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Conserved domains on  [gi|1393169536|ref|NP_001350671|]
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autophagy-related protein 16-1 isoform 6 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
217-621 6.15e-61

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 208.23  E-value: 6.15e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536 217 QARLQKELAEAAKEPLPVEQDDDIEVIVDETSDHTEETSPVRAISRAATKRLSQPAGGLLDSITNIFGLSESPLLGHHSS 296
Cdd:COG2319     1 ALSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536 297 SDAARRRsvssfpvPQDNVDTHPGSGKEVRV----PATALCVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWEVFGEK 372
Cdd:COG2319    81 VLSVAFS-------PDGRLLASASADGTVRLwdlaTGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGK 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536 373 CEfkGSLSGSNAGITSIEFDSAGSYLLAASNDFASRIWTVDDYRLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLW 452
Cdd:COG2319   154 LL--RTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLW 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536 453 DLRSKVCIKTV-FAGSSCNDIVCT--EQCVMSGHFDKKIRFWDIRSESIVREME-LLGKITALDLNPERTELLSCSRDDL 528
Cdd:COG2319   232 DLATGKLLRTLtGHSGSVRSVAFSpdGRLLASGSADGTVRLWDLATGELLRTLTgHSGGVNSVAFSPDGKLLASGSDDGT 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536 529 LKVIDLRTNAIKQTFSAPgfkcGSDWTRVVFSPDGSYVAAGSAEGSLYIWSVLTGKVEKVLsKQHSSSINAVAWSPSGSH 608
Cdd:COG2319   312 VRLWDLATGKLLRTLTGH----TGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTL-TGHTGAVTSVAFSPDGRT 386

                         410
                  ....*....|...
gi 1393169536 609 VVSVDKGCKAVLW 621
Cdd:COG2319   387 LASGSADGTVRLW 399
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 31-206 7.86e-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: 192.07  E-value: 7.86e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536  31 AFEEIILQYNKLLEKSDLHSVLAQKLQAEKHDVPNRHEISPGHDGTWNDNQLQEMAQLRIKHQEELTELHKKRGELAQLV 110
Cdd:pfam08614   1 AFLELIDAYNRLLDRTALLEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQLREELAELYRSRGELAQRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536 111 IDLNNQMQRKDREMQMNEAKIAECLQTISDLETECLDLRTKLCDLERANQTLKDEYDALQITFTALEGKLRKTTEENQEL 190
Cdd:pfam08614  81 VDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQDELVALQLQLNMAEEKLRKLEKENREL 160

                         170
                  ....*....|....*.
gi 1393169536 191 VTRWMAEKAQEANRLN 206
Cdd:pfam08614 161 VERWMKRKGQEAEAMN 176
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
217-621 6.15e-61

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 208.23  E-value: 6.15e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536 217 QARLQKELAEAAKEPLPVEQDDDIEVIVDETSDHTEETSPVRAISRAATKRLSQPAGGLLDSITNIFGLSESPLLGHHSS 296
Cdd:COG2319     1 ALSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536 297 SDAARRRsvssfpvPQDNVDTHPGSGKEVRV----PATALCVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWEVFGEK 372
Cdd:COG2319    81 VLSVAFS-------PDGRLLASASADGTVRLwdlaTGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGK 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536 373 CEfkGSLSGSNAGITSIEFDSAGSYLLAASNDFASRIWTVDDYRLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLW 452
Cdd:COG2319   154 LL--RTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLW 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536 453 DLRSKVCIKTV-FAGSSCNDIVCT--EQCVMSGHFDKKIRFWDIRSESIVREME-LLGKITALDLNPERTELLSCSRDDL 528
Cdd:COG2319   232 DLATGKLLRTLtGHSGSVRSVAFSpdGRLLASGSADGTVRLWDLATGELLRTLTgHSGGVNSVAFSPDGKLLASGSDDGT 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536 529 LKVIDLRTNAIKQTFSAPgfkcGSDWTRVVFSPDGSYVAAGSAEGSLYIWSVLTGKVEKVLsKQHSSSINAVAWSPSGSH 608
Cdd:COG2319   312 VRLWDLATGKLLRTLTGH----TGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTL-TGHTGAVTSVAFSPDGRT 386

                         410
                  ....*....|...
gi 1393169536 609 VVSVDKGCKAVLW 621
Cdd:COG2319   387 LASGSADGTVRLW 399
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 332-622 2.85e-58

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: 197.56  E-value: 2.85e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536 332 LCVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWEVfgEKCEFKGSLSGSNAGITSIEFDSAGSYLLAASNDFASRIWT 411
Cdd:cd00200     2 RRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDL--ETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536 412 VDDYRLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTvFAG----------SSCNDIVCteqcvmS 481
Cdd:cd00200    80 LETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTT-LRGhtdwvnsvafSPDGTFVA------S 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536 482 GHFDKKIRFWDIRSESIVREMEL-LGKITALDLNPERTELLSCSRDDLLKVIDLRTNAIKQTFSAPgfkcgSDW-TRVVF 559
Cdd:cd00200   153 SSQDGTIKLWDLRTGKCVATLTGhTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGH-----ENGvNSVAF 227

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1393169536 560 SPDGSYVAAGSAEGSLYIWSVLTGKVEKVLSkQHSSSINAVAWSPSGSHVVSVDKGCKAVLWA 622
Cdd:cd00200   228 SPDGYLLASGSEDGTIRVWDLRTGECVQTLS-GHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 31-206 7.86e-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: 192.07  E-value: 7.86e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536  31 AFEEIILQYNKLLEKSDLHSVLAQKLQAEKHDVPNRHEISPGHDGTWNDNQLQEMAQLRIKHQEELTELHKKRGELAQLV 110
Cdd:pfam08614   1 AFLELIDAYNRLLDRTALLEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQLREELAELYRSRGELAQRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536 111 IDLNNQMQRKDREMQMNEAKIAECLQTISDLETECLDLRTKLCDLERANQTLKDEYDALQITFTALEGKLRKTTEENQEL 190
Cdd:pfam08614  81 VDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQDELVALQLQLNMAEEKLRKLEKENREL 160

                         170
                  ....*....|....*.
gi 1393169536 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 9.29e-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: 112.66  E-value: 9.29e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536 120 KDREMQMNEAKIAECLQTISDLETECLDLRTKLCDLERANQTLKDEYDALQITFTALEGKLRKTTEENQELVTRWMAEKA 199
Cdd:cd22887     2 LESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEENDELVERWMAKKQ 81

                          90
                  ....*....|
gi 1393169536 200 QEANRLNAEN 209
Cdd:cd22887    82 QEADKMNEAN 91
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
79-264 5.46e-08

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 55.29  E-value: 5.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536  79 DNQLQEMAQLRIKHQEELTELHKKRGELAQL---VIDLNNQMQRKDREMQMNEAKIAECLQTISDLETECLDLRTKLCDL 155
Cdd:COG4372    41 DKLQEELEQLREELEQAREELEQLEEELEQArseLEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEEL 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536 156 ERANQTLKDEYDALQITFTALEGKLRKTTEENQELVTRwMAEKAQEANRLNAENEKDSRRR-QARLQKELAEAAKEPLPV 234
Cdd:COG4372   121 QKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ-LESLQEELAALEQELQALSEAEaEQALDELLKEANRNAEKE 199

                         170       180       190
                  ....*....|....*....|....*....|
gi 1393169536 235 EQDDDIEVIVDETSDHTEETSPVRAISRAA 264
Cdd:COG4372   200 EELAEAEKLIESLPRELAEELLEAKDSLEA 229
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 332-367 8.01e-08

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 48.46  E-value: 8.01e-08
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1393169536  332 LCVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWE 367
Cdd:smart00320   5 LKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
332-367 2.79e-07

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 46.95  E-value: 2.79e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1393169536 332 LCVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWE 367
Cdd:pfam00400   4 LKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 160-578 1.47e-06

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 51.24  E-value: 1.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536 160 QTLKDEYDALQITFTALEGKLRKTTEENQELVTRWMAEKAQEANRlnaenekdSRRRQARLQKElAEAAKEPLPVEQDDD 239
Cdd:PLN00181  303 QRKQEAADKLQDTISLLSSDIDQVVKRQLVLQQKGSDVRSFLASR--------KRIRQGAETLA-AEEENDDNSSKLDDT 373

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536 240 IEVIVDETSDHTEETSPVRAISRAATKRLSQPAGGLLDSITNifglsESPLLGHHSSSDAARRRSVSSFPVPQDNVDTHP 319
Cdd:PLN00181  374 LESTLLESSRLMRNLKKLESVYFATRYRQIKAAAAAEKPLAR-----YYSALSENGRSSEKSSMSNPAKPPDFYINDSRQ 448

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536 320 G--------------SGKEVRVPAtalcvfDAHDGE-------VNAVQFSPGSRLLATGGMDRRVKLWEVF-----GEKC 373
Cdd:PLN00181  449 GgwidpfleglckylSFSKLRVKA------DLKQGDllnssnlVCAIGFDRDGEFFATAGVNKKIKIFECEsiikdGRDI 522

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536 374 EFKGSLSGSNAGITSIEFDSAGSYLLAASN-DFASRIWTVDDYRLRHTLTGHSGKVLSAKFL-LDNARIVSGSHDRTLKL 451
Cdd:PLN00181  523 HYPVVELASRSKLSGICWNSYIKSQVASSNfEGVVQVWDVARSQLVTEMKEHEKRVWSIDYSsADPTLLASGSDDGSVKL 602

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536 452 WDLRSKVCIKTVfagSSCNDIVCTE------QCVMSGHFDKKIRFWDIRSESI-VREMELLGKITALDLNPERTELLSCS 524
Cdd:PLN00181  603 WSINQGVSIGTI---KTKANICCVQfpsesgRSLAFGSADHKVYYYDLRNPKLpLCTMIGHSKTVSYVRFVDSSTLVSSS 679

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1393169536 525 RDDLLKVIDLRTNA--IKQT--FSAPGFKCGSDWTRVVFSpDGsYVAAGSAEGSLYIW 578
Cdd:PLN00181  680 TDNTLKLWDLSMSIsgINETplHSFMGHTNVKNFVGLSVS-DG-YIATGSETNEVFVY 735
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 83-230 2.23e-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: 2.23e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536   83 QEMAQLRIKHQeeltELHKKRGELAQLVIDLNNQMQRKDREMQMNEAKIAECLQTISDLETECLDLRTKLCDLERANQTL 162
Cdd:TIGR02168  267 EKLEELRLEVS----ELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAEL 342

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1393169536  163 KDEYDALQITFTALEGKLRKTTEENQELVTRWmAEKAQEANRLNAEnEKDSRRRQARLQKELAEAAKE 230
Cdd:TIGR02168  343 EEKLEELKEELESLEAELEELEAELEELESRL-EELEEQLETLRSK-VAQLELQIASLNNEIERLEAR 408
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
46-230 2.19e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 44.26  E-value: 2.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536  46 SDLHSVLAQKLQAEKHDVPNRHEispghdgtwndnqlQEMAQLR--IKHQEELTELHKKRGELAQLVIDLNNQMQRkdrE 123
Cdd:PRK02224  190 DQLKAQIEEKEEKDLHERLNGLE--------------SELAELDeeIERYEEQREQARETRDEADEVLEEHEERRE---E 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536 124 MQMNEAKIAECLQTISDLETECLDLRTKLCDLERANQTLKDEYDAL--QITFTALEGK----LRKTTEENQELVTRWMAE 197
Cdd:PRK02224  253 LETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLlaEAGLDDADAEaveaRREELEDRDEELRDRLEE 332

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1393169536 198 KAQEANRLN------AENEKDSRRRQARLQKELAEAAKE 230
Cdd:PRK02224  333 CRVAAQAHNeeaeslREDADDLEERAEELREEAAELESE 371
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
217-621 6.15e-61

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 208.23  E-value: 6.15e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536 217 QARLQKELAEAAKEPLPVEQDDDIEVIVDETSDHTEETSPVRAISRAATKRLSQPAGGLLDSITNIFGLSESPLLGHHSS 296
Cdd:COG2319     1 ALSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536 297 SDAARRRsvssfpvPQDNVDTHPGSGKEVRV----PATALCVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWEVFGEK 372
Cdd:COG2319    81 VLSVAFS-------PDGRLLASASADGTVRLwdlaTGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGK 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536 373 CEfkGSLSGSNAGITSIEFDSAGSYLLAASNDFASRIWTVDDYRLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLW 452
Cdd:COG2319   154 LL--RTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLW 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536 453 DLRSKVCIKTV-FAGSSCNDIVCT--EQCVMSGHFDKKIRFWDIRSESIVREME-LLGKITALDLNPERTELLSCSRDDL 528
Cdd:COG2319   232 DLATGKLLRTLtGHSGSVRSVAFSpdGRLLASGSADGTVRLWDLATGELLRTLTgHSGGVNSVAFSPDGKLLASGSDDGT 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536 529 LKVIDLRTNAIKQTFSAPgfkcGSDWTRVVFSPDGSYVAAGSAEGSLYIWSVLTGKVEKVLsKQHSSSINAVAWSPSGSH 608
Cdd:COG2319   312 VRLWDLATGKLLRTLTGH----TGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTL-TGHTGAVTSVAFSPDGRT 386

                         410
                  ....*....|...
gi 1393169536 609 VVSVDKGCKAVLW 621
Cdd:COG2319   387 LASGSADGTVRLW 399
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 332-622 2.85e-58

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: 197.56  E-value: 2.85e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536 332 LCVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWEVfgEKCEFKGSLSGSNAGITSIEFDSAGSYLLAASNDFASRIWT 411
Cdd:cd00200     2 RRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDL--ETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536 412 VDDYRLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTvFAG----------SSCNDIVCteqcvmS 481
Cdd:cd00200    80 LETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTT-LRGhtdwvnsvafSPDGTFVA------S 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536 482 GHFDKKIRFWDIRSESIVREMEL-LGKITALDLNPERTELLSCSRDDLLKVIDLRTNAIKQTFSAPgfkcgSDW-TRVVF 559
Cdd:cd00200   153 SSQDGTIKLWDLRTGKCVATLTGhTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGH-----ENGvNSVAF 227

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1393169536 560 SPDGSYVAAGSAEGSLYIWSVLTGKVEKVLSkQHSSSINAVAWSPSGSHVVSVDKGCKAVLWA 622
Cdd:cd00200   228 SPDGYLLASGSEDGTIRVWDLRTGECVQTLS-GHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 31-206 7.86e-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: 192.07  E-value: 7.86e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536  31 AFEEIILQYNKLLEKSDLHSVLAQKLQAEKHDVPNRHEISPGHDGTWNDNQLQEMAQLRIKHQEELTELHKKRGELAQLV 110
Cdd:pfam08614   1 AFLELIDAYNRLLDRTALLEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQLREELAELYRSRGELAQRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536 111 IDLNNQMQRKDREMQMNEAKIAECLQTISDLETECLDLRTKLCDLERANQTLKDEYDALQITFTALEGKLRKTTEENQEL 190
Cdd:pfam08614  81 VDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQDELVALQLQLNMAEEKLRKLEKENREL 160

                         170
                  ....*....|....*.
gi 1393169536 191 VTRWMAEKAQEANRLN 206
Cdd:pfam08614 161 VERWMKRKGQEAEAMN 176
WD40 COG2319
WD40 repeat [General function prediction only];
320-580 6.85e-49

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 175.48  E-value: 6.85e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536 320 GSGKEVRV----PATALCVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWEVFGEKCEFkgSLSGSNAGITSIEFDSAG 395
Cdd:COG2319   139 SADGTVRLwdlaTGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLR--TLTGHTGAVRSVAFSPDG 216

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536 396 SYLLAASNDFASRIWTVDDYRLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTvFAGSSC--NDIV 473
Cdd:COG2319   217 KLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRT-LTGHSGgvNSVA 295

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536 474 CT--EQCVMSGHFDKKIRFWDIRSESIVREME-LLGKITALDLNPERTELLSCSRDDLLKVIDLRTNAIKQTFSAPgfkc 550
Cdd:COG2319   296 FSpdGKLLASGSDDGTVRLWDLATGKLLRTLTgHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGH---- 371

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1393169536 551 gSDW-TRVVFSPDGSYVAAGSAEGSLYIWSV 580
Cdd:COG2319   372 -TGAvTSVAFSPDGRTLASGSADGTVRLWDL 401
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 417-621 2.94e-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: 134.77  E-value: 2.94e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536 417 LRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTV----FAGSSCNDIVCTEQCVmSGHFDKKIRFWD 492
Cdd:cd00200     1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLkghtGPVRDVAASADGTYLA-SGSSDKTIRLWD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536 493 IRSESIVREMEL-LGKITALDLNPERTELLSCSRDDLLKVIDLRTNAIKQTFSAPgfkcgSDWTR-VVFSPDGSYVAAGS 570
Cdd:cd00200    80 LETGECVRTLTGhTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGH-----TDWVNsVAFSPDGTFVASSS 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1393169536 571 AEGSLYIWSVLTGKVEKVLsKQHSSSINAVAWSPSGSHVV--SVDKGCKavLW 621
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 9.29e-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: 112.66  E-value: 9.29e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536 120 KDREMQMNEAKIAECLQTISDLETECLDLRTKLCDLERANQTLKDEYDALQITFTALEGKLRKTTEENQELVTRWMAEKA 199
Cdd:cd22887     2 LESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEENDELVERWMAKKQ 81

                          90
                  ....*....|
gi 1393169536 200 QEANRLNAEN 209
Cdd:cd22887    82 QEADKMNEAN 91
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
79-264 5.46e-08

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 55.29  E-value: 5.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536  79 DNQLQEMAQLRIKHQEELTELHKKRGELAQL---VIDLNNQMQRKDREMQMNEAKIAECLQTISDLETECLDLRTKLCDL 155
Cdd:COG4372    41 DKLQEELEQLREELEQAREELEQLEEELEQArseLEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEEL 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536 156 ERANQTLKDEYDALQITFTALEGKLRKTTEENQELVTRwMAEKAQEANRLNAENEKDSRRR-QARLQKELAEAAKEPLPV 234
Cdd:COG4372   121 QKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ-LESLQEELAALEQELQALSEAEaEQALDELLKEANRNAEKE 199

                         170       180       190
                  ....*....|....*....|....*....|
gi 1393169536 235 EQDDDIEVIVDETSDHTEETSPVRAISRAA 264
Cdd:COG4372   200 EELAEAEKLIESLPRELAEELLEAKDSLEA 229
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 332-367 8.01e-08

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 48.46  E-value: 8.01e-08
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1393169536  332 LCVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWE 367
Cdd:smart00320   5 LKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 416-453 1.86e-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: 1.86e-07
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1393169536  416 RLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWD 453
Cdd:smart00320   3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
332-367 2.79e-07

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 46.95  E-value: 2.79e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1393169536 332 LCVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWE 367
Cdd:pfam00400   4 LKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 pfam00400
WD domain, G-beta repeat;
416-453 5.03e-07

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 46.18  E-value: 5.03e-07
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1393169536 416 RLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWD 453
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
88-238 1.35e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 51.31  E-value: 1.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536  88 LRIKHQEELTELHKKRGELAQLVIDLNNQMQRKDREMQMNEAKIAECLQTISDLETECLDLRTKLCDLERANQTLKDEYD 167
Cdd:COG4717    47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1393169536 168 ALQitftaLEGKLRKTTEENQELVTRWMAEKAQEANRLNAENEKDSRRRQ-ARLQKELAEAAKEPLPVEQDD 238
Cdd:COG4717   127 LLP-----LYQELEALEAELAELPERLEELEERLEELRELEEELEELEAElAELQEELEELLEQLSLATEEE 193
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 160-578 1.47e-06

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 51.24  E-value: 1.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536 160 QTLKDEYDALQITFTALEGKLRKTTEENQELVTRWMAEKAQEANRlnaenekdSRRRQARLQKElAEAAKEPLPVEQDDD 239
Cdd:PLN00181  303 QRKQEAADKLQDTISLLSSDIDQVVKRQLVLQQKGSDVRSFLASR--------KRIRQGAETLA-AEEENDDNSSKLDDT 373

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536 240 IEVIVDETSDHTEETSPVRAISRAATKRLSQPAGGLLDSITNifglsESPLLGHHSSSDAARRRSVSSFPVPQDNVDTHP 319
Cdd:PLN00181  374 LESTLLESSRLMRNLKKLESVYFATRYRQIKAAAAAEKPLAR-----YYSALSENGRSSEKSSMSNPAKPPDFYINDSRQ 448

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536 320 G--------------SGKEVRVPAtalcvfDAHDGE-------VNAVQFSPGSRLLATGGMDRRVKLWEVF-----GEKC 373
Cdd:PLN00181  449 GgwidpfleglckylSFSKLRVKA------DLKQGDllnssnlVCAIGFDRDGEFFATAGVNKKIKIFECEsiikdGRDI 522

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536 374 EFKGSLSGSNAGITSIEFDSAGSYLLAASN-DFASRIWTVDDYRLRHTLTGHSGKVLSAKFL-LDNARIVSGSHDRTLKL 451
Cdd:PLN00181  523 HYPVVELASRSKLSGICWNSYIKSQVASSNfEGVVQVWDVARSQLVTEMKEHEKRVWSIDYSsADPTLLASGSDDGSVKL 602

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536 452 WDLRSKVCIKTVfagSSCNDIVCTE------QCVMSGHFDKKIRFWDIRSESI-VREMELLGKITALDLNPERTELLSCS 524
Cdd:PLN00181  603 WSINQGVSIGTI---KTKANICCVQfpsesgRSLAFGSADHKVYYYDLRNPKLpLCTMIGHSKTVSYVRFVDSSTLVSSS 679

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1393169536 525 RDDLLKVIDLRTNA--IKQT--FSAPGFKCGSDWTRVVFSpDGsYVAAGSAEGSLYIW 578
Cdd:PLN00181  680 TDNTLKLWDLSMSIsgINETplHSFMGHTNVKNFVGLSVS-DG-YIATGSETNEVFVY 735
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 83-230 2.23e-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: 2.23e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536   83 QEMAQLRIKHQeeltELHKKRGELAQLVIDLNNQMQRKDREMQMNEAKIAECLQTISDLETECLDLRTKLCDLERANQTL 162
Cdd:TIGR02168  267 EKLEELRLEVS----ELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAEL 342

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1393169536  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 2.74e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.71  E-value: 2.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536  81 QLQEMAQLRIKHQEELTELHKKRGEL-------AQLVIDLNNQMQRKDREMQMNEAKIAECLQTISDLETECLDLRTKLC 153
Cdd:COG1196   275 ELEELELELEEAQAEEYELLAELARLeqdiarlEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536 154 DLERANQTLKDEYDALQITFTALEGKLRKTTEENQELVTRWMAEKAQEANRlnAENEKDSRRRQARLQKELAEAAKEPLP 233
Cdd:COG1196   355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL--EEAEEALLERLERLEEELEELEEALAE 432

                         170       180
                  ....*....|....*....|
gi 1393169536 234 VEQDDDIEVIVDETSDHTEE 253
Cdd:COG1196   433 LEEEEEEEEEALEEAAEEEA 452
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
375-583 4.71e-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: 4.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536 375 FKGSLSGSNAGITSIEFDSAGSYLLAASNDFASRIWTVDDYRLRHTLTGHSGKVLSAKFLLDNARI-VSGSHDRTLKLWD 453
Cdd:COG3391    17 ALAALAVAVAALGLGGGGPLLAAASGGVVGAAVGGGGVALLAGLGLGAAAVADADGADAGADGRRLyVANSGSGRVSVID 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536 454 LRSKVCIKTVFAGSSCNDIVCTE---QCVMSGHFDKKIRFWDIRSESIVREMELLGKITALDLNPERTELLSCSRDD--- 527
Cdd:COG3391    97 LATGKVVATIPVGGGPRGLAVDPdggRLYVADSGNGRVSVIDTATGKVVATIPVGAGPHGIAVDPDGKRLYVANSGSntv 176

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1393169536 528 --LLKVIDLRTNAIKQTFSApgfkcGSDWTRVVFSPDGS--YVA------AGSAEGSLYIWSVLTG 583
Cdd:COG3391   177 svIVSVIDTATGKVVATIPV-----GGGPVGVAVSPDGRrlYVAnrgsntSNGGSNTVSVIDLATL 237
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 79-230 2.53e-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: 46.07  E-value: 2.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536  79 DNQLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQRKDREMQMNEAKIAECLQTISDLET---------ECLDLR 149
Cdd:COG1579    16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlgnvrnnkEYEALQ 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536 150 TKLCDLERANQTLKDEYDALQITFTALEGKLRKTTEENQELVTRWmAEKAQEANRLNAENEKDsrrrQARLQKELAEAAK 229
Cdd:COG1579    96 KEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAEL-EEKKAELDEELAELEAE----LEELEAEREELAA 170


                  .
gi 1393169536 230 E 230
Cdd:COG1579   171 K 171
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 41-221 3.21e-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: 47.09  E-value: 3.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536   41 KLLEK--SDLHSVLAQKLQAEKH--DVPNRHE--ISPGHDGTWNDNQL-QEMAQLRIKHQEELTELHKKRGELAQLVIDL 113
Cdd:pfam01576  155 KLLEEriSEFTSNLAEEEEKAKSlsKLKNKHEamISDLEERLKKEEKGrQELEKAKRKLEGESTDLQEQIAELQAQIAEL 234

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536  114 NNQMQRKDREMQMNEAKIAE-------CLQTISDLETECLDLRTKLcDLERANQT--------LKDEYDALQitfTALEG 178
Cdd:pfam01576  235 RAQLAKKEEELQAALARLEEetaqknnALKKIRELEAQISELQEDL-ESERAARNkaekqrrdLGEELEALK---TELED 310

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1393169536  179 KLrKTTEENQELVTRwmaeKAQEANRLNAENEKDSRRRQARLQ 221
Cdd:pfam01576  311 TL-DTTAAQQELRSK----REQEVTELKKALEEETRSHEAQLQ 348
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 114-266 4.35e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.97  E-value: 4.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536  114 NNQMQRKDREMQMNEAKIAECLQTISDLETECLDLRTKLCDLERANQTLKDEYDALQITFTALEGKLRKTTEEnQELVTR 193
Cdd:TIGR02168  669 NSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE-VEQLEE 747

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1393169536  194 WMAEKAQEANRLNAE-NEKDSRRRQARLQKELAEAAKEPLPVEQDDDIEVIVDETSDHTEETSPVRAISRAATK 266
Cdd:TIGR02168  748 RIAQLSKELTELEAEiEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAAN 821
TolB COG0823
Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, ...
 531-610 4.35e-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: 4.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536 531 VIDLRTNAIKQTFSAPGFKCGSDWtrvvfSPDGSYVAAGSAEGS---LYIWSVLTGKVEKVLSKQHSSSinAVAWSPSGS 607
Cdd:COG0823    15 VVDLDGGEPRRLTNSPGIDTSPAW-----SPDGRRIAFTSDRGGgpqIYVVDADGGEPRRLTFGGGYNA--SPSWSPDGK 87


                  ...
gi 1393169536 608 HVV 610
Cdd:COG0823    88 RLA 90
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 83-270 4.46e-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: 46.60  E-value: 4.46e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536   83 QEMAQLRIKHQEELTELHKKRGELAQLVIDLnnQMQRKDREMQMNEakiaeclqtISDLETECLDLRTKLCDLERANQTL 162
Cdd:TIGR02169  315 RELEDAEERLAKLEAEIDKLLAEIEELEREI--EEERKRRDKLTEE---------YAELKEELEDLRAELEEVDKEFAET 383

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536  163 KDEYDALQitfTALEGKLRKTTEENQELVTRWMAEKAQEANRLNAENE-KDSRRRQARLQKELAEAAKEPLPVEQddDIE 241
Cdd:TIGR02169  384 RDELKDYR---EKLEKLKREINELKRELDRLQEELQRLSEELADLNAAiAGIEAKINELEEEKEDKALEIKKQEW--KLE 458

                          170       180
                   ....*....|....*....|....*....
gi 1393169536  242 VIVDETSDHTEETSPVRAISRAATKRLSQ 270
Cdd:TIGR02169  459 QLAADLSKYEQELYDLKEEYDRVEKELSK 487
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 79-253 4.50e-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: 4.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536   79 DNQLQEMAQLRIKH---QEELTELHKKRGELAQLVIDLNNQMQRKDREMQMNEAKIAECLQTISDLETECLDLRTKLCDL 155
Cdd:TIGR02168  792 EQLKEELKALREALdelRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL 871

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536  156 --------------ERANQTLKDEYDALQITFTALEGKLRKTTEENQELvtrwMAEKAQEANRLN-AENEKDSRRRQARL 220
Cdd:TIGR02168  872 eseleallneraslEEALALLRSELEELSEELRELESKRSELRRELEEL----REKLAQLELRLEgLEVRIDNLQERLSE 947

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1393169536  221 QKELAEAAKEPLPVEQDDDIEVIVDETSDHTEE 253
Cdd:TIGR02168  948 EYSLTLEEAEALENKIEDDEEEARRRLKRLENK 980
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 81-274 5.19e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 5.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536  81 QLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQRKDREMQMNEAKIAECLQTISDLETECLDLRTKLCDLERANQ 160
Cdd:COG1196   331 ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536 161 TLKDEYDALQitftalegklrkttEENQELVTrwmAEKAQEANRLNAENEKDSRRRQARLQKELAEAAKEPL--PVEQDD 238
Cdd:COG1196   411 ALLERLERLE--------------EELEELEE---ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLaeLLEEAA 473

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1393169536 239 DIEVIVDETSDHTEETSPVRAISRAATKRLSQPAGG 274
Cdd:COG1196   474 LLEAALAELLEELAEAAARLLLLLEAEADYEGFLEG 509
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 79-249 5.71e-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: 46.21  E-value: 5.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536   79 DNQLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQRKDREMQMN--------EAKIAECLQTISDLETEcldlrt 150
Cdd:TIGR02169  243 ERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRvkekigelEAEIASLERSIAEKERE------ 316

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536  151 kLCDLERANQTLKDEYDALQITFTALEGKLR-------KTTEENQELVTRwMAEKAQEANRLNAENeKDSRRRQARLQKE 223
Cdd:TIGR02169  317 -LEDAEERLAKLEAEIDKLLAEIEELEREIEeerkrrdKLTEEYAELKEE-LEDLRAELEEVDKEF-AETRDELKDYREK 393

                          170       180
                   ....*....|....*....|....*...
gi 1393169536  224 LAEAAKE--PLPVEQDDDIEVIVDETSD 249
Cdd:TIGR02169  394 LEKLKREinELKRELDRLQEELQRLSEE 421
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
46-230 2.19e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 44.26  E-value: 2.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536  46 SDLHSVLAQKLQAEKHDVPNRHEispghdgtwndnqlQEMAQLR--IKHQEELTELHKKRGELAQLVIDLNNQMQRkdrE 123
Cdd:PRK02224  190 DQLKAQIEEKEEKDLHERLNGLE--------------SELAELDeeIERYEEQREQARETRDEADEVLEEHEERRE---E 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536 124 MQMNEAKIAECLQTISDLETECLDLRTKLCDLERANQTLKDEYDAL--QITFTALEGK----LRKTTEENQELVTRWMAE 197
Cdd:PRK02224  253 LETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLlaEAGLDDADAEaveaRREELEDRDEELRDRLEE 332

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1393169536 198 KAQEANRLN------AENEKDSRRRQARLQKELAEAAKE 230
Cdd:PRK02224  333 CRVAAQAHNeeaeslREDADDLEERAEELREEAAELESE 371
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
80-262 2.21e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.74  E-value: 2.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536  80 NQLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQRKDREMQMNEAKIAECLQTISDLETECLDLRTKLCDLERAN 159
Cdd:COG4372    87 EQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEEL 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536 160 QTLKDEYDALQITFTALEGKLRKTTEENQELVTRWMAEKAQEANRLNAENEKDSRRRQARLQKELAEAAKEPLPVEQDDD 239
Cdd:COG4372   167 AALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEE 246

                         170       180
                  ....*....|....*....|...
gi 1393169536 240 IEVIVDETSDHTEETSPVRAISR 262
Cdd:COG4372   247 DKEELLEEVILKEIEELELAILV 269
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 582-621 2.71e-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: 2.71e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1393169536  582 TGKVEKVLsKQHSSSINAVAWSPSGSHVVSVDKGCKAVLW 621
Cdd:smart00320   1 SGELLKTL-KGHTGPVTSVAFSPDGKYLASGSDDGTIKLW 39
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 80-253 2.76e-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: 43.86  E-value: 2.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536  80 NQLQEMaqlrikhQEELTELHKKRGElaQLVIDLNNQMQRKDREMQM-------NEAKIAECLQTISDLETECLDLRT-- 150
Cdd:TIGR04523 288 KQLNQL-------KSEISDLNNQKEQ--DWNKELKSELKNQEKKLEEiqnqisqNNKIISQLNEQISQLKKELTNSESen 358

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536 151 ------------KLCDLERANQTLKDEYDALQITFTALEGKLRKTTEENQELvtrwmaekaqEANRLNAENEKDSRRRQA 218
Cdd:TIGR04523 359 sekqreleekqnEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQK----------DEQIKKLQQEKELLEKEI 428

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1393169536 219 RLQKELAEAAKEPLP--VEQDDDIEVIVDETSDHTEE 253
Cdd:TIGR04523 429 ERLKETIIKNNSEIKdlTNQDSVKELIIKNLDNTRES 465
COG4946 COG4946
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown] ...
 558-606 3.54e-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: 3.54e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1393169536  558 VFSPDGSYVAAGSAEGSLYIWSVLTGKVEKVLSKQHSSSINAVAWSPSG 606
Cdd:COG4946    395 VWSPDGKKIAFTDNRGRLWVVDLASGKVRKVDTDGYGDGISDLAWSPDS 443
TolB COG0823
Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, ...
 531-621 4.48e-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: 4.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536 531 VIDLRTNAIKQ-TFSapgfkcGSDWTRVVFSPDGSYVA-AGSAEGSLYIWSV-LTGKVEKVLSKqhssSINAVAWSPSGS 607
Cdd:COG0823    59 VVDADGGEPRRlTFG------GGYNASPSWSPDGKRLAfVSRSDGRFDIYVLdLDGGAPRRLTD----GPGSPSWSPDGR 128

                          90
                  ....*....|....*
gi 1393169536 608 HVV-SVDKGCKAVLW 621
Cdd:COG0823   129 RIVfSSDRGGRPDLY 143
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
78-241 5.39e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 5.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536   78 NDNQLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQ--RKDREMQMNEAKIAECLQTISDLETECLDLRTKLCDL 155
Cdd:COG4913    608 NRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREalQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDL 687

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536  156 ERANQTLKD---EYDALQITFTALEGKLRKTTEENQELVTRWmaekAQEANRLNAENEKDSRRRQARLQKELAEAAKEPL 232
Cdd:COG4913    688 AALEEQLEEleaELEELEEELDELKGEIGRLEKELEQAEEEL----DELQDRLEAAEDLARLELRALLEERFAAALGDAV 763


                   ....*....
gi 1393169536  233 PVEQDDDIE 241
Cdd:COG4913    764 ERELRENLE 772
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 14-232 6.23e-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: 43.12  E-value: 6.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536   14 KRHISEQLRRRDRLQRQAFEEIILQYNKLLEKS-DLHSVLAQK--LQAEKHDVPNRHEISpghdgtwnDNQLQEMAQLRI 90
Cdd:TIGR02168  304 KQILRERLANLERQLEELEAQLEELESKLDELAeELAELEEKLeeLKEELESLEAELEEL--------EAELEELESRLE 375

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536   91 KHQEELTELHKKRGELAQLVIDLNNQMQRKDREMQMNEAKIAECLQTISDLETECLDLRTKLCDLERAnqTLKDEYDALQ 170
Cdd:TIGR02168  376 ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELE--ELEEELEELQ 453

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1393169536  171 ITFTALEGKLRKTTEENQELvTRWMAEKAQEANRLNAenEKDSRRRQARLQKELAEAAKEPL 232
Cdd:TIGR02168  454 EELERLEEALEELREELEEA-EQALDAAERELAQLQA--RLDSLERLQENLEGFSEGVKALL 512
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 27-270 1.32e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.85  E-value: 1.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536  27 LQRQA----------FEEIILQYNKLLEKSDLHSVLAQKLQAEKHDVPNRHEispgHDGTWNDNQLQEMAQLRIKHQEEL 96
Cdd:COG1196   205 LERQAekaeryrelkEELKELEAELLLLKLRELEAELEELEAELEELEAELE----ELEAELAELEAELEELRLELEELE 280

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536  97 TELHKKRGELAQL---VIDLNNQMQRKDREMQMNEAKIAECLQTISDLETECLDLRTKLCDLERANQTLKDEYDALQITF 173
Cdd:COG1196   281 LELEEAQAEEYELlaeLARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536 174 TALEGKLRKTTEENQELVTRWMAEKAQEANRLNAENEKDSRRRQARLQKELAEAAKEPLPVEQDDDIEVIVDETSDHTEE 253
Cdd:COG1196   361 AEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE 440

                         250
                  ....*....|....*..
gi 1393169536 254 TSPVRAISRAATKRLSQ 270
Cdd:COG1196   441 EEALEEAAEEEAELEEE 457
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 43-215 2.84e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.82  E-value: 2.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536   43 LEKSDLHSVLaQKLQAEKHDVpnRHEISPghdgtwNDNQLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQRKDR 122
Cdd:TIGR02169  784 LEARLSHSRI-PEIQAELSKL--EEEVSR------IEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEK 854

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536  123 EMQMNEAKIAECLQTISDLETECLDLRTKLCDLERANQTLKDEYDALQITFTALEGKLRKTTEENQELvtrwmAEKAQEA 202
Cdd:TIGR02169  855 EIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSEL-----KAKLEAL 929

                          170
                   ....*....|...
gi 1393169536  203 NRLNAENEKDSRR 215
Cdd:TIGR02169  930 EEELSEIEDPKGE 942
COG4946 COG4946
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown] ...
 557-621 3.20e-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: 3.20e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1393169536  557 VVFSPDGSYVAAGS-AEGS--LYIWSVLTGKVEKVLSKQHSSSINAVAWSPSGSHVVSVDKGCKavLW 621
Cdd:COG4946    348 PAWSPDGKSIAYFSdASGEyeLYIAPADGSGEPKQLTLGDLGRVFNPVWSPDGKKIAFTDNRGR--LW 413
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 91-226 3.23e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.82  E-value: 3.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536   91 KHQEELTELhKKRGELAQLVID-LNNQMQRKDREMQMNEakiaeclqtisdletECLDLRTKLCDLE-----RANQTLKD 164
Cdd:TIGR02169  174 KALEELEEV-EENIERLDLIIDeKRQQLERLRREREKAE---------------RYQALLKEKREYEgyellKEKEALER 237

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1393169536  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, ...
 114-270 3.52e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.13  E-value: 3.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536 114 NNQMQRKDREMQMNEAKIAECLQTISDLETECLDLRTKLCDLERANQTLKDEYDALQITFTALEGKLRKTTEENQELVTR 193
Cdd:COG4942    19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536 194 WMAEKAQEANR----------------LNAENEKDSRRRQARLQ------KELAEAAKeplpvEQDDDIEVIVDETSDHT 251
Cdd:COG4942    99 LEAQKEELAELlralyrlgrqpplallLSPEDFLDAVRRLQYLKylaparREQAEELR-----ADLAELAALRAELEAER 173

                         170
                  ....*....|....*....
gi 1393169536 252 EETSPVRAISRAATKRLSQ 270
Cdd:COG4942   174 AELEALLAELEEERAALEA 192
COG4946 COG4946
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown] ...
 505-608 4.46e-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: 4.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536  505 LGKITALDLNPERTELLSCSRDDLLKVIDLRTNAIKQTFSAPGFKCGSDwtrVVFSPDGSYVA----AGSAEGSLYIWSV 580
Cdd:COG4946    388 LGRVFNPVWSPDGKKIAFTDNRGRLWVVDLASGKVRKVDTDGYGDGISD---LAWSPDSKWLAyskpGPNQLSQIFLYDV 464

                           90       100
                   ....*....|....*....|....*...
gi 1393169536  581 LTGKVEKVLSKQHSSSinAVAWSPSGSH 608
Cdd:COG4946    465 ETGKTVQLTDGRYDDG--SPAFSPDGKY 490
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 54-211 4.70e-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: 40.03  E-value: 4.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536   54 QKLQAEKHDVPNRHE-ISPGHDGTWNDNQLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQ---MQRKDREMQMNEA 129
Cdd:TIGR00606  795 ERFQMELKDVERKIAqQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQiqhLKSKTNELKSEKL 874

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536  130 KIAECLQTISDLETECLDLRTKLCDLERANQTLKDEydalqitFTALEGKLRKTTEENQELVTRWMAEKAQEANRLNAEN 209
Cdd:TIGR00606  875 QIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQ-------DSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIK 947


                   ..
gi 1393169536  210 EK 211
Cdd:TIGR00606  948 EK 949
PRK12704 PRK12704
phosphodiesterase; Provisional
 83-204 4.89e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 39.76  E-value: 4.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536  83 QEMAQLRIKHQEELTElhkKRGELAQL---VID----LNNQMQ---RKDREMQMNEAKIAECLQTISDLETECLDLRTKL 152
Cdd:PRK12704   64 EEIHKLRNEFEKELRE---RRNELQKLekrLLQkeenLDRKLElleKREEELEKKEKELEQKQQELEKKEEELEELIEEQ 140

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1393169536 153 CD-LERANQTLKDEydALQITFTALEGKLRkttEENQELVTRWMAEKAQEANR 204
Cdd:PRK12704  141 LQeLERISGLTAEE--AKEILLEKVEEEAR---HEAAVLIKEIEEEAKEEADK 188
Ge1_WD40 pfam16529
WD40 region of Ge1, enhancer of mRNA-decapping protein; Ge1_WD40 is the N-terminal region of ...
 382-463 5.17e-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: 5.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536 382 SNAGITSIEFDSAGSYLLAASNDFASRIWTV-----DDYRLRHTLTGHSGKVLSAKFLLDNAR----------IVSGS-H 445
Cdd:pfam16529 185 EHSLLVDAAFSPDGTALATASLDGEVKFFQIylfdnRNPRCLHEWKPHDGKPLSSLFFLDNHKkppevqfwrfAITGAdN 264

                          90
                  ....*....|....*...
gi 1393169536 446 DRTLKLWDLRSKVCIKTV 463
Cdd:pfam16529 265 NSELKLWSCESWTCLQTI 282
ADIP pfam11559
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ...
 117-226 5.72e-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: 37.68  E-value: 5.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536 117 MQRKDREMQMNEAKiaecLQTISDLETECLDLR-------TKLCDLERANQTLKDEYDALQITFTALEGKLRKTTEENQE 189
Cdd:pfam11559  44 LQQRDRDLEFRESL----NETIRTLEAEIERLQskierlkTQLEDLERELALLQAKERQLEKKLKTLEQKLKNEKEELQR 119

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1393169536 190 LVTRWMAEKAQeanrlnAENEKDSRRRQ-ARLQKELAE 226
Cdd:pfam11559 120 LKNALQQIKTQ------FAHEVKKRDREiEKLKERLAQ 151
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 555-579 6.58e-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: 6.58e-03
                           10        20
                   ....*....|....*....|....*
gi 1393169536  555 TRVVFSPDGSYVAAGSAEGSLYIWS 579
Cdd:smart00320  16 TSVAFSPDGKYLASGSDDGTIKLWD 40
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 78-186 7.03e-03

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


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 38.35  E-value: 7.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536  78 NDNQLQEMAQLRIKHQEELTELHKKRGELAQlviDLNNQmqRKDRE-MQMNEAKIAECLQTISDLETECLDLRTKLCDLE 156
Cdd:pfam13851  45 NEKLMSEIQQENKRLTEPLQKAQEEVEELRK---QLENY--EKDKQsLKNLKARLKVLEKELKDLKWEHEVLEQRFEKVE 119

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1393169536 157 RANQTLKDE-----YDALQITF---TALEGKLRKTTEE 186
Cdd:pfam13851 120 RERDELYDKfeaaiQDVQQKTGlknLLLEKKLQALGET 157
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 86-230 7.30e-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: 7.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536  86 AQLRIKHQEELTELHKKRGELAQLVIDLNNQMQRKDREMQMNEAKIAECLQTISDLETECLDLRTKLCDLERANQTLKDE 165
Cdd:COG4942    19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1393169536 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 7.78e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.51  E-value: 7.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536   79 DNQLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQRKD-REMQMNEAKIAECLQTISDLETECLDLRTKLCDLER 157
Cdd:COG4913    294 EAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGL 373

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536  158 ANQTLKDEYDALQITFTALEGKLRKTTEENQELVTRWMAEKaqeanrlnaeneKDSRRRQARLQKELA--EAAKEPLPVE 235
Cdd:COG4913    374 PLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAAL------------RDLRRELRELEAEIAslERRKSNIPAR 441

                          170
                   ....*....|....*...
gi 1393169536  236 QDDDIEVIVDETSDHTEE 253
Cdd:COG4913    442 LLALRDALAEALGLDEAE 459
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
80-208 8.95e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 38.74  E-value: 8.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536  80 NQLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQRKDREMQMNEAK---IAECLQTISDLE----TECLD----- 147
Cdd:COG1340    57 EEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAggsIDKLRKEIERLEwrqqTEVLSpeeek 136

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1393169536 148 --------LRTKLCDLERAN------QTLKDEYDALQITFTALEGKLRKTTEENQELVTRwMAEKAQEANRLNAE 208
Cdd:COG1340   137 elvekikeLEKELEKAKKALekneklKELRAELKELRKEAEEIHKKIKELAEEAQELHEE-MIELYKEADELRKE 210
46 PHA02562
endonuclease subunit; Provisional
 80-244 9.83e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 38.84  E-value: 9.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536  80 NQLQEMAQLRIKHQEELTELHKKrgeLAQLVIDLNNQMQRKDREMQMNE--AKIAECLQTISD-------LETECLDLRT 150
Cdd:PHA02562  237 EELTDELLNLVMDIEDPSAALNK---LNTAAAKIKSKIEQFQKVIKMYEkgGVCPTCTQQISEgpdritkIKDKLKELQH 313

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393169536 151 KLCDLERANQTLK---DEYDALQITFTALEGKLRKtteENQELVT-RWMAEKAQEA-NRLNAENeKDSRRRQARLQKELA 225
Cdd:PHA02562  314 SLEKLDTAIDELEeimDEFNEQSKKLLELKNKIST---NKQSLITlVDKAKKVKAAiEELQAEF-VDNAEELAKLQDELD 389

                         170
                  ....*....|....*....
gi 1393169536 226 EAAKEPLPVEQDDDIEVIV 244
Cdd:PHA02562  390 KIVKTKSELVKEKYHRGIV 408
 
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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