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Conserved domains on  [gi|767968969|ref|XP_011543636|]
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protein Atg16l2 isoform X5 [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 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
225-513 1.21e-55

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: 187.93  E-value: 1.21e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969 225 VLDAHLSEVNAVRFGPNSSLLATGGADRLIHLWNVVGSRLEanQTLEGAGGSITSVDFDPSGYQVLAATYNQAAQLWKVG 304
Cdd:cd00200    4 TLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELL--RTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969 305 EAQSKETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWDLGRAYCSRTIN-VLSYCNDVV--CGDHIIISGHNDQKIRF 381
Cdd:cd00200   82 TGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRgHTDWVNSVAfsPDGTFVASSSQDGTIKL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969 382 WDSRGPHCTQVIPV-QGRVTSLSLSHDQLHLLSCSRDNTLKVIDLRVSNIRQVFRADGFKCGSdwtkAVFSPDRSYALAG 460
Cdd:cd00200  162 WDLRTGKCVATLTGhTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNS----VAFSPDGYLLASG 237
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767968969 461 SCDGALYIWDVDTGKLESRLQGpHCAAVNAVAWCYSGSHMVSVDQGRKVVLWQ 513
Cdd:cd00200  238 SEDGTIRVWDLRTGECVQTLSG-HTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
1-97 7.22e-29

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: 430106 [Multi-domain]  Cd Length: 176  Bit Score: 112.33  E-value: 7.22e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969    1 MAYQVVEKGAALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQE 80
Cdd:pfam08614  76 LAQQLVDLNEELQELEKKLREDERRLAELEAERAQLEEKLRDREEELREKRKLNQDLQDELVALQLQLNMAEEKLRKLEK 155
                          90
                  ....*....|....*..
gi 767968969   81 EARDLLERLVQRKARAA 97
Cdd:pfam08614 156 ENRELVERWMKRKGQEA 172
SMC_prok_A super family cl37070
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
15-189 3.61e-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]


The actual alignment was detected with superfamily member TIGR02169:

Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.60  E-value: 3.61e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969    15 LESELQQRQSRLAALEARVAQLREARA---QQAQQVE----EWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDLLE 87
Cdd:TIGR02169  341 LEREIEEERKRRDKLTEEYAELKEELEdlrAELEEVDkefaETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSE 420
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969    88 RLVQRKARAAAERNLRNERRERAKQARvsQELKKAAKRTVSISEGPDTLGDGMRERRETL--------ALAPEPEPLEKE 159
Cdd:TIGR02169  421 ELADLNAAIAGIEAKINELEEEKEDKA--LEIKKQEWKLEQLAADLSKYEQELYDLKEEYdrvekelsKLQRELAEAEAQ 498
                          170       180       190
                   ....*....|....*....|....*....|
gi 767968969   160 AcEKWKRPFRSASATSLTLSHCVDVVKGLL 189
Cdd:TIGR02169  499 A-RASEERVRGGRAVEEVLKASIQGVHGTV 527
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
225-513 1.21e-55

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: 187.93  E-value: 1.21e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969 225 VLDAHLSEVNAVRFGPNSSLLATGGADRLIHLWNVVGSRLEanQTLEGAGGSITSVDFDPSGYQVLAATYNQAAQLWKVG 304
Cdd:cd00200    4 TLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELL--RTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969 305 EAQSKETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWDLGRAYCSRTIN-VLSYCNDVV--CGDHIIISGHNDQKIRF 381
Cdd:cd00200   82 TGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRgHTDWVNSVAfsPDGTFVASSSQDGTIKL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969 382 WDSRGPHCTQVIPV-QGRVTSLSLSHDQLHLLSCSRDNTLKVIDLRVSNIRQVFRADGFKCGSdwtkAVFSPDRSYALAG 460
Cdd:cd00200  162 WDLRTGKCVATLTGhTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNS----VAFSPDGYLLASG 237
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767968969 461 SCDGALYIWDVDTGKLESRLQGpHCAAVNAVAWCYSGSHMVSVDQGRKVVLWQ 513
Cdd:cd00200  238 SEDGTIRVWDLRTGECVQTLSG-HTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
218-513 2.01e-33

WD40 repeat [General function prediction only];


Pssm-ID: 225201 [Multi-domain]  Cd Length: 466  Bit Score: 132.13  E-value: 2.01e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969 218 LPTRAQDVLDAHLSEVNAVRFGPNSSLLATGGADRLIHLWNVVGSRLEANQTLEGAGGSITSVDF-DPSGYQVLAAT--Y 294
Cdd:COG2319   53 LPDLSSLLLRGHEDSITSIAFSPDGELLLSGSSDGTIKLWDLDNGEKLIKSLEGLHDSSVSKLALsSPDGNSILLASssL 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969 295 NQAAQLWKV-GEAQSKETLSGHKDKVTAAKF-KLTRHQAVTGSRDRTVKEWDLGRAYCSRTINVLSYCNDVVC----GDH 368
Cdd:COG2319  133 DGTVKLWDLsTPGKLIRTLEGHSESVTSLAFsPDGKLLASGSSLDGTIKLWDLRTGKPLSTLAGHTDPVSSLAfspdGGL 212
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969 369 IIISGHNDQKIRFWDSR-GPHCTQVIPVQGRVTSLSLSHDQLHLLSCSRDNTLKVIDLRVSNIRQVFRADgfkcGSDWTK 447
Cdd:COG2319  213 LIASGSSDGTIRLWDLStGKLLRSTLSGHSDSVVSSFSPDGSLLASGSSDGTIRLWDLRSSSSLLRTLSG----HSSSVL 288
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767968969 448 AV-FSPDRSYALAGSCDGALYIWDVDTGKLESRL-QGPHCAAVNAVAWCYSGSHMV-SVDQGRKVVLWQ 513
Cdd:COG2319  289 SVaFSPDGKLLASGSSDGTVRLWDLETGKLLSSLtLKGHEGPVSSLSFSPDGSLLVsGGSDDGTIRLWD 357
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
1-97 7.22e-29

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: 430106 [Multi-domain]  Cd Length: 176  Bit Score: 112.33  E-value: 7.22e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969    1 MAYQVVEKGAALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQE 80
Cdd:pfam08614  76 LAQQLVDLNEELQELEKKLREDERRLAELEAERAQLEEKLRDREEELREKRKLNQDLQDELVALQLQLNMAEEKLRKLEK 155
                          90
                  ....*....|....*..
gi 767968969   81 EARDLLERLVQRKARAA 97
Cdd:pfam08614 156 ENRELVERWMKRKGQEA 172
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
14-97 3.97e-22

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: 90.32  E-value: 3.97e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969  14 TLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDLLERLVQRK 93
Cdd:cd22887    1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEENDELVERWMAKK 80

                 ....
gi 767968969  94 ARAA 97
Cdd:cd22887   81 QQEA 84
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
225-258 1.22e-06

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: 45.00  E-value: 1.22e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 767968969   225 VLDAHLSEVNAVRFGPNSSLLATGGADRLIHLWN 258
Cdd:smart00320   7 TLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
225-258 3.08e-06

WD domain, G-beta repeat;


Pssm-ID: 425662 [Multi-domain]  Cd Length: 39  Bit Score: 43.87  E-value: 3.08e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 767968969  225 VLDAHLSEVNAVRFGPNSSLLATGGADRLIHLWN 258
Cdd:pfam00400   6 TLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
233-428 1.17e-05

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 48.16  E-value: 1.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969 233 VNAVRFGPNSSLLATGGADRLIHLWN----VVGSRLEANQTLEGAGGS-ITSVDFDPS-GYQVLAATYNQAAQLWKVGEA 306
Cdd:PLN00181 486 VCAIGFDRDGEFFATAGVNKKIKIFEcesiIKDGRDIHYPVVELASRSkLSGICWNSYiKSQVASSNFEGVVQVWDVARS 565
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969 307 QSKETLSGHKDKVTAAKFKLTRHQAV-TGSRDRTVKEWDLGRAYCSRTINVLSycnDVVC------GDHIIISGHNDQKI 379
Cdd:PLN00181 566 QLVTEMKEHEKRVWSIDYSSADPTLLaSGSDDGSVKLWSINQGVSIGTIKTKA---NICCvqfpseSGRSLAFGSADHKV 642
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767968969 380 RFWDSRGPH---CTQVipvqGRVTSLSLSH--DQLHLLSCSRDNTLKVIDLRVS 428
Cdd:PLN00181 643 YYYDLRNPKlplCTMI----GHSKTVSYVRfvDSSTLVSSSTDNTLKLWDLSMS 692
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
15-189 3.61e-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: 3.61e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969    15 LESELQQRQSRLAALEARVAQLREARA---QQAQQVE----EWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDLLE 87
Cdd:TIGR02169  341 LEREIEEERKRRDKLTEEYAELKEELEdlrAELEEVDkefaETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSE 420
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969    88 RLVQRKARAAAERNLRNERRERAKQARvsQELKKAAKRTVSISEGPDTLGDGMRERRETL--------ALAPEPEPLEKE 159
Cdd:TIGR02169  421 ELADLNAAIAGIEAKINELEEEKEDKA--LEIKKQEWKLEQLAADLSKYEQELYDLKEEYdrvekelsKLQRELAEAEAQ 498
                          170       180       190
                   ....*....|....*....|....*....|
gi 767968969   160 AcEKWKRPFRSASATSLTLSHCVDVVKGLL 189
Cdd:TIGR02169  499 A-RASEERVRGGRAVEEVLKASIQGVHGTV 527
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
10-118 1.50e-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: 44.66  E-value: 1.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969    10 AALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRahvglreAALRRLQEEARDLLERL 89
Cdd:TIGR02168  754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR-------AELTLLNEEAANLRERL 826
                           90       100
                   ....*....|....*....|....*....
gi 767968969    90 VQRKARAAAERNLRNERRERAKQARVSQE 118
Cdd:TIGR02168  827 ESLERRIAATERRLEDLEEQIEELSEDIE 855
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
7-163 2.49e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.88  E-value: 2.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969   7 EKGAALGTLESELQ-------QRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQ 79
Cdd:PRK02224 360 ELREEAAELESELEeareaveDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTAR 439
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969  80 ---EEARDLLE------------------RLVQRKARAA--AERNLRNERRERAKQARVSQ--ELKKAAKRTVSISEGPD 134
Cdd:PRK02224 440 ervEEAEALLEagkcpecgqpvegsphveTIEEDRERVEelEAELEDLEEEVEEVEERLERaeDLVEAEDRIERLEERRE 519
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 767968969 135 TLGDGMRERRETLA--------LAPEPEPLEKEACEK 163
Cdd:PRK02224 520 DLEELIAERRETIEekreraeeLRERAAELEAEAEEK 556
TolA COG3064
Membrane protein involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
20-131 3.03e-04

Membrane protein involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 225606 [Multi-domain]  Cd Length: 387  Bit Score: 43.01  E-value: 3.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969  20 QQRQSRLAALEARVAQLREAR--AQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDLLERLVQRKARAA 97
Cdd:COG3064  105 QLEKERLKAQEQQKQAEEAEKqaQLEQKQQEEQARKAAAEQKKKAEAAKAKAAAEAAKLKAAAEAKKKAEEAAKAAEEAK 184
                         90       100       110
                 ....*....|....*....|....*....|....
gi 767968969  98 AERNLRNERRERAKQARVSQELKKAAKRTVSISE 131
Cdd:COG3064  185 AKAEAAAAKKKAEAEAKAAAEKAKAEAEAKAKAE 218
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
7-226 1.67e-03

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 41.24  E-value: 1.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969    7 EKGAALGTLESELQQRQSRLAALEARVAQLREARAQ-QAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDL 85
Cdd:COG1196   337 EELEERETLLEELEQLLAELEEAKEELEEKLSALLEeLEELFEALREELAELEAELAEIRNELEELKREIESLEERLERL 416
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969   86 LERLVQRKARAAAernlrnerrerakqarVSQELKKAAKRTVSISEGPDTLGDGMRERRETLALAPEPEPLEKEACEKWK 165
Cdd:COG1196   417 SERLEDLKEELKE----------------LEAELEELQTELEELNEELEELEEQLEELRDRLKELERELAELQEELQRLE 480
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969  166 RPFRSASA---TSLTLSHCVDVVKGLLDFKKRRGHSIGGA------PEQRYQIipvCVAARLPTRAQDVL 226
Cdd:COG1196   481 KELSSLEArldRLEAEQRASQGVRAVLEALESGLPGVYGPvaelikVKEKYET---ALEAALGNRLQAVV 547
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
225-513 1.21e-55

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: 187.93  E-value: 1.21e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969 225 VLDAHLSEVNAVRFGPNSSLLATGGADRLIHLWNVVGSRLEanQTLEGAGGSITSVDFDPSGYQVLAATYNQAAQLWKVG 304
Cdd:cd00200    4 TLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELL--RTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969 305 EAQSKETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWDLGRAYCSRTIN-VLSYCNDVV--CGDHIIISGHNDQKIRF 381
Cdd:cd00200   82 TGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRgHTDWVNSVAfsPDGTFVASSSQDGTIKL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969 382 WDSRGPHCTQVIPV-QGRVTSLSLSHDQLHLLSCSRDNTLKVIDLRVSNIRQVFRADGFKCGSdwtkAVFSPDRSYALAG 460
Cdd:cd00200  162 WDLRTGKCVATLTGhTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNS----VAFSPDGYLLASG 237
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767968969 461 SCDGALYIWDVDTGKLESRLQGpHCAAVNAVAWCYSGSHMVSVDQGRKVVLWQ 513
Cdd:cd00200  238 SEDGTIRVWDLRTGECVQTLSG-HTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
268-513 2.04e-40

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: 147.48  E-value: 2.04e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969 268 QTLEGAGGSITSVDFDPSGYQVLAATYNQAAQLWKVGEAQSKETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWDLGR 347
Cdd:cd00200    3 RTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLET 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969 348 AYCSRTINvlSYCNDVVCGD-----HIIISGHNDQKIRFWDSRGPHCTQVIP-VQGRVTSLSLSHDQLHLLSCSRDNTLK 421
Cdd:cd00200   83 GECVRTLT--GHTSYVSSVAfspdgRILSSSSRDKTIKVWDVETGKCLTTLRgHTDWVNSVAFSPDGTFVASSSQDGTIK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969 422 VIDLRVSNIRQVFraDGFKcgsDWTKAV-FSPDRSYALAGSCDGALYIWDVDTGKLESRLQGpHCAAVNAVAWCYSGSHM 500
Cdd:cd00200  161 LWDLRTGKCVATL--TGHT---GEVNSVaFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRG-HENGVNSVAFSPDGYLL 234
                        250
                 ....*....|...
gi 767968969 501 VSVDQGRKVVLWQ 513
Cdd:cd00200  235 ASGSEDGTIRVWD 247
WD40 COG2319
WD40 repeat [General function prediction only];
218-513 2.01e-33

WD40 repeat [General function prediction only];


Pssm-ID: 225201 [Multi-domain]  Cd Length: 466  Bit Score: 132.13  E-value: 2.01e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969 218 LPTRAQDVLDAHLSEVNAVRFGPNSSLLATGGADRLIHLWNVVGSRLEANQTLEGAGGSITSVDF-DPSGYQVLAAT--Y 294
Cdd:COG2319   53 LPDLSSLLLRGHEDSITSIAFSPDGELLLSGSSDGTIKLWDLDNGEKLIKSLEGLHDSSVSKLALsSPDGNSILLASssL 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969 295 NQAAQLWKV-GEAQSKETLSGHKDKVTAAKF-KLTRHQAVTGSRDRTVKEWDLGRAYCSRTINVLSYCNDVVC----GDH 368
Cdd:COG2319  133 DGTVKLWDLsTPGKLIRTLEGHSESVTSLAFsPDGKLLASGSSLDGTIKLWDLRTGKPLSTLAGHTDPVSSLAfspdGGL 212
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969 369 IIISGHNDQKIRFWDSR-GPHCTQVIPVQGRVTSLSLSHDQLHLLSCSRDNTLKVIDLRVSNIRQVFRADgfkcGSDWTK 447
Cdd:COG2319  213 LIASGSSDGTIRLWDLStGKLLRSTLSGHSDSVVSSFSPDGSLLASGSSDGTIRLWDLRSSSSLLRTLSG----HSSSVL 288
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767968969 448 AV-FSPDRSYALAGSCDGALYIWDVDTGKLESRL-QGPHCAAVNAVAWCYSGSHMV-SVDQGRKVVLWQ 513
Cdd:COG2319  289 SVaFSPDGKLLASGSSDGTVRLWDLETGKLLSSLtLKGHEGPVSSLSFSPDGSLLVsGGSDDGTIRLWD 357
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
1-97 7.22e-29

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: 430106 [Multi-domain]  Cd Length: 176  Bit Score: 112.33  E-value: 7.22e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969    1 MAYQVVEKGAALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQE 80
Cdd:pfam08614  76 LAQQLVDLNEELQELEKKLREDERRLAELEAERAQLEEKLRDREEELREKRKLNQDLQDELVALQLQLNMAEEKLRKLEK 155
                          90
                  ....*....|....*..
gi 767968969   81 EARDLLERLVQRKARAA 97
Cdd:pfam08614 156 ENRELVERWMKRKGQEA 172
WD40 COG2319
WD40 repeat [General function prediction only];
219-512 1.28e-27

WD40 repeat [General function prediction only];


Pssm-ID: 225201 [Multi-domain]  Cd Length: 466  Bit Score: 115.57  E-value: 1.28e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969 219 PTRAQDVLDAHLSEVNAVRFGPNSSLLATGG-ADRLIHLWNVVGSRLEanQTLEGAGGSITSVDFDPSG-YQVLAATYNQ 296
Cdd:COG2319  144 PGKLIRTLEGHSESVTSLAFSPDGKLLASGSsLDGTIKLWDLRTGKPL--STLAGHTDPVSSLAFSPDGgLLIASGSSDG 221
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969 297 AAQLWKVGEAQS-KETLSGHKDKVTAAkFKLTRHQAVTGSRDRTVKEWDLgrAYCSRTINVLSYCNDVVCG------DHI 369
Cdd:COG2319  222 TIRLWDLSTGKLlRSTLSGHSDSVVSS-FSPDGSLLASGSSDGTIRLWDL--RSSSSLLRTLSGHSSSVLSvafspdGKL 298
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969 370 IISGHNDQKIRFWDSRGPHCTQVIPVQG---RVTSLSLSHDQLHLL-SCSRDNTLKVIDLRVSNIRQVFRadgfkcGSDW 445
Cdd:COG2319  299 LASGSSDGTVRLWDLETGKLLSSLTLKGhegPVSSLSFSPDGSLLVsGGSDDGTIRLWDLRTGKPLKTLE------GHSN 372
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767968969 446 TKAV-FSPDRSYALAGSCDGALYIWDVDTGKLESRLQGPHCaAVNAVAWCYSGSHMVSVDQGRKVVLW 512
Cdd:COG2319  373 VLSVsFSPDGRVVSSGSTDGTVRLWDLSTGSLLRNLDGHTS-RVTSLDFSPDGKSLASGSSDNTIRLW 439
WD40 COG2319
WD40 repeat [General function prediction only];
225-480 9.17e-27

WD40 repeat [General function prediction only];


Pssm-ID: 225201 [Multi-domain]  Cd Length: 466  Bit Score: 112.87  E-value: 9.17e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969 225 VLDAHLSEVNAVRFGPNSS-LLATGGADRLIHLWNVvGSRLEANQTLEGAGGSITSVdFDPSGYQVLAATYNQAAQLWKV 303
Cdd:COG2319  193 TLAGHTDPVSSLAFSPDGGlLIASGSSDGTIRLWDL-STGKLLRSTLSGHSDSVVSS-FSPDGSLLASGSSDGTIRLWDL 270
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969 304 -GEAQSKETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWDLGRAYCSRTINVLSYCNDVVC------GDHIIISGHND 376
Cdd:COG2319  271 rSSSSLLRTLSGHSSSVLSVAFSPDGKLLASGSSDGTVRLWDLETGKLLSSLTLKGHEGPVSSlsfspdGSLLVSGGSDD 350
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969 377 QKIRFWDSRGPHCTQVIPVQGRVTSLSLSHDQLHLLSCSRDNTLKVIDLRVSNIRQVFRADgfkcGSDWTKAVFSPDRSY 456
Cdd:COG2319  351 GTIRLWDLRTGKPLKTLEGHSNVLSVSFSPDGRVVSSGSTDGTVRLWDLSTGSLLRNLDGH----TSRVTSLDFSPDGKS 426
                        250       260
                 ....*....|....*....|....
gi 767968969 457 ALAGSCDGALYIWDVDTGKLESRL 480
Cdd:COG2319  427 LASGSSDNTIRLWDLKTSLKSVSF 450
WD40 COG2319
WD40 repeat [General function prediction only];
223-443 2.97e-24

WD40 repeat [General function prediction only];


Pssm-ID: 225201 [Multi-domain]  Cd Length: 466  Bit Score: 105.56  E-value: 2.97e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969 223 QDVLDAHLSEVNAVrFGPNSSLLATGGADRLIHLWNVVGSRlEANQTLEGAGGSITSVDFDPSGYQVLAATYNQAAQLWK 302
Cdd:COG2319  235 RSTLSGHSDSVVSS-FSPDGSLLASGSSDGTIRLWDLRSSS-SLLRTLSGHSSSVLSVAFSPDGKLLASGSSDGTVRLWD 312
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969 303 V--GEAQSKETLSGHKDKVTAAKFKLTRHQAVTG-SRDRTVKEWDLGRAYCSRTINVLSYCNDVVCGDHIII--SGHNDQ 377
Cdd:COG2319  313 LetGKLLSSLTLKGHEGPVSSLSFSPDGSLLVSGgSDDGTIRLWDLRTGKPLKTLEGHSNVLSVSFSPDGRVvsSGSTDG 392
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767968969 378 KIRFWD-SRGPHCTQVIPVQGRVTSLSLSHDQLHLLSCSRDNTLKVIDLRVSNIRQVFRADGFKCGS 443
Cdd:COG2319  393 TVRLWDlSTGSLLRNLDGHTSRVTSLDFSPDGKSLASGSSDNTIRLWDLKTSLKSVSFSPDGKVLAS 459
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
14-97 3.97e-22

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: 90.32  E-value: 3.97e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969  14 TLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDLLERLVQRK 93
Cdd:cd22887    1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEENDELVERWMAKK 80

                 ....
gi 767968969  94 ARAA 97
Cdd:cd22887   81 QQEA 84
WD40 COG2319
WD40 repeat [General function prediction only];
225-419 5.37e-18

WD40 repeat [General function prediction only];


Pssm-ID: 225201 [Multi-domain]  Cd Length: 466  Bit Score: 86.30  E-value: 5.37e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969 225 VLDAHLSEVNAVRFGPNSSLLATGGADRLIHLWNVVGSRLEANQTLEGAGGSITSVDFDPSGYQVLAA-TYNQAAQLWKV 303
Cdd:COG2319  279 TLSGHSSSVLSVAFSPDGKLLASGSSDGTVRLWDLETGKLLSSLTLKGHEGPVSSLSFSPDGSLLVSGgSDDGTIRLWDL 358
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969 304 GEAQSKETLSGHkDKVTAAKFKLTRHQAVTGSRDRTVKEWDLGRAYCSRTINVLS---YCNDVVCGDHIIISGHNDQKIR 380
Cdd:COG2319  359 RTGKPLKTLEGH-SNVLSVSFSPDGRVVSSGSTDGTVRLWDLSTGSLLRNLDGHTsrvTSLDFSPDGKSLASGSSDNTIR 437
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 767968969 381 FWDsrgphctqvipVQGRVTSLSLSHDQLHLLSCSRDNT 419
Cdd:COG2319  438 LWD-----------LKTSLKSVSFSPDGKVLASKSSDLS 465
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
225-258 1.22e-06

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: 45.00  E-value: 1.22e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 767968969   225 VLDAHLSEVNAVRFGPNSSLLATGGADRLIHLWN 258
Cdd:smart00320   7 TLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
225-258 3.08e-06

WD domain, G-beta repeat;


Pssm-ID: 425662 [Multi-domain]  Cd Length: 39  Bit Score: 43.87  E-value: 3.08e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 767968969  225 VLDAHLSEVNAVRFGPNSSLLATGGADRLIHLWN 258
Cdd:pfam00400   6 TLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
233-428 1.17e-05

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 48.16  E-value: 1.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969 233 VNAVRFGPNSSLLATGGADRLIHLWN----VVGSRLEANQTLEGAGGS-ITSVDFDPS-GYQVLAATYNQAAQLWKVGEA 306
Cdd:PLN00181 486 VCAIGFDRDGEFFATAGVNKKIKIFEcesiIKDGRDIHYPVVELASRSkLSGICWNSYiKSQVASSNFEGVVQVWDVARS 565
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969 307 QSKETLSGHKDKVTAAKFKLTRHQAV-TGSRDRTVKEWDLGRAYCSRTINVLSycnDVVC------GDHIIISGHNDQKI 379
Cdd:PLN00181 566 QLVTEMKEHEKRVWSIDYSSADPTLLaSGSDDGSVKLWSINQGVSIGTIKTKA---NICCvqfpseSGRSLAFGSADHKV 642
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767968969 380 RFWDSRGPH---CTQVipvqGRVTSLSLSH--DQLHLLSCSRDNTLKVIDLRVS 428
Cdd:PLN00181 643 YYYDLRNPKlplCTMI----GHSKTVSYVRfvDSSTLVSSSTDNTLKLWDLSMS 692
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
15-189 3.61e-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: 3.61e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969    15 LESELQQRQSRLAALEARVAQLREARA---QQAQQVE----EWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDLLE 87
Cdd:TIGR02169  341 LEREIEEERKRRDKLTEEYAELKEELEdlrAELEEVDkefaETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSE 420
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969    88 RLVQRKARAAAERNLRNERRERAKQARvsQELKKAAKRTVSISEGPDTLGDGMRERRETL--------ALAPEPEPLEKE 159
Cdd:TIGR02169  421 ELADLNAAIAGIEAKINELEEEKEDKA--LEIKKQEWKLEQLAADLSKYEQELYDLKEEYdrvekelsKLQRELAEAEAQ 498
                          170       180       190
                   ....*....|....*....|....*....|
gi 767968969   160 AcEKWKRPFRSASATSLTLSHCVDVVKGLL 189
Cdd:TIGR02169  499 A-RASEERVRGGRAVEEVLKASIQGVHGTV 527
PTZ00421 PTZ00421
coronin; Provisional
236-344 1.16e-04

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 44.50  E-value: 1.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969 236 VRFGP-NSSLLATGGADRLIHLWNVVGSRLEANQT-----LEGAGGSITSVDFDPSGYQVLA-ATYNQAAQLWKVGEAQS 308
Cdd:PTZ00421  81 VAFNPfDPQKLFTASEDGTIMGWGIPEEGLTQNISdpivhLQGHTKKVGIVSFHPSAMNVLAsAGADMVVNVWDVERGKA 160
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 767968969 309 KETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWD 344
Cdd:PTZ00421 161 VEVIKCHSDQITSLEWNLDGSLLCTTSKDKKLNIID 196
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
311-344 1.35e-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: 39.22  E-value: 1.35e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 767968969   311 TLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWD 344
Cdd:smart00320   7 TLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
311-344 1.48e-04

WD domain, G-beta repeat;


Pssm-ID: 425662 [Multi-domain]  Cd Length: 39  Bit Score: 39.25  E-value: 1.48e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 767968969  311 TLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWD 344
Cdd:pfam00400   6 TLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
10-118 1.50e-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: 44.66  E-value: 1.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969    10 AALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRahvglreAALRRLQEEARDLLERL 89
Cdd:TIGR02168  754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR-------AELTLLNEEAANLRERL 826
                           90       100
                   ....*....|....*....|....*....
gi 767968969    90 VQRKARAAAERNLRNERRERAKQARVSQE 118
Cdd:TIGR02168  827 ESLERRIAATERRLEDLEEQIEELSEDIE 855
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
7-163 2.49e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.88  E-value: 2.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969   7 EKGAALGTLESELQ-------QRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQ 79
Cdd:PRK02224 360 ELREEAAELESELEeareaveDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTAR 439
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969  80 ---EEARDLLE------------------RLVQRKARAA--AERNLRNERRERAKQARVSQ--ELKKAAKRTVSISEGPD 134
Cdd:PRK02224 440 ervEEAEALLEagkcpecgqpvegsphveTIEEDRERVEelEAELEDLEEEVEEVEERLERaeDLVEAEDRIERLEERRE 519
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 767968969 135 TLGDGMRERRETLA--------LAPEPEPLEKEACEK 163
Cdd:PRK02224 520 DLEELIAERRETIEekreraeeLRERAAELEAEAEEK 556
TolA COG3064
Membrane protein involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
20-131 3.03e-04

Membrane protein involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 225606 [Multi-domain]  Cd Length: 387  Bit Score: 43.01  E-value: 3.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969  20 QQRQSRLAALEARVAQLREAR--AQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDLLERLVQRKARAA 97
Cdd:COG3064  105 QLEKERLKAQEQQKQAEEAEKqaQLEQKQQEEQARKAAAEQKKKAEAAKAKAAAEAAKLKAAAEAKKKAEEAAKAAEEAK 184
                         90       100       110
                 ....*....|....*....|....*....|....
gi 767968969  98 AERNLRNERRERAKQARVSQELKKAAKRTVSISE 131
Cdd:COG3064  185 AKAEAAAAKKKAEAEAKAAAEKAKAEAEAKAKAE 218
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
15-93 5.44e-04

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 42.78  E-value: 5.44e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767968969   15 LESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDLLERLVQRK 93
Cdd:COG1196   826 LEQEIEELEEEIEELEEKLDELEEELEELEKELEELKEELEELEAEKEELEDELKELEEEKEELEEELRELESELAELK 904
FliJ COG2882
Flagellar biosynthesis chaperone FliJ [Cell motility];
4-95 6.22e-04

Flagellar biosynthesis chaperone FliJ [Cell motility];


Pssm-ID: 225437 [Multi-domain]  Cd Length: 148  Bit Score: 40.03  E-value: 6.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969   4 QVVEKGAAlGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWR---AQNAVQRAAYEALRAhvglREAALRRLQE 80
Cdd:COG2882   52 NLNEKLKS-GVSAAQWQNYQQFISQLEVAIDQQQSQLSKLRKQVEQKReiwQEKQIELKALEKLKE----RQKTEFLLEE 126
                         90
                 ....*....|....*..
gi 767968969  81 EARD--LLERLVQRKAR 95
Cdd:COG2882  127 NRREqkIMDELAQRAFP 143
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
7-89 7.02e-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: 42.35  E-value: 7.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969     7 EKGAALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDLL 86
Cdd:TIGR02168  863 ELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQ 942

                   ...
gi 767968969    87 ERL 89
Cdd:TIGR02168  943 ERL 945
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
396-424 7.91e-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: 36.91  E-value: 7.91e-04
                           10        20
                   ....*....|....*....|....*....
gi 767968969   396 QGRVTSLSLSHDQLHLLSCSRDNTLKVID 424
Cdd:smart00320  12 TGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
PTZ00121 PTZ00121
MAEBL; Provisional
17-162 1.02e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969   17 SELQQRQSRLAALEARVA-QLREA----RAQQAQQVEEWRAQNAVQRAAYEALRAHvglreaALRRLQEEARDLLERLvQ 91
Cdd:PTZ00121 1263 AHFARRQAAIKAEEARKAdELKKAeekkKADEAKKAEEKKKADEAKKKAEEAKKAD------EAKKKAEEAKKKADAA-K 1335
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767968969   92 RKARAA--AERNLRNERRERAKQARVSQELKKAAK-RTVSISEGPDTLGDGMRERRETLALAPEPEPLEKEACE 162
Cdd:PTZ00121 1336 KKAEEAkkAAEAAKAEAEAAADEAEAAEEKAEAAEkKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADE 1409
PTZ00121 PTZ00121
MAEBL; Provisional
16-166 1.05e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969   16 ESELQQRQSRLAALEARVAQLREA-----RAQQAQQVEEWRaQNAVQRAAYEALRAHVGLREAALR----RLQEEARDLL 86
Cdd:PTZ00121 1209 EEERKAEEARKAEDAKKAEAVKKAeeakkDAEEAKKAEEER-NNEEIRKFEEARMAHFARRQAAIKaeeaRKADELKKAE 1287
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969   87 ERLVQRKARAAAERNLRNERRERAKQARVSQELKKAAKRTVSISEGPDTLGDGMRERRETLALAPEPEPLEKEACEKWKR 166
Cdd:PTZ00121 1288 EKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAE 1367
PRK12704 PRK12704
phosphodiesterase; Provisional
15-89 1.13e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.30  E-value: 1.13e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767968969  15 LESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDLLERL 89
Cdd:PRK12704  73 FEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERI 147
RND_mfp TIGR01730
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ...
4-84 1.35e-03

RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion protein) component of the RND family of transporters. RND refers to Resistance, Nodulation, and cell Division. It is, in part, a subfamily of pfam00529 (Pfam release 7.5) but hits substantial numbers of proteins missed by that model. The related HlyD secretion protein, for which pfam00529 is named, is outside the scope of this model. Attributed functions imply outward transport. These functions include nodulation, acriflavin resistance, heavy metal efflux, and multidrug resistance proteins. Most members of this family are found in Gram-negative bacteria. The proposed function of MFP proteins is to bring the inner and outer membranes together and enable transport to the outside of the outer membrane. Note, however, that a few members of this family are found in Gram-positive bacteria, where there is no outer membrane. [Transport and binding proteins, Unknown substrate]


Pssm-ID: 273776 [Multi-domain]  Cd Length: 322  Bit Score: 40.76  E-value: 1.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969    4 QVVEKGAALGTLESELQQrqsrlAALEARVAQLREARAQ------QAQQVEEWRAQNAV-------QRAAYEALRAHVGL 70
Cdd:TIGR01730  46 QKVKKGQVLARLDDDDYQ-----LALQAALAQLAAAEAQlelaqrSFERAERLVKRNAVsqadlddAKAAVEAAQADLEA 120
                          90
                  ....*....|....
gi 767968969   71 REAALRRLQEEARD 84
Cdd:TIGR01730 121 AKASLASAQLNLRY 134
COG4372 COG4372
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
16-149 1.66e-03

Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 226809 [Multi-domain]  Cd Length: 499  Bit Score: 40.78  E-value: 1.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969  16 ESELQQRQSRLAALEARVAQlREARAQQAQQVEEWRAQNAVQRAAYEALRAH-VGLREAALRRLqEEARDLLERLVqrkA 94
Cdd:COG4372  202 AQNLATRANAAQARTEELAR-RAAAAQQTAQAIQQRDAQISQKAQQIAARAEqIRERERQLQRL-ETAQARLEQEV---A 276
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767968969  95 RAAAERNLRNERRERAKQARVSQELKKAAKRTVSISEGPDTLGDGMRERRETLAL 149
Cdd:COG4372  277 QLEAYYQAYVRLRQQAAATQRGQVLAGAAQRVAQAQAQAQAQAQLLSSANRPAAL 331
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
7-226 1.67e-03

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 41.24  E-value: 1.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969    7 EKGAALGTLESELQQRQSRLAALEARVAQLREARAQ-QAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDL 85
Cdd:COG1196   337 EELEERETLLEELEQLLAELEEAKEELEEKLSALLEeLEELFEALREELAELEAELAEIRNELEELKREIESLEERLERL 416
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969   86 LERLVQRKARAAAernlrnerrerakqarVSQELKKAAKRTVSISEGPDTLGDGMRERRETLALAPEPEPLEKEACEKWK 165
Cdd:COG1196   417 SERLEDLKEELKE----------------LEAELEELQTELEELNEELEELEEQLEELRDRLKELERELAELQEELQRLE 480
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969  166 RPFRSASA---TSLTLSHCVDVVKGLLDFKKRRGHSIGGA------PEQRYQIipvCVAARLPTRAQDVL 226
Cdd:COG1196   481 KELSSLEArldRLEAEQRASQGVRAVLEALESGLPGVYGPvaelikVKEKYET---ALEAALGNRLQAVV 547
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
473-512 1.69e-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: 36.14  E-value: 1.69e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 767968969   473 TGKLESRLQGpHCAAVNAVAWCYSGSHMVSVDQGRKVVLW 512
Cdd:smart00320   1 SGELLKTLKG-HTGPVTSVAFSPDGKYLASGSDDGTIKLW 39
PRK09039 PRK09039
peptidoglycan -binding protein;
4-84 2.00e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 40.33  E-value: 2.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969   4 QVVEKGAALGTLESELQQRQS-------RLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALR 76
Cdd:PRK09039  82 SVANLRASLSAAEAERSRLQAllaelagAGAAAEGRAGELAQELDSEKQVSARALAQVELLNQQIAALRRQLAALEAALD 161

                 ....*...
gi 767968969  77 rlQEEARD 84
Cdd:PRK09039 162 --ASEKRD 167
WD40 pfam00400
WD domain, G-beta repeat;
396-424 2.86e-03

WD domain, G-beta repeat;


Pssm-ID: 425662 [Multi-domain]  Cd Length: 39  Bit Score: 35.40  E-value: 2.86e-03
                          10        20
                  ....*....|....*....|....*....
gi 767968969  396 QGRVTSLSLSHDQLHLLSCSRDNTLKVID 424
Cdd:pfam00400  11 TGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
EmrA COG1566
Multidrug resistance efflux pump [Defense mechanisms];
3-124 3.89e-03

Multidrug resistance efflux pump [Defense mechanisms];


Pssm-ID: 224482 [Multi-domain]  Cd Length: 352  Bit Score: 39.62  E-value: 3.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969   3 YQVVEKGAALGTLESE-----LQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRR 77
Cdd:COG1566   72 NQLVKKGDVLFRIDPRdyraaLEQAEAALAAAEAQLRNLRAQLASAQALIAQAEAQDLDQAQNELERRAELAQRGVVSRE 151
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 767968969  78 LQEEARDLLErlVQRKARAAAERNLRNERRERAKQARVSQELKKAAK 124
Cdd:COG1566  152 ELDRARAALQ--AAEAALAAAQAAQKQNLALLESEVSGAQAQVASAE 196
PTZ00121 PTZ00121
MAEBL; Provisional
6-166 4.41e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.74  E-value: 4.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969    6 VEKGAALGTLESELQQRQSRLAALEARVAQLReaRAQQAQQVEEWRAQNAVQRAAYEALRAHvGLREAALRRLQEEARdl 85
Cdd:PTZ00121 1187 VRKAEELRKAEDARKAEAARKAEEERKAEEAR--KAEDAKKAEAVKKAEEAKKDAEEAKKAE-EERNNEEIRKFEEAR-- 1261
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969   86 LERLVQRKARAAAERNLRNERRERAKQARVSQELKKA-AKRTVsisegpDTLGDGMRERRETLALAPEPEPLEKEACEKW 164
Cdd:PTZ00121 1262 MAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAeEKKKA------DEAKKKAEEAKKADEAKKKAEEAKKKADAAK 1335

                  ..
gi 767968969  165 KR 166
Cdd:PTZ00121 1336 KK 1337
Uso1_p115_C pfam04871
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ...
10-95 5.09e-03

Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular transport factor, Transcytosis associate protein (TAP) and Vesicle docking protein, this myosin-shaped molecule consists of an N-terminal globular head region, a coiled-coil tail which mediates dimerization, and a short C-terminal acidic region. p115 tethers COP1 vesicles to the Golgi by binding the coiled coil proteins giantin (on the vesicles) and GM130 (on the Golgi), via its C-terminal acidic region. It is required for intercisternal transport in the golgi stack. This family consists of the acidic C-terminus, which binds to the golgins giantin and GM130. p115 is thought to juxtapose two membranes by binding giantin with one acidic region, and GM130 with another.


Pssm-ID: 428166 [Multi-domain]  Cd Length: 124  Bit Score: 37.01  E-value: 5.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969   10 AALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEEAR------ 83
Cdd:pfam04871   1 AKASELESEAASLKDENTELKAELQALSDQYQSLEQKKKAAESQAKELEAENKKLEEELKKLRAELSEEKQKEKekqsel 80
                          90
                  ....*....|...
gi 767968969   84 -DLLERLVQRKAR 95
Cdd:pfam04871  81 eDLLLLLGDLEEK 93
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
14-166 5.15e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.64  E-value: 5.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969  14 TLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEEaRDLLERLVQRK 93
Cdd:PRK02224 520 DLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKER-IESLERIRTLL 598
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767968969  94 ARAAAernlrnerrerAKQARVSQELKKAAKRTVSiSEGPDTLGDgMRERRETLALAPEPEPLEkEACEKWKR 166
Cdd:PRK02224 599 AAIAD-----------AEDEIERLREKREALAELN-DERRERLAE-KRERKRELEAEFDEARIE-EAREDKER 657
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
10-147 5.31e-03

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 39.70  E-value: 5.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969   10 AALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDLLERL 89
Cdd:COG1196   793 EELEELEEELEEAERRLDALERELESLEQRRERLEQEIEELEEEIEELEEKLDELEEELEELEKELEELKEELEELEAEK 872
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767968969   90 VQRKARAAaernlrnerRERAKQARVSQELKKAAKRTVSISEGPDTLgdgmRERRETL 147
Cdd:COG1196   873 EELEDELK---------ELEEEKEELEEELRELESELAELKEEIEKL----RERLEEL 917
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
17-131 7.93e-03

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 38.97  E-value: 7.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969  17 SELQQRQSRLAALEARVAQLREaraqqaqQVEEWRAQNAVQRAAYEALRAhvgLREA--ALRRLQEEARDLLERLVQRK- 93
Cdd:COG0419  284 EELEEKIERLEELEREIEELEE-------ELEGLRALLEELEELLEKLKS---LEERleKLEEKLEKLESELEELAEEKn 353
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 767968969  94 --ARAAAERNLRNERRERAKQARVSQELKKAAKRTVSISE 131
Cdd:COG0419  354 elAKLLEERLKELEERLEELEKELEKALERLKQLEEAIQE 393
ZapB pfam06005
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is ...
1-80 8.46e-03

Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is required for proper Z-ring formation.


Pssm-ID: 428718 [Multi-domain]  Cd Length: 71  Bit Score: 34.93  E-value: 8.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968969    1 MAYQVVEKgaalgtLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVglrEAALRRLQE 80
Cdd:pfam06005   1 MSLELLEQ------LETKIQAAVDTIALLQMENEELKEENEELKEEANELEEENQQLKQERNQWQERI---RGLLGKLDE 71
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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