI---KTKANICCVQfpsesgRSLAFGSADHKV 642

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478 453 RFWDIRSESI-VREMELLGKITALDLNPERTELLSCSRDDLLKVIDLRTNA--IKQT--FSAPGFKCGSDWTRVVFSpDG 527
Cdd:PLN00181 643 YYYDLRNPKLpLCTMIGHSKTVSYVRFVDSSTLVSSSTDNTLKLWDLSMSIsgINETplHSFMGHTNVKNFVGLSVS-DG 721

                        250
                 ....*....|....*
gi 124256478 528 sYVAAGSAEGSLYIW 542
Cdd:PLN00181 722 -YIATGSETNEVFVY 735
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 83-230 2.55e-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: 2.55e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478    83 QEMAQLRIKHQeeltELHKKRGELAQLVIDLNNQMQRKDREMQMNEAKIAECLQTISDLETECLDLRTKLCDLERANQTL 162
Cdd:TIGR02168  267 EKLEELRLEVS----ELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAEL 342

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124256478   163 KDEYDALQITFTALEGKLRKTTEENQELVTRWmAEKAQEANRLNAEnEKDSRRRQARLQKELAEAAKE 230
Cdd:TIGR02168  343 EEKLEELKEELESLEAELEELEAELEELESRL-EELEEQLETLRSK-VAQLELQIASLNNEIERLEAR 408
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 81-253 3.24e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.32  E-value: 3.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478  81 QLQEMAQLRIKHQEELTELHKKRGEL-------AQLVIDLNNQMQRKDREMQMNEAKIAECLQTISDLETECLDLRTKLC 153
Cdd:COG1196  275 ELEELELELEEAQAEEYELLAELARLeqdiarlEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478 154 DLERANQTLKDEYDALQITFTALEGKLRKTTEENQELVTRWMAEKAQEANRlnAENEKDSRRRQARLQKELAEAAKEPLP 233
Cdd:COG1196  355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL--EEAEEALLERLERLEEELEELEEALAE 432

                        170       180
                 ....*....|....*....|
gi 124256478 234 VEQDDDIEVIVDETSDHTEE 253
Cdd:COG1196  433 LEEEEEEEEEALEEAAEEEA 452
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
339-547 4.36e-06

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


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 48.15  E-value: 4.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478 339 FKGSLSGSNAGITSIEFDSAGSYLLAASNDFASRIWTVDDYRLRHTLTGHSGKVLSAKFLLDNARI-VSGSHDRTLKLWD 417
Cdd:COG3391   17 ALAALAVAVAALGLGGGGPLLAAASGGVVGAAVGGGGVALLAGLGLGAAAVADADGADAGADGRRLyVANSGSGRVSVID 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478 418 LRSKVCIKTVFAGSSCNDIVCTE---QCVMSGHFDKKIRFWDIRSESIVREMELLGKITALDLNPERTELLSCSRDD--- 491
Cdd:COG3391   97 LATGKVVATIPVGGGPRGLAVDPdggRLYVADSGNGRVSVIDTATGKVVATIPVGAGPHGIAVDPDGKRLYVANSGSntv 176

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124256478 492 --LLKVIDLRTNAIKQTFSApgfkcGSDWTRVVFSPDGS--YVA------AGSAEGSLYIWSVLTG 547
Cdd:COG3391  177 svIVSVIDTATGKVVATIPV-----GGGPVGVAVSPDGRrlYVAnrgsntSNGGSNTVSVIDLATL 237
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 302-418 8.54e-06

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 48.93  E-value: 8.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478 302 HDGEVNAVQFSPGS-RLLATGGMDRRVKLWEVFgekcefKGSLSGS---NAGITSIEFDSAGSYLLAasndFASRIWTVD 377
Cdd:PLN00181 574 HEKRVWSIDYSSADpTLLASGSDDGSVKLWSIN------QGVSIGTiktKANICCVQFPSESGRSLA----FGSADHKVY 643

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 124256478 378 DYRLRH------TLTGHSGKVLSAKFLlDNARIVSGSHDRTLKLWDL 418
Cdd:PLN00181 644 YYDLRNpklplcTMIGHSKTVSYVRFV-DSSTLVSSSTDNTLKLWDL 689
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 79-230 3.71e-05

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 45.30  E-value: 3.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478  79 DNQLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQRKDREMQMNEAKIAECLQTISDLET---------ECLDLR 149
Cdd:COG1579   16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlgnvrnnkEYEALQ 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478 150 TKLCDLERANQTLKDEYDALQITFTALEGKLRKTTEENQELVTRWmAEKAQEANRLNAENEKDsrrrQARLQKELAEAAK 229
Cdd:COG1579   96 KEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAEL-EEKKAELDEELAELEAE----LEELEAEREELAA 170


                 .
gi 124256478 230 E 230
Cdd:COG1579  171 K 171
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 83-274 3.96e-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: 3.96e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478    83 QEMAQLRIKHQEELTELHKKRGELAQLVIDLnnQMQRKDREMQMNEakiaeclqtISDLETECLDLRTKLCDLERANQTL 162
Cdd:TIGR02169  315 RELEDAEERLAKLEAEIDKLLAEIEELEREI--EEERKRRDKLTEE---------YAELKEELEDLRAELEEVDKEFAET 383

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478   163 KDEYDALQitfTALEGKLRKTTEENQELVTRWMAEKAQEANRLNAENE-KDSRRRQARLQKELAEAAKEPLPVEQD---- 237
Cdd:TIGR02169  384 RDELKDYR---EKLEKLKREINELKRELDRLQEELQRLSEELADLNAAiAGIEAKINELEEEKEDKALEIKKQEWKleql 460

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 124256478   238 ---------------DDIEVIVDETSDHTEETSPVRAISRAATRRSVSSFPV 274
Cdd:TIGR02169  461 aadlskyeqelydlkEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAV 512
TolB COG0823
Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, ...
 495-574 4.06e-05

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: 44.28  E-value: 4.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478 495 VIDLRTNAIKQTFSAPGFKCGSDWtrvvfSPDGSYVAAGSAEGS---LYIWSVLTGKVEKVLSKQHSSSinAVAWSPSGS 571
Cdd:COG0823   15 VVDLDGGEPRRLTNSPGIDTSPAW-----SPDGRRIAFTSDRGGgpqIYVVDADGGEPRRLTFGGGYNA--SPSWSPDGK 87


                 ...
gi 124256478 572 HVV 574
Cdd:COG0823   88 RLA 90
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 114-266 4.10e-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: 46.59  E-value: 4.10e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478   114 NNQMQRKDREMQMNEAKIAECLQTISDLETECLDLRTKLCDLERANQTLKDEYDALQITFTALEGKLRKTTEEnQELVTR 193
Cdd:TIGR02168  669 NSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE-VEQLEE 747

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124256478   194 WMAEKAQEANRLNAE-NEKDSRRRQARLQKELAEAAKEPLPVEQDDDIEVIVDETSDHTEETSPVRAISRAATR 266
Cdd:TIGR02168  748 RIAQLSKELTELEAEiEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAAN 821
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 83-221 5.46e-05

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 46.32  E-value: 5.46e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478    83 QEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQRKDREMQMNEAKIAE-------CLQTISDLETECLDLRTKLcDL 155
Cdd:pfam01576  204 QELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEetaqknnALKKIRELEAQISELQEDL-ES 282

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124256478   156 ERANQT--------LKDEYDALQitfTALEGKLrKTTEENQELVTRwmaeKAQEANRLNAENEKDSRRRQARLQ 221
Cdd:pfam01576  283 ERAARNkaekqrrdLGEELEALK---TELEDTL-DTTAAQQELRSK----REQEVTELKKALEEETRSHEAQLQ 348
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 79-253 5.68e-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: 5.68e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478    79 DNQLQEMAQLRIKH---QEELTELHKKRGELAQLVIDLNNQMQRKDREMQMNEAKIAECLQTISDLETECLDLRTKLCDL 155
Cdd:TIGR02168  792 EQLKEELKALREALdelRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL 871

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478   156 --------------ERANQTLKDEYDALQITFTALEGKLRKTTEENQELvtrwMAEKAQEANRLN-AENEKDSRRRQARL 220
Cdd:TIGR02168  872 eseleallneraslEEALALLRSELEELSEELRELESKRSELRRELEEL----REKLAQLELRLEgLEVRIDNLQERLSE 947

                          170       180       190
                   ....*....|....*....|....*....|...
gi 124256478   221 QKELAEAAKEPLPVEQDDDIEVIVDETSDHTEE 253
Cdd:TIGR02168  948 EYSLTLEEAEALENKIEDDEEEARRRLKRLENK 980
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 81-232 5.96e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.08  E-value: 5.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478  81 QLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQRKDREMQMNEAKIAECLQTISDLETECLDLRTKLCDLERANQ 160
Cdd:COG1196  331 ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124256478 161 TLKDEYDALQitftalegklrkttEENQELVTrwmAEKAQEANRLNAENEKDSRRRQARLQKELAEAAKEPL 232
Cdd:COG1196  411 ALLERLERLE--------------EELEELEE---ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 79-249 7.32e-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: 45.83  E-value: 7.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478    79 DNQLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQRKDREMQMN--------EAKIAECLQTISDLETEcldlrt 150
Cdd:TIGR02169  243 ERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRvkekigelEAEIASLERSIAEKERE------ 316

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478   151 kLCDLERANQTLKDEYDALQITFTALEGKLR-------KTTEENQELVTRwMAEKAQEANRLNAENeKDSRRRQARLQKE 223
Cdd:TIGR02169  317 -LEDAEERLAKLEAEIDKLLAEIEELEREIEeerkrrdKLTEEYAELKEE-LEDLRAELEEVDKEF-AETRDELKDYREK 393

                          170       180
                   ....*....|....*....|....*...
gi 124256478   224 LAEAAKE--PLPVEQDDDIEVIVDETSD 249
Cdd:TIGR02169  394 LEKLKREinELKRELDRLQEELQRLSEE 421
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 81-306 1.03e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 44.75  E-value: 1.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478  81 QLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQRKDREMQMNEAKIAECLQTISDLETE---------------- 144
Cdd:COG4942   42 ELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEElaellralyrlgrqpp 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478 145 ---------CLDLRTKLCDLERANQTLKDEYDALQITFTALEGKLRKTTEENQELVTRwMAEKAQEANRLNAEnEKDSRR 215
Cdd:COG4942  122 lalllspedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL-LAELEEERAALEAL-KAERQK 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478 216 RQARLQKELAEAAKEPLPVEQD-DDIEVIVDETSDHTEETSPVRAISRAATRRSVSSFPV----------PQDNVDTHPG 284
Cdd:COG4942  200 LLARLEKELAELAAELAELQQEaEELEALIARLEAEAAAAAERTPAAGFAALKGKLPWPVsgrvvrrfgeRDGGGGRNKG 279

                        250       260
                 ....*....|....*....|....*...
gi 124256478 285 ------SGKEVRVPAtalcvfdahDGEV 306
Cdd:COG4942  280 idiaapPGAPVRAVA---------DGTV 298
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
78-290 1.81e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.52  E-value: 1.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478   78 NDNQLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQ--RKDREMQMNEAKIAECLQTISDLETECLDLRTKLCDL 155
Cdd:COG4913   608 NRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREalQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDL 687

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478  156 ERANQTLKD---EYDALQITFTALEGKLRKTTEENQELVTRWmaekAQEANRLNAENEKDSRRRQARLQKELAEAAKEPL 232
Cdd:COG4913   688 AALEEQLEEleaELEELEEELDELKGEIGRLEKELEQAEEEL----DELQDRLEAAEDLARLELRALLEERFAAALGDAV 763

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 124256478  233 PVEQDDDIE-VIVDETSDHTEETSPVRAISRAATRRsvssFPVPQDNVDTHPGSGKEVR 290
Cdd:COG4913   764 ERELRENLEeRIDALRARLNRAEEELERAMRAFNRE----WPAETADLDADLESLPEYL 818
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 546-585 2.36e-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: 38.83  E-value: 2.36e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 124256478   546 TGKVEKVLsKQHSSSINAVAWSPSGSHVVSVDKGCKAVLW 585
Cdd:smart00320   1 SGELLKTL-KGHTGPVTSVAFSPDGKYLASGSDDGTIKLW 39
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
46-230 2.82e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.88  E-value: 2.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478  46 SDLHSVLAQKLQAEKHDVPNRHEispghdgtwndnqlQEMAQLR--IKHQEELTELHKKRGELAQLVIDLNNQMQRkdrE 123
Cdd:PRK02224 190 DQLKAQIEEKEEKDLHERLNGLE--------------SELAELDeeIERYEEQREQARETRDEADEVLEEHEERRE---E 252

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478 124 MQMNEAKIAECLQTISDLETECLDLRTKLCDLERANQTLKDEYDAL--QITFTALEGK----LRKTTEENQELVTRWMAE 197
Cdd:PRK02224 253 LETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLlaEAGLDDADAEaveaRREELEDRDEELRDRLEE 332

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 124256478 198 KAQEANRLN------AENEKDSRRRQARLQKELAEAAKE 230
Cdd:PRK02224 333 CRVAAQAHNeeaeslREDADDLEERAEELREEAAELESE 371
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
80-262 3.19e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.35  E-value: 3.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478  80 NQLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQRKDREMQMNEAKIAECLQTISDLETECLDLRTKLCDLERAN 159
Cdd:COG4372   87 EQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEEL 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478 160 QTLKDEYDALQITFTALEGKLRKTTEENQELVTRWMAEKAQEANRLNAENEKDSRRRQARLQKELAEAAKEPLPVEQDDD 239
Cdd:COG4372  167 AALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEE 246

                        170       180
                 ....*....|....*....|...
gi 124256478 240 IEVIVDETSDHTEETSPVRAISR 262
Cdd:COG4372  247 DKEELLEEVILKEIEELELAILV 269
COG4946 COG4946
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown] ...
 522-570 3.26e-04

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


Pssm-ID: 443973 [Multi-domain]  Cd Length: 1072  Bit Score: 43.87  E-value: 3.26e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 124256478  522 VFSPDGSYVAAGSAEGSLYIWSVLTGKVEKVLSKQHSSSINAVAWSPSG 570
Cdd:COG4946   395 VWSPDGKKIAFTDNRGRLWVVDLASGKVRKVDTDGYGDGISDLAWSPDS 443
TolB COG0823
Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, ...
 495-585 4.18e-04

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: 41.20  E-value: 4.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478 495 VIDLRTNAIKQ-TFSapgfkcGSDWTRVVFSPDGSYVA-AGSAEGSLYIWSV-LTGKVEKVLSKqhssSINAVAWSPSGS 571
Cdd:COG0823   59 VVDADGGEPRRlTFG------GGYNASPSWSPDGKRLAfVSRSDGRFDIYVLdLDGGAPRRLTD----GPGSPSWSPDGR 128

                         90
                 ....*....|....*
gi 124256478 572 HVV-SVDKGCKAVLW 585
Cdd:COG0823  129 RIVfSSDRGGRPDLY 143
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 80-253 5.00e-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: 5.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478   80 NQLQEMaqlrikhQEELTELHKKRGElaQLVIDLNNQMQRKDREMQM-------NEAKIAECLQTISDLETECLDLRT-- 150
Cdd:TIGR04523 288 KQLNQL-------KSEISDLNNQKEQ--DWNKELKSELKNQEKKLEEiqnqisqNNKIISQLNEQISQLKKELTNSESen 358

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478  151 ------------KLCDLERANQTLKDEYDALQITFTALEGKLRKTTEENQELvtrwmaekaqEANRLNAENEKDSRRRQA 218
Cdd:TIGR04523 359 sekqreleekqnEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQK----------DEQIKKLQQEKELLEKEI 428

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 124256478  219 RLQKELAEAAKEPLP--VEQDDDIEVIVDETSDHTEE 253
Cdd:TIGR04523 429 ERLKETIIKNNSEIKdlTNQDSVKELIIKNLDNTRES 465
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 14-232 6.81e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.74  E-value: 6.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478    14 KRHISEQLRRRDRLQRQAFEEIILQYNKLLEKS-DLHSVLAQK--LQAEKHDVPNRHEISpghdgtwnDNQLQEMAQLRI 90
Cdd:TIGR02168  304 KQILRERLANLERQLEELEAQLEELESKLDELAeELAELEEKLeeLKEELESLEAELEEL--------EAELEELESRLE 375

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478    91 KHQEELTELHKKRGELAQLVIDLNNQMQRKDREMQMNEAKIAECLQTISDLETECLDLRTKLCDLERAnqTLKDEYDALQ 170
Cdd:TIGR02168  376 ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELE--ELEEELEELQ 453

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124256478   171 ITFTALEGKLRKTTEENQELvTRWMAEKAQEANRLNAenEKDSRRRQARLQKELAEAAKEPL 232
Cdd:TIGR02168  454 EELERLEEALEELREELEEA-EQALDAAERELAQLQA--RLDSLERLQENLEGFSEGVKALL 512
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 27-266 1.67e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 1.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478  27 LQRQA----------FEEIILQYNKLLEKSDLHSVLAQKLQAEKHDVPNRHEispgHDGTWNDNQLQEMAQLRIKHQEEL 96
Cdd:COG1196  205 LERQAekaeryrelkEELKELEAELLLLKLRELEAELEELEAELEELEAELE----ELEAELAELEAELEELRLELEELE 280

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478  97 TELHKKRGELAQL---VIDLNNQMQRKDREMQMNEAKIAECLQTISDLETECLDLRTKLCDLERANQTLKDEYDALQITF 173
Cdd:COG1196  281 LELEEAQAEEYELlaeLARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478 174 TALEGKLRKTTEENQELVTRWMAEKAQEANRLNAENEKDSRRRQARLQKELAEAAKEPLPVEQDDDIEVIVDETSDHTEE 253
Cdd:COG1196  361 AEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE 440

                        250
                 ....*....|...
gi 124256478 254 TSPVRAISRAATR 266
Cdd:COG1196  441 EEALEEAAEEEAE 453
COG4946 COG4946
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown] ...
 521-585 2.95e-03

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


Pssm-ID: 443973 [Multi-domain]  Cd Length: 1072  Bit Score: 40.79  E-value: 2.95e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124256478  521 VVFSPDGSYVAAGS-AEGS--LYIWSVLTGKVEKVLSKQHSSSINAVAWSPSGSHVVSVDKGCKavLW 585
Cdd:COG4946   348 PAWSPDGKSIAYFSdASGEyeLYIAPADGSGEPKQLTLGDLGRVFNPVWSPDGKKIAFTDNRGR--LW 413
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 43-215 3.25e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.44  E-value: 3.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478    43 LEKSDLHSVLaQKLQAEKHDVpnRHEISPghdgtwNDNQLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQRKDR 122
Cdd:TIGR02169  784 LEARLSHSRI-PEIQAELSKL--EEEVSR------IEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEK 854

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478   123 EMQMNEAKIAECLQTISDLETECLDLRTKLCDLERANQTLKDEYDALQITFTALEGKLRKTTEENQELvtrwmAEKAQEA 202
Cdd:TIGR02169  855 EIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSEL-----KAKLEAL 929

                          170
                   ....*....|...
gi 124256478   203 NRLNAENEKDSRR 215
Cdd:TIGR02169  930 EEELSEIEDPKGE 942
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 91-226 4.02e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.44  E-value: 4.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478    91 KHQEELTELhKKRGELAQLVID-LNNQMQRKDREMQMNEakiaeclqtisdletECLDLRTKLCDLE-----RANQTLKD 164
Cdd:TIGR02169  174 KALEELEEV-EENIERLDLIIDeKRQQLERLRREREKAE---------------RYQALLKEKREYEgyellKEKEALER 237

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124256478   165 EYDALQITFTALEGKLRKTTEENQELVTRwMAEKAQEANRLNAENEKDSRRRQARLQKELAE 226
Cdd:TIGR02169  238 QKEAIERQLASLEEELEKLTEEISELEKR-LEEIEQLLEELNKKIKDLGEEEQLRVKEKIGE 298
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 114-207 4.12e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.75  E-value: 4.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478 114 NNQMQRKDREMQMNEAKIAECLQTISDLETECLDLRTKLCDLERANQTLKDEYDALQITFTALEGKLRKTTEENQELVTR 193
Cdd:COG4942   19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98

                         90
                 ....*....|....
gi 124256478 194 WMAEKAQEANRLNA 207
Cdd:COG4942   99 LEAQKEELAELLRA 112
COG4946 COG4946
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown] ...
 469-572 4.12e-03

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


Pssm-ID: 443973 [Multi-domain]  Cd Length: 1072  Bit Score: 40.41  E-value: 4.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478  469 LGKITALDLNPERTELLSCSRDDLLKVIDLRTNAIKQTFSAPGFKCGSDwtrVVFSPDGSYVA----AGSAEGSLYIWSV 544
Cdd:COG4946   388 LGRVFNPVWSPDGKKIAFTDNRGRLWVVDLASGKVRKVDTDGYGDGISD---LAWSPDSKWLAyskpGPNQLSQIFLYDV 464

                          90       100
                  ....*....|....*....|....*...
gi 124256478  545 LTGKVEKVLSKQHSSSinAVAWSPSGSH 572
Cdd:COG4946   465 ETGKTVQLTDGRYDDG--SPAFSPDGKY 490
Ge1_WD40 pfam16529
WD40 region of Ge1, enhancer of mRNA-decapping protein; Ge1_WD40 is the N-terminal region of ...
 346-427 4.92e-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: 39.36  E-value: 4.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478  346 SNAGITSIEFDSAGSYLLAASNDFASRIWTV-----DDYRLRHTLTGHSGKVLSAKFLLDNAR----------IVSGS-H 409
Cdd:pfam16529 185 EHSLLVDAAFSPDGTALATASLDGEVKFFQIylfdnRNPRCLHEWKPHDGKPLSSLFFLDNHKkppevqfwrfAITGAdN 264

                          90
                  ....*....|....*...
gi 124256478  410 DRTLKLWDLRSKVCIKTV 427
Cdd:pfam16529 265 NSELKLWSCESWTCLQTI 282
PRK12704 PRK12704
phosphodiesterase; Provisional
 83-204 5.66e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 39.38  E-value: 5.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478  83 QEMAQLRIKHQEELTElhkKRGELAQL---VID----LNNQMQ---RKDREMQMNEAKIAECLQTISDLETECLDLRTKL 152
Cdd:PRK12704  64 EEIHKLRNEFEKELRE---RRNELQKLekrLLQkeenLDRKLElleKREEELEKKEKELEQKQQELEKKEEELEELIEEQ 140

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 124256478 153 CD-LERANQTLKDEydALQITFTALEGKLRkttEENQELVTRWMAEKAQEANR 204
Cdd:PRK12704 141 LQeLERISGLTAEE--AKEILLEKVEEEAR---HEAAVLIKEIEEEAKEEADK 188
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 519-543 5.68e-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: 34.98  E-value: 5.68e-03
                           10        20
                   ....*....|....*....|....*
gi 124256478   519 TRVVFSPDGSYVAAGSAEGSLYIWS 543
Cdd:smart00320  16 TSVAFSPDGKYLASGSDDGTIKLWD 40
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 54-211 5.91e-03

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 39.64  E-value: 5.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478    54 QKLQAEKHDVPNRHE-ISPGHDGTWNDNQLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQ---MQRKDREMQMNEA 129
Cdd:TIGR00606  795 ERFQMELKDVERKIAqQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQiqhLKSKTNELKSEKL 874

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478   130 KIAECLQTISDLETECLDLRTKLCDLERANQTLKDEydalqitFTALEGKLRKTTEENQELVTRWMAEKAQEANRLNAEN 209
Cdd:TIGR00606  875 QIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQ-------DSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIK 947


                   ..
gi 124256478   210 EK 211
Cdd:TIGR00606  948 EK 949
ADIP pfam11559
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ...
 117-226 7.02e-03

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


Pssm-ID: 463295 [Multi-domain]  Cd Length: 151  Bit Score: 37.30  E-value: 7.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478  117 MQRKDREMQMNEAKiaecLQTISDLETECLDLR-------TKLCDLERANQTLKDEYDALQITFTALEGKLRKTTEENQE 189
Cdd:pfam11559  44 LQQRDRDLEFRESL----NETIRTLEAEIERLQskierlkTQLEDLERELALLQAKERQLEKKLKTLEQKLKNEKEELQR 119

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 124256478  190 LVTRWMAEKAQeanrlnAENEKDSRRRQ-ARLQKELAE 226
Cdd:pfam11559 120 LKNALQQIKTQ------FAHEVKKRDREiEKLKERLAQ 151
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 86-230 7.99e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 38.98  E-value: 7.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478  86 AQLRIKHQEELTELHKKRGELAQLVIDLNNQMQRKDREMQMNEAKIAECLQTISDLETECLDLRTKLCDLERANQTLKDE 165
Cdd:COG4942   19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124256478 166 YDALQITFTALEGKLRKT-----------TEENQELVTRWMAEKA-QEANRLNAENEKDSRRRQARLQKELAEAAKE 230
Cdd:COG4942   99 LEAQKEELAELLRALYRLgrqpplalllsPEDFLDAVRRLQYLKYlAPARREQAEELRADLAELAALRAELEAERAE 175
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
79-253 8.25e-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: 8.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478   79 DNQLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQRKD-REMQMNEAKIAECLQTISDLETECLDLRTKLCDLER 157
Cdd:COG4913   294 EAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGL 373

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478  158 ANQTLKDEYDALQITFTALEGKLRKTTEENQELVTRWMAEKaqeanrlnaeneKDSRRRQARLQKELA--EAAKEPLPVE 235
Cdd:COG4913   374 PLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAAL------------RDLRRELRELEAEIAslERRKSNIPAR 441

                         170
                  ....*....|....*...
gi 124256478  236 QDDDIEVIVDETSDHTEE 253
Cdd:COG4913   442 LLALRDALAEALGLDEAE 459
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 78-186 9.89e-03

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


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 37.58  E-value: 9.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124256478   78 NDNQLQEMAQLRIKHQEELTELHKKRGELAQlviDLNNQmqRKDRE-MQMNEAKIAECLQTISDLETECLDLRTKLCDLE 156
Cdd:pfam13851  45 NEKLMSEIQQENKRLTEPLQKAQEEVEELRK---QLENY--EKDKQsLKNLKARLKVLEKELKDLKWEHEVLEQRFEKVE 119

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 124256478  157 RANQTLKDE-----YDALQITF---TALEGKLRKTTEE 186
Cdd:pfam13851 120 RERDELYDKfeaaiQDVQQKTGlknLLLEKKLQALGET 157
 
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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