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Conserved domains on  [gi|55743108|ref|NP_203746|]
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protein Atg16l2 isoform 1 [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 ...
 331-619 7.24e-56

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: 191.01  E-value: 7.24e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108 331 VLDAHLSEVNAVRFGPNSSLLATGGADRLIHLWNVVGSRLEanQTLEGAGGSITSVDFDPSGYQVLAATYNQAAQLWKVG 410
Cdd:cd00200   4 TLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELL--RTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLE 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108 411 EAQSKETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWDLGRAYCSRTIN-VLSYCNDVV--CGDHIIISGHNDQKIRF 487
Cdd:cd00200  82 TGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRgHTDWVNSVAfsPDGTFVASSSQDGTIKL 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108 488 WDSRGPHCTQVIPV-QGRVTSLSLSHDQLHLLSCSRDNTLKVIDLRVSNIRQVFRADGFKCGSdwtkAVFSPDRSYALAG 566
Cdd:cd00200 162 WDLRTGKCVATLTGhTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNS----VAFSPDGYLLASG 237

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 55743108 567 SCDGALYIWDVDTGKLESRLQGpHCAAVNAVAWCYSGSHMVSVDQGRKVVLWQ 619
Cdd:cd00200 238 SEDGTIRVWDLRTGECVQTLSG-HTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 32-203 9.65e-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: 186.68  E-value: 9.65e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108    32 LFLELVPAYNHLLEKAELLDKFSKKLQPEPNSVTPTTHQGPWEESELDSDQVPSLVALRVKWQEEEEGLRLVCGEMAYQV 111
Cdd:pfam08614   1 AFLELIDAYNRLLDRTALLEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQLREELAELYRSRGELAQRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108   112 VEKGAALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDL 191
Cdd:pfam08614  81 VDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQDELVALQLQLNMAEEKLRKLEKENREL 160

                         170
                  ....*....|..
gi 55743108   192 LERLVQRKARAA 203
Cdd:pfam08614 161 VERWMKRKGQEA 172
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 121-295 6.93e-05

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


The actual alignment was detected with superfamily member TIGR02169:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1164  Bit Score: 46.21  E-value: 6.93e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108    121 LESELQQRQSRLAALEARVAQLREARA---QQAQQVE----EWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDLLE 193
Cdd:TIGR02169  341 LEREIEEERKRRDKLTEEYAELKEELEdlrAELEEVDkefaETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSE 420

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108    194 RLVQRKARAAAERNLRNERRERAKQARvsQELKKAAKRTVSISEGPDTLGDGMRERRETL--------ALAPEPEPLEKE 265
Cdd:TIGR02169  421 ELADLNAAIAGIEAKINELEEEKEDKA--LEIKKQEWKLEQLAADLSKYEQELYDLKEEYdrvekelsKLQRELAEAEAQ 498

                          170       180       190
                   ....*....|....*....|....*....|
gi 55743108    266 AcEKWKRPFRSASATSLTLSHCVDVVKGLL 295
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 ...
 331-619 7.24e-56

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: 191.01  E-value: 7.24e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108 331 VLDAHLSEVNAVRFGPNSSLLATGGADRLIHLWNVVGSRLEanQTLEGAGGSITSVDFDPSGYQVLAATYNQAAQLWKVG 410
Cdd:cd00200   4 TLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELL--RTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLE 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108 411 EAQSKETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWDLGRAYCSRTIN-VLSYCNDVV--CGDHIIISGHNDQKIRF 487
Cdd:cd00200  82 TGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRgHTDWVNSVAfsPDGTFVASSSQDGTIKL 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108 488 WDSRGPHCTQVIPV-QGRVTSLSLSHDQLHLLSCSRDNTLKVIDLRVSNIRQVFRADGFKCGSdwtkAVFSPDRSYALAG 566
Cdd:cd00200 162 WDLRTGKCVATLTGhTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNS----VAFSPDGYLLASG 237

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 55743108 567 SCDGALYIWDVDTGKLESRLQGpHCAAVNAVAWCYSGSHMVSVDQGRKVVLWQ 619
Cdd:cd00200 238 SEDGTIRVWDLRTGECVQTLSG-HTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 32-203 9.65e-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: 186.68  E-value: 9.65e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108    32 LFLELVPAYNHLLEKAELLDKFSKKLQPEPNSVTPTTHQGPWEESELDSDQVPSLVALRVKWQEEEEGLRLVCGEMAYQV 111
Cdd:pfam08614   1 AFLELIDAYNRLLDRTALLEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQLREELAELYRSRGELAQRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108   112 VEKGAALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDL 191
Cdd:pfam08614  81 VDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQDELVALQLQLNMAEEKLRKLEKENREL 160

                         170
                  ....*....|..
gi 55743108   192 LERLVQRKARAA 203
Cdd:pfam08614 161 VERWMKRKGQEA 172
WD40 COG2319
WD40 repeat [General function prediction only];
331-619 7.72e-51

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 180.88  E-value: 7.72e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108 331 VLDAHLSEVNAVRFGPNSSLLATGGADRLIHLWNVVGSRLEanQTLEGAGGSITSVDFDPSGYQVLAATYNQAAQLWKVG 410
Cdd:COG2319 115 TLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLL--RTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLA 192

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108 411 EAQSKETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWDLGRAYCSRT-------INVLSYCNDvvcgDHIIISGHNDQ 483
Cdd:COG2319 193 TGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTltghsgsVRSVAFSPD----GRLLASGSADG 268

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108 484 KIRFWDSRGPHCTQVIPVQ-GRVTSLSLSHDQLHLLSCSRDNTLKVIDLRVSNIRQVFRADGFKCGSdwtkAVFSPDRSY 562
Cdd:COG2319 269 TVRLWDLATGELLRTLTGHsGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRS----VAFSPDGKT 344

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 55743108 563 ALAGSCDGALYIWDVDTGKLESRLQGpHCAAVNAVAWCYSGSHMVSVDQGRKVVLWQ 619
Cdd:COG2319 345 LASGSDDGTVRLWDLATGELLRTLTG-HTGAVTSVAFSPDGRTLASGSADGTVRLWD 400
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 120-203 1.38e-21

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: 89.16  E-value: 1.38e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108 120 TLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDLLERLVQRK 199
Cdd:cd22887   1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEENDELVERWMAKK 80


                ....
gi 55743108 200 ARAA 203
Cdd:cd22887  81 QQEA 84
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 92-231 4.60e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.48  E-value: 4.60e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108  92 KWQEEEEGLRLVcgEMAYQVVEKGAALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALR 171
Cdd:COG1196 217 ELKEELKELEAE--LLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108 172 AHVGLREAALRRLQEEARDLLERLVQRKARAAAerNLRNERRERAKQARVSQELKKAAKR 231
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAE--LEEELEELEEELEELEEELEEAEEE 352
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 331-364 9.03e-07

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 45.77  E-value: 9.03e-07
                           10        20        30
                   ....*....|....*....|....*....|....
gi 55743108    331 VLDAHLSEVNAVRFGPNSSLLATGGADRLIHLWN 364
Cdd:smart00320   7 TLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
331-364 2.42e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 44.26  E-value: 2.42e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 55743108   331 VLDAHLSEVNAVRFGPNSSLLATGGADRLIHLWN 364
Cdd:pfam00400   6 TLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 339-534 1.61e-05

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 48.16  E-value: 1.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108  339 VNAVRFGPNSSLLATGGADRLIHLWN----VVGSRLEANQTLEGAGGS-ITSVDFDPS-GYQVLAATYNQAAQLWKVGEA 412
Cdd:PLN00181 486 VCAIGFDRDGEFFATAGVNKKIKIFEcesiIKDGRDIHYPVVELASRSkLSGICWNSYiKSQVASSNFEGVVQVWDVARS 565

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108  413 QSKETLSGHKDKVTAAKFKLTRHQAV-TGSRDRTVKEWDLGRAYCSRTINVLSycnDVVC------GDHIIISGHNDQKI 485
Cdd:PLN00181 566 QLVTEMKEHEKRVWSIDYSSADPTLLaSGSDDGSVKLWSINQGVSIGTIKTKA---NICCvqfpseSGRSLAFGSADHKV 642

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 55743108  486 RFWDSRGPH---CTQVipvqGRVTSLSLSH--DQLHLLSCSRDNTLKVIDLRVS 534
Cdd:PLN00181 643 YYYDLRNPKlplCTMI----GHSKTVSYVRfvDSSTLVSSSTDNTLKLWDLSMS 692
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 121-295 6.93e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.21  E-value: 6.93e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108    121 LESELQQRQSRLAALEARVAQLREARA---QQAQQVE----EWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDLLE 193
Cdd:TIGR02169  341 LEREIEEERKRRDKLTEEYAELKEELEdlrAELEEVDkefaETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSE 420

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108    194 RLVQRKARAAAERNLRNERRERAKQARvsQELKKAAKRTVSISEGPDTLGDGMRERRETL--------ALAPEPEPLEKE 265
Cdd:TIGR02169  421 ELADLNAAIAGIEAKINELEEEKEDKA--LEIKKQEWKLEQLAADLSKYEQELYDLKEEYdrvekelsKLQRELAEAEAQ 498

                          170       180       190
                   ....*....|....*....|....*....|
gi 55743108    266 AcEKWKRPFRSASATSLTLSHCVDVVKGLL 295
Cdd:TIGR02169  499 A-RASEERVRGGRAVEEVLKASIQGVHGTV 527
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 94-224 1.25e-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: 1.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108     94 QEEEEGLRLVCGEMAYQVVEKGAALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRah 173
Cdd:TIGR02168  732 RKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR-- 809

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 55743108    174 vglreAALRRLQEEARDLLERLVQRKARAAAERNLRNERRERAKQARVSQE 224
Cdd:TIGR02168  810 -----AELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIE 855
PTZ00121 PTZ00121
MAEBL; Provisional
 122-272 1.39e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 1.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108   122 ESELQQRQSRLAALEARVAQLREA-----RAQQAQQVEEWRaQNAVQRAAYEALRAHVGLREAALR----RLQEEARDLL 192
Cdd:PTZ00121 1209 EEERKAEEARKAEDAKKAEAVKKAeeakkDAEEAKKAEEER-NNEEIRKFEEARMAHFARRQAAIKaeeaRKADELKKAE 1287

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108   193 ERLVQRKARAAAERNLRNERRERAKQARVSQELKKAAKRTVSISEGPDTLGDGMRERRETLALAPEPEPLEKEACEKWKR 272
Cdd:PTZ00121 1288 EKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAE 1367
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 331-619 7.24e-56

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: 191.01  E-value: 7.24e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108 331 VLDAHLSEVNAVRFGPNSSLLATGGADRLIHLWNVVGSRLEanQTLEGAGGSITSVDFDPSGYQVLAATYNQAAQLWKVG 410
Cdd:cd00200   4 TLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELL--RTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLE 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108 411 EAQSKETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWDLGRAYCSRTIN-VLSYCNDVV--CGDHIIISGHNDQKIRF 487
Cdd:cd00200  82 TGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRgHTDWVNSVAfsPDGTFVASSSQDGTIKL 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108 488 WDSRGPHCTQVIPV-QGRVTSLSLSHDQLHLLSCSRDNTLKVIDLRVSNIRQVFRADGFKCGSdwtkAVFSPDRSYALAG 566
Cdd:cd00200 162 WDLRTGKCVATLTGhTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNS----VAFSPDGYLLASG 237

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 55743108 567 SCDGALYIWDVDTGKLESRLQGpHCAAVNAVAWCYSGSHMVSVDQGRKVVLWQ 619
Cdd:cd00200 238 SEDGTIRVWDLRTGECVQTLSG-HTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 32-203 9.65e-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: 186.68  E-value: 9.65e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108    32 LFLELVPAYNHLLEKAELLDKFSKKLQPEPNSVTPTTHQGPWEESELDSDQVPSLVALRVKWQEEEEGLRLVCGEMAYQV 111
Cdd:pfam08614   1 AFLELIDAYNRLLDRTALLEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQLREELAELYRSRGELAQRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108   112 VEKGAALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDL 191
Cdd:pfam08614  81 VDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQDELVALQLQLNMAEEKLRKLEKENREL 160

                         170
                  ....*....|..
gi 55743108   192 LERLVQRKARAA 203
Cdd:pfam08614 161 VERWMKRKGQEA 172
WD40 COG2319
WD40 repeat [General function prediction only];
331-619 7.72e-51

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 180.88  E-value: 7.72e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108 331 VLDAHLSEVNAVRFGPNSSLLATGGADRLIHLWNVVGSRLEanQTLEGAGGSITSVDFDPSGYQVLAATYNQAAQLWKVG 410
Cdd:COG2319 115 TLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLL--RTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLA 192

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108 411 EAQSKETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWDLGRAYCSRT-------INVLSYCNDvvcgDHIIISGHNDQ 483
Cdd:COG2319 193 TGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTltghsgsVRSVAFSPD----GRLLASGSADG 268

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108 484 KIRFWDSRGPHCTQVIPVQ-GRVTSLSLSHDQLHLLSCSRDNTLKVIDLRVSNIRQVFRADGFKCGSdwtkAVFSPDRSY 562
Cdd:COG2319 269 TVRLWDLATGELLRTLTGHsGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRS----VAFSPDGKT 344

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 55743108 563 ALAGSCDGALYIWDVDTGKLESRLQGpHCAAVNAVAWCYSGSHMVSVDQGRKVVLWQ 619
Cdd:COG2319 345 LASGSDDGTVRLWDLATGELLRTLTG-HTGAVTSVAFSPDGRTLASGSADGTVRLWD 400
WD40 COG2319
WD40 repeat [General function prediction only];
320-618 8.87e-48

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 172.40  E-value: 8.87e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108 320 VAARLPTRAQDVLDAHLSEVNAVRFGPNSSLLATGGADRLIHLWNVVGSRLEAnqTLEGAGGSITSVDFDPSGYQVLAAT 399
Cdd:COG2319  62 LLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLR--TLTGHTGAVRSVAFSPDGKTLASGS 139

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108 400 YNQAAQLWKVGEAQSKETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWDLGRAYCSRT-------INVLSYCNDvvcg 472
Cdd:COG2319 140 ADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTltghtgaVRSVAFSPD---- 215

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108 473 DHIIISGHNDQKIRFWDSRGPHCTQVIPV-QGRVTSLSLSHDQLHLLSCSRDNTLKVIDLRVSNIRQVFRADgfkcgSDW 551
Cdd:COG2319 216 GKLLASGSADGTVRLWDLATGKLLRTLTGhSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGH-----SGG 290

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 55743108 552 TKAV-FSPDRSYALAGSCDGALYIWDVDTGKLESRLQGpHCAAVNAVAWCYSGSHMVSVDQGRKVVLW 618
Cdd:COG2319 291 VNSVaFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTG-HTGAVRSVAFSPDGKTLASGSDDGTVRLW 357
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 374-619 9.75e-41

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: 149.79  E-value: 9.75e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108 374 QTLEGAGGSITSVDFDPSGYQVLAATYNQAAQLWKVGEAQSKETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWDLGR 453
Cdd:cd00200   3 RTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLET 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108 454 AYCSRTINvlSYCNDVVCGD-----HIIISGHNDQKIRFWDSRGPHCTQVIP-VQGRVTSLSLSHDQLHLLSCSRDNTLK 527
Cdd:cd00200  83 GECVRTLT--GHTSYVSSVAfspdgRILSSSSRDKTIKVWDVETGKCLTTLRgHTDWVNSVAFSPDGTFVASSSQDGTIK 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108 528 VIDLRVSNIRQVFraDGFKcgsDWTKAV-FSPDRSYALAGSCDGALYIWDVDTGKLESRLQGpHCAAVNAVAWCYSGSHM 606
Cdd:cd00200 161 LWDLRTGKCVATL--TGHT---GEVNSVaFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRG-HENGVNSVAFSPDGYLL 234

                       250
                ....*....|...
gi 55743108 607 VSVDQGRKVVLWQ 619
Cdd:cd00200 235 ASGSEDGTIRVWD 247
WD40 COG2319
WD40 repeat [General function prediction only];
320-618 1.29e-39

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 150.06  E-value: 1.29e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108 320 VAARLPTRAQDVLDAHLSEVNAVRFGPNSSLLATGGADRLIHLWNVVGSRLEAnqTLEGAGGSITSVDFDPSGYQVLAAT 399
Cdd:COG2319  20 LLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLA--TLLGHTAAVLSVAFSPDGRLLASAS 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108 400 YNQAAQLWKVGEAQSKETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWDLGRAYCSRT-------INVLSYCNDvvcg 472
Cdd:COG2319  98 ADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTltghsgaVTSVAFSPD---- 173

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108 473 DHIIISGHNDQKIRFWDSRGPHCTQVIPV-QGRVTSLSLSHDQLHLLSCSRDNTLKVIDLRVSNIRQVFRADgfkcgSDW 551
Cdd:COG2319 174 GKLLASGSDDGTVRLWDLATGKLLRTLTGhTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGH-----SGS 248

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 55743108 552 TKAV-FSPDRSYALAGSCDGALYIWDVDTGKLESRLQGpHCAAVNAVAWCYSGSHMVSVDQGRKVVLW 618
Cdd:COG2319 249 VRSVaFSPDGRLLASGSADGTVRLWDLATGELLRTLTG-HSGGVNSVAFSPDGKLLASGSDDGTVRLW 315
WD40 COG2319
WD40 repeat [General function prediction only];
331-579 3.77e-38

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 145.82  E-value: 3.77e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108 331 VLDAHLSEVNAVRFGPNSSLLATGGADRLIHLWNVVGSRLEanQTLEGAGGSITSVDFDPSGYQVLAATYNQAAQLWKVG 410
Cdd:COG2319 157 TLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLL--RTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLA 234

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108 411 EAQSKETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWDLGRAYCSRTinvLSYCNDVVCG------DHIIISGHNDQK 484
Cdd:COG2319 235 TGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRT---LTGHSGGVNSvafspdGKLLASGSDDGT 311

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108 485 IRFWDSRGPHCTQVIPV-QGRVTSLSLSHDQLHLLSCSRDNTLKVIDLRVSNIRQVFRAdgfkcGSDWTKAV-FSPDRSY 562
Cdd:COG2319 312 VRLWDLATGKLLRTLTGhTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTG-----HTGAVTSVaFSPDGRT 386

                       250
                ....*....|....*..
gi 55743108 563 ALAGSCDGALYIWDVDT 579
Cdd:COG2319 387 LASGSADGTVRLWDLAT 403
WD40 COG2319
WD40 repeat [General function prediction only];
343-619 1.35e-30

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 124.25  E-value: 1.35e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108 343 RFGPNSSLLATGGADRLIHLWNVVGSRLEAnqTLEGAGGSITSVDFDPSGYQVLAATYNQAAQLWKVGEAQSKETLSGHK 422
Cdd:COG2319   1 ALSADGAALAAASADLALALLAAALGALLL--LLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHT 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108 423 DKVTAAKFKLTRHQAVTGSRDRTVKEWDLGRAYCSRTINVL-SYCNDVVC--GDHIIISGHNDQKIRFWDSRGPHCTQVI 499
Cdd:COG2319  79 AAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHtGAVRSVAFspDGKTLASGSADGTVRLWDLATGKLLRTL 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108 500 PV-QGRVTSLSLSHDQLHLLSCSRDNTLKVIDLRVSNIRQVFRADgfkcgSDWTKAV-FSPDRSYALAGSCDGALYIWDV 577
Cdd:COG2319 159 TGhSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGH-----TGAVRSVaFSPDGKLLASGSADGTVRLWDL 233

                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 55743108 578 DTGKLESRLQGpHCAAVNAVAWCYSGSHMVSVDQGRKVVLWQ 619
Cdd:COG2319 234 ATGKLLRTLTG-HSGSVRSVAFSPDGRLLASGSADGTVRLWD 274
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 120-203 1.38e-21

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: 89.16  E-value: 1.38e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108 120 TLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDLLERLVQRK 199
Cdd:cd22887   1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEENDELVERWMAKK 80


                ....
gi 55743108 200 ARAA 203
Cdd:cd22887  81 QQEA 84
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 92-231 4.60e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.48  E-value: 4.60e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108  92 KWQEEEEGLRLVcgEMAYQVVEKGAALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALR 171
Cdd:COG1196 217 ELKEELKELEAE--LLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108 172 AHVGLREAALRRLQEEARDLLERLVQRKARAAAerNLRNERRERAKQARVSQELKKAAKR 231
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAE--LEEELEELEEELEELEEELEEAEEE 352
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 94-256 2.18e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.17  E-value: 2.18e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108  94 QEEEEGLRLVCGEMAYQVVEKGAALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAH 173
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108 174 VGLREAALRRLQEEARDLLERLVQRKARAAAERNLRNERRERAKQARvsQELKKAAKRTVSISEGPDTLGDGMRERRETL 253
Cdd:COG1196 395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE--EALEEAAEEEAELEEEEEALLELLAELLEEA 472


                ...
gi 55743108 254 ALA 256
Cdd:COG1196 473 ALL 475
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
92-237 3.77e-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: 3.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108   92 KWQEEEEGLRLVCGEMAYQVVEK-----GAALGTLESELQQRQSRLAALEARVAQLREARAQQ-AQQVEEWRAQNAV--- 162
Cdd:COG4913  273 ELEYLRAALRLWFAQRRLELLEAeleelRAELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERler 352

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108  163 -------QRAAYEALRAHVGLR----EAALRRLQEEARDLLERLVQRKARAAAERNLRNERRERAKQAR--VSQELKKAA 229
Cdd:COG4913  353 eleererRRARLEALLAALGLPlpasAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELreLEAEIASLE 432


                 ....*...
gi 55743108  230 KRTVSISE 237
Cdd:COG4913  433 RRKSNIPA 440
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 331-364 9.03e-07

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 45.77  E-value: 9.03e-07
                           10        20        30
                   ....*....|....*....|....*....|....
gi 55743108    331 VLDAHLSEVNAVRFGPNSSLLATGGADRLIHLWN 364
Cdd:smart00320   7 TLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
331-364 2.42e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 44.26  E-value: 2.42e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 55743108   331 VLDAHLSEVNAVRFGPNSSLLATGGADRLIHLWN 364
Cdd:pfam00400   6 TLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
110-233 3.14e-06

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 49.66  E-value: 3.14e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108 110 QVVEKGAALGTLESElqQRQSRLAALEARVAQLrEARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQ---- 185
Cdd:COG1566  65 DRVKKGQVLARLDPT--DLQAALAQAEAQLAAA-EAQLARLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQalyk 141

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 55743108 186 ---------EEARDLLERLVQRKARAAAERNLRNERRERAKQARVSQELKKAAKRTV 233
Cdd:COG1566 142 kgavsqqelDEARAALDAAQAQLEAAQAQLAQAQAGLREEEELAAAQAQVAQAEAAL 198
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
 110-196 1.24e-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: 1.24e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108 110 QVVEKGAALGTLESELQQrqsrlAALEARVAQLREARAQ------QAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRR 183
Cdd:COG0845  43 DRVKKGQVLARLDPPDLQ-----AALAQAQAQLAAAQAQlelakaELERYKALLKKGAVSQQELDQAKAALDQAQAALAA 117

                        90
                ....*....|....*.
gi 55743108 184 LQ---EEARDLLERLV 196
Cdd:COG0845 118 AQaalEQARANLAYTT 133
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 339-534 1.61e-05

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 48.16  E-value: 1.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108  339 VNAVRFGPNSSLLATGGADRLIHLWN----VVGSRLEANQTLEGAGGS-ITSVDFDPS-GYQVLAATYNQAAQLWKVGEA 412
Cdd:PLN00181 486 VCAIGFDRDGEFFATAGVNKKIKIFEcesiIKDGRDIHYPVVELASRSkLSGICWNSYiKSQVASSNFEGVVQVWDVARS 565

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108  413 QSKETLSGHKDKVTAAKFKLTRHQAV-TGSRDRTVKEWDLGRAYCSRTINVLSycnDVVC------GDHIIISGHNDQKI 485
Cdd:PLN00181 566 QLVTEMKEHEKRVWSIDYSSADPTLLaSGSDDGSVKLWSINQGVSIGTIKTKA---NICCvqfpseSGRSLAFGSADHKV 642

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 55743108  486 RFWDSRGPH---CTQVipvqGRVTSLSLSH--DQLHLLSCSRDNTLKVIDLRVS 534
Cdd:PLN00181 643 YYYDLRNPKlplCTMI----GHSKTVSYVRfvDSSTLVSSSTDNTLKLWDLSMS 692
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 121-204 1.75e-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: 1.75e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108 121 LESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDLLERLVQRKA 200
Cdd:COG4942  25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104


                ....
gi 55743108 201 RAAA 204
Cdd:COG4942 105 ELAE 108
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
118-265 2.82e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.82  E-value: 2.82e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108 118 LGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDLLERLVQ 197
Cdd:COG4372  82 LEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLES 161

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 55743108 198 RKARAAAERNLRNERRERAKQARVSQELKKAAKRTVSISEGPDTLGDGMRERRETLALAPEPEPLEKE 265
Cdd:COG4372 162 LQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEA 229
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 74-224 3.71e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.85  E-value: 3.71e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108  74 EESELDSDQVPSLVALRVKWQEEEEGLRLVCGEMAYQVVEKGAALGTLESE-----------------LQQRQSRlaaLE 136
Cdd:COG1196 246 AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAElarleqdiarleerrreLEERLEE---LE 322

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108 137 ARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDLLERLVQRKARAAAERNLRNERRERA 216
Cdd:COG1196 323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402


                ....*...
gi 55743108 217 KQARVSQE 224
Cdd:COG1196 403 EELEEAEE 410
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 121-295 6.93e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.21  E-value: 6.93e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108    121 LESELQQRQSRLAALEARVAQLREARA---QQAQQVE----EWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDLLE 193
Cdd:TIGR02169  341 LEREIEEERKRRDKLTEEYAELKEELEdlrAELEEVDkefaETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSE 420

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108    194 RLVQRKARAAAERNLRNERRERAKQARvsQELKKAAKRTVSISEGPDTLGDGMRERRETL--------ALAPEPEPLEKE 265
Cdd:TIGR02169  421 ELADLNAAIAGIEAKINELEEEKEDKA--LEIKKQEWKLEQLAADLSKYEQELYDLKEEYdrvekelsKLQRELAEAEAQ 498

                          170       180       190
                   ....*....|....*....|....*....|
gi 55743108    266 AcEKWKRPFRSASATSLTLSHCVDVVKGLL 295
Cdd:TIGR02169  499 A-RASEERVRGGRAVEEVLKASIQGVHGTV 527
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
120-204 9.50e-05

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


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 44.05  E-value: 9.50e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108 120 TLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDLLERLVQR- 198
Cdd:COG1842  95 ELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAAKAQEKVNEALSGIDSDDATSALERMEEKi 174


                ....*....
gi 55743108 199 ---KARAAA 204
Cdd:COG1842 175 eemEARAEA 183
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 417-450 1.08e-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: 39.99  E-value: 1.08e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 55743108    417 TLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWD 450
Cdd:smart00320   7 TLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
417-450 1.21e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 39.64  E-value: 1.21e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 55743108   417 TLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWD 450
Cdd:pfam00400   6 TLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 94-224 1.25e-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: 1.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108     94 QEEEEGLRLVCGEMAYQVVEKGAALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRah 173
Cdd:TIGR02168  732 RKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR-- 809

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 55743108    174 vglreAALRRLQEEARDLLERLVQRKARAAAERNLRNERRERAKQARVSQE 224
Cdd:TIGR02168  810 -----AELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIE 855
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 110-445 1.33e-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: 45.05  E-value: 1.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108    110 QVVEKGAALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEEAR 189
Cdd:TIGR02168  317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108    190 DL---LERLVQRKARAAAERNLrnerrerAKQARVSQELKKAAKRTVSISEGPDTLGDGMRERRETLALAPEPEPLEKEA 266
Cdd:TIGR02168  397 SLnneIERLEARLERLEDRRER-------LQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREE 469

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108    267 CEKWKRPFRSASATSLTLSHCVDVVKGLLD------------FKKRRGHSIGGAP-------EQRYQIipvCVAARLPTR 327
Cdd:TIGR02168  470 LEEAEQALDAAERELAQLQARLDSLERLQEnlegfsegvkalLKNQSGLSGILGVlselisvDEGYEA---AIEAALGGR 546

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108    328 AQDVL----DAHLSEVNA---VRFGPNSSLLATGGADRLIhlwnvVGSRLEANQTLEGAGGSITSVDFDPSGYQVL---- 396
Cdd:TIGR02168  547 LQAVVvenlNAAKKAIAFlkqNELGRVTFLPLDSIKGTEI-----QGNDREILKNIEGFLGVAKDLVKFDPKLRKAlsyl 621

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 55743108    397 ------AATYNQAAQLWKvgEAQSKETLsghkdkVTAAKFKLTRHQAVTGSRDRT 445
Cdd:TIGR02168  622 lggvlvVDDLDNALELAK--KLRPGYRI------VTLDGDLVRPGGVITGGSAKT 668
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
116-237 1.55e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 44.62  E-value: 1.55e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108 116 AALGTLESELQQRQSRLAALEARVAQLREARAQ---------QAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQE 186
Cdd:COG3206 219 QQLSELESQLAEARAELAEAEARLAALRAQLGSgpdalpellQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRA 298

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 55743108 187 EARDLLERLVQRKARAAAeRNLRNERRERAKQARVSQELKKAAKRTVSISE 237
Cdd:COG3206 299 QIAALRAQLQQEAQRILA-SLEAELEALQAREASLQAQLAQLEARLAELPE 348
PTZ00421 PTZ00421
coronin; Provisional
 342-450 1.67e-04

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 44.50  E-value: 1.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108  342 VRFGP-NSSLLATGGADRLIHLWNVVGSRLEANQT-----LEGAGGSITSVDFDPSGYQVLA-ATYNQAAQLWKVGEAQS 414
Cdd:PTZ00421  81 VAFNPfDPQKLFTASEDGTIMGWGIPEEGLTQNISdpivhLQGHTKKVGIVSFHPSAMNVLAsAGADMVVNVWDVERGKA 160

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 55743108  415 KETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWD 450
Cdd:PTZ00421 161 VEVIKCHSDQITSLEWNLDGSLLCTTSKDKKLNIID 196
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
129-231 3.30e-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: 3.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108  129 QSRLAALEARVAQLREARAQ---QAQQVEEWRAQNAVQRAAYEALRAH------VGLREAALRRLQEEARDL------LE 193
Cdd:COG4913  609 RAKLAALEAELAELEEELAEaeeRLEALEAELDALQERREALQRLAEYswdeidVASAEREIAELEAELERLdassddLA 688

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 55743108  194 RLVQR--KARAAAERNLRNERRERAKQARVSQELKKAAKR 231
Cdd:COG4913  689 ALEEQleELEAELEELEEELDELKGEIGRLEKELEQAEEE 728
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 94-195 4.16e-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: 43.51  E-value: 4.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108     94 QEEEEGLRLVCGEMAYQVVEKGAALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAH 173
Cdd:TIGR02168  844 EEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923

                           90       100
                   ....*....|....*....|..
gi 55743108    174 VGLREAALRRLQEEARDLLERL 195
Cdd:TIGR02168  924 LAQLELRLEGLEVRIDNLQERL 945
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
118-200 4.42e-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: 4.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108  118 LGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHvGLREAALRRLQEEARDLLERLVQ 197
Cdd:COG4913  663 VASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRL-EKELEQAEEELDELQDRLEAAED 741


                 ...
gi 55743108  198 RKA 200
Cdd:COG4913  742 LAR 744
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
81-198 5.06e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.22  E-value: 5.06e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108  81 DQVPSLVALRVKWQEEEEGLRLVCGEMayQVVEKGAALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQN 160
Cdd:COG4717 392 EQAEEYQELKEELEELEEQLEELLGEL--EELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDG 469

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 55743108 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 5.53e-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: 42.44  E-value: 5.53e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108 116 AALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDL---L 192
Cdd:COG4942 150 EQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELealI 229

                        90
                ....*....|..
gi 55743108 193 ERLVQRKARAAA 204
Cdd:COG4942 230 ARLEAEAAAAAE 241
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 502-530 6.51e-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: 37.68  E-value: 6.51e-04
                           10        20
                   ....*....|....*....|....*....
gi 55743108    502 QGRVTSLSLSHDQLHLLSCSRDNTLKVID 530
Cdd:smart00320  12 TGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 110-233 9.83e-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: 9.83e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108 110 QVVEKGAALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEW-RAQNAVQRAAYEALRAHVGLREAALRRLQ--- 185
Cdd:COG4942  63 RIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELlRALYRLGRQPPLALLLSPEDFLDAVRRLQylk 142

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 55743108 186 ----------EEARDLLERLVQRKARAAAERNLRNERRERAKQARVSQELKKAAKRTV 233
Cdd:COG4942 143 ylaparreqaEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKL 200
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 124-245 1.15e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.74  E-value: 1.15e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108 124 ELQQRQSRL----AALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDLLERLVQRK 199
Cdd:COG3883 137 ELKADKAELeakkAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 55743108 200 ARAAAERNLRNERRERAKQARVSQELKKAAKRTVSISEGPDTLGDG 245
Cdd:COG3883 217 AAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSA 262
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
110-204 1.23e-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: 1.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108  110 QVVEKGAALGTLES------ELQQRQSRLAALEARVAQLREAR---AQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAA 180
Cdd:COG4913  642 ALQERREALQRLAEyswdeiDVASAEREIAELEAELERLDASSddlAALEEQLEELEAELEELEEELDELKGEIGRLEKE 721

                         90       100
                 ....*....|....*....|....
gi 55743108  181 LRRLQEEARDLLERLVQRKARAAA 204
Cdd:COG4913  722 LEQAEEELDELQDRLEAAEDLARL 745
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 579-618 1.35e-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: 36.52  E-value: 1.35e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 55743108    579 TGKLESRLQGpHCAAVNAVAWCYSGSHMVSVDQGRKVVLW 618
Cdd:smart00320   1 SGELLKTLKG-HTGPVTSVAFSPDGKYLASGSDDGTIKLW 39
RND_mfp TIGR01730
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ...
 110-190 1.39e-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: 1.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108   110 QVVEKGAALGTLESELQQrqsrlAALEARVAQLREARAQ------QAQQVEEWRAQNAV-------QRAAYEALRAHVGL 176
Cdd:TIGR01730  46 QKVKKGQVLARLDDDDYQ-----LALQAALAQLAAAEAQlelaqrSFERAERLVKRNAVsqadlddAKAAVEAAQADLEA 120

                          90
                  ....*....|....
gi 55743108   177 REAALRRLQEEARD 190
Cdd:TIGR01730 121 AKASLASAQLNLRY 134
PTZ00121 PTZ00121
MAEBL; Provisional
 122-272 1.39e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 1.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108   122 ESELQQRQSRLAALEARVAQLREA-----RAQQAQQVEEWRaQNAVQRAAYEALRAHVGLREAALR----RLQEEARDLL 192
Cdd:PTZ00121 1209 EEERKAEEARKAEDAKKAEAVKKAeeakkDAEEAKKAEEER-NNEEIRKFEEARMAHFARRQAAIKaeeaRKADELKKAE 1287

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108   193 ERLVQRKARAAAERNLRNERRERAKQARVSQELKKAAKRTVSISEGPDTLGDGMRERRETLALAPEPEPLEKEACEKWKR 272
Cdd:PTZ00121 1288 EKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAE 1367
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 95-231 1.41e-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: 1.41e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108  95 EEEEGLRLVCGEMAYQVVEKGAALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHV 174
Cdd:COG1196 641 TLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEE 720

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 55743108 175 GLREAALRRLQEEARDLLERLVQRKARAAAERNLRNERRERAKQARvsQELKKAAKR 231
Cdd:COG1196 721 LEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELE--RELERLERE 775
PTZ00121 PTZ00121
MAEBL; Provisional
 94-268 1.45e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 1.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108    94 QEEEEGLRlvcGEMAYQVVEKGAALGTLESELQQRQSRLAALEARVA-QLREA----RAQQAQQVEEWRAQNAVQRAAYE 168
Cdd:PTZ00121 1237 KDAEEAKK---AEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKAdELKKAeekkKADEAKKAEEKKKADEAKKKAEE 1313

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108   169 ALRAHvglreaALRRLQEEARDLLERLvQRKARAA--AERNLRNERRERAKQARVSQELKKAAK-RTVSISEGPDTLGDG 245
Cdd:PTZ00121 1314 AKKAD------EAKKKAEEAKKKADAA-KKKAEEAkkAAEAAKAEAEAAADEAEAAEEKAEAAEkKKEEAKKKADAAKKK 1386

                         170       180
                  ....*....|....*....|...
gi 55743108   246 MRERRETLALAPEPEPLEKEACE 268
Cdd:PTZ00121 1387 AEEKKKADEAKKKAEEDKKKADE 1409
PRK12704 PRK12704
phosphodiesterase; Provisional
 121-195 1.55e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.30  E-value: 1.55e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 55743108  121 LESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDLLERL 195
Cdd:PRK12704  73 FEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERI 147
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
112-231 1.56e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 1.56e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108 112 VEKGAALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNA----VQRAAYEALRAHVGLREAALRRLQEE 187
Cdd:COG4717 121 LEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAelaeLQEELEELLEQLSLATEEELQDLAEE 200

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 55743108 188 ARDLLERLVQRKARAAAERNLRNERRERAKQARVSQELKKAAKR 231
Cdd:COG4717 201 LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEER 244
PRK09039 PRK09039
peptidoglycan -binding protein;
105-190 1.89e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 40.72  E-value: 1.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108  105 GEMAYQVVEKGAALGTLESELQQRQS-------RLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLR 177
Cdd:PRK09039  77 QDLQDSVANLRASLSAAEAERSRLQAllaelagAGAAAEGRAGELAQELDSEKQVSARALAQVELLNQQIAALRRQLAAL 156

                         90
                 ....*....|...
gi 55743108  178 EAALRrlQEEARD 190
Cdd:PRK09039 157 EAALD--ASEKRD 167
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 92-226 1.90e-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: 1.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108     92 KWQEEEEGLRLVCGEMAYQVVEKGAALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQ------------ 159
Cdd:TIGR02168  341 ELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARlerledrrerlq 420

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 55743108    160 ---NAVQRAAYEALRAHVGLREAALRRLQEEARDLLERLVQRKARAAAERNLRNERRERAKQ--ARVSQELK 226
Cdd:TIGR02168  421 qeiEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERelAQLQARLD 492
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
113-254 1.91e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.18  E-value: 1.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108  113 EKGAALGTLESELQQRQSRLAALEARVAQLREAR--AQQAQQVEEwRAQNAVQRAAYEalRAHVGLREAALRRLQEEARD 190
Cdd:PRK02224 472 EDRERVEELEAELEDLEEEVEEVEERLERAEDLVeaEDRIERLEE-RREDLEELIAER--RETIEEKRERAEELRERAAE 548

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 55743108  191 LLE-----RLVQRKARAAAERNLRNERRERAKQARVSQE---LKKAAKRTVSISEGPDTLGDgMRERRETLA 254
Cdd:PRK02224 549 LEAeaeekREAAAEAEEEAEEAREEVAELNSKLAELKERiesLERIRTLLAAIADAEDEIER-LREKREALA 619
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
124-269 2.37e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 2.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108  124 ELQQRQSRLAALEARVAQLREARAQQAqqVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEEARDLLERL----VQRK 199
Cdd:COG4913  263 RYAAARERLAELEYLRAALRLWFAQRR--LELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIrgngGDRL 340

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108  200 ARAAAernlrNERRERAKQARVSQELKKAAKRTVSISEGPDTLGDGMRERRETLALAPEPEPLEKEACEK 269
Cdd:COG4913  341 EQLER-----EIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEE 405
WD40 pfam00400
WD domain, G-beta repeat;
502-530 2.47e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 35.78  E-value: 2.47e-03
                          10        20
                  ....*....|....*....|....*....
gi 55743108   502 QGRVTSLSLSHDQLHLLSCSRDNTLKVID 530
Cdd:pfam00400  11 TGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
113-231 2.61e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 2.61e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108 113 EKGAALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQR--AAYEALRAHVGLREAALRRLQEEARD 190
Cdd:COG4717  78 EELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEERLEE 157

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 55743108 191 LLERLVQRKARAAAERNLRNERRERAKQ--ARVSQELKKAAKR 231
Cdd:COG4717 158 LRELEEELEELEAELAELQEELEELLEQlsLATEEELQDLAEE 200
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 15-201 3.79e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.44  E-value: 3.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108     15 KRHIVRQLRLRDRTQKALFLELVPAYNHLLEKAELLDKFSKKLQPEpnsVTPTTHQGPWEESELDS-DQVPSLVALRVKW 93
Cdd:TIGR02169  207 REKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEE---LEKLTEEISELEKRLEEiEQLLEELNKKIKD 283

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108     94 QEEEEGLRLV--CGEMAYQVVEKGAALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALR 171
Cdd:TIGR02169  284 LGEEEQLRVKekIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELK 363

                          170       180       190
                   ....*....|....*....|....*....|
gi 55743108    172 AHVGLREAALRRLQEEARDLLERLVQRKAR 201
Cdd:TIGR02169  364 EELEDLRAELEEVDKEFAETRDELKDYREK 393
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 118-204 3.87e-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: 39.14  E-value: 3.87e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108 118 LGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHV-GLREAALRRLQEEARDLLERLV 196
Cdd:COG1579 105 ISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELeAEREELAAKIPPELLALYERIR 184


                ....*...
gi 55743108 197 QRKARAAA 204
Cdd:COG1579 185 KRKNGLAV 192
mukB PRK04863
chromosome partition protein MukB;
2-201 4.48e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 40.33  E-value: 4.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108     2 AGPGVPGAPAARWKRHIVRQLRlrdrTQKALFLELVPAYNHL--LEKA--------ELLDKFSKKLQpepnsvtptthQG 71
Cdd:PRK04863  485 IAGEVSRSEAWDVARELLRRLR----EQRHLAEQLQQLRMRLseLEQRlrqqqraeRLLAEFCKRLG-----------KN 549

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108    72 PWEESELDsdqvpslvALRVKWQEEEEGLRlvcgEMAYQVVEKGAALGTLESELQQRQSRLAALE-------ARVAQLRE 144
Cdd:PRK04863  550 LDDEDELE--------QLQEELEARLESLS----ESVSEARERRMALRQQLEQLQARIQRLAARApawlaaqDALARLRE 617

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 55743108   145 ARAQQ---AQQVEEWRAQNAVQRAAYEALRAHVglrEAALRRLQEEARDL-------LERLVQRKAR 201
Cdd:PRK04863  618 QSGEEfedSQDVTEYMQQLLERERELTVERDEL---AARKQALDEEIERLsqpggseDPRLNALAER 681
PTZ00121 PTZ00121
MAEBL; Provisional
 112-272 5.69e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.12  E-value: 5.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108   112 VEKGAALGTLESELQQRQSRLAALEARVAQLReaRAQQAQQVEEWRAQNAVQRAAYEALRAHvGLREAALRRLQEEARdl 191
Cdd:PTZ00121 1187 VRKAEELRKAEDARKAEAARKAEEERKAEEAR--KAEDAKKAEAVKKAEEAKKDAEEAKKAE-EERNNEEIRKFEEAR-- 1261

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108   192 LERLVQRKARAAAERNLRNERRERAKQARVSQELKKA-AKRTVsisegpDTLGDGMRERRETLALAPEPEPLEKEACEKW 270
Cdd:PTZ00121 1262 MAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAeEKKKA------DEAKKKAEEAKKADEAKKKAEEAKKKADAAK 1335


                  ..
gi 55743108   271 KR 272
Cdd:PTZ00121 1336 KK 1337
FliJ pfam02050
Flagellar FliJ protein;
86-198 5.90e-03

Flagellar FliJ protein;


Pssm-ID: 426581 [Multi-domain]  Cd Length: 123  Bit Score: 37.26  E-value: 5.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108    86 LVALRVKWQEEEEGLRLVCGEMA-YQVVEKGAALGTLESELQQRQSRLAalearvaQLREARAQQAQQVEEWRAQNAVQR 164
Cdd:pfam02050   7 LAEAQRELQQAEEKLEELQQYRAeYQQQLSGAGQGISAAELRNYQAFIS-------QLDEAIAQQQQELAQAEAQVEKAR 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 55743108   165 AAYEALRahvgLREAALRRLQE----EARDLLERLVQR 198
Cdd:pfam02050  80 EEWQEAR----QERKSLEKLRErekkEERKEQNRREQK 113
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
118-200 6.75e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.12  E-value: 6.75e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108 118 LGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQnavqraaYEALRAHVGLREAALRRLQEEARDLLERLVQ 197
Cdd:COG4372  47 LEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQ-------LQAAQAELAQAQEELESLQEEAEELQEELEE 119


                ...
gi 55743108 198 RKA 200
Cdd:COG4372 120 LQK 122
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 106-231 6.98e-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: 6.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108  106 EMAYQVVEKGAAlgtleselqqRQSRLAALEARVAQLREARAQQAQqveewrAQNAvqraayEALRAHVGLREAALRRlQ 185
Cdd:COG3096  475 EKAYELVCKIAG----------EVERSQAWQTARELLRRYRSQQAL------AQRL------QQLRAQLAELEQRLRQ-Q 531

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 55743108  186 EEARDLLERLVQRKAR--AAAERNLRNERRERAKQARVSQELKKAAKR 231
Cdd:COG3096  532 QNAERLLEEFCQRIGQqlDAAEELEELLAELEAQLEELEEQAAEAVEQ 579
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 116-232 8.34e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.15  E-value: 8.34e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108 116 AALGTLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRA----HVGLREAALRRLQEEARDL 191
Cdd:COG1196 442 EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEaeadYEGFLEGVKAALLLAGLRG 521

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 55743108 192 LERLVQ-------------RKARAAAERNLRNERRERAKQARVSQELKKAAKRT 232
Cdd:COG1196 522 LAGAVAvligveaayeaalEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRAT 575
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
120-272 9.50e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.25  E-value: 9.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743108  120 TLESELQQRQSRLAALEARVAQLREARAQQAQQVEEWRAQNAVQRAAYEALRAHVGLREAALRRLQEEaRDLLERLVQRK 199
Cdd:PRK02224 520 DLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKER-IESLERIRTLL 598

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 55743108  200 ARAAAernlrnerrerAKQARVSQELKKAAKRTVSiSEGPDTLGDgMRERRETLALAPEPEPLEkEACEKWKR 272
Cdd:PRK02224 599 AAIAD-----------AEDEIERLREKREALAELN-DERRERLAE-KRERKRELEAEFDEARIE-EAREDKER 657
 
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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