NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1044375977|ref|XP_017393168|]
View 

autophagy-related protein 16-1 isoform X2 [Cebus imitator]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
257-604 1.31e-61

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 209.77  E-value: 1.31e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977 257 VRAISRAATKRLSQPAGGLLDSITNIFGRRSVSSFPVPQDNVDTHPGSGKEVRV----PTTALCVFDAHDGEVNAVQFSP 332
Cdd:COG2319    51 LAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLwdlaTGLLLRTLTGHTGAVRSVAFSP 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977 333 GSRLLATGGMDRRVKLWEVFGEKCEfkGSLSGSNAGITSIEFDSAGSYLLAASNDFASRIWTVDDYRLRHTLTGHSGKVL 412
Cdd:COG2319   131 DGKTLASGSADGTVRLWDLATGKLL--RTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVR 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977 413 SAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTV-FAGSSCNDIVCT--EQCVMSGHFDKKIRFWDIRSESIVREME-LL 488
Cdd:COG2319   209 SVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLtGHSGSVRSVAFSpdGRLLASGSADGTVRLWDLATGELLRTLTgHS 288

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977 489 GKITALDLNPERTELLTCSRDDLLKVIDLRTNAVKQTFSAPgfkcGSDWTRVVFSPDGSYVAAGSAEGSLYIWSVLTGKV 568
Cdd:COG2319   289 GGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGH----TGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGEL 364

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1044375977 569 EKVLsKQHSSSINAVAWSPSGSHVVSVDKGCRAVLW 604
Cdd:COG2319   365 LRTL-TGHTGAVTSVAFSPDGRTLASGSADGTVRLW 399
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 31-206 2.71e-57

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: 190.53  E-value: 2.71e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977  31 AFEEIILQYNKLLEKSDLHSVLAQKLQAEKHDVPNRHEISPGHDGTWNDSQLQEMAQLRIKHQEELTELHKKRGELAQLV 110
Cdd:pfam08614   1 AFLELIDAYNRLLDRTALLEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQLREELAELYRSRGELAQRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977 111 IDLNNQMQQKDREMQMNEAKIAECLQTISDLETECLDLRTKLQDLEIANQTLKDEYDALQITFTALEEKLRKTTEENQEL 190
Cdd:pfam08614  81 VDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQDELVALQLQLNMAEEKLRKLEKENREL 160

                         170
                  ....*....|....*.
gi 1044375977 191 VTRWMAEKAQEANRLN 206
Cdd:pfam08614 161 VERWMKRKGQEAEAMN 176
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
257-604 1.31e-61

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 209.77  E-value: 1.31e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977 257 VRAISRAATKRLSQPAGGLLDSITNIFGRRSVSSFPVPQDNVDTHPGSGKEVRV----PTTALCVFDAHDGEVNAVQFSP 332
Cdd:COG2319    51 LAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLwdlaTGLLLRTLTGHTGAVRSVAFSP 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977 333 GSRLLATGGMDRRVKLWEVFGEKCEfkGSLSGSNAGITSIEFDSAGSYLLAASNDFASRIWTVDDYRLRHTLTGHSGKVL 412
Cdd:COG2319   131 DGKTLASGSADGTVRLWDLATGKLL--RTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVR 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977 413 SAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTV-FAGSSCNDIVCT--EQCVMSGHFDKKIRFWDIRSESIVREME-LL 488
Cdd:COG2319   209 SVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLtGHSGSVRSVAFSpdGRLLASGSADGTVRLWDLATGELLRTLTgHS 288

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977 489 GKITALDLNPERTELLTCSRDDLLKVIDLRTNAVKQTFSAPgfkcGSDWTRVVFSPDGSYVAAGSAEGSLYIWSVLTGKV 568
Cdd:COG2319   289 GGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGH----TGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGEL 364

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1044375977 569 EKVLsKQHSSSINAVAWSPSGSHVVSVDKGCRAVLW 604
Cdd:COG2319   365 LRTL-TGHTGAVTSVAFSPDGRTLASGSADGTVRLW 399
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 315-605 2.87e-59

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 199.87  E-value: 2.87e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977 315 LCVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWEVFGEKCEFkgSLSGSNAGITSIEFDSAGSYLLAASNDFASRIWT 394
Cdd:cd00200     2 RRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLR--TLKGHTGPVRDVAASADGTYLASGSSDKTIRLWD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977 395 VDDYRLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTvFAG----------SSCNDIVCteqcvmS 464
Cdd:cd00200    80 LETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTT-LRGhtdwvnsvafSPDGTFVA------S 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977 465 GHFDKKIRFWDIRSESIVREMEL-LGKITALDLNPERTELLTCSRDDLLKVIDLRTNAVKQTFSAPgfkcgSDW-TRVVF 542
Cdd:cd00200   153 SSQDGTIKLWDLRTGKCVATLTGhTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGH-----ENGvNSVAF 227

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1044375977 543 SPDGSYVAAGSAEGSLYIWSVLTGKVEKVLSkQHSSSINAVAWSPSGSHVVSVDKGCRAVLWA 605
Cdd:cd00200   228 SPDGYLLASGSEDGTIRVWDLRTGECVQTLS-GHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 31-206 2.71e-57

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: 190.53  E-value: 2.71e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977  31 AFEEIILQYNKLLEKSDLHSVLAQKLQAEKHDVPNRHEISPGHDGTWNDSQLQEMAQLRIKHQEELTELHKKRGELAQLV 110
Cdd:pfam08614   1 AFLELIDAYNRLLDRTALLEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQLREELAELYRSRGELAQRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977 111 IDLNNQMQQKDREMQMNEAKIAECLQTISDLETECLDLRTKLQDLEIANQTLKDEYDALQITFTALEEKLRKTTEENQEL 190
Cdd:pfam08614  81 VDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQDELVALQLQLNMAEEKLRKLEKENREL 160

                         170
                  ....*....|....*.
gi 1044375977 191 VTRWMAEKAQEANRLN 206
Cdd:pfam08614 161 VERWMKRKGQEAEAMN 176
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 119-209 1.09e-29

Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.


Pssm-ID: 439196 [Multi-domain]  Cd Length: 91  Bit Score: 112.27  E-value: 1.09e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977 119 QKDREMQMNEAKIAECLQTISDLETECLDLRTKLQDLEIANQTLKDEYDALQITFTALEEKLRKTTEENQELVTRWMAEK 198
Cdd:cd22887     1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEENDELVERWMAKK 80

                          90
                  ....*....|.
gi 1044375977 199 AQEANRLNAEN 209
Cdd:cd22887    81 QQEADKMNEAN 91
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
79-264 9.59e-09

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 57.60  E-value: 9.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977  79 DSQLQEMAQLRIKHQEELTELHKKRGELAQL---VIDLNNQMQQKDREMQMNEAKIAECLQTISDLETECLDLRTKLQDL 155
Cdd:COG4372    41 DKLQEELEQLREELEQAREELEQLEEELEQArseLEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEEL 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977 156 EIANQTLKDEYDALQITFTALEEKLRKTTEENQELVTRwMAEKAQEANRLNAENEKDSRRR-QARLQKELAEAAKEPLPV 234
Cdd:COG4372   121 QKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ-LESLQEELAALEQELQALSEAEaEQALDELLKEANRNAEKE 199

                         170       180       190
                  ....*....|....*....|....*....|
gi 1044375977 235 EQDDDIEVIVDETSDHTEETSPVRAISRAA 264
Cdd:COG4372   200 EELAEAEKLIESLPRELAEELLEAKDSLEA 229
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 315-350 6.16e-08

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 48.85  E-value: 6.16e-08
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1044375977  315 LCVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWE 350
Cdd:smart00320   5 LKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
315-350 2.23e-07

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 47.34  E-value: 2.23e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1044375977 315 LCVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWE 350
Cdd:pfam00400   4 LKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 114-266 1.33e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.60  E-value: 1.33e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977  114 NNQMQQKDREMQMNEAKIAECLQTISDLETECLDLRTKLQDLEIANQTLKDEYDALQITFTALEEKLRKTTEEnQELVTR 193
Cdd:TIGR02168  669 NSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE-VEQLEE 747

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1044375977  194 WMAEKAQEANRLNAE-NEKDSRRRQARLQKELAEAAKEPLPVEQDDDIEVIVDETSDHTEETSPVRAISRAATK 266
Cdd:TIGR02168  748 RIAQLSKELTELEAEiEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAAN 821
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 321-437 9.02e-06

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 48.93  E-value: 9.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977 321 HDGEVNAVQFSPGS-RLLATGGMDRRVKLWEVFgekcefKGSLSGS---NAGITSIEFDSAGSYLLAasndFASRIWTVD 396
Cdd:PLN00181  574 HEKRVWSIDYSSADpTLLASGSDDGSVKLWSIN------QGVSIGTiktKANICCVQFPSESGRSLA----FGSADHKVY 643

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1044375977 397 DYRLRH------TLTGHSGKVLSAKFLlDNARIVSGSHDRTLKLWDL 437
Cdd:PLN00181  644 YYDLRNpklplcTMIGHSKTVSYVRFV-DSSTLVSSSTDNTLKLWDL 689
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
46-230 2.36e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 47.34  E-value: 2.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977  46 SDLHSVLAQKLQAEKHDVPNRHEispghdgtwndsqlQEMAQLR--IKHQEELTELHKKRGELAQLVIDLNNQMQQkdrE 123
Cdd:PRK02224  190 DQLKAQIEEKEEKDLHERLNGLE--------------SELAELDeeIERYEEQREQARETRDEADEVLEEHEERRE---E 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977 124 MQMNEAKIAECLQTISDLETECLDLRTKLQDLEIANQTLKDEYDAL--QITFTALE----EKLRKTTEENQELVTRWMAE 197
Cdd:PRK02224  253 LETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLlaEAGLDDADaeavEARREELEDRDEELRDRLEE 332

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1044375977 198 KAQEANRLN------AENEKDSRRRQARLQKELAEAAKE 230
Cdd:PRK02224  333 CRVAAQAHNeeaeslREDADDLEERAEELREEAAELESE 371
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
257-604 1.31e-61

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 209.77  E-value: 1.31e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977 257 VRAISRAATKRLSQPAGGLLDSITNIFGRRSVSSFPVPQDNVDTHPGSGKEVRV----PTTALCVFDAHDGEVNAVQFSP 332
Cdd:COG2319    51 LAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLwdlaTGLLLRTLTGHTGAVRSVAFSP 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977 333 GSRLLATGGMDRRVKLWEVFGEKCEfkGSLSGSNAGITSIEFDSAGSYLLAASNDFASRIWTVDDYRLRHTLTGHSGKVL 412
Cdd:COG2319   131 DGKTLASGSADGTVRLWDLATGKLL--RTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVR 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977 413 SAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTV-FAGSSCNDIVCT--EQCVMSGHFDKKIRFWDIRSESIVREME-LL 488
Cdd:COG2319   209 SVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLtGHSGSVRSVAFSpdGRLLASGSADGTVRLWDLATGELLRTLTgHS 288

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977 489 GKITALDLNPERTELLTCSRDDLLKVIDLRTNAVKQTFSAPgfkcGSDWTRVVFSPDGSYVAAGSAEGSLYIWSVLTGKV 568
Cdd:COG2319   289 GGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGH----TGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGEL 364

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1044375977 569 EKVLsKQHSSSINAVAWSPSGSHVVSVDKGCRAVLW 604
Cdd:COG2319   365 LRTL-TGHTGAVTSVAFSPDGRTLASGSADGTVRLW 399
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 315-605 2.87e-59

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 199.87  E-value: 2.87e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977 315 LCVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWEVFGEKCEFkgSLSGSNAGITSIEFDSAGSYLLAASNDFASRIWT 394
Cdd:cd00200     2 RRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLR--TLKGHTGPVRDVAASADGTYLASGSSDKTIRLWD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977 395 VDDYRLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTvFAG----------SSCNDIVCteqcvmS 464
Cdd:cd00200    80 LETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTT-LRGhtdwvnsvafSPDGTFVA------S 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977 465 GHFDKKIRFWDIRSESIVREMEL-LGKITALDLNPERTELLTCSRDDLLKVIDLRTNAVKQTFSAPgfkcgSDW-TRVVF 542
Cdd:cd00200   153 SSQDGTIKLWDLRTGKCVATLTGhTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGH-----ENGvNSVAF 227

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1044375977 543 SPDGSYVAAGSAEGSLYIWSVLTGKVEKVLSkQHSSSINAVAWSPSGSHVVSVDKGCRAVLWA 605
Cdd:cd00200   228 SPDGYLLASGSEDGTIRVWDLRTGECVQTLS-GHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 31-206 2.71e-57

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: 190.53  E-value: 2.71e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977  31 AFEEIILQYNKLLEKSDLHSVLAQKLQAEKHDVPNRHEISPGHDGTWNDSQLQEMAQLRIKHQEELTELHKKRGELAQLV 110
Cdd:pfam08614   1 AFLELIDAYNRLLDRTALLEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQLREELAELYRSRGELAQRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977 111 IDLNNQMQQKDREMQMNEAKIAECLQTISDLETECLDLRTKLQDLEIANQTLKDEYDALQITFTALEEKLRKTTEENQEL 190
Cdd:pfam08614  81 VDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQDELVALQLQLNMAEEKLRKLEKENREL 160

                         170
                  ....*....|....*.
gi 1044375977 191 VTRWMAEKAQEANRLN 206
Cdd:pfam08614 161 VERWMKRKGQEAEAMN 176
WD40 COG2319
WD40 repeat [General function prediction only];
303-563 3.27e-49

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 176.26  E-value: 3.27e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977 303 GSGKEVRV----PTTALCVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWEVFGEKCEFkgSLSGSNAGITSIEFDSAG 378
Cdd:COG2319   139 SADGTVRLwdlaTGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLR--TLTGHTGAVRSVAFSPDG 216

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977 379 SYLLAASNDFASRIWTVDDYRLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTvFAGSSC--NDIV 456
Cdd:COG2319   217 KLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRT-LTGHSGgvNSVA 295

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977 457 CT--EQCVMSGHFDKKIRFWDIRSESIVREME-LLGKITALDLNPERTELLTCSRDDLLKVIDLRTNAVKQTFSAPgfkc 533
Cdd:COG2319   296 FSpdGKLLASGSDDGTVRLWDLATGKLLRTLTgHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGH---- 371

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1044375977 534 gSDW-TRVVFSPDGSYVAAGSAEGSLYIWSV 563
Cdd:COG2319   372 -TGAvTSVAFSPDGRTLASGSADGTVRLWDL 401
WD40 COG2319
WD40 repeat [General function prediction only];
329-604 1.61e-35

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 138.12  E-value: 1.61e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977 329 QFSPGSRLLATGGMDRRVKLWEVFGEKCEfkGSLSGSNAGITSIEFDSAGSYLLAASNDFASRIWTVDDYRLRHTLTGHS 408
Cdd:COG2319     1 ALSADGAALAAASADLALALLAAALGALL--LLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977 409 GKVLSAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTVFA-GSSCNDIVCTE--QCVMSGHFDKKIRFWDIRSESIVREM 485
Cdd:COG2319    79 AAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGhTGAVRSVAFSPdgKTLASGSADGTVRLWDLATGKLLRTL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977 486 EL-LGKITALDLNPERTELLTCSRDDLLKVIDLRTNAVKQTFSAPgfkcgSDW-TRVVFSPDGSYVAAGSAEGSLYIWSV 563
Cdd:COG2319   159 TGhSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGH-----TGAvRSVAFSPDGKLLASGSADGTVRLWDL 233

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1044375977 564 LTGKVEKVLsKQHSSSINAVAWSPSGSHVVSVDKGCRAVLW 604
Cdd:COG2319   234 ATGKLLRTL-TGHSGSVRSVAFSPDGRLLASGSADGTVRLW 273
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 400-604 4.40e-35

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 134.00  E-value: 4.40e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977 400 LRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTV----FAGSSCNDIVCTEQCVmSGHFDKKIRFWD 475
Cdd:cd00200     1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLkghtGPVRDVAASADGTYLA-SGSSDKTIRLWD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977 476 IRSESIVREMEL-LGKITALDLNPERTELLTCSRDDLLKVIDLRTNAVKQTFSAPgfkcgSDWTR-VVFSPDGSYVAAGS 553
Cdd:cd00200    80 LETGECVRTLTGhTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGH-----TDWVNsVAFSPDGTFVASSS 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1044375977 554 AEGSLYIWSVLTGKVEKVLsKQHSSSINAVAWSPSGSHVV--SVDKGCRavLW 604
Cdd:cd00200   155 QDGTIKLWDLRTGKCVATL-TGHTGEVNSVAFSPDGEKLLssSSDGTIK--LW 204
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 119-209 1.09e-29

Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.


Pssm-ID: 439196 [Multi-domain]  Cd Length: 91  Bit Score: 112.27  E-value: 1.09e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977 119 QKDREMQMNEAKIAECLQTISDLETECLDLRTKLQDLEIANQTLKDEYDALQITFTALEEKLRKTTEENQELVTRWMAEK 198
Cdd:cd22887     1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEENDELVERWMAKK 80

                          90
                  ....*....|.
gi 1044375977 199 AQEANRLNAEN 209
Cdd:cd22887    81 QQEADKMNEAN 91
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
79-264 9.59e-09

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 57.60  E-value: 9.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977  79 DSQLQEMAQLRIKHQEELTELHKKRGELAQL---VIDLNNQMQQKDREMQMNEAKIAECLQTISDLETECLDLRTKLQDL 155
Cdd:COG4372    41 DKLQEELEQLREELEQAREELEQLEEELEQArseLEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEEL 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977 156 EIANQTLKDEYDALQITFTALEEKLRKTTEENQELVTRwMAEKAQEANRLNAENEKDSRRR-QARLQKELAEAAKEPLPV 234
Cdd:COG4372   121 QKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ-LESLQEELAALEQELQALSEAEaEQALDELLKEANRNAEKE 199

                         170       180       190
                  ....*....|....*....|....*....|
gi 1044375977 235 EQDDDIEVIVDETSDHTEETSPVRAISRAA 264
Cdd:COG4372   200 EELAEAEKLIESLPRELAEELLEAKDSLEA 229
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 315-350 6.16e-08

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 48.85  E-value: 6.16e-08
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1044375977  315 LCVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWE 350
Cdd:smart00320   5 LKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 81-270 1.05e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.33  E-value: 1.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977  81 QLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQQKDREMQMNEAKIAEclqtisdLETECLDLRTKLQDLEIANQ 160
Cdd:COG1196   275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAE-------LEEELEELEEELEELEEELE 347

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977 161 TLKDEYDALQITFTALEEKLRKTTEENQELVTRWMAEKAQEANRLNAENEKDSRRRQARLQKELAEAAKEPLPVEQDDDI 240
Cdd:COG1196   348 EAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE 427

                         170       180       190
                  ....*....|....*....|....*....|
gi 1044375977 241 EVIVDETSDHTEETSPVRAISRAATKRLSQ 270
Cdd:COG1196   428 EALAELEEEEEEEEEALEEAAEEEAELEEE 457
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 399-436 1.49e-07

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 47.69  E-value: 1.49e-07
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1044375977  399 RLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWD 436
Cdd:smart00320   3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
315-350 2.23e-07

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 47.34  E-value: 2.23e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1044375977 315 LCVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWE 350
Cdd:pfam00400   4 LKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 pfam00400
WD domain, G-beta repeat;
399-436 4.06e-07

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 46.57  E-value: 4.06e-07
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1044375977 399 RLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWD 436
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
88-238 4.51e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 52.85  E-value: 4.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977  88 LRIKHQEELTELHKKRGELAQLVIDLNNQMQQKDREMQMNEAKIAECLQTISDLETECLDLRTKLQDLEIANQTLKDEYD 167
Cdd:COG4717    47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1044375977 168 ALQitftaLEEKLRKTTEENQELVTRWMAEKAQEANRLNAENEKDSRRRQ-ARLQKELAEAAKEPLPVEQDD 238
Cdd:COG4717   127 LLP-----LYQELEALEAELAELPERLEELEERLEELRELEEELEELEAElAELQEELEELLEQLSLATEEE 193
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
358-566 6.80e-07

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


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 50.85  E-value: 6.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977 358 FKGSLSGSNAGITSIEFDSAGSYLLAASNDFASRIWTVDDYRLRHTLTGHSGKVLSAKFLLDNARI-VSGSHDRTLKLWD 436
Cdd:COG3391    17 ALAALAVAVAALGLGGGGPLLAAASGGVVGAAVGGGGVALLAGLGLGAAAVADADGADAGADGRRLyVANSGSGRVSVID 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977 437 LRSKVCIKTVFAGSSCNDIVCTE---QCVMSGHFDKKIRFWDIRSESIVREMELLGKITALDLNPERTELLTCSRDD--- 510
Cdd:COG3391    97 LATGKVVATIPVGGGPRGLAVDPdggRLYVADSGNGRVSVIDTATGKVVATIPVGAGPHGIAVDPDGKRLYVANSGSntv 176

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1044375977 511 --LLKVIDLRTNAVKQTFSApgfkcGSDWTRVVFSPDGS--YVA------AGSAEGSLYIWSVLTG 566
Cdd:COG3391   177 svIVSVIDTATGKVVATIPV-----GGGPVGVAVSPDGRrlYVAnrgsntSNGGSNTVSVIDLATL 237
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 79-230 9.09e-07

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: 50.31  E-value: 9.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977  79 DSQLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQQKDREMQMNEAKIAECLQTISDLEtecldlrTKLQdlEIA 158
Cdd:COG1579    16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE-------EQLG--NVR 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1044375977 159 NQtlkDEYDALQITFTALEEKLRKTTEENQELVTRwmAEKAQ----EANRLNAENEKDSRRRQARLQKELAEAAKE 230
Cdd:COG1579    87 NN---KEYEALQKEIESLKRRISDLEDEILELMER--IEELEeelaELEAELAELEAELEEKKAELDEELAELEAE 157
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 114-266 1.33e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.60  E-value: 1.33e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977  114 NNQMQQKDREMQMNEAKIAECLQTISDLETECLDLRTKLQDLEIANQTLKDEYDALQITFTALEEKLRKTTEEnQELVTR 193
Cdd:TIGR02168  669 NSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE-VEQLEE 747

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1044375977  194 WMAEKAQEANRLNAE-NEKDSRRRQARLQKELAEAAKEPLPVEQDDDIEVIVDETSDHTEETSPVRAISRAATK 266
Cdd:TIGR02168  748 RIAQLSKELTELEAEiEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAAN 821
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 83-270 1.37e-06

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: 51.61  E-value: 1.37e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977   83 QEMAQLRIKHQEELTELHKKRGELAQLVIDLnnQMQQKDREMQMNEakiaeclqtISDLETECLDLRTKLQDLEIANQTL 162
Cdd:TIGR02169  315 RELEDAEERLAKLEAEIDKLLAEIEELEREI--EEERKRRDKLTEE---------YAELKEELEDLRAELEEVDKEFAET 383

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977  163 KDEYDALQitftaleEKLRKTTEENQELVT---RWMAEKAQ-EANRLNAENE-KDSRRRQARLQKELAEAAKEPLPVEQd 237
Cdd:TIGR02169  384 RDELKDYR-------EKLEKLKREINELKReldRLQEELQRlSEELADLNAAiAGIEAKINELEEEKEDKALEIKKQEW- 455

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1044375977  238 dDIEVIVDETSDHTEETSPVRAISRAATKRLSQ 270
Cdd:TIGR02169  456 -KLEQLAADLSKYEQELYDLKEEYDRVEKELSK 487
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 80-325 1.68e-06

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: 50.53  E-value: 1.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977  80 SQLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQQKDREMQMNEAKIAECLQTISDLETE--------------- 144
Cdd:COG4942    41 KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEElaellralyrlgrqp 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977 145 ----------CLDLRTKLQDLEIANQTLKDEYDALQITFTALEEKLRKTTEENQELVTRwMAEKAQEANRLNAEnEKDSR 214
Cdd:COG4942   121 plalllspedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL-LAELEEERAALEAL-KAERQ 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977 215 RRQARLQKELAEAAKEPLPVEQDDD-----IEVIVDETSDHTEETSPVRAIsrAATKRLSQPAGGlldSITNIFGRRsvs 289
Cdd:COG4942   199 KLLARLEKELAELAAELAELQQEAEelealIARLEAEAAAAAERTPAAGFA--ALKGKLPWPVSG---RVVRRFGER--- 270

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1044375977 290 sfpvpQDNVDTHPG------SGKEVRVPttalcvfdaHDGEV 325
Cdd:COG4942   271 -----DGGGGRNKGidiaapPGAPVRAV---------ADGTV 298
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 83-230 2.03e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.21  E-value: 2.03e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977   83 QEMAQLRIKHQE---ELTELHKKRGELAQLVIDLNNQMQQKDREMQMNEAKIAEclqtisdLETECLDLRTKLQDLEIAN 159
Cdd:TIGR02168  267 EKLEELRLEVSEleeEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE-------LEAQLEELESKLDELAEEL 339

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1044375977  160 QTLKDEYDALQITFTALEEKLRKTTEENQELVTRWmAEKAQEANRLNAEnEKDSRRRQARLQKELAEAAKE 230
Cdd:TIGR02168  340 AELEEKLEELKEELESLEAELEELEAELEELESRL-EELEEQLETLRSK-VAQLELQIASLNNEIERLEAR 408
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 81-232 6.08e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.55  E-value: 6.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977  81 QLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQQKDREMQMNEAKIAECLQTISDLETECLDLRTKLQDLEIANQ 160
Cdd:COG1196   331 ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1044375977 161 TLKDEydalqitftalEEKLRKTTEENQElvtrwmAEKAQEANRLNAENEKDSRRRQARLQKELAEAAKEPL 232
Cdd:COG1196   411 ALLER-----------LERLEEELEELEE------ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
78-241 7.69e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.14  E-value: 7.69e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977   78 NDSQLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQ--QKDREMQMNEAKIAECLQTISDLETECLDLRTKLQDL 155
Cdd:COG4913    608 NRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREalQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDL 687

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977  156 EianqTLKDEYDALQITFTALEEKLRKTTEENQELVTRW---MAEKAQEANRLNAENEKDSRRRQARLQKELAEAAKEPL 232
Cdd:COG4913    688 A----ALEEQLEELEAELEELEEELDELKGEIGRLEKELeqaEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAV 763


                   ....*....
gi 1044375977  233 PVEQDDDIE 241
Cdd:COG4913    764 ERELRENLE 772
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 321-437 9.02e-06

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 48.93  E-value: 9.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977 321 HDGEVNAVQFSPGS-RLLATGGMDRRVKLWEVFgekcefKGSLSGS---NAGITSIEFDSAGSYLLAasndFASRIWTVD 396
Cdd:PLN00181  574 HEKRVWSIDYSSADpTLLASGSDDGSVKLWSIN------QGVSIGTiktKANICCVQFPSESGRSLA----FGSADHKVY 643

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1044375977 397 DYRLRH------TLTGHSGKVLSAKFLlDNARIVSGSHDRTLKLWDL 437
Cdd:PLN00181  644 YYDLRNpklplcTMIGHSKTVSYVRFV-DSSTLVSSSTDNTLKLWDL 689
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 325-521 9.66e-06

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 48.54  E-value: 9.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977 325 VNAVQFSPGSRLLATGGMDRRVKLWEVF-----GEKCEFKGSLSGSNAGITSIEFDSAGSYLLAASN-DFASRIWTVDDY 398
Cdd:PLN00181  486 VCAIGFDRDGEFFATAGVNKKIKIFECEsiikdGRDIHYPVVELASRSKLSGICWNSYIKSQVASSNfEGVVQVWDVARS 565

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977 399 RLRHTLTGHSGKVLSAKFL-LDNARIVSGSHDRTLKLWDLRSKVCIKTVfagSSCNDIVCTE------QCVMSGHFDKKI 471
Cdd:PLN00181  566 QLVTEMKEHEKRVWSIDYSsADPTLLASGSDDGSVKLWSINQGVSIGTI---KTKANICCVQfpsesgRSLAFGSADHKV 642

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1044375977 472 RFWDIRSESI-VREMELLGKITALDLNPERTELLTCSRDDLLKVIDLRTNA 521
Cdd:PLN00181  643 YYYDLRNPKLpLCTMIGHSKTVSYVRFVDSSTLVSSSTDNTLKLWDLSMSI 693
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 78-226 2.32e-05

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 47.32  E-value: 2.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977  78 NDSQLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQQK---DREMQMNEAKIAECLQTISDLETECLDLRTKLQD 154
Cdd:TIGR04523 379 NQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKellEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKN 458

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1044375977 155 LEIANQTLKDEYDALQITFTALEEKLRKTTEEnqelvtrwMAEKAQEANRLNAENeKDSRRRQARLQKELAE 226
Cdd:TIGR04523 459 LDNTRESLETQLKVLSRSINKIKQNLEQKQKE--------LKSKEKELKKLNEEK-KELEEKVKDLTKKISS 521
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
46-230 2.36e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 47.34  E-value: 2.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977  46 SDLHSVLAQKLQAEKHDVPNRHEispghdgtwndsqlQEMAQLR--IKHQEELTELHKKRGELAQLVIDLNNQMQQkdrE 123
Cdd:PRK02224  190 DQLKAQIEEKEEKDLHERLNGLE--------------SELAELDeeIERYEEQREQARETRDEADEVLEEHEERRE---E 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977 124 MQMNEAKIAECLQTISDLETECLDLRTKLQDLEIANQTLKDEYDAL--QITFTALE----EKLRKTTEENQELVTRWMAE 197
Cdd:PRK02224  253 LETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLlaEAGLDDADaeavEARREELEDRDEELRDRLEE 332

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1044375977 198 KAQEANRLN------AENEKDSRRRQARLQKELAEAAKE 230
Cdd:PRK02224  333 CRVAAQAHNeeaeslREDADDLEERAEELREEAAELESE 371
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 81-237 3.18e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.36  E-value: 3.18e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977   81 QLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQQKDREMQMNEAKIAECLQTISDLETECLDLRTKLQ----DLE 156
Cdd:TIGR02168  324 QLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAslnnEIE 403

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977  157 IANQTLKDEYDALQITFTALEEKLRKTTEENQELVTRWMAEKAQEANRLNAENEkDSRRRQARLQKELAEAAKEPLPVEQ 236
Cdd:TIGR02168  404 RLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELE-RLEEALEELREELEEAEQALDAAER 482


                   .
gi 1044375977  237 D 237
Cdd:TIGR02168  483 E 483
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
79-253 5.13e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.45  E-value: 5.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977   79 DSQLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQQKD-REMQMNEAKIAECLQTISDLETECLDLRTKLQDLEI 157
Cdd:COG4913    294 EAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGL 373

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977  158 ANQTLKDEYDALQITFTALEEKLRKTTEENQELVTRWMAEKaqeanrlnaeneKDSRRRQARLQKELA--EAAKEPLPVE 235
Cdd:COG4913    374 PLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAAL------------RDLRRELRELEAEIAslERRKSNIPAR 441

                          170
                   ....*....|....*...
gi 1044375977  236 QDDDIEVIVDETSDHTEE 253
Cdd:COG4913    442 LLALRDALAEALGLDEAE 459
TolB COG0823
Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, ...
 514-593 5.71e-05

Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 440585 [Multi-domain]  Cd Length: 158  Bit Score: 43.89  E-value: 5.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977 514 VIDLRTNAVKQTFSAPGFKCGSDWtrvvfSPDGSYVAAGSAEGS---LYIWSVLTGKVEKVLSKQHSSSinAVAWSPSGS 590
Cdd:COG0823    15 VVDLDGGEPRRLTNSPGIDTSPAW-----SPDGRRIAFTSDRGGgpqIYVVDADGGEPRRLTFGGGYNA--SPSWSPDGK 87


                  ...
gi 1044375977 591 HVV 593
Cdd:COG0823    88 RLA 90
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 93-253 1.67e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 44.66  E-value: 1.67e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977   93 QEELTELHKKRGELAQLVIDLNNQMQQKDREMQMNEAKIAECLQTISDLETECLDLRTKLQDLEI--------------A 158
Cdd:TIGR02168  809 RAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESeleallnerasleeA 888

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977  159 NQTLKDEYDALQITFTALEEKLRKTTEENQELvtrwMAEKAQEANRLN-AENEKDSRRRQARLQKELAEAAKEPLPVEQD 237
Cdd:TIGR02168  889 LALLRSELEELSEELRELESKRSELRRELEEL----REKLAQLELRLEgLEVRIDNLQERLSEEYSLTLEEAEALENKIE 964

                          170
                   ....*....|....*.
gi 1044375977  238 DDIEVIVDETSDHTEE 253
Cdd:TIGR02168  965 DDEEEARRRLKRLENK 980
TolB COG0823
Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, ...
 514-604 1.85e-04

Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 440585 [Multi-domain]  Cd Length: 158  Bit Score: 42.35  E-value: 1.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977 514 VIDLRTNAVKQ-TFSapgfkcGSDWTRVVFSPDGSYVA-AGSAEGSLYIWSV-LTGKVEKVLSKqhssSINAVAWSPSGS 590
Cdd:COG0823    59 VVDADGGEPRRlTFG------GGYNASPSWSPDGKRLAfVSRSDGRFDIYVLdLDGGAPRRLTD----GPGSPSWSPDGR 128

                          90
                  ....*....|....*
gi 1044375977 591 HVV-SVDKGCRAVLW 604
Cdd:COG0823   129 RIVfSSDRGGRPDLY 143
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
80-262 2.10e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.12  E-value: 2.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977  80 SQLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQQKDREMQMNEAKIAECLQTISDLETECLDLRTKLQDLEIAN 159
Cdd:COG4372    87 EQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEEL 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977 160 QTLKDEYDALQITFTALEEKLRKTTEENQELVTRWMAEKAQEANRLNAENEKDSRRRQARLQKELAEAAKEPLPVEQDDD 239
Cdd:COG4372   167 AALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEE 246

                         170       180
                  ....*....|....*....|...
gi 1044375977 240 IEVIVDETSDHTEETSPVRAISR 262
Cdd:COG4372   247 DKEELLEEVILKEIEELELAILV 269
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 41-221 2.75e-04

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 44.01  E-value: 2.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977   41 KLLEK--SDLHSVLAQKLQAEKH--DVPNRHE--ISPGHDGTWNDSQL-QEMAQLRIKHQEELTELHKKRGELAQLVIDL 113
Cdd:pfam01576  155 KLLEEriSEFTSNLAEEEEKAKSlsKLKNKHEamISDLEERLKKEEKGrQELEKAKRKLEGESTDLQEQIAELQAQIAEL 234

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977  114 NNQMQQKDREMQMNEAKIAE-------CLQTISDLETECLDLRTKLQD-------LEIANQTLKDEYDALQitfTALEEK 179
Cdd:pfam01576  235 RAQLAKKEEELQAALARLEEetaqknnALKKIRELEAQISELQEDLESeraarnkAEKQRRDLGEELEALK---TELEDT 311

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1044375977  180 LrKTTEENQELVTRwmaeKAQEANRLNAENEKDSRRRQARLQ 221
Cdd:pfam01576  312 L-DTTAAQQELRSK----REQEVTELKKALEEETRSHEAQLQ 348
COG4946 COG4946
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown] ...
 541-589 3.41e-04

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


Pssm-ID: 443973 [Multi-domain]  Cd Length: 1072  Bit Score: 43.87  E-value: 3.41e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1044375977  541 VFSPDGSYVAAGSAEGSLYIWSVLTGKVEKVLSKQHSSSINAVAWSPSG 589
Cdd:COG4946    395 VWSPDGKKIAFTDNRGRLWVVDLASGKVRKVDTDGYGDGISDLAWSPDS 443
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 565-604 3.51e-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: 38.45  E-value: 3.51e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1044375977  565 TGKVEKVLsKQHSSSINAVAWSPSGSHVVSVDKGCRAVLW 604
Cdd:smart00320   1 SGELLKTL-KGHTGPVTSVAFSPDGKYLASGSDDGTIKLW 39
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 83-226 3.84e-04

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 43.47  E-value: 3.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977  83 QEMAQLRIKHQEELTELHKKRGELAQ---LVIDLNNQMQQ--------------------------KDREMQMNEAKIAE 133
Cdd:TIGR04523 253 TQLNQLKDEQNKIKKQLSEKQKELEQnnkKIKELEKQLNQlkseisdlnnqkeqdwnkelkselknQEKKLEEIQNQISQ 332

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977 134 CLQTISDLETECLDLRTKLQDLEIANQTLKDEydalqitftaLEEK---LRKTTEENQelvtrwmaEKAQEANRLnaENE 210
Cdd:TIGR04523 333 NNKIISQLNEQISQLKKELTNSESENSEKQRE----------LEEKqneIEKLKKENQ--------SYKQEIKNL--ESQ 392

                         170
                  ....*....|....*.
gi 1044375977 211 KDSRRRQARLQKELAE 226
Cdd:TIGR04523 393 INDLESKIQNQEKLNQ 408
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 80-227 5.06e-04

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 43.19  E-value: 5.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977  80 SQLQ-EMAQLRIKHQEELTELHKKRGELAQLV---IDLNNQMQQKDREMQMNEAKIAECLQ--------TISDLETECLD 147
Cdd:pfam05557  12 SQLQnEKKQMELEHKRARIELEKKASALKRQLdreSDRNQELQKRIRLLEKREAEAEEALReqaelnrlKKKYLEALNKK 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977 148 LRTKLQDLEIANQT---LKDEYDALQITFTALEEKLRKTTEENQELVTR--WMAEKAQEANRLNAENEKDsrrrqarlQK 222
Cdd:pfam05557  92 LNEKESQLADAREViscLKNELSELRRQIQRAELELQSTNSELEELQERldLLKAKASEAEQLRQNLEKQ--------QS 163


                  ....*
gi 1044375977 223 ELAEA 227
Cdd:pfam05557 164 SLAEA 168
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 114-207 5.68e-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: 5.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977 114 NNQMQQKDREMQMNEAKIAECLQTISDLETECLDLRTKLQDLEIANQTLKDEYDALQITFTALEEKLRKTTEENQELVTR 193
Cdd:COG4942    19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98

                          90
                  ....*....|....
gi 1044375977 194 WMAEKAQEANRLNA 207
Cdd:COG4942    99 LEAQKEELAELLRA 112
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
31-188 6.88e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 6.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977  31 AFEEIILQYNKLLEKSDLHSVLAQKLQAEKhdvPNRHEISPGHDGTWNDSQLQEMAQLRIKHQEELTELHKKRGELaqlv 110
Cdd:COG4717   386 ELRAALEQAEEYQELKEELEELEEQLEELL---GELEELLEALDEEELEEELEELEEELEELEEELEELREELAEL---- 458

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1044375977 111 idlNNQMQQkdremqmneakiAECLQTISDLETECLDLRTKLQDLEianqtlkDEYDALQITFTALEEKLRKTTEENQ 188
Cdd:COG4717   459 ---EAELEQ------------LEEDGELAELLQELEELKAELRELA-------EEWAALKLALELLEEAREEYREERL 514
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 147-243 7.40e-04

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 42.76  E-value: 7.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977 147 DLRTKLQDLEIANQTLKDEYD-ALQITFTALEEKLRKTTEENQELVTRWMAEKA--QEANRLNAENEKDSRRRQArLQKE 223
Cdd:COG0542   415 ELERRLEQLEIEKEALKKEQDeASFERLAELRDELAELEEELEALKARWEAEKEliEEIQELKEELEQRYGKIPE-LEKE 493

                          90       100
                  ....*....|....*....|....*...
gi 1044375977 224 LAEA-----AKEPLPVEQ--DDDI-EVI 243
Cdd:COG0542   494 LAELeeelaELAPLLREEvtEEDIaEVV 521
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 79-193 8.51e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 42.36  E-value: 8.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977   79 DSQLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQQ--------KDREMQMNEAK-----IAECLQTISDLETEC 145
Cdd:TIGR02169  881 ESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSElkaklealEEELSEIEDPKgedeeIPEEELSLEDVQAEL 960

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1044375977  146 LDLRTKLQDLEIANQTLKDEYDALQITFTALEEKLRKTTEENQELVTR 193
Cdd:TIGR02169  961 QRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILER 1008
46 PHA02562
endonuclease subunit; Provisional
 80-244 9.61e-04

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 41.92  E-value: 9.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977  80 SQLQEMAQLRIKHQEELTELHKKrgeLAQLVIDLNNQMQQKDREMQMNE--AKIAECLQTISD-------LETECLDLRT 150
Cdd:PHA02562  237 EELTDELLNLVMDIEDPSAALNK---LNTAAAKIKSKIEQFQKVIKMYEkgGVCPTCTQQISEgpdritkIKDKLKELQH 313

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977 151 KLQDLEIANQTLK---DEYDALQITFTALEEKLRKtteENQELVT-RWMAEKAQEA-NRLNAENeKDSRRRQARLQKELA 225
Cdd:PHA02562  314 SLEKLDTAIDELEeimDEFNEQSKKLLELKNKIST---NKQSLITlVDKAKKVKAAiEELQAEF-VDNAEELAKLQDELD 389

                         170
                  ....*....|....*....
gi 1044375977 226 EAAKEPLPVEQDDDIEVIV 244
Cdd:PHA02562  390 KIVKTKSELVKEKYHRGIV 408
COG4946 COG4946
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown] ...
 540-604 9.90e-04

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


Pssm-ID: 443973 [Multi-domain]  Cd Length: 1072  Bit Score: 42.33  E-value: 9.90e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1044375977  540 VVFSPDGSYVAAGS-AEGS--LYIWSVLTGKVEKVLSKQHSSSINAVAWSPSGSHVVSVDKGCRavLW 604
Cdd:COG4946    348 PAWSPDGKSIAYFSdASGEyeLYIAPADGSGEPKQLTLGDLGRVFNPVWSPDGKKIAFTDNRGR--LW 413
COG4946 COG4946
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown] ...
 488-591 1.14e-03

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


Pssm-ID: 443973 [Multi-domain]  Cd Length: 1072  Bit Score: 41.95  E-value: 1.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977  488 LGKITALDLNPERTELLTCSRDDLLKVIDLRTNAVKQTFSAPGFKCGSDwtrVVFSPDGSYVA----AGSAEGSLYIWSV 563
Cdd:COG4946    388 LGRVFNPVWSPDGKKIAFTDNRGRLWVVDLASGKVRKVDTDGYGDGISD---LAWSPDSKWLAyskpGPNQLSQIFLYDV 464

                           90       100
                   ....*....|....*....|....*...
gi 1044375977  564 LTGKVEKVLSKQHSSSinAVAWSPSGSH 591
Cdd:COG4946    465 ETGKTVQLTDGRYDDG--SPAFSPDGKY 490
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 81-238 1.34e-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: 41.98  E-value: 1.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977   81 QLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQQKDREMQMNEAKIAECLQTISDLETECLDLRTKLQDLEIANQ 160
Cdd:TIGR02169  675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIE 754

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977  161 TLKDEYDALQITFTALEEKLRKTTEENQELVTRWMAEKAQEANRLNAENEKDSRRRQARLQ------------KELAEAA 228
Cdd:TIGR02169  755 NVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLReieqklnrltleKEYLEKE 834

                          170
                   ....*....|
gi 1044375977  229 KEPLPVEQDD 238
Cdd:TIGR02169  835 IQELQEQRID 844
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 86-270 1.38e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.29  E-value: 1.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977  86 AQLRIKHQEELTELHKKRGELAQLVIDLNNQMQQKDREMQMNEAKIAECLQTISDLETECLDLRTKLQDLEIANQTLKDE 165
Cdd:COG4942    19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977 166 YDALQitfTALEEKLRK--TTEENQELVTRWMAEKAQEANR----LNAENEKDsRRRQARLQKELAE-AAKEPLPVEQDD 238
Cdd:COG4942    99 LEAQK---EELAELLRAlyRLGRQPPLALLLSPEDFLDAVRrlqyLKYLAPAR-REQAEELRADLAElAALRAELEAERA 174

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1044375977 239 DIEVIVDETSDHTEETSPVRAISRAATKRLSQ 270
Cdd:COG4942   175 ELEALLAELEEERAALEALKAERQKLLARLEK 206
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
80-208 1.40e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 41.05  E-value: 1.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977  80 SQLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQQKDREMQMNEAK---IAECLQTISDLE----TECLD----- 147
Cdd:COG1340    57 EEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAggsIDKLRKEIERLEwrqqTEVLSpeeek 136

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1044375977 148 --------LRTKLQDLEIAN------QTLKDEYDALQITFTALEEKLRKTTEENQELVTRwMAEKAQEANRLNAE 208
Cdd:COG1340   137 elvekikeLEKELEKAKKALekneklKELRAELKELRKEAEEIHKKIKELAEEAQELHEE-MIELYKEADELRKE 210
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 54-211 1.42e-03

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 41.96  E-value: 1.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977   54 QKLQAEKHDVPNRHE-ISPGHDGTWNDSQLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQ---MQQKDREMQMNEA 129
Cdd:TIGR00606  795 ERFQMELKDVERKIAqQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQiqhLKSKTNELKSEKL 874

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977  130 KIAECLQTISDLETECLDLRTKLQDLEIANQTLKDEydalqitFTALEEKLRKTTEENQELVTRWMAEKAQEANRLNAEN 209
Cdd:TIGR00606  875 QIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQ-------DSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIK 947


                   ..
gi 1044375977  210 EK 211
Cdd:TIGR00606  948 EK 949
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
103-230 1.67e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 41.38  E-value: 1.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977 103 RGE-LAQLVIDLNNQMQQKDREMQMNEAKIAEclQTISDLETECLDLRTKLQDLEIANQTLKDEYDALQITFTALEEKLR 181
Cdd:COG2433   374 RGLsIEEALEELIEKELPEEEPEAEREKEHEE--RELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELS 451

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1044375977 182 KT-TEENQELvtrwmaEKAQEANRLNAENEkdsrrrqaRLQKELAEAAKE 230
Cdd:COG2433   452 EArSEERREI------RKDREISRLDREIE--------RLERELEEERER 487
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 43-215 1.67e-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: 41.59  E-value: 1.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977   43 LEKSDLHSVLaQKLQAEKHDVpnRHEISPghdgtwNDSQLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQQKDR 122
Cdd:TIGR02169  784 LEARLSHSRI-PEIQAELSKL--EEEVSR------IEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEK 854

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977  123 EMQMNEAKIAECLQTISDLETECLDLRTKLQDLEIANQTLKDEYDALQITFTALEEKLRKTTEENQELvtrwmAEKAQEA 202
Cdd:TIGR02169  855 EIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSEL-----KAKLEAL 929

                          170
                   ....*....|...
gi 1044375977  203 NRLNAENEKDSRR 215
Cdd:TIGR02169  930 EEELSEIEDPKGE 942
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
93-243 1.75e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.04  E-value: 1.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977  93 QEELTELHKKRGELAQLvidlNNQMQQKDREMQMNEAKIAECLQTISDLETECLDLRTKLQDLEIANQTLKDEYDALQIT 172
Cdd:COG4372    34 RKALFELDKLQEELEQL----REELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEE 109

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1044375977 173 FTALEEKLRKTTEENQELVTRWMAEKAQEANRLNAENEKDSR-----RRQARLQKELAEAAKEPLPVEQDDDIEVI 243
Cdd:COG4372   110 AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEElkeleEQLESLQEELAALEQELQALSEAEAEQAL 185
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
86-238 2.25e-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: 2.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977   86 AQLRIKHQEELTELHKKRGELAQlvidlnnQMQQKDREMQMNEAKIAEclQTISDLETECLDLRTKLQDLEIANQTLKDE 165
Cdd:COG4913    247 AREQIELLEPIRELAERYAAARE-------RLAELEYLRAALRLWFAQ--RRLELLEAELEELRAELARLEAELERLEAR 317

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1044375977  166 YDALQITFTALEEKLRkttEENQELVTRWMAEKAQeanrlnAENEKDSRRRQARLQKELAEAAKEPLPVEQDD 238
Cdd:COG4913    318 LDALREELDELEAQIR---GNGGDRLEQLEREIER------LERELEERERRRARLEALLAALGLPLPASAEE 381
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 104-230 3.71e-03

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 39.66  E-value: 3.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977 104 GELAQLVIDLNNQMQQKDREMQMNEAK--IAECLQTISDLETECLDLRTKLQDLEiaNQTLKDEyDALQITFTALEEKLr 181
Cdd:cd22656    94 AEILELIDDLADATDDEELEEAKKTIKalLDDLLKEAKKYQDKAAKVVDKLTDFE--NQTEKDQ-TALETLEKALKDLL- 169

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1044375977 182 ktteenqelvtrwmaekAQEANRLNAENEKDSRRRQARLQKELAEAAKE 230
Cdd:cd22656   170 -----------------TDEGGAIARKEIKDLQKELEKLNEEYAAKLKA 201
PTZ00332 PTZ00332
paraflagellar rod protein; Provisional
 10-226 3.87e-03

paraflagellar rod protein; Provisional


Pssm-ID: 240364 [Multi-domain]  Cd Length: 589  Bit Score: 40.33  E-value: 3.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977  10 FPRWKRHISE-ELRRRDRLQRQAFEEIILQYNKLLEKSDLHSVLA-------QKLQAEK-HDVPNRHeispghdgtwnDS 80
Cdd:PTZ00332  341 FEEVKRRIEEnDREEKRRVEYQQFLEVAGQHKKLLELTVYNCDLAlrctglvEELVSEGcAAVKARH-----------DK 409

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977  81 QLQEMAQLRIK-HQEELTELHKKRGELAQLVIDLNNQMQQKDREMQMNEAKIAECLQTI-------SDLETECLDLRTKL 152
Cdd:PTZ00332  410 TNQDLAALRLQvHKEHLEYFRMLYLTLGSLIYKKEKRLEEIDRNIRTTHIQLEFCVETFdpnakkhADMKKELYKLRQGV 489

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977 153 QDlEIAnqTLKDEYDALQITFTALEEKLRKT--------TEENQELVTRW--MAE-----KAQEANRLNAENEKDSRRRQ 217
Cdd:PTZ00332  490 EE-ELA--MLKEKQAQALEMFKESEEALDAAgiefvhpvDENNEEVLTRRskMVEyrshlAKQEEVKIAAEREEIKRARL 566


                  ....*....
gi 1044375977 218 ARLQKELAE 226
Cdd:PTZ00332  567 LRSQGYRGE 575
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
83-230 4.44e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.00  E-value: 4.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977  83 QEMAQLRIKHQeeLTELHKKRGELAQLVIDLNNQMQQKDREMQMNEAKIAECLQTISDLETECLDLRTK--LQDLEIANQ 160
Cdd:COG3206   196 AALEEFRQKNG--LVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLA 273

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1044375977 161 TLKDEYDALQITFTALEEKLRKTTEENQELvtrwMAEKAQEANRL--NAENEKDS-RRRQARLQKELAEAAKE 230
Cdd:COG3206   274 ELEAELAELSARYTPNHPDVIALRAQIAAL----RAQLQQEAQRIlaSLEAELEAlQAREASLQAQLAQLEAR 342
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 81-245 4.45e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 40.16  E-value: 4.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977   81 QLQEMAQLRIKHQEELTELHKKRGELAQLVIDL----------NNQMQQKDREMQMN----EAKIAECLQTISDLETECL 146
Cdd:pfam01576   48 QLQAETELCAEAEEMRARLAARKQELEEILHELesrleeeeerSQQLQNEKKKMQQHiqdlEEQLDEEEAARQKLQLEKV 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977  147 DLRTKLQDLEIANQTLKDEYDALQITFTALEEKLRKTTEENQElvtrwMAEKAQEANRLNAENE------KDSRRRQARL 220
Cdd:pfam01576  128 TTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAE-----EEEKAKSLSKLKNKHEamisdlEERLKKEEKG 202

                          170       180
                   ....*....|....*....|....*
gi 1044375977  221 QKELaEAAKEPLPVEQDDDIEVIVD 245
Cdd:pfam01576  203 RQEL-EKAKRKLEGESTDLQEQIAE 226
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 83-252 4.57e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 40.00  E-value: 4.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977  83 QEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQQKDR-----EMQMNEAKIAECLQTISDLETECLDLRTKLQDLEI 157
Cdd:TIGR04523 517 KKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKenlekEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEK 596

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977 158 ANQTLKDEYDALQITFTALEEKLRKTTEENQELvtrwmaekaqEANRLNAENEKDSRRRQARLQKELAEAAKEPLP--VE 235
Cdd:TIGR04523 597 EKKDLIKEIEEKEKKISSLEKELEKAKKENEKL----------SSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPeiIK 666

                         170
                  ....*....|....*..
gi 1044375977 236 QDDDIEVIVDETSDHTE 252
Cdd:TIGR04523 667 KIKESKTKIDDIIELMK 683
Ge1_WD40 pfam16529
WD40 region of Ge1, enhancer of mRNA-decapping protein; Ge1_WD40 is the N-terminal region of ...
 365-446 4.86e-03

WD40 region of Ge1, enhancer of mRNA-decapping protein; Ge1_WD40 is the N-terminal region of Ge-1 or enhancer of mRNA-decapping proteins. WD40-repeat regions are involved in protein-protein interactions.


Pssm-ID: 465162 [Multi-domain]  Cd Length: 328  Bit Score: 39.36  E-value: 4.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977 365 SNAGITSIEFDSAGSYLLAASNDFASRIWTV-----DDYRLRHTLTGHSGKVLSAKFLLDNAR----------IVSGS-H 428
Cdd:pfam16529 185 EHSLLVDAAFSPDGTALATASLDGEVKFFQIylfdnRNPRCLHEWKPHDGKPLSSLFFLDNHKkppevqfwrfAITGAdN 264

                          90
                  ....*....|....*...
gi 1044375977 429 DRTLKLWDLRSKVCIKTV 446
Cdd:pfam16529 265 NSELKLWSCESWTCLQTI 282
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 89-230 5.01e-03

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 39.81  E-value: 5.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977  89 RIKHQEELTElHKKRGELAQLVIDLNNQMQQKD---REMQMNEAKIAECLQTISDLETECLDLRTKLQDLEIANQTLKDE 165
Cdd:pfam10174 454 RLKEQRERED-RERLEELESLKKENKDLKEKVSalqPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEE 532

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1044375977 166 ydalqitFTALEEKLRKTteENQELVTRWMAEKAQEANRLNAE---NEKDSRRRQARLQKeLAEAAKE 230
Cdd:pfam10174 533 -------CSKLENQLKKA--HNAEEAVRTNPEINDRIRLLEQEvarYKEESGKAQAEVER-LLGILRE 590
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 538-562 5.47e-03

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 34.98  E-value: 5.47e-03
                           10        20
                   ....*....|....*....|....*
gi 1044375977  538 TRVVFSPDGSYVAAGSAEGSLYIWS 562
Cdd:smart00320  16 TSVAFSPDGKYLASGSDDGTIKLWD 40
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 79-189 5.81e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 39.62  E-value: 5.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977  79 DSQLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQQKDREMQMNEAKIAECLQTISDLETECLDLRTKLQDLEIA 158
Cdd:TIGR04523 327 QNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKL 406

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1044375977 159 NQTLKDEYDALQITFTALE---EKLRKTTEENQE 189
Cdd:TIGR04523 407 NQQKDEQIKKLQQEKELLEkeiERLKETIIKNNS 440
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
81-246 7.12e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.37  E-value: 7.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977  81 QLQEMAQLRIKHQEELTELHKKRG-------ELAQLVIDLNNQMQQKDREM--QMNEAKIAECLQTISDLETECldlrtK 151
Cdd:COG4717   306 ELQALPALEELEEEELEELLAALGlppdlspEELLELLDRIEELQELLREAeeLEEELQLEELEQEIAALLAEA-----G 380

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977 152 LQDLE--IANQTLKDEYDALQITFTALEEKLRKTTEENQELVTRWMAEKAQEANRLNAENEKDSRRRQARLQKELAEAAK 229
Cdd:COG4717   381 VEDEEelRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEA 460

                         170
                  ....*....|....*..
gi 1044375977 230 EPLPVEQDDDIEVIVDE 246
Cdd:COG4717   461 ELEQLEEDGELAELLQE 477
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 112-305 8.13e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.04  E-value: 8.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977 112 DLNNQMQQKDREMQMNEAKIAECLQTISDLETECLDLRTKLQDLEianqTLKDEYDALQitftaleEKLRKTTEENQELV 191
Cdd:COG3883   116 DFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELE----ALKAELEAAK-------AELEAQQAEQEALL 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044375977 192 TRWMAEKAQEANRLNAENEKDSRRRQARLQKELAEAAKEPLPVEQDDDIEVIVDETSDHTEETSPVRAISRAATKRLSQP 271
Cdd:COG3883   185 AQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGA 264

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1044375977 272 AGGLLDSITNIFGRRSVSSFPVPQDNVDTHPGSG 305
Cdd:COG3883   265 AGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGA 298
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH