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Conserved domains on  [gi|27777650|ref|NP_084122|]
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autophagy-related protein 16-1 isoform 2 [Mus musculus]

Protein Classification

WD repeat ATG16 family protein( domain architecture ID 12095058)

WD repeat ATG16 (autophagy-related 16) family protein similar to human ATG16L1 that plays an essential role in autophagy; it interacts with ATG12-ATG5 to mediate the conjugation of phosphatidylethanolamine to LC3, and thus, controls the elongation of the nascent autophagosomal membrane

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
257-604 9.30e-59

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 202.06  E-value: 9.30e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650 257 VRAVSRAATKRLSQPAGGLLDSITNIFGRRSVSSIPVPQDIMDTHPASGKDVRVPTTAS----YVFDAHDGEVNAVQFSP 332
Cdd:COG2319  51 LAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATglllRTLTGHTGAVRSVAFSP 130

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650 333 GSRLLATGGMDRRVKLWEAFGDKCEfkGSLSGSNAGITSIEFDSAGAYLLAASNDFASRIWTVDDYRLRHTLTGHSGKVL 412
Cdd:COG2319 131 DGKTLASGSADGTVRLWDLATGKLL--RTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVR 208

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650 413 SAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTV-FAGSSCNDIVCT--EQCVMSGHFDKKIRFWDIRSESVVREME-LL 488
Cdd:COG2319 209 SVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLtGHSGSVRSVAFSpdGRLLASGSADGTVRLWDLATGELLRTLTgHS 288

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650 489 GKITALDLNPERTELLSCSRDDLLKVIDLRTNAVKQTFSAPgfkcGSDWTRVVFSPDGSYVAAGSAEGSLYVWSVLTGKV 568
Cdd:COG2319 289 GGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGH----TGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGEL 364

                       330       340       350
                ....*....|....*....|....*....|....*.
gi 27777650 569 EKVLsKQHSSSINAVAWAPSGLHVVSVDKGSRAVLW 604
Cdd:COG2319 365 LRTL-TGHTGAVTSVAFSPDGRTLASGSADGTVRLW 399
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 31-206 3.95e-55

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: 184.75  E-value: 3.95e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650    31 AFEEIILQYTKLLEKSDLHSVLTQKLQAEKHDMPNRHEISPGHDGAWNDSQLQEMAQLRIKHQEELTELHKKRGELAQLV 110
Cdd:pfam08614   1 AFLELIDAYNRLLDRTALLEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQLREELAELYRSRGELAQRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650   111 IDLNNQMQQKDKEIQMNEAKISEYLQTISDLETNCLDLRTKLQDLEVANQTLKDEYDALQITFTALEEKLRKTTEENQEL 190
Cdd:pfam08614  81 VDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQDELVALQLQLNMAEEKLRKLEKENREL 160

                         170
                  ....*....|....*.
gi 27777650   191 VTRWMAEKAQEANRLN 206
Cdd:pfam08614 161 VERWMKRKGQEAEAMN 176
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
257-604 9.30e-59

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 202.06  E-value: 9.30e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650 257 VRAVSRAATKRLSQPAGGLLDSITNIFGRRSVSSIPVPQDIMDTHPASGKDVRVPTTAS----YVFDAHDGEVNAVQFSP 332
Cdd:COG2319  51 LAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATglllRTLTGHTGAVRSVAFSP 130

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650 333 GSRLLATGGMDRRVKLWEAFGDKCEfkGSLSGSNAGITSIEFDSAGAYLLAASNDFASRIWTVDDYRLRHTLTGHSGKVL 412
Cdd:COG2319 131 DGKTLASGSADGTVRLWDLATGKLL--RTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVR 208

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650 413 SAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTV-FAGSSCNDIVCT--EQCVMSGHFDKKIRFWDIRSESVVREME-LL 488
Cdd:COG2319 209 SVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLtGHSGSVRSVAFSpdGRLLASGSADGTVRLWDLATGELLRTLTgHS 288

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650 489 GKITALDLNPERTELLSCSRDDLLKVIDLRTNAVKQTFSAPgfkcGSDWTRVVFSPDGSYVAAGSAEGSLYVWSVLTGKV 568
Cdd:COG2319 289 GGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGH----TGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGEL 364

                       330       340       350
                ....*....|....*....|....*....|....*.
gi 27777650 569 EKVLsKQHSSSINAVAWAPSGLHVVSVDKGSRAVLW 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 ...
 317-605 2.18e-57

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: 194.86  E-value: 2.18e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650 317 VFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWEAFGDKCEFkgSLSGSNAGITSIEFDSAGAYLLAASNDFASRIWTVD 396
Cdd:cd00200   4 TLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLR--TLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLE 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650 397 DYRLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTvFAG----------SSCNDIVCteqcvmSGH 466
Cdd:cd00200  82 TGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTT-LRGhtdwvnsvafSPDGTFVA------SSS 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650 467 FDKKIRFWDIRSESVVREMEL-LGKITALDLNPERTELLSCSRDDLLKVIDLRTNAVKQTFSAPgfkcgSDW-TRVVFSP 544
Cdd:cd00200 155 QDGTIKLWDLRTGKCVATLTGhTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGH-----ENGvNSVAFSP 229

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27777650 545 DGSYVAAGSAEGSLYVWSVLTGKVEKVLSkQHSSSINAVAWAPSGLHVVSVDKGSRAVLWA 605
Cdd:cd00200 230 DGYLLASGSEDGTIRVWDLRTGECVQTLS-GHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 31-206 3.95e-55

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: 184.75  E-value: 3.95e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650    31 AFEEIILQYTKLLEKSDLHSVLTQKLQAEKHDMPNRHEISPGHDGAWNDSQLQEMAQLRIKHQEELTELHKKRGELAQLV 110
Cdd:pfam08614   1 AFLELIDAYNRLLDRTALLEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQLREELAELYRSRGELAQRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650   111 IDLNNQMQQKDKEIQMNEAKISEYLQTISDLETNCLDLRTKLQDLEVANQTLKDEYDALQITFTALEEKLRKTTEENQEL 190
Cdd:pfam08614  81 VDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQDELVALQLQLNMAEEKLRKLEKENREL 160

                         170
                  ....*....|....*.
gi 27777650   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 4.68e-30

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


Pssm-ID: 439196 [Multi-domain]  Cd Length: 91  Bit Score: 113.43  E-value: 4.68e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650 119 QKDKEIQMNEAKISEYLQTISDLETNCLDLRTKLQDLEVANQTLKDEYDALQITFTALEEKLRKTTEENQELVTRWMAEK 198
Cdd:cd22887   1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEENDELVERWMAKK 80

                        90
                ....*....|.
gi 27777650 199 AQEANRLNAEN 209
Cdd:cd22887  81 QQEADKMNEAN 91
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
79-264 1.52e-08

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 56.83  E-value: 1.52e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650  79 DSQLQEMAQLRIKHQEELTELHKKRGELAQL---VIDLNNQMQQKDKEIQMNEAKISEYLQTISDLETNCLDLRTKLQDL 155
Cdd:COG4372  41 DKLQEELEQLREELEQAREELEQLEEELEQArseLEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEEL 120

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650 156 EVANQTLKDEYDALQITFTALEEKLRKTTEENQELVTRwMAEKAQEANRLNAENEKDSRRR-QARLQKELAEAAKEPLPV 234
Cdd:COG4372 121 QKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ-LESLQEELAALEQELQALSEAEaEQALDELLKEANRNAEKE 199

                       170       180       190
                ....*....|....*....|....*....|
gi 27777650 235 EQDDDIEVIVDETSDHTEETSPVRAVSRAA 264
Cdd:COG4372 200 EELAEAEKLIESLPRELAEELLEAKDSLEA 229
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 316-350 7.35e-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: 7.35e-08
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 27777650    316 YVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWE 350
Cdd:smart00320   6 KTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
316-350 1.89e-07

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 47.73  E-value: 1.89e-07
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 27777650   316 YVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWE 350
Cdd:pfam00400   5 KTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 79-230 2.50e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.83  E-value: 2.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650     79 DSQLQEMAQLRIKH-------QEELTELHKKRGELAQLVID-------LNNQMQQKDKEIQMNEAKISEYLQTISDLETN 144
Cdd:TIGR02168  245 QEELKEAEEELEELtaelqelEEKLEELRLEVSELEEEIEElqkelyaLANEISRLEQQKQILRERLANLERQLEELEAQ 324

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650    145 CLDLRTKLQDLEVANQTLKDEYDALQITFTALEEKLRKTTEENQELVTRWmAEKAQEANRLNAEnEKDSRRRQARLQKEL 224
Cdd:TIGR02168  325 LEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRL-EELEEQLETLRSK-VAQLELQIASLNNEI 402


                   ....*.
gi 27777650    225 AEAAKE 230
Cdd:TIGR02168  403 ERLEAR 408
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 325-561 5.98e-06

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 49.31  E-value: 5.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650  325 VNAVQFSPGSRLLATGGMDRRVKLWEAF-----GDKCEFKGSLSGSNAGITSIEFDSAGAYLLAASN-DFASRIWTVDDY 398
Cdd:PLN00181 486 VCAIGFDRDGEFFATAGVNKKIKIFECEsiikdGRDIHYPVVELASRSKLSGICWNSYIKSQVASSNfEGVVQVWDVARS 565

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650  399 RLRHTLTGHSGKVLSAKFL-LDNARIVSGSHDRTLKLWDLRSKVCIKTVfagSSCNDIVCTE------QCVMSGHFDKKI 471
Cdd:PLN00181 566 QLVTEMKEHEKRVWSIDYSsADPTLLASGSDDGSVKLWSINQGVSIGTI---KTKANICCVQfpsesgRSLAFGSADHKV 642

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650  472 RFWDIRSE-----SVVREMELLGKITALDlnpeRTELLSCSRDDLLKVIDLRTNA--VKQT--FSAPGFKCGSDWTRVVF 542
Cdd:PLN00181 643 YYYDLRNPklplcTMIGHSKTVSYVRFVD----SSTLVSSSTDNTLKLWDLSMSIsgINETplHSFMGHTNVKNFVGLSV 718

                        250
                 ....*....|....*....
gi 27777650  543 SpDGsYVAAGSAEGSLYVW 561
Cdd:PLN00181 719 S-DG-YIATGSETNEVFVY 735
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
46-230 2.40e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 44.26  E-value: 2.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650   46 SDLHSVLTQKLQAEKHDMPNRHEispghdgawndsqlQEMAQLR--IKHQEELTELHKKRGELAQLVIDLNNQMQQkdkE 123
Cdd:PRK02224 190 DQLKAQIEEKEEKDLHERLNGLE--------------SELAELDeeIERYEEQREQARETRDEADEVLEEHEERRE---E 252

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650  124 IQMNEAKISEYLQTISDLETNCLDLRTKLQDLEVANQTLKDEYDAL--QITFTALE----EKLRKTTEENQELVTRWMAE 197
Cdd:PRK02224 253 LETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLlaEAGLDDADaeavEARREELEDRDEELRDRLEE 332

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 27777650  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 9.30e-59

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 202.06  E-value: 9.30e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650 257 VRAVSRAATKRLSQPAGGLLDSITNIFGRRSVSSIPVPQDIMDTHPASGKDVRVPTTAS----YVFDAHDGEVNAVQFSP 332
Cdd:COG2319  51 LAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATglllRTLTGHTGAVRSVAFSP 130

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650 333 GSRLLATGGMDRRVKLWEAFGDKCEfkGSLSGSNAGITSIEFDSAGAYLLAASNDFASRIWTVDDYRLRHTLTGHSGKVL 412
Cdd:COG2319 131 DGKTLASGSADGTVRLWDLATGKLL--RTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVR 208

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650 413 SAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTV-FAGSSCNDIVCT--EQCVMSGHFDKKIRFWDIRSESVVREME-LL 488
Cdd:COG2319 209 SVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLtGHSGSVRSVAFSpdGRLLASGSADGTVRLWDLATGELLRTLTgHS 288

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650 489 GKITALDLNPERTELLSCSRDDLLKVIDLRTNAVKQTFSAPgfkcGSDWTRVVFSPDGSYVAAGSAEGSLYVWSVLTGKV 568
Cdd:COG2319 289 GGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGH----TGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGEL 364

                       330       340       350
                ....*....|....*....|....*....|....*.
gi 27777650 569 EKVLsKQHSSSINAVAWAPSGLHVVSVDKGSRAVLW 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 ...
 317-605 2.18e-57

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: 194.86  E-value: 2.18e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650 317 VFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWEAFGDKCEFkgSLSGSNAGITSIEFDSAGAYLLAASNDFASRIWTVD 396
Cdd:cd00200   4 TLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLR--TLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLE 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650 397 DYRLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTvFAG----------SSCNDIVCteqcvmSGH 466
Cdd:cd00200  82 TGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTT-LRGhtdwvnsvafSPDGTFVA------SSS 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650 467 FDKKIRFWDIRSESVVREMEL-LGKITALDLNPERTELLSCSRDDLLKVIDLRTNAVKQTFSAPgfkcgSDW-TRVVFSP 544
Cdd:cd00200 155 QDGTIKLWDLRTGKCVATLTGhTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGH-----ENGvNSVAFSP 229

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27777650 545 DGSYVAAGSAEGSLYVWSVLTGKVEKVLSkQHSSSINAVAWAPSGLHVVSVDKGSRAVLWA 605
Cdd:cd00200 230 DGYLLASGSEDGTIRVWDLRTGECVQTLS-GHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 31-206 3.95e-55

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: 184.75  E-value: 3.95e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650    31 AFEEIILQYTKLLEKSDLHSVLTQKLQAEKHDMPNRHEISPGHDGAWNDSQLQEMAQLRIKHQEELTELHKKRGELAQLV 110
Cdd:pfam08614   1 AFLELIDAYNRLLDRTALLEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQLREELAELYRSRGELAQRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650   111 IDLNNQMQQKDKEIQMNEAKISEYLQTISDLETNCLDLRTKLQDLEVANQTLKDEYDALQITFTALEEKLRKTTEENQEL 190
Cdd:pfam08614  81 VDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQDELVALQLQLNMAEEKLRKLEKENREL 160

                         170
                  ....*....|....*.
gi 27777650   191 VTRWMAEKAQEANRLN 206
Cdd:pfam08614 161 VERWMKRKGQEAEAMN 176
WD40 COG2319
WD40 repeat [General function prediction only];
316-563 7.85e-48

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 172.40  E-value: 7.85e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650 316 YVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWEAFGDKCEFkgSLSGSNAGITSIEFDSAGAYLLAASNDFASRIWTV 395
Cdd:COG2319 156 RTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLR--TLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDL 233

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650 396 DDYRLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTvFAGSSC--NDIVCT--EQCVMSGHFDKKI 471
Cdd:COG2319 234 ATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRT-LTGHSGgvNSVAFSpdGKLLASGSDDGTV 312

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650 472 RFWDIRSESVVREME-LLGKITALDLNPERTELLSCSRDDLLKVIDLRTNAVKQTFSAPgfkcgSDW-TRVVFSPDGSYV 549
Cdd:COG2319 313 RLWDLATGKLLRTLTgHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGH-----TGAvTSVAFSPDGRTL 387

                       250
                ....*....|....
gi 27777650 550 AAGSAEGSLYVWSV 563
Cdd:COG2319 388 ASGSADGTVRLWDL 401
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 316-562 1.15e-37

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: 141.32  E-value: 1.15e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650 316 YVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWEAFGDKCEFkgSLSGSNAGITSIEFDSAGAYLLAASNDFASRIWTV 395
Cdd:cd00200  87 RTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLT--TLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDL 164

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650 396 DDYRLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTvfagsscndivcteqcvMSGHfdkkirfwd 475
Cdd:cd00200 165 RTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGT-----------------LRGH--------- 218

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650 476 irsesvvremelLGKITALDLNPERTELLSCSRDDLLKVIDLRTNAVKQTFSAPGFKCGSdwtrVVFSPDGSYVAAGSAE 555
Cdd:cd00200 219 ------------ENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTS----LAWSPDGKRLASGSAD 282


                ....*..
gi 27777650 556 GSLYVWS 562
Cdd:cd00200 283 GTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
317-519 6.90e-37

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 141.97  E-value: 6.90e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650 317 VFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWEAFGDKCEFkgSLSGSNAGITSIEFDSAGAYLLAASNDFASRIWTVD 396
Cdd:COG2319 199 TLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLR--TLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLA 276

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650 397 DYRLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTvFAG--SSCNDIVCT--EQCVMSGHFDKKIR 472
Cdd:COG2319 277 TGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRT-LTGhtGAVRSVAFSpdGKTLASGSDDGTVR 355

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 27777650 473 FWDIRSESVVREME-LLGKITALDLNPERTELLSCSRDDLLKVIDLRT 519
Cdd:COG2319 356 LWDLATGELLRTLTgHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
WD40 COG2319
WD40 repeat [General function prediction only];
329-604 2.52e-34

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 134.65  E-value: 2.52e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650 329 QFSPGSRLLATGGMDRRVKLWEAFGDKCEfkGSLSGSNAGITSIEFDSAGAYLLAASNDFASRIWTVDDYRLRHTLTGHS 408
Cdd:COG2319   1 ALSADGAALAAASADLALALLAAALGALL--LLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHT 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650 409 GKVLSAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTVFA-GSSCNDIVCTE--QCVMSGHFDKKIRFWDIRSESVVREM 485
Cdd:COG2319  79 AAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGhTGAVRSVAFSPdgKTLASGSADGTVRLWDLATGKLLRTL 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650 486 EL-LGKITALDLNPERTELLSCSRDDLLKVIDLRTNAVKQTFSAPgfkcgSDW-TRVVFSPDGSYVAAGSAEGSLYVWSV 563
Cdd:COG2319 159 TGhSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGH-----TGAvRSVAFSPDGKLLASGSADGTVRLWDL 233

                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 27777650 564 LTGKVEKVLsKQHSSSINAVAWAPSGLHVVSVDKGSRAVLW 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 ...
 400-594 6.58e-34

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 130.53  E-value: 6.58e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650 400 LRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTV----FAGSSCNDIVCTEQCVmSGHFDKKIRFWD 475
Cdd:cd00200   1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLkghtGPVRDVAASADGTYLA-SGSSDKTIRLWD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650 476 IRSESVVREMEL-LGKITALDLNPERTELLSCSRDDLLKVIDLRTNAVKQTFSAPgfkcgSDWTR-VVFSPDGSYVAAGS 553
Cdd:cd00200  80 LETGECVRTLTGhTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGH-----TDWVNsVAFSPDGTFVASSS 154

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 27777650 554 AEGSLYVWSVLTGKVEKVLsKQHSSSINAVAWAPSGLHVVS 594
Cdd:cd00200 155 QDGTIKLWDLRTGKCVATL-TGHTGEVNSVAFSPDGEKLLS 194
WD40 COG2319
WD40 repeat [General function prediction only];
316-478 4.71e-32

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 128.11  E-value: 4.71e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650 316 YVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWEAFGDKCefKGSLSGSNAGITSIEFDSAGAYLLAASNDFASRIWTV 395
Cdd:COG2319 240 RTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGEL--LRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDL 317

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650 396 DDYRLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTvFAGSScnDIVCT------EQCVMSGHFDK 469
Cdd:COG2319 318 ATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRT-LTGHT--GAVTSvafspdGRTLASGSADG 394


                ....*....
gi 27777650 470 KIRFWDIRS 478
Cdd:COG2319 395 TVRLWDLAT 403
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 119-209 4.68e-30

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


Pssm-ID: 439196 [Multi-domain]  Cd Length: 91  Bit Score: 113.43  E-value: 4.68e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650 119 QKDKEIQMNEAKISEYLQTISDLETNCLDLRTKLQDLEVANQTLKDEYDALQITFTALEEKLRKTTEENQELVTRWMAEK 198
Cdd:cd22887   1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEENDELVERWMAKK 80

                        90
                ....*....|.
gi 27777650 199 AQEANRLNAEN 209
Cdd:cd22887  81 QQEADKMNEAN 91
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
79-264 1.52e-08

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 56.83  E-value: 1.52e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650  79 DSQLQEMAQLRIKHQEELTELHKKRGELAQL---VIDLNNQMQQKDKEIQMNEAKISEYLQTISDLETNCLDLRTKLQDL 155
Cdd:COG4372  41 DKLQEELEQLREELEQAREELEQLEEELEQArseLEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEEL 120

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650 156 EVANQTLKDEYDALQITFTALEEKLRKTTEENQELVTRwMAEKAQEANRLNAENEKDSRRR-QARLQKELAEAAKEPLPV 234
Cdd:COG4372 121 QKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ-LESLQEELAALEQELQALSEAEaEQALDELLKEANRNAEKE 199

                       170       180       190
                ....*....|....*....|....*....|
gi 27777650 235 EQDDDIEVIVDETSDHTEETSPVRAVSRAA 264
Cdd:COG4372 200 EELAEAEKLIESLPRELAEELLEAKDSLEA 229
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
88-238 2.64e-08

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 56.70  E-value: 2.64e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650  88 LRIKHQEELTELHKKRGELAQLVIDlnnQMQQKDKEIQMNEAKISEYLQTISDLETncldLRTKLQDLEVANQTLKDEYD 167
Cdd:COG4717  47 LLERLEKEADELFKPQGRKPELNLK---ELKELEEELKEAEEKEEEYAELQEELEE----LEEELEELEAELEELREELE 119

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27777650 168 AL--QITFTALEEKLRKTTEENQELVTRWMAEKAQEANRLNAENEKDSRRRQ-ARLQKELAEAAKEPLPVEQDD 238
Cdd:COG4717 120 KLekLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAElAELQEELEELLEQLSLATEEE 193
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 316-350 7.35e-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: 7.35e-08
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 27777650    316 YVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWE 350
Cdd:smart00320   6 KTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 399-436 1.30e-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: 48.08  E-value: 1.30e-07
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 27777650    399 RLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWD 436
Cdd:smart00320   3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
316-350 1.89e-07

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 47.73  E-value: 1.89e-07
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 27777650   316 YVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWE 350
Cdd:pfam00400   5 KTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 81-270 1.90e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.17  E-value: 1.90e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650  81 QLQEMAQLRIKHQEELTELHKKRGELAQlvidlnnQMQQKDKEIQMNEAKISEYLQTISDLETNCLDLRTKLQDLEVANQ 160
Cdd:COG1196 275 ELEELELELEEAQAEEYELLAELARLEQ-------DIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELE 347

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650 161 TLKDEYDALQITFTALEEKLRKTTEENQELVTRWMAEKAQEANRLNAENEKDSRRRQARLQKELAEAAKEPLPVEQDDDI 240
Cdd:COG1196 348 EAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE 427

                       170       180       190
                ....*....|....*....|....*....|
gi 27777650 241 EVIVDETSDHTEETSPVRAVSRAATKRLSQ 270
Cdd:COG1196 428 EALAELEEEEEEEEEALEEAAEEEAELEEE 457
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
358-566 2.05e-07

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


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 52.39  E-value: 2.05e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650 358 FKGSLSGSNAGITSIEFDSAGAYLLAASNDFASRIWTVDDYRLRHTLTGHSGKVLSAKFLLDNARI-VSGSHDRTLKLWD 436
Cdd:COG3391  17 ALAALAVAVAALGLGGGGPLLAAASGGVVGAAVGGGGVALLAGLGLGAAAVADADGADAGADGRRLyVANSGSGRVSVID 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650 437 LRSKVCIKTVFAGSSCNDIVCTE---QCVMSGHFDKKIRFWDIRSESVVREMELLGKITALDLNPERTELLSCSRDD--- 510
Cdd:COG3391  97 LATGKVVATIPVGGGPRGLAVDPdggRLYVADSGNGRVSVIDTATGKVVATIPVGAGPHGIAVDPDGKRLYVANSGSntv 176

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27777650 511 --LLKVIDLRTNAVKQTFSApgfkcGSDWTRVVFSPDGS--YVA------AGSAEGSLYVWSVLTG 566
Cdd:COG3391 177 svIVSVIDTATGKVVATIPV-----GGGPVGVAVSPDGRrlYVAnrgsntSNGGSNTVSVIDLATL 237
WD40 pfam00400
WD domain, G-beta repeat;
399-436 3.61e-07

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 46.57  E-value: 3.61e-07
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 27777650   399 RLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWD 436
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 79-230 6.23e-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: 50.69  E-value: 6.23e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650  79 DSQLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQQKDKEIQMNEAKISEYLQTISDLEtncldlrTKLQdlEVA 158
Cdd:COG1579  16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE-------EQLG--NVR 86

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27777650 159 NQtlkDEYDALQITFTALEEKLRKTTEENQELVTRwmAEKAQ----EANRLNAENEKDSRRRQARLQKELAEAAKE 230
Cdd:COG1579  87 NN---KEYEALQKEIESLKRRISDLEDEILELMER--IEELEeelaELEAELAELEAELEEKKAELDEELAELEAE 157
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 80-286 1.47e-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: 50.92  E-value: 1.47e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650  80 SQLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQQKDKEIQMNEAKISEYLQTISDLE----------------- 142
Cdd:COG4942  41 KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKeelaellralyrlgrqp 120

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650 143 --------TNCLDLRTKLQDLEVANQTLKDEYDALQITFTALEEKLRKTTEENQELVTRwMAEKAQEANRLNAEnEKDSR 214
Cdd:COG4942 121 plalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL-LAELEEERAALEAL-KAERQ 198

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27777650 215 RRQARLQKELAEAAKEPLPVEQDDD-----IEVIVDETSDHTEETSPVRAVsrAATKRLSQPAGGlldSITNIFGRR 286
Cdd:COG4942 199 KLLARLEKELAELAAELAELQQEAEelealIARLEAEAAAAAERTPAAGFA--ALKGKLPWPVSG---RVVRRFGER 270
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 79-230 2.50e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.83  E-value: 2.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650     79 DSQLQEMAQLRIKH-------QEELTELHKKRGELAQLVID-------LNNQMQQKDKEIQMNEAKISEYLQTISDLETN 144
Cdd:TIGR02168  245 QEELKEAEEELEELtaelqelEEKLEELRLEVSELEEEIEElqkelyaLANEISRLEQQKQILRERLANLERQLEELEAQ 324

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650    145 CLDLRTKLQDLEVANQTLKDEYDALQITFTALEEKLRKTTEENQELVTRWmAEKAQEANRLNAEnEKDSRRRQARLQKEL 224
Cdd:TIGR02168  325 LEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRL-EELEEQLETLRSK-VAQLELQIASLNNEI 402


                   ....*.
gi 27777650    225 AEAAKE 230
Cdd:TIGR02168  403 ERLEAR 408
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 325-561 5.98e-06

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 49.31  E-value: 5.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650  325 VNAVQFSPGSRLLATGGMDRRVKLWEAF-----GDKCEFKGSLSGSNAGITSIEFDSAGAYLLAASN-DFASRIWTVDDY 398
Cdd:PLN00181 486 VCAIGFDRDGEFFATAGVNKKIKIFECEsiikdGRDIHYPVVELASRSKLSGICWNSYIKSQVASSNfEGVVQVWDVARS 565

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650  399 RLRHTLTGHSGKVLSAKFL-LDNARIVSGSHDRTLKLWDLRSKVCIKTVfagSSCNDIVCTE------QCVMSGHFDKKI 471
Cdd:PLN00181 566 QLVTEMKEHEKRVWSIDYSsADPTLLASGSDDGSVKLWSINQGVSIGTI---KTKANICCVQfpsesgRSLAFGSADHKV 642

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650  472 RFWDIRSE-----SVVREMELLGKITALDlnpeRTELLSCSRDDLLKVIDLRTNA--VKQT--FSAPGFKCGSDWTRVVF 542
Cdd:PLN00181 643 YYYDLRNPklplcTMIGHSKTVSYVRFVD----SSTLVSSSTDNTLKLWDLSMSIsgINETplHSFMGHTNVKNFVGLSV 718

                        250
                 ....*....|....*....
gi 27777650  543 SpDGsYVAAGSAEGSLYVW 561
Cdd:PLN00181 719 S-DG-YIATGSETNEVFVY 735
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 78-226 6.52e-06

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: 49.25  E-value: 6.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650    78 NDSQLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQQK---DKEIQMNEAKISEYLQTISDLETNCLDLRTKLQD 154
Cdd:TIGR04523 379 NQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKellEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKN 458

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27777650   155 LEVANQTLKDEYDALQITFTALEEKLRKTTEEnqelvtrwMAEKAQEANRLNAENeKDSRRRQARLQKELAE 226
Cdd:TIGR04523 459 LDNTRESLETQLKVLSRSINKIKQNLEQKQKE--------LKSKEKELKKLNEEK-KELEEKVKDLTKKISS 521
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
93-241 1.21e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 48.37  E-value: 1.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650   93 QEELTELHKKRGELAQLVIDLNNQMQQKDkEIQMNEAKISEYLQTISD---LETNCLDLRTKLQDLEVAN---QTLKDEY 166
Cdd:COG4913  616 EAELAELEEELAEAEERLEALEAELDALQ-ERREALQRLAEYSWDEIDvasAEREIAELEAELERLDASSddlAALEEQL 694

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27777650  167 DALQITFTALEEKLRKTTEENQELVTRW---MAEKAQEANRLNAENEKDSRRRQARLQKELAEAAKEPLPVEQDDDIE 241
Cdd:COG4913  695 EELEAELEELEEELDELKGEIGRLEKELeqaEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLE 772
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 321-437 1.26e-05

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 48.54  E-value: 1.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650  321 HDGEVNAVQFSPGS-RLLATGGMDRRVKLWEAfgDKCEFKGSLSgSNAGITSIEFDSAGAYLLAasndFASRIWTVDDYR 399
Cdd:PLN00181 574 HEKRVWSIDYSSADpTLLASGSDDGSVKLWSI--NQGVSIGTIK-TKANICCVQFPSESGRSLA----FGSADHKVYYYD 646

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 27777650  400 LRH------TLTGHSGKVLSAKFLlDNARIVSGSHDRTLKLWDL 437
Cdd:PLN00181 647 LRNpklplcTMIGHSKTVSYVRFV-DSSTLVSSSTDNTLKLWDL 689
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 79-189 2.44e-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: 2.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650    79 DSQLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQQKDKEIQMNEAKISEYLQTISDLETNCLDLRTKLQDLEVA 158
Cdd:TIGR04523 327 QNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKL 406

                          90       100       110
                  ....*....|....*....|....*....|....
gi 27777650   159 NQTLKDEYDALQITFTALE---EKLRKTTEENQE 189
Cdd:TIGR04523 407 NQQKDEQIKKLQQEKELLEkeiERLKETIIKNNS 440
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 55-230 2.59e-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: 2.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650     55 KLQAEKHDMpnRHEISPGHDGAWNDSQLQEMAQLRIKHQE-ELTELHKKRGELAQLVIDLNNQMQQKDKEIQMNEAKISE 133
Cdd:TIGR02168  716 QLRKELEEL--SRQISALRKDLARLEAEVEQLEERIAQLSkELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ 793

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650    134 YLQTISDLETNCLDLRTKLQDL--EVANQT-----LKDEYDALQITFTALEEKLRKTTEEnQELVTRWMAEKAQEANRLN 206
Cdd:TIGR02168  794 LKEELKALREALDELRAELTLLneEAANLRerlesLERRIAATERRLEDLEEQIEELSED-IESLAAEIEELEELIEELE 872

                          170       180       190
                   ....*....|....*....|....*....|
gi 27777650    207 AE-----NEKDSRRRQ-ARLQKELAEAAKE 230
Cdd:TIGR02168  873 SEleallNERASLEEAlALLRSELEELSEE 902
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 95-226 2.83e-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: 2.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650    95 ELTELHKKRGElaQLVIDLNNQMQQKDKEIQMNEAKISEYLQTISDLETNCLDLRTKLQDLEVANQTLKDEydalqitft 174
Cdd:TIGR04523 296 EISDLNNQKEQ--DWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRE--------- 364

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 27777650   175 aLEEK---LRKTTEENQelvtrwmaEKAQEANRLnaENEKDSRRRQARLQKELAE 226
Cdd:TIGR04523 365 -LEEKqneIEKLKKENQ--------SYKQEIKNL--ESQINDLESKIQNQEKLNQ 408
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
48-230 2.93e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.07  E-value: 2.93e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650  48 LHSVLTQKLQAEKHDMPNRHeispGHDGAWNDSQLQEMaqlrikhQEELTELHKKRGELAQLVidlnNQMQQKDKEIQMN 127
Cdd:COG4717  43 IRAMLLERLEKEADELFKPQ----GRKPELNLKELKEL-------EEELKEAEEKEEEYAELQ----EELEELEEELEEL 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650 128 EAKISEYLQTISDLET--NCLDLRTKLQDLEVANQTLKDEYDALQITFTALEEKLRKTTEENQELvTRWMAEKAQEANRL 205
Cdd:COG4717 108 EAELEELREELEKLEKllQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAEL-AELQEELEELLEQL 186

                       170       180
                ....*....|....*....|....*...
gi 27777650 206 NAENE---KDSRRRQARLQKELAEAAKE 230
Cdd:COG4717 187 SLATEeelQDLAEELEELQQRLAELEEE 214
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 80-230 3.83e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.85  E-value: 3.83e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650  80 SQLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQQKDKEIQMNEAKISEYLQTISDLETNCLDLRTKLQDLEVAN 159
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27777650 160 QTLKDEYDALQITFTALEEKLRKTTEENQELVTRwMAEKAQEANRLNAENEKDSRRRQARLQKELAEAAKE 230
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQLEELEEA-EEALLERLERLEEELEELEEALAELEEEEEEEEEAL 444
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
79-253 4.14e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.83  E-value: 4.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650   79 DSQLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQQKD-KEIQMNEAKISEYLQTISDLETNCLDLRTKLQDLEV 157
Cdd:COG4913  294 EAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGL 373

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650  158 ANQTLKDEYDALQITFTALEEKLRKTTEENQELVTRWMAEKaqeanrlnaeneKDSRRRQARLQKELA--EAAKEPLPVE 235
Cdd:COG4913  374 PLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAAL------------RDLRRELRELEAEIAslERRKSNIPAR 441

                        170
                 ....*....|....*...
gi 27777650  236 QDDDIEVIVDETSDHTEE 253
Cdd:COG4913  442 LLALRDALAEALGLDEAE 459
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 81-274 4.66e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 4.66e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650  81 QLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQQKDKEIQMNEAKISEYLQTISDLETNCLDLRTKLQDLEVANQ 160
Cdd:COG1196 317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650 161 TLKDEYDALQITFTALEEKLRKTTEENQELVTrwmAEKAQEANRLNAENEKDSRRRQARLQKELAEAAKEPL--PVEQDD 238
Cdd:COG1196 397 ELAAQLEELEEAEEALLERLERLEEELEELEE---ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLaeLLEEAA 473

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 27777650 239 DIEVIVDETSDHTEETSPVRAVSRAATKRLSQPAGG 274
Cdd:COG1196 474 LLEAALAELLEELAEAAARLLLLLEAEADYEGFLEG 509
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 83-252 6.28e-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: 46.17  E-value: 6.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650    83 QEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQQKD-----KEIQMNEAKISEYLQTISDLETNCLDLRTKLQDLEV 157
Cdd:TIGR04523 517 KKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKkenleKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEK 596

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650   158 ANQTLKDEYDALQITFTALEEKLRKTTEENQELvtrwmaekaqEANRLNAENEKDSRRRQARLQKELAEAAKEPLP--VE 235
Cdd:TIGR04523 597 EKKDLIKEIEEKEKKISSLEKELEKAKKENEKL----------SSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPeiIK 666

                         170
                  ....*....|....*..
gi 27777650   236 QDDDIEVIVDETSDHTE 252
Cdd:TIGR04523 667 KIKESKTKIDDIIELMK 683
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 101-270 1.07e-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: 44.75  E-value: 1.07e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650 101 KKRGELAQLVIDLNNQMQQKDKEIQMNEAKISEYLQTISDLETNCLDLRTKLQDLEVANQTLKDEYDALQITFTALEEKL 180
Cdd:COG4942  20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650 181 RKTTEENQELVTRW--MAEKAQEANRLNAENEKDSRRRQARLQ------KELAEAAKeplpvEQDDDIEVIVDETSDHTE 252
Cdd:COG4942 100 EAQKEELAELLRALyrLGRQPPLALLLSPEDFLDAVRRLQYLKylaparREQAEELR-----ADLAELAALRAELEAERA 174

                       170
                ....*....|....*...
gi 27777650 253 ETSPVRAVSRAATKRLSQ 270
Cdd:COG4942 175 ELEALLAELEEERAALEA 192
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 83-221 1.14e-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: 45.17  E-value: 1.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650     83 QEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQQKDKEIQMNEAKISE-------YLQTISDLETNCLDLRTKLQD- 154
Cdd:pfam01576  204 QELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEetaqknnALKKIRELEAQISELQEDLESe 283

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27777650    155 ------LEVANQTLKDEYDALQitfTALEEKLrKTTEENQELVTRwmaeKAQEANRLNAENEKDSRRRQARLQ 221
Cdd:pfam01576  284 raarnkAEKQRRDLGEELEALK---TELEDTL-DTTAAQQELRSK----REQEVTELKKALEEETRSHEAQLQ 348
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 82-238 1.26e-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: 45.06  E-value: 1.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650     82 LQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQQKDKEIQMNEAKISEYLQTISDLETncldlrtKLQDLEVANQT 161
Cdd:TIGR02169  683 LEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEE-------DLSSLEQEIEN 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650    162 LKDEYDALQITFTALEEKLRKTTEENQELVTRWMAEKAQEANRLNAENEKDSRRRQARLQ------------KELAEAAK 229
Cdd:TIGR02169  756 VKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLReieqklnrltleKEYLEKEI 835


                   ....*....
gi 27777650    230 EPLPVEQDD 238
Cdd:TIGR02169  836 QELQEQRID 844
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 79-249 1.27e-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: 45.06  E-value: 1.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650     79 DSQLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQQKDKEIQMN-EAKISEYLQTISDLETNCLDLRTKLQDLEV 157
Cdd:TIGR02169  243 ERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRvKEKIGELEAEIASLERSIAEKERELEDAEE 322

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650    158 ANQTLKDEYDALQITFTALEEKLR-------KTTEENQELVTRwMAEKAQEANRLNAENeKDSRRRQARLQKELAEAAKE 230
Cdd:TIGR02169  323 RLAKLEAEIDKLLAEIEELEREIEeerkrrdKLTEEYAELKEE-LEDLRAELEEVDKEF-AETRDELKDYREKLEKLKRE 400

                          170       180
                   ....*....|....*....|.
gi 27777650    231 --PLPVEQDDDIEVIVDETSD 249
Cdd:TIGR02169  401 inELKRELDRLQEELQRLSEE 421
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 83-230 1.48e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.93  E-value: 1.48e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650  83 QEMAQLRIKH-QEELTELHKKRGELAQLVIDLNNQMQQKDKEIQMNEAKISEYLQTISDLETNCLDLRTKLQDLEVANQT 161
Cdd:COG1196 227 AELLLLKLRElEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIAR 306

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27777650 162 LKDEYDALQITFTALEEKLRKTTEENQELVTR---WMAEKAQEANRLNAENEKDSRRRQARLQKELAEAAKE 230
Cdd:COG1196 307 LEERRRELEERLEELEEELAELEEELEELEEEleeLEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 81-237 1.65e-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: 1.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650     81 QLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQQKDKEIQMNEAKISEYLQTISDLETNCLDLRTKLQ----DLE 156
Cdd:TIGR02168  324 QLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAslnnEIE 403

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650    157 VANQTLKDEYDALQITFTALEEKLRKTTEENQELVTRWMAEKAQEANRLNAENEkDSRRRQARLQKELAEAAKEPLPVEQ 236
Cdd:TIGR02168  404 RLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELE-RLEEALEELREELEEAEQALDAAER 482


                   .
gi 27777650    237 D 237
Cdd:TIGR02168  483 E 483
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
46-230 2.40e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 44.26  E-value: 2.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650   46 SDLHSVLTQKLQAEKHDMPNRHEispghdgawndsqlQEMAQLR--IKHQEELTELHKKRGELAQLVIDLNNQMQQkdkE 123
Cdd:PRK02224 190 DQLKAQIEEKEEKDLHERLNGLE--------------SELAELDeeIERYEEQREQARETRDEADEVLEEHEERRE---E 252

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650  124 IQMNEAKISEYLQTISDLETNCLDLRTKLQDLEVANQTLKDEYDAL--QITFTALE----EKLRKTTEENQELVTRWMAE 197
Cdd:PRK02224 253 LETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLlaEAGLDDADaeavEARREELEDRDEELRDRLEE 332

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 27777650  198 KAQEANRLN------AENEKDSRRRQARLQKELAEAAKE 230
Cdd:PRK02224 333 CRVAAQAHNeeaeslREDADDLEERAEELREEAAELESE 371
46 PHA02562
endonuclease subunit; Provisional
 80-244 5.98e-04

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 42.69  E-value: 5.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650   80 SQLQEMAQLRIKHQEELTELHKKrgeLAQLVIDLNNQMQQKDKEIQMNE---------AKISEYLQTISDLETNCLDLRT 150
Cdd:PHA02562 237 EELTDELLNLVMDIEDPSAALNK---LNTAAAKIKSKIEQFQKVIKMYEkggvcptctQQISEGPDRITKIKDKLKELQH 313

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650  151 KLQDLEVANQTLK---DEYDALQITFTALEEKLRKtteENQELVT-RWMAEKAQEA-NRLNAENeKDSRRRQARLQKELA 225
Cdd:PHA02562 314 SLEKLDTAIDELEeimDEFNEQSKKLLELKNKIST---NKQSLITlVDKAKKVKAAiEELQAEF-VDNAEELAKLQDELD 389

                        170
                 ....*....|....*....
gi 27777650  226 EAAKEPLPVEQDDDIEVIV 244
Cdd:PHA02562 390 KIVKTKSELVKEKYHRGIV 408
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 80-230 6.42e-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: 42.75  E-value: 6.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650     80 SQLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQQKDKEIQMNEAKISEYLQTISDLETNclDLRTKLQDLEVAN 159
Cdd:TIGR02169  723 KEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEAR--LSHSRIPEIQAEL 800

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27777650    160 QTLKDEYDALQITFTALEEKLRKTTEENQELvtRWMAEKAQEANRLNAENEKDSRRRQARLQKELAEAAKE 230
Cdd:TIGR02169  801 SKLEEEVSRIEARLREIEQKLNRLTLEKEYL--EKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE 869
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 79-193 9.83e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 42.36  E-value: 9.83e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650     79 DSQLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQQKDKEIQMNEAKISEYLQ-------------TISDLETNC 145
Cdd:TIGR02169  881 ESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDpkgedeeipeeelSLEDVQAEL 960

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 27777650    146 LDLRTKLQDLEVANQTLKDEYDALQITFTALEEKLRKTTEENQELVTR 193
Cdd:TIGR02169  961 QRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILER 1008
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
80-249 1.14e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.43  E-value: 1.14e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650  80 SQLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQQKDKEIQMNEAKISEYLQTISDLETNCLDLRTKLQDLEVAN 159
Cdd:COG4372  87 EQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEEL 166

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650 160 QTLKDEYDALQITFTALEEKLRKTTEENQELVTRWMAEKAQEANRLNAENEKDSRRRQARLQKELAEAAKEPLPVEQDDD 239
Cdd:COG4372 167 AALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEE 246

                       170
                ....*....|
gi 27777650 240 IEVIVDETSD 249
Cdd:COG4372 247 DKEELLEEVI 256
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
80-208 1.32e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 41.05  E-value: 1.32e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650  80 SQLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQQKDKEIQMNEAK---ISEYLQTISDLE----TNCLD----- 147
Cdd:COG1340  57 EEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAggsIDKLRKEIERLEwrqqTEVLSpeeek 136

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27777650 148 --------LRTKLQDLEVAN------QTLKDEYDALQITFTALEEKLRKTTEENQELVTRwMAEKAQEANRLNAE 208
Cdd:COG1340 137 elvekikeLEKELEKAKKALekneklKELRAELKELRKEAEEIHKKIKELAEEAQELHEE-MIELYKEADELRKE 210
TolB COG0823
Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, ...
 514-604 1.56e-03

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: 39.66  E-value: 1.56e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650 514 VIDLRTNAVKQ-TFSapgfkcGSDWTRVVFSPDGSYVAAGSAEGS---LYVWSVLTGKVEKVLSKQHSSSinavaWAPSG 589
Cdd:COG0823  59 VVDADGGEPRRlTFG------GGYNASPSWSPDGKRLAFVSRSDGrfdIYVLDLDGGAPRRLTDGPGSPS-----WSPDG 127

                        90
                ....*....|....*.
gi 27777650 590 LHVV-SVDKGSRAVLW 604
Cdd:COG0823 128 RRIVfSSDRGGRPDLY 143
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 79-229 1.66e-03

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: 41.26  E-value: 1.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650    79 DSQLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQQKDKEIQ-------MNEAKISEYLQTISDLETNCLDLRT- 150
Cdd:pfam05557  89 NKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEelqerldLLKAKASEAEQLRQNLEKQQSSLAEa 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650   151 --KLQDLEVANQtlKDEYDAL--------QITFTALEEKLRKTTEENQELvtrwmaEKAQEANRLNAENEKDSRRRQARL 220
Cdd:pfam05557 169 eqRIKELEFEIQ--SQEQDSEivknskseLARIPELEKELERLREHNKHL------NENIENKLLLKEEVEDLKRKLERE 240


                  ....*....
gi 27777650   221 QKELAEAAK 229
Cdd:pfam05557 241 EKYREEAAT 249
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 315-350 1.76e-03

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: 40.78  E-value: 1.76e-03
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 27777650 315 SYVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWE 350
Cdd:cd00200 254 VQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
COG4946 COG4946
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown] ...
 541-607 2.14e-03

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


Pssm-ID: 443973 [Multi-domain]  Cd Length: 1072  Bit Score: 41.18  E-value: 2.14e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27777650  541 VFSPDGSYVAAGSAEGSLYVWSVLTGKVEKVLSKQHSSSINAVAWAPsglhvvsvDkgSRAVLWAQP 607
Cdd:COG4946  395 VWSPDGKKIAFTDNRGRLWVVDLASGKVRKVDTDGYGDGISDLAWSP--------D--SKWLAYSKP 451
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 79-230 2.15e-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: 41.16  E-value: 2.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650    79 DSQLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQQKDKEIQMNEAKISEYLQTISDLETNCLDLRTKLQDLEVA 158
Cdd:TIGR04523 411 DEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKE 490

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27777650   159 NQTLKDEYDALQITFTALEEKLRKTTEENQELVTRW------MAEKAQEANRLNAE-NEKDSRRRQARLQKELAEAAKE 230
Cdd:TIGR04523 491 LKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIekleseKKEKESKISDLEDElNKDDFELKKENLEKEIDEKNKE 569
TolB COG0823
Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, ...
 514-593 2.31e-03

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: 38.88  E-value: 2.31e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650 514 VIDLRTNAVKQTFSAPGFKCGSDWtrvvfSPDGSYVAAGSAEGS---LYVWSVLTGKVEKVLSKQHSSSinAVAWAPSGL 590
Cdd:COG0823  15 VVDLDGGEPRRLTNSPGIDTSPAW-----SPDGRRIAFTSDRGGgpqIYVVDADGGEPRRLTFGGGYNA--SPSWSPDGK 87


                ...
gi 27777650 591 HVV 593
Cdd:COG0823  88 RLA 90
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 94-226 2.39e-03

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 40.86  E-value: 2.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650    94 EELTELHKKRGELAQLVIDLNNQMQQ-----KDKEIQMNEAKISEYLQTISDLEtncldlrtKLQDLEVANQ----TLKD 164
Cdd:pfam05483 169 EKTKKYEYEREETRQVYMDLNNNIEKmilafEELRVQAENARLEMHFKLKEDHE--------KIQHLEEEYKkeinDKEK 240

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27777650   165 EYDALQITFTALEEKLRKTTEENQElvTRWMAEKAQEANRLNAENEKDSRRRQARLQKELAE 226
Cdd:pfam05483 241 QVSLLLIQITEKENKMKDLTFLLEE--SRDKANQLEEKTKLQDENLKELIEKKDHLTKELED 300
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
82-238 2.56e-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: 2.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650   82 LQEMAQLRiKHQEELTELHKKRGELAQLViDLNNQMQQKDKEIQMNEakiseYLQTISDLETNcldlRTKLQDLEVANQT 161
Cdd:COG4913  231 VEHFDDLE-RAHEALEDAREQIELLEPIR-ELAERYAAARERLAELE-----YLRAALRLWFA----QRRLELLEAELEE 299

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650  162 LKDEYDALQITFTALEEKLRKTTEENQELVTRWMAEKAQEANRL-----NAENEKDSRRRQARLQKELAEAAKEPLPVEQ 236
Cdd:COG4913  300 LRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLereieRLERELEERERRRARLEALLAALGLPLPASA 379


                 ..
gi 27777650  237 DD 238
Cdd:COG4913  380 EE 381
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
93-243 2.90e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.27  E-value: 2.90e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650  93 QEELTELHKKRGELAQLvidlNNQMQQKDKEIQMNEAKISEYLQTISDLETNCLDLRTKLQDLEVANQTLKDEYDALQIT 172
Cdd:COG4372  34 RKALFELDKLQEELEQL----REELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEE 109

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27777650 173 FTALEEKLRKTTEENQELVTRWMAEKAQEANRLNAENEKDSR-----RRQARLQKELAEAAKEPLPVEQDDDIEVI 243
Cdd:COG4372 110 AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEElkeleEQLESLQEELAALEQELQALSEAEAEQAL 185
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 76-333 3.04e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.20  E-value: 3.04e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650  76 AWNDSQLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQQKDKEIQMNEAKISEYLQTISDLETNCLDLRTKLQD- 154
Cdd:COG3883  12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEr 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650 155 -------------LEV----------------------ANQTLKDEYDALQITFTALEEKLRKTTEENQELVTRwMAEKA 199
Cdd:COG3883  92 aralyrsggsvsyLDVllgsesfsdfldrlsalskiadADADLLEELKADKAELEAKKAELEAKLAELEALKAE-LEAAK 170

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650 200 QEANRLNAENEKDSRRRQARLQKELAEAAKEPLPVEQDDDIEVIVDETSDHTEETSPVRAVSRAATKRLSQPAGGLLDSI 279
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAG 250

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 27777650 280 TNIFGRRSVSSIPVPQDIMDTHPASGKDVRVPTTASYVFDAHDGEVNAVQFSPG 333
Cdd:COG3883 251 AAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSG 304
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 147-243 3.20e-03

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 40.45  E-value: 3.20e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650 147 DLRTKLQDLEVANQTLKDEYD-ALQITFTALEEKLRKTTEENQELVTRWMAEKA--QEANRLNAENEKDSRRRQArLQKE 223
Cdd:COG0542 415 ELERRLEQLEIEKEALKKEQDeASFERLAELRDELAELEEELEALKARWEAEKEliEEIQELKEELEQRYGKIPE-LEKE 493

                        90       100
                ....*....|....*....|....*...
gi 27777650 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 ...
 43-215 3.48e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.44  E-value: 3.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650     43 LEKSDLHSVLtQKLQAEKHDMPNRHeispghdgAWNDSQLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQQKDK 122
Cdd:TIGR02169  784 LEARLSHSRI-PEIQAELSKLEEEV--------SRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEK 854

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650    123 EIQMNEAKISEYLQTISDLETNCLDLRTKLQDLEVANQTLKDEYDALQITFTALEEKLRKTTEENQELvtrwmAEKAQEA 202
Cdd:TIGR02169  855 EIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSEL-----KAKLEAL 929

                          170
                   ....*....|...
gi 27777650    203 NRLNAENEKDSRR 215
Cdd:TIGR02169  930 EEELSEIEDPKGE 942
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 93-230 3.53e-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: 40.39  E-value: 3.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650    93 QEELTELHKKRGELAQLVIDLNNQMQQKDKEIQMNEAKISEYLQTISDLETNCLDLRT-KLQDLevaNQTLKDEYDALQI 171
Cdd:TIGR04523 245 TTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNqKEQDW---NKELKSELKNQEK 321

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 27777650   172 TFTALEEKLRKTTEENQELvTRWMAEKAQEANRLNAENEKdsrrrqarLQKELAEAAKE 230
Cdd:TIGR04523 322 KLEEIQNQISQNNKIISQL-NEQISQLKKELTNSESENSE--------KQRELEEKQNE 371
PRK12704 PRK12704
phosphodiesterase; Provisional
 90-230 4.52e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 39.76  E-value: 4.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650   90 IKHQEELT---ELHKKRGELAQLVIDLNNQMQQKDKEIQMNEAKISEYLQTISDLEtncldlrTKLQDLEVANQTLKDEY 166
Cdd:PRK12704  54 IKKEALLEakeEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKRE-------EELEKKEKELEQKQQEL 126

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27777650  167 DALQitftalEEKLRKTTEENQELvTRWMAEKAQEA-NRLNAENEKDSRRRQARLQKELAEAAKE 230
Cdd:PRK12704 127 EKKE------EELEELIEEQLQEL-ERISGLTAEEAkEILLEKVEEEARHEAAVLIKEIEEEAKE 184
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
120-230 5.94e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 39.46  E-value: 5.94e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650 120 KDKEIQMNEAKISEYLQTISDLETNCLDLRTKLQDLEVANQTLKDEYDALQITFTALEEKLRKT-TEENQELvtrwmaEK 198
Cdd:COG2433 390 LPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEArSEERREI------RK 463

                        90       100       110
                ....*....|....*....|....*....|..
gi 27777650 199 AQEANRLNAENEkdsrrrqaRLQKELAEAAKE 230
Cdd:COG2433 464 DREISRLDREIE--------RLERELEEERER 487
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 565-604 6.22e-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: 6.22e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 27777650    565 TGKVEKVLsKQHSSSINAVAWAPSGLHVVSVDKGSRAVLW 604
Cdd:smart00320   1 SGELLKTL-KGHTGPVTSVAFSPDGKYLASGSDDGTIKLW 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 538-562 6.60e-03

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 34.60  E-value: 6.60e-03
                           10        20
                   ....*....|....*....|....*
gi 27777650    538 TRVVFSPDGSYVAAGSAEGSLYVWS 562
Cdd:smart00320  16 TSVAFSPDGKYLASGSDDGTIKLWD 40
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
31-188 6.64e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.37  E-value: 6.64e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650  31 AFEEIILQYTKLLEKSDLHSVLTQKLQAEKhdmPNRHEISPGHDGAWNDSQLQEMAQLRIKHQEELTELHKKRGELaqlv 110
Cdd:COG4717 386 ELRAALEQAEEYQELKEELEELEEQLEELL---GELEELLEALDEEELEEELEELEEELEELEEELEELREELAEL---- 458

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27777650 111 idlnnqmqqkdkEIQMNEAKISEYLQtisdletnclDLRTKLQDLEVANQTLKDEYDALQITFTALEEKLRKTTEENQ 188
Cdd:COG4717 459 ------------EAELEQLEEDGELA----------ELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERL 514
Ge1_WD40 pfam16529
WD40 region of Ge1, enhancer of mRNA-decapping protein; Ge1_WD40 is the N-terminal region of ...
 365-446 7.15e-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: 38.98  E-value: 7.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27777650   365 SNAGITSIEFDSAGAYLLAASNDFASRIWTV-----DDYRLRHTLTGHSGKVLSAKFLLDNAR----------IVSGS-H 428
Cdd:pfam16529 185 EHSLLVDAAFSPDGTALATASLDGEVKFFQIylfdnRNPRCLHEWKPHDGKPLSSLFFLDNHKkppevqfwrfAITGAdN 264

                          90
                  ....*....|....*...
gi 27777650   429 DRTLKLWDLRSKVCIKTV 446
Cdd:pfam16529 265 NSELKLWSCESWTCLQTI 282
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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