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Conserved domains on  [gi|2462528575|ref|XP_054226394|]
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protein Atg16l2 isoform X4 [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
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 32-203 2.71e-56

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: 187.06  E-value: 2.71e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575  32 LFLELVPAYNHLLEKAELLDKFSKKLQPEPNSVTPTTHQGPWEESELDSDQVPSLVALRVKWQEEEEGLRLVCGEMAYQV 111
Cdd:pfam08614   1 AFLELIDAYNRLLDRTALLEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQLREELAELYRSRGELAQRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575 112 VEKGAALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDL 191
Cdd:pfam08614  81 VDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQDELVALQLQLNMAEEKLRKLEKENREL 160

                         170
                  ....*....|..
gi 2462528575 192 LERLVQRKARAA 203
Cdd:pfam08614 161 VERWMKRKGQEA 172
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 293-550 4.41e-50

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: 174.45  E-value: 4.41e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575 293 VLDAHLSEVNAVRFGPNSSLLATGGADRLIHLWNVVGSRLEanQTLEGAGGSITSVDFDPSGYQVLAATYNQAAQLWKVG 372
Cdd:cd00200     4 TLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELL--RTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575 373 EAQSKETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWDLGRAYCSRTIN-VLSYCNDVV--CGDHIIISGHNDQKIRF 449
Cdd:cd00200    82 TGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRgHTDWVNSVAfsPDGTFVASSSQDGTIKL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575 450 WDSRGPHCTQVIPV-QGRVTSLSLSHDQLHLLSCSRDNTLKVIDLRVSNIRQVFRADGFKCGSdwtkAVFSPDRSYALAG 528
Cdd:cd00200   162 WDLRTGKCVATLTGhTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNS----VAFSPDGYLLASG 237

                         250       260
                  ....*....|....*....|..
gi 2462528575 529 SCDGALYIWDVDTGKLESRLQG 550
Cdd:cd00200   238 SEDGTIRVWDLRTGECVQTLSG 259
 
Name Accession Description Interval E-value
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 32-203 2.71e-56

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: 187.06  E-value: 2.71e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575  32 LFLELVPAYNHLLEKAELLDKFSKKLQPEPNSVTPTTHQGPWEESELDSDQVPSLVALRVKWQEEEEGLRLVCGEMAYQV 111
Cdd:pfam08614   1 AFLELIDAYNRLLDRTALLEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQLREELAELYRSRGELAQRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575 112 VEKGAALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDL 191
Cdd:pfam08614  81 VDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQDELVALQLQLNMAEEKLRKLEKENREL 160

                         170
                  ....*....|..
gi 2462528575 192 LERLVQRKARAA 203
Cdd:pfam08614 161 VERWMKRKGQEA 172
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 293-550 4.41e-50

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: 174.45  E-value: 4.41e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575 293 VLDAHLSEVNAVRFGPNSSLLATGGADRLIHLWNVVGSRLEanQTLEGAGGSITSVDFDPSGYQVLAATYNQAAQLWKVG 372
Cdd:cd00200     4 TLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELL--RTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575 373 EAQSKETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWDLGRAYCSRTIN-VLSYCNDVV--CGDHIIISGHNDQKIRF 449
Cdd:cd00200    82 TGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRgHTDWVNSVAfsPDGTFVASSSQDGTIKL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575 450 WDSRGPHCTQVIPV-QGRVTSLSLSHDQLHLLSCSRDNTLKVIDLRVSNIRQVFRADGFKCGSdwtkAVFSPDRSYALAG 528
Cdd:cd00200   162 WDLRTGKCVATLTGhTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNS----VAFSPDGYLLASG 237

                         250       260
                  ....*....|....*....|..
gi 2462528575 529 SCDGALYIWDVDTGKLESRLQG 550
Cdd:cd00200   238 SEDGTIRVWDLRTGECVQTLSG 259
WD40 COG2319
WD40 repeat [General function prediction only];
293-550 8.20e-44

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 160.85  E-value: 8.20e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575 293 VLDAHLSEVNAVRFGPNSSLLATGGADRLIHLWNVVGSRLEanQTLEGAGGSITSVDFDPSGYQVLAATYNQAAQLWKVG 372
Cdd:COG2319   115 TLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLL--RTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLA 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575 373 EAQSKETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWDLGRAYCSRT-------INVLSYCNDvvcgDHIIISGHNDQ 445
Cdd:COG2319   193 TGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTltghsgsVRSVAFSPD----GRLLASGSADG 268

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575 446 KIRFWDSRGPHCTQVIPVQ-GRVTSLSLSHDQLHLLSCSRDNTLKVIDLRVSNIRQVFRADGFKCGSdwtkAVFSPDRSY 524
Cdd:COG2319   269 TVRLWDLATGELLRTLTGHsGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRS----VAFSPDGKT 344

                         250       260
                  ....*....|....*....|....*.
gi 2462528575 525 ALAGSCDGALYIWDVDTGKLESRLQG 550
Cdd:COG2319   345 LASGSDDGTVRLWDLATGELLRTLTG 370
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 120-203 9.94e-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: 89.55  E-value: 9.94e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575 120 TLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDLLERLVQRK 199
Cdd:cd22887     1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEENDELVERWMAKK 80


                  ....
gi 2462528575 200 ARAA 203
Cdd:cd22887    81 QQEA 84
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 92-244 2.09e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 57.25  E-value: 2.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575  92 KWQEEEEGLRLVcgEMAYQVVEKGAALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALR 171
Cdd:COG1196   217 ELKEELKELEAE--LLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462528575 172 AHVGLREAALRRLQEEARDLLERLVQRKARAAAERNLRNERRERAKQARVSQELKKAAKRTVSISESASATSL 244
Cdd:COG1196   295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 293-326 1.23e-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: 1.23e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2462528575  293 VLDAHLSEVNAVRFGPNSSLLATGGADRLIHLWN 326
Cdd:smart00320   7 TLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
293-326 3.03e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 43.87  E-value: 3.03e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2462528575 293 VLDAHLSEVNAVRFGPNSSLLATGGADRLIHLWN 326
Cdd:pfam00400   6 TLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 301-496 1.41e-05

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 48.16  E-value: 1.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575 301 VNAVRFGPNSSLLATGGADRLIHLWN----VVGSRLEANQTLEGAGGS-ITSVDFDPS-GYQVLAATYNQAAQLWKVGEA 374
Cdd:PLN00181  486 VCAIGFDRDGEFFATAGVNKKIKIFEcesiIKDGRDIHYPVVELASRSkLSGICWNSYiKSQVASSNFEGVVQVWDVARS 565

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575 375 QSKETLSGHKDKVTAAKFKLTRHQAV-TGSRDRTVKEWDLGRAYCSRTINVLSycnDVVC------GDHIIISGHNDQKI 447
Cdd:PLN00181  566 QLVTEMKEHEKRVWSIDYSSADPTLLaSGSDDGSVKLWSINQGVSIGTIKTKA---NICCvqfpseSGRSLAFGSADHKV 642

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462528575 448 RFWDSRGPH---CTQVipvqGRVTSLSLSH--DQLHLLSCSRDNTLKVIDLRVS 496
Cdd:PLN00181  643 YYYDLRNPKlplCTMI----GHSKTVSYVRfvDSSTLVSSSTDNTLKLWDLSMS 692
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 94-224 1.05e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.43  E-value: 1.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575   94 QEEEEGLRLVCGEMAYQVVEKGAALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRah 173
Cdd:TIGR02168  732 RKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR-- 809

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2462528575  174 vglreAALRRLQEEARDLLERLVQRKARAAAERNLRNERRERAKQARVSQE 224
Cdd:TIGR02168  810 -----AELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIE 855
PTZ00121 PTZ00121
MAEBL; Provisional
 122-239 1.20e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 1.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575  122 ESELQQRQSRLAALEARVAQLREA-----RAQQAQQVEEWRaQNAVQRAAYEALRAHVGLREAALR----RLQEEARDLL 192
Cdd:PTZ00121  1209 EEERKAEEARKAEDAKKAEAVKKAeeakkDAEEAKKAEEER-NNEEIRKFEEARMAHFARRQAAIKaeeaRKADELKKAE 1287

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2462528575  193 ERLVQRKARAAAERNLRNERRERAKQARVSQELKKAAKRTVSISESA 239
Cdd:PTZ00121  1288 EKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAA 1334
 
Name Accession Description Interval E-value
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 32-203 2.71e-56

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: 187.06  E-value: 2.71e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575  32 LFLELVPAYNHLLEKAELLDKFSKKLQPEPNSVTPTTHQGPWEESELDSDQVPSLVALRVKWQEEEEGLRLVCGEMAYQV 111
Cdd:pfam08614   1 AFLELIDAYNRLLDRTALLEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQLREELAELYRSRGELAQRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575 112 VEKGAALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDL 191
Cdd:pfam08614  81 VDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQDELVALQLQLNMAEEKLRKLEKENREL 160

                         170
                  ....*....|..
gi 2462528575 192 LERLVQRKARAA 203
Cdd:pfam08614 161 VERWMKRKGQEA 172
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 293-550 4.41e-50

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: 174.45  E-value: 4.41e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575 293 VLDAHLSEVNAVRFGPNSSLLATGGADRLIHLWNVVGSRLEanQTLEGAGGSITSVDFDPSGYQVLAATYNQAAQLWKVG 372
Cdd:cd00200     4 TLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELL--RTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575 373 EAQSKETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWDLGRAYCSRTIN-VLSYCNDVV--CGDHIIISGHNDQKIRF 449
Cdd:cd00200    82 TGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRgHTDWVNSVAfsPDGTFVASSSQDGTIKL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575 450 WDSRGPHCTQVIPV-QGRVTSLSLSHDQLHLLSCSRDNTLKVIDLRVSNIRQVFRADGFKCGSdwtkAVFSPDRSYALAG 528
Cdd:cd00200   162 WDLRTGKCVATLTGhTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNS----VAFSPDGYLLASG 237

                         250       260
                  ....*....|....*....|..
gi 2462528575 529 SCDGALYIWDVDTGKLESRLQG 550
Cdd:cd00200   238 SEDGTIRVWDLRTGECVQTLSG 259
WD40 COG2319
WD40 repeat [General function prediction only];
293-550 8.20e-44

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 160.85  E-value: 8.20e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575 293 VLDAHLSEVNAVRFGPNSSLLATGGADRLIHLWNVVGSRLEanQTLEGAGGSITSVDFDPSGYQVLAATYNQAAQLWKVG 372
Cdd:COG2319   115 TLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLL--RTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLA 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575 373 EAQSKETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWDLGRAYCSRT-------INVLSYCNDvvcgDHIIISGHNDQ 445
Cdd:COG2319   193 TGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTltghsgsVRSVAFSPD----GRLLASGSADG 268

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575 446 KIRFWDSRGPHCTQVIPVQ-GRVTSLSLSHDQLHLLSCSRDNTLKVIDLRVSNIRQVFRADGFKCGSdwtkAVFSPDRSY 524
Cdd:COG2319   269 TVRLWDLATGELLRTLTGHsGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRS----VAFSPDGKT 344

                         250       260
                  ....*....|....*....|....*.
gi 2462528575 525 ALAGSCDGALYIWDVDTGKLESRLQG 550
Cdd:COG2319   345 LASGSDDGTVRLWDLATGELLRTLTG 370
WD40 COG2319
WD40 repeat [General function prediction only];
282-556 1.85e-41

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 154.30  E-value: 1.85e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575 282 VAARLPTRAQDVLDAHLSEVNAVRFGPNSSLLATGGADRLIHLWNVVGSRLEAnqTLEGAGGSITSVDFDPSGYQVLAAT 361
Cdd:COG2319    62 LLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLR--TLTGHTGAVRSVAFSPDGKTLASGS 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575 362 YNQAAQLWKVGEAQSKETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWDLGRAYCSRT-------INVLSYCNDvvcg 434
Cdd:COG2319   140 ADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTltghtgaVRSVAFSPD---- 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575 435 DHIIISGHNDQKIRFWDSRGPHCTQVIPV-QGRVTSLSLSHDQLHLLSCSRDNTLKVIDLRVSNIRQVFRADgfkcgSDW 513
Cdd:COG2319   216 GKLLASGSADGTVRLWDLATGKLLRTLTGhSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGH-----SGG 290

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 2462528575 514 TKAV-FSPDRSYALAGSCDGALYIWDVDTGKLESRLQGPHWYLN 556
Cdd:COG2319   291 VNSVaFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVR 334
WD40 COG2319
WD40 repeat [General function prediction only];
293-541 9.28e-38

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 143.90  E-value: 9.28e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575 293 VLDAHLSEVNAVRFGPNSSLLATGGADRLIHLWNVVGSRLEanQTLEGAGGSITSVDFDPSGYQVLAATYNQAAQLWKVG 372
Cdd:COG2319   157 TLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLL--RTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLA 234

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575 373 EAQSKETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWDLGRAYCSRTinvLSYCNDVVCG------DHIIISGHNDQK 446
Cdd:COG2319   235 TGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRT---LTGHSGGVNSvafspdGKLLASGSDDGT 311

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575 447 IRFWDSRGPHCTQVIPV-QGRVTSLSLSHDQLHLLSCSRDNTLKVIDLRVSNIRQVFRAdgfkcGSDWTKAV-FSPDRSY 524
Cdd:COG2319   312 VRLWDLATGKLLRTLTGhTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTG-----HTGAVTSVaFSPDGRT 386

                         250
                  ....*....|....*..
gi 2462528575 525 ALAGSCDGALYIWDVDT 541
Cdd:COG2319   387 LASGSADGTVRLWDLAT 403
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 293-490 8.49e-34

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 130.15  E-value: 8.49e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575 293 VLDAHLSEVNAVRFGPNSSLLATGGADRLIHLWNVVGSRLEanQTLEGAGGSITSVDFDPSGYQVLAATYNQAAQLWKVG 372
Cdd:cd00200    88 TLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCL--TTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLR 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575 373 EAQSKETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWDLgraYCSRTINVLSYCNDVVCG------DHIIISGHNDQK 446
Cdd:cd00200   166 TGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDL---STGKCLGTLRGHENGVNSvafspdGYLLASGSEDGT 242

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2462528575 447 IRFWDSRGPHCTQVIP-VQGRVTSLSLSHDQLHLLSCSRDNTLKV 490
Cdd:cd00200   243 IRVWDLRTGECVQTLSgHTNSVTSLAWSPDGKRLASGSADGTIRI 287
WD40 COG2319
WD40 repeat [General function prediction only];
305-556 1.24e-24

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 106.15  E-value: 1.24e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575 305 RFGPNSSLLATGGADRLIHLWNVVGSRLEAnqTLEGAGGSITSVDFDPSGYQVLAATYNQAAQLWKVGEAQSKETLSGHK 384
Cdd:COG2319     1 ALSADGAALAAASADLALALLAAALGALLL--LLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575 385 DKVTAAKFKLTRHQAVTGSRDRTVKEWDLGRAYCSRTINVL-SYCNDVVC--GDHIIISGHNDQKIRFWDSRGPHCTQVI 461
Cdd:COG2319    79 AAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHtGAVRSVAFspDGKTLASGSADGTVRLWDLATGKLLRTL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575 462 PV-QGRVTSLSLSHDQLHLLSCSRDNTLKVIDLRVSNIRQVFRADgfkcgSDWTKAV-FSPDRSYALAGSCDGALYIWDV 539
Cdd:COG2319   159 TGhSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGH-----TGAVRSVaFSPDGKLLASGSADGTVRLWDL 233

                         250
                  ....*....|....*..
gi 2462528575 540 DTGKLESRLQGPHWYLN 556
Cdd:COG2319   234 ATGKLLRTLTGHSGSVR 250
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 120-203 9.94e-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: 89.55  E-value: 9.94e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575 120 TLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDLLERLVQRK 199
Cdd:cd22887     1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEENDELVERWMAKK 80


                  ....
gi 2462528575 200 ARAA 203
Cdd:cd22887    81 QQEA 84
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 293-412 2.05e-17

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: 82.77  E-value: 2.05e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575 293 VLDAHLSEVNAVRFGPNSSLLATGGADRLIHLWNVVGSRLEanQTLEGAGGSITSVDFDPSGYQVLAATYNQAAQLWKVG 372
Cdd:cd00200   172 TLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCL--GTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLR 249

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2462528575 373 EAQSKETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWD 412
Cdd:cd00200   250 TGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 92-244 2.09e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 57.25  E-value: 2.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575  92 KWQEEEEGLRLVcgEMAYQVVEKGAALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALR 171
Cdd:COG1196   217 ELKEELKELEAE--LLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462528575 172 AHVGLREAALRRLQEEARDLLERLVQRKARAAAERNLRNERRERAKQARVSQELKKAAKRTVSISESASATSL 244
Cdd:COG1196   295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 94-231 2.97e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.40  E-value: 2.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575  94 QEEEEGLRLVCGEMAYQVVEKGAALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAH 173
Cdd:COG1196   315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462528575 174 VGLREAALRRLQEEARDLLERLVQRKARAAAERNLRNERRERAKQARVSQELKKAAKR 231
Cdd:COG1196   395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
92-237 3.25e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.38  E-value: 3.25e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575   92 KWQEEEEGLRLVCGEMAYQVVEK-----GAALGTLESELQQRQSRLAALEARVAQLREARAQQ-AQQVEEWRAQNAV--- 162
Cdd:COG4913    273 ELEYLRAALRLWFAQRRLELLEAeleelRAELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERler 352

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575  163 -------QRAAYEALRAHVGLR----EAALRRLQEEARDLLERLVQRKARAAAERNLRNERRERAKQAR--VSQELKKAA 229
Cdd:COG4913    353 eleererRRARLEALLAALGLPlpasAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELreLEAEIASLE 432


                   ....*...
gi 2462528575  230 KRTVSISE 237
Cdd:COG4913    433 RRKSNIPA 440
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 293-326 1.23e-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: 1.23e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2462528575  293 VLDAHLSEVNAVRFGPNSSLLATGGADRLIHLWN 326
Cdd:smart00320   7 TLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
110-233 2.95e-06

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 49.28  E-value: 2.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575 110 QVVEKGAALGTLESElqQRQSRLAALEARVAQLrEARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQ---- 185
Cdd:COG1566    65 DRVKKGQVLARLDPT--DLQAALAQAEAQLAAA-EAQLARLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQalyk 141

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462528575 186 ---------EEARDLLERLVQRKARAAAERNLRNERRERAKQARVSQELKKAAKRTV 233
Cdd:COG1566   142 kgavsqqelDEARAALDAAQAQLEAAQAQLAQAQAGLREEEELAAAQAQVAQAEAAL 198
WD40 pfam00400
WD domain, G-beta repeat;
293-326 3.03e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 43.87  E-value: 3.03e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2462528575 293 VLDAHLSEVNAVRFGPNSSLLATGGADRLIHLWN 326
Cdd:pfam00400   6 TLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
 110-196 1.10e-05

Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope biogenesis, Defense mechanisms];


Pssm-ID: 440606 [Multi-domain]  Cd Length: 324  Bit Score: 47.63  E-value: 1.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575 110 QVVEKGAALGTLESELQQrqsrlAALEARVAQLREARAQ------QAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRR 183
Cdd:COG0845    43 DRVKKGQVLARLDPPDLQ-----AALAQAQAQLAAAQAQlelakaELERYKALLKKGAVSQQELDQAKAALDQAQAALAA 117

                          90
                  ....*....|....*.
gi 2462528575 184 LQ---EEARDLLERLV 196
Cdd:COG0845   118 AQaalEQARANLAYTT 133
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 301-496 1.41e-05

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 48.16  E-value: 1.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575 301 VNAVRFGPNSSLLATGGADRLIHLWN----VVGSRLEANQTLEGAGGS-ITSVDFDPS-GYQVLAATYNQAAQLWKVGEA 374
Cdd:PLN00181  486 VCAIGFDRDGEFFATAGVNKKIKIFEcesiIKDGRDIHYPVVELASRSkLSGICWNSYiKSQVASSNFEGVVQVWDVARS 565

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575 375 QSKETLSGHKDKVTAAKFKLTRHQAV-TGSRDRTVKEWDLGRAYCSRTINVLSycnDVVC------GDHIIISGHNDQKI 447
Cdd:PLN00181  566 QLVTEMKEHEKRVWSIDYSSADPTLLaSGSDDGSVKLWSINQGVSIGTIKTKA---NICCvqfpseSGRSLAFGSADHKV 642

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462528575 448 RFWDSRGPH---CTQVipvqGRVTSLSLSH--DQLHLLSCSRDNTLKVIDLRVS 496
Cdd:PLN00181  643 YYYDLRNPKlplCTMI----GHSKTVSYVRfvDSSTLVSSSTDNTLKLWDLSMS 692
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 121-204 1.63e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 47.45  E-value: 1.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575 121 LESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDLLERLVQRKA 200
Cdd:COG4942    25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104


                  ....
gi 2462528575 201 RAAA 204
Cdd:COG4942   105 ELAE 108
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 74-224 2.74e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.24  E-value: 2.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575  74 EESELDSDQVPSLVALRVKWQEEEEGLRLVCGEMAYQVVEKGAALGTLESE-----------------LQQRQSRlaaLE 136
Cdd:COG1196   246 AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAElarleqdiarleerrreLEERLEE---LE 322

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575 137 ARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDLLERLVQRKARAAAERNLRNERRERA 216
Cdd:COG1196   323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402


                  ....*...
gi 2462528575 217 KQARVSQE 224
Cdd:COG1196   403 EELEEAEE 410
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
120-204 6.62e-05

Phage shock protein A [Transcription, Signal transduction mechanisms];


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 44.43  E-value: 6.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575 120 TLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDLLERLVQR- 198
Cdd:COG1842    95 ELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAAKAQEKVNEALSGIDSDDATSALERMEEKi 174


                  ....*....
gi 2462528575 199 ---KARAAA 204
Cdd:COG1842   175 eemEARAEA 183
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
118-247 8.16e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.28  E-value: 8.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575 118 LGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDLLERLVQ 197
Cdd:COG4372    82 LEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLES 161

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462528575 198 RKARAAAERNLRNERRERAKQARVSQELKKAAKRTVSISESASATSLTLS 247
Cdd:COG4372   162 LQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIES 211
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 94-224 1.05e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.43  E-value: 1.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575   94 QEEEEGLRLVCGEMAYQVVEKGAALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRah 173
Cdd:TIGR02168  732 RKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR-- 809

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2462528575  174 vglreAALRRLQEEARDLLERLVQRKARAAAERNLRNERRERAKQARVSQE 224
Cdd:TIGR02168  810 -----AELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIE 855
PTZ00421 PTZ00421
coronin; Provisional
 304-412 1.23e-04

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 44.88  E-value: 1.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575 304 VRFGP-NSSLLATGGADRLIHLWNVVGSRLEANQT-----LEGAGGSITSVDFDPSGYQVLA-ATYNQAAQLWKVGEAQS 376
Cdd:PTZ00421   81 VAFNPfDPQKLFTASEDGTIMGWGIPEEGLTQNISdpivhLQGHTKKVGIVSFHPSAMNVLAsAGADMVVNVWDVERGKA 160

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2462528575 377 KETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWD 412
Cdd:PTZ00421  161 VEVIKCHSDQITSLEWNLDGSLLCTTSKDKKLNIID 196
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 379-412 1.38e-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: 1.38e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2462528575  379 TLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWD 412
Cdd:smart00320   7 TLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
379-412 1.44e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 39.25  E-value: 1.44e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2462528575 379 TLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWD 412
Cdd:pfam00400   6 TLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
116-237 1.97e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 44.24  E-value: 1.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575 116 AALGTLESELQQRQSRLAALEARVAQLREARAQ---------QAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQE 186
Cdd:COG3206   219 QQLSELESQLAEARAELAEAEARLAALRAQLGSgpdalpellQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRA 298

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462528575 187 EARDLLERLVQRKARAAAeRNLRNERRERAKQARVSQELKKAAKRTVSISE 237
Cdd:COG3206   299 QIAALRAQLQQEAQRILA-SLEAELEALQAREASLQAQLAQLEARLAELPE 348
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
129-231 2.87e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.75  E-value: 2.87e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575  129 QSRLAALEARVAQLREARAQ---QAQQVEEWRAQNAVQRAAYEALRAH------VGLREAALRRLQEEARDL------LE 193
Cdd:COG4913    609 RAKLAALEAELAELEEELAEaeeRLEALEAELDALQERREALQRLAEYswdeidVASAEREIAELEAELERLdassddLA 688

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 2462528575  194 RLVQR--KARAAAERNLRNERRERAKQARVSQELKKAAKR 231
Cdd:COG4913    689 ALEEQleELEAELEELEEELDELKGEIGRLEKELEQAEEE 728
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 124-357 3.24e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 43.28  E-value: 3.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575 124 ELQQRQSRL----AALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDLLERLVQRK 199
Cdd:COG3883   137 ELKADKAELeakkAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575 200 ARAAAERNLRNERRERAKQARVSQELKKAAKRTVSISESASATSLTLSHCVDvvkglldfkkRRGHSIGGAPEQRYQIIP 279
Cdd:COG3883   217 AAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAA----------AGAAGAGAAAASAAGGGA 286

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462528575 280 VCVAARLPTRAQDVLDAHLSEVNAVRFGPNSSLLATGGADRLIHLWNVVGSRLEANQTLEGAGGSITSVDFDPSGYQV 357
Cdd:COG3883   287 GGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAVVGGASAGGGGGSGGGGGSSGGGSGGGGGGGGGGGGSSSGGGG 364
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 94-195 3.32e-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: 43.89  E-value: 3.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575   94 QEEEEGLRLVCGEMAYQVVEKGAALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAH 173
Cdd:TIGR02168  844 EEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923

                           90       100
                   ....*....|....*....|..
gi 2462528575  174 VGLREAALRRLQEEARDLLERL 195
Cdd:TIGR02168  924 LAQLELRLEGLEVRIDNLQERL 945
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
118-200 3.90e-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: 3.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575  118 LGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHvGLREAALRRLQEEARDLLERLVQ 197
Cdd:COG4913    663 VASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRL-EKELEQAEEELDELQDRLEAAED 741


                   ...
gi 2462528575  198 RKA 200
Cdd:COG4913    742 LAR 744
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
81-198 4.75e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.22  E-value: 4.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575  81 DQVPSLVALRVKWQEEEEGLRLVCGEMayQVVEKGAALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQN 160
Cdd:COG4717   392 EQAEEYQELKEELEELEEQLEELLGEL--EELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDG 469

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2462528575 161 AVQRAAYEALRAhvglrEAALRRLQEE------ARDLLERLVQR 198
Cdd:COG4717   470 ELAELLQELEEL-----KAELRELAEEwaalklALELLEEAREE 508
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 116-204 5.22e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.44  E-value: 5.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575 116 AALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDL---L 192
Cdd:COG4942   150 EQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELealI 229

                          90
                  ....*....|..
gi 2462528575 193 ERLVQRKARAAA 204
Cdd:COG4942   230 ARLEAEAAAAAE 241
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 464-492 8.33e-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: 37.29  E-value: 8.33e-04
                           10        20
                   ....*....|....*....|....*....
gi 2462528575  464 QGRVTSLSLSHDQLHLLSCSRDNTLKVID 492
Cdd:smart00320  12 TGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 121-247 9.24e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 42.36  E-value: 9.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575  121 LESELQQRQSRLAALEARVAQLREARA---QQAQQVE----EWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDLLE 193
Cdd:TIGR02169  341 LEREIEEERKRRDKLTEEYAELKEELEdlrAELEEVDkefaETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSE 420

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462528575  194 RLVQRKARAAAERNLRN--ERRERAKQARVS---QELKKAAKRTVSISESASATSLTLS 247
Cdd:TIGR02169  421 ELADLNAAIAGIEAKINelEEEKEDKALEIKkqeWKLEQLAADLSKYEQELYDLKEEYD 479
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 110-233 9.53e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.67  E-value: 9.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575 110 QVVEKGAALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEW-RAQNAVQRAAYEALRAHVGLREAALRRLQ--- 185
Cdd:COG4942    63 RIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELlRALYRLGRQPPLALLLSPEDFLDAVRRLQylk 142

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462528575 186 ----------EEARDLLERLVQRKARAAAERNLRNERRERAKQARVSQELKKAAKRTV 233
Cdd:COG4942   143 ylaparreqaEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKL 200
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
110-234 9.61e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.81  E-value: 9.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575 110 QVVEKGAALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNavqraayEALRAHVGLREAALRRLQEEAR 189
Cdd:COG4372    88 QLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQI-------AELQSEIAEREEELKELEEQLE 160

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462528575 190 DL------LERLVQRKARAAAERNLRNERRERAKQARVSQELKKAAKRTVS 234
Cdd:COG4372   161 SLqeelaaLEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIES 211
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
110-204 1.07e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 1.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575  110 QVVEKGAALGTLES------ELQQRQSRLAALEARVAQLREAR---AQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAA 180
Cdd:COG4913    642 ALQERREALQRLAEyswdeiDVASAEREIAELEAELERLDASSddlAALEEQLEELEAELEELEEELDELKGEIGRLEKE 721

                           90       100
                   ....*....|....*....|....
gi 2462528575  181 LRRLQEEARDLLERLVQRKARAAA 204
Cdd:COG4913    722 LEQAEEELDELQDRLEAAEDLARL 745
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 95-231 1.15e-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: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575  95 EEEEGLRLVCGEMAYQVVEKGAALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHV 174
Cdd:COG1196   641 TLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEE 720

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462528575 175 GLREAALRRLQEEARDLLERLVQRKARAAAERNLRNERRERAKQARvsQELKKAAKR 231
Cdd:COG1196   721 LEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELE--RELERLERE 775
PTZ00121 PTZ00121
MAEBL; Provisional
 122-239 1.20e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 1.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575  122 ESELQQRQSRLAALEARVAQLREA-----RAQQAQQVEEWRaQNAVQRAAYEALRAHVGLREAALR----RLQEEARDLL 192
Cdd:PTZ00121  1209 EEERKAEEARKAEDAKKAEAVKKAeeakkDAEEAKKAEEER-NNEEIRKFEEARMAHFARRQAAIKaeeaRKADELKKAE 1287

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2462528575  193 ERLVQRKARAAAERNLRNERRERAKQARVSQELKKAAKRTVSISESA 239
Cdd:PTZ00121  1288 EKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAA 1334
PRK12704 PRK12704
phosphodiesterase; Provisional
 121-195 1.25e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.69  E-value: 1.25e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462528575 121 LESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDLLERL 195
Cdd:PRK12704   73 FEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERI 147
RND_mfp TIGR01730
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ...
 110-190 1.26e-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: 41.15  E-value: 1.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575 110 QVVEKGAALGTLESELQQrqsrlAALEARVAQLREARAQ------QAQQVEEWRAQNAV-------QRAAYEALRAHVGL 176
Cdd:TIGR01730  46 QKVKKGQVLARLDDDDYQ-----LALQAALAQLAAAEAQlelaqrSFERAERLVKRNAVsqadlddAKAAVEAAQADLEA 120

                          90
                  ....*....|....
gi 2462528575 177 REAALRRLQEEARD 190
Cdd:TIGR01730 121 AKASLASAQLNLRY 134
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
112-247 1.29e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 1.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575 112 VEKGAALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNA----VQRAAYEALRAHVGLREAALRRLQEE 187
Cdd:COG4717   121 LEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAelaeLQEELEELLEQLSLATEEELQDLAEE 200

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575 188 ARDLLERLVQRKARAAAERNLRNERRERAKQARVSQELKKAAKRTVSISESASATSLTLS 247
Cdd:COG4717   201 LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLA 260
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 92-226 1.59e-03

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: 41.58  E-value: 1.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575   92 KWQEEEEGLRLVCGEMAYQVVEKGAALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQ------------ 159
Cdd:TIGR02168  341 ELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARlerledrrerlq 420

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462528575  160 ---NAVQRAAYEALRAHVGLREAALRRLQEEARDLLERLVQRKARAAAERNLRNERRERAKQ--ARVSQELK 226
Cdd:TIGR02168  421 qeiEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERelAQLQARLD 492
PRK09039 PRK09039
peptidoglycan -binding protein;
105-190 1.68e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 40.72  E-value: 1.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575 105 GEMAYQVVEKGAALGTLESELQQRQS-------RLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLR 177
Cdd:PRK09039   77 QDLQDSVANLRASLSAAEAERSRLQAllaelagAGAAAEGRAGELAQELDSEKQVSARALAQVELLNQQIAALRRQLAAL 156

                          90
                  ....*....|...
gi 2462528575 178 EAALRrlQEEARD 190
Cdd:PRK09039  157 EAALD--ASEKRD 167
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
113-231 2.39e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 2.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575 113 EKGAALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQR--AAYEALRAHVGLREAALRRLQEEARD 190
Cdd:COG4717    78 EELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEERLEE 157

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2462528575 191 LLERLVQRKARAAAERNLRNERRERAKQ--ARVSQELKKAAKR 231
Cdd:COG4717   158 LRELEEELEELEAELAELQEELEELLEQlsLATEEELQDLAEE 200
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 118-204 2.52e-03

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: 39.91  E-value: 2.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575 118 LGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHV-GLREAALRRLQEEARDLLERLV 196
Cdd:COG1579   105 ISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELeAEREELAAKIPPELLALYERIR 184


                  ....*...
gi 2462528575 197 QRKARAAA 204
Cdd:COG1579   185 KRKNGLAV 192
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 15-201 2.55e-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: 2.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575   15 KRHIVRQLRLRDRTQKALFLELVPAYNHLLEKAELLDKFSKKLQPEpnsVTPTTHQGPWEESELDS-DQVPSLVALRVKW 93
Cdd:TIGR02169  207 REKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEE---LEKLTEEISELEKRLEEiEQLLEELNKKIKD 283

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575   94 QEEEEGLRLV--CGEMAYQVVEKGAALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALR 171
Cdd:TIGR02169  284 LGEEEQLRVKekIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELK 363

                          170       180       190
                   ....*....|....*....|....*....|
gi 2462528575  172 AHVGLREAALRRLQEEARDLLERLVQRKAR 201
Cdd:TIGR02169  364 EELEDLRAELEEVDKEFAETRDELKDYREK 393
WD40 pfam00400
WD domain, G-beta repeat;
464-492 2.92e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 35.78  E-value: 2.92e-03
                          10        20
                  ....*....|....*....|....*....
gi 2462528575 464 QGRVTSLSLSHDQLHLLSCSRDNTLKVID 492
Cdd:pfam00400  11 TGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
mukB PRK04863
chromosome partition protein MukB;
2-201 3.93e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 40.33  E-value: 3.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575    2 AGPGVPGAPAARWKRHIVRQLRlrdrTQKALFLELVPAYNHL--LEKA--------ELLDKFSKKLQpepnsvtptthQG 71
Cdd:PRK04863   485 IAGEVSRSEAWDVARELLRRLR----EQRHLAEQLQQLRMRLseLEQRlrqqqraeRLLAEFCKRLG-----------KN 549

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575   72 PWEESELDsdqvpslvALRVKWQEEEEGLRlvcgEMAYQVVEKGAALGTLESELQQRQSRLAALE-------ARVAQLRE 144
Cdd:PRK04863   550 LDDEDELE--------QLQEELEARLESLS----ESVSEARERRMALRQQLEQLQARIQRLAARApawlaaqDALARLRE 617

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462528575  145 ARAQQ---AQQVEEWRAQNAVQRAAYEALRAHVglrEAALRRLQEEARDL-------LERLVQRKAR 201
Cdd:PRK04863   618 QSGEEfedSQDVTEYMQQLLERERELTVERDEL---AARKQALDEEIERLsqpggseDPRLNALAER 681
FliJ pfam02050
Flagellar FliJ protein;
86-198 5.29e-03

Flagellar FliJ protein;


Pssm-ID: 426581 [Multi-domain]  Cd Length: 123  Bit Score: 37.26  E-value: 5.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575  86 LVALRVKWQEEEEGLRLVCGEMA-YQVVEKGAALGTLESELQQRQSRLAalearvaQLREARAQQAQQVEEWRAQNAVQR 164
Cdd:pfam02050   7 LAEAQRELQQAEEKLEELQQYRAeYQQQLSGAGQGISAAELRNYQAFIS-------QLDEAIAQQQQELAQAEAQVEKAR 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2462528575 165 AAYEALRahvgLREAALRRLQE----EARDLLERLVQR 198
Cdd:pfam02050  80 EEWQEAR----QERKSLEKLRErekkEERKEQNRREQK 113
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 116-232 6.03e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.53  E-value: 6.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575 116 AALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRA----HVGLREAALRRLQEEARDL 191
Cdd:COG1196   442 EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEaeadYEGFLEGVKAALLLAGLRG 521

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462528575 192 LERLVQ-------------RKARAAAERNLRNERRERAKQARVSQELKKAAKRT 232
Cdd:COG1196   522 LAGAVAvligveaayeaalEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRAT 575
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 106-231 6.04e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 39.55  E-value: 6.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575  106 EMAYQVVEKGAAlgtleselqqRQSRLAALEARVAQLREARAQQAQqveewrAQNAvqraayEALRAHVGLREAALRRlQ 185
Cdd:COG3096    475 EKAYELVCKIAG----------EVERSQAWQTARELLRRYRSQQAL------AQRL------QQLRAQLAELEQRLRQ-Q 531

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 2462528575  186 EEARDLLERLVQRKAR--AAAERNLRNERRERAKQARVSQELKKAAKR 231
Cdd:COG3096    532 QNAERLLEEFCQRIGQqlDAAEELEELLAELEAQLEELEEQAAEAVEQ 579
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
118-200 6.50e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.12  E-value: 6.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575 118 LGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQnavqraaYEALRAHVGLREAALRRLQEEARDLLERLVQ 197
Cdd:COG4372    47 LEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQ-------LQAAQAELAQAQEELESLQEEAEELQEELEE 119


                  ...
gi 2462528575 198 RKA 200
Cdd:COG4372   120 LQK 122
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 124-204 7.59e-03

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: 38.37  E-value: 7.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575 124 ELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDLLERLVQRKARAA 203
Cdd:COG1579    90 EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELA 169


                  .
gi 2462528575 204 A 204
Cdd:COG1579   170 A 170
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 121-243 8.17e-03

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: 39.27  E-value: 8.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528575  121 LESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDLLERLVQRKA 200
Cdd:TIGR02168  696 LEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEE 775

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 2462528575  201 RAAAernlrnerrERAKQARVSQELKKAAKRTVSISESASATS 243
Cdd:TIGR02168  776 ELAE---------AEAEIEELEAQIEQLKEELKALREALDELR 809
 
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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