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Conserved domains on  [gi|158711749|ref|NP_001102279|]
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autophagy-related protein 16-1 [Rattus norvegicus]

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 4.55e-59

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 202.83  E-value: 4.55e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 257 VRAISRAATKRLSQPAGGLLDSITNIFGRRSVSSIPVPQDVVDTHPASGKDVRVPTTAS----YVFDAHDGEVNAVQFSP 332
Cdd:COG2319   51 LAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATglllRTLTGHTGAVRSVAFSP 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 333 GSRLLATGGMDRRVKLWEAFGDKCEfkGSLSGSNAGITSIEFDSAGAYLLAASNDFASRIWTVDDYRLRHTLTGHSGKVL 412
Cdd:COG2319  131 DGKTLASGSADGTVRLWDLATGKLL--RTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVR 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 413 SAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTV-FAGSSCNDIVCT--EQCVMSGHFDKKIRFWDIRSESVVREME-LL 488
Cdd:COG2319  209 SVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLtGHSGSVRSVAFSpdGRLLASGSADGTVRLWDLATGELLRTLTgHS 288
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 489 GKITALDLNPERTELLSCSRDDLLKIIDLRTNAIKQSFSAPgfkcGSDWTRVVFSPDGSYVAAGSADGSLYVWSVLTGKV 568
Cdd:COG2319  289 GGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGH----TGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGEL 364
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 158711749 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 1.31e-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: 185.91  E-value: 1.31e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749   31 AFEEIILQYTKLLEKSDLHSVLTQKLQAEKHDVPNRHEISPGHDGAWNDSQLQEMAQLKMKHQEELTELHKKRGELAQLV 110
Cdd:pfam08614   1 AFLELIDAYNRLLDRTALLEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQLREELAELYRSRGELAQRL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749  111 IDLNNQMQQKDKEIQTNEAKIAECLQTISDLEADCLDLRTKLQDLEVANQTLKDEYDALQITFTALEEKLRKTTEENQEL 190
Cdd:pfam08614  81 VDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQDELVALQLQLNMAEEKLRKLEKENREL 160
                         170
                  ....*....|....*.
gi 158711749  191 VTRWMAEKAQEANRLN 206
Cdd:pfam08614 161 VERWMKRKGQEAEAMN 176
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
257-604 4.55e-59

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 202.83  E-value: 4.55e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 257 VRAISRAATKRLSQPAGGLLDSITNIFGRRSVSSIPVPQDVVDTHPASGKDVRVPTTAS----YVFDAHDGEVNAVQFSP 332
Cdd:COG2319   51 LAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATglllRTLTGHTGAVRSVAFSP 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 333 GSRLLATGGMDRRVKLWEAFGDKCEfkGSLSGSNAGITSIEFDSAGAYLLAASNDFASRIWTVDDYRLRHTLTGHSGKVL 412
Cdd:COG2319  131 DGKTLASGSADGTVRLWDLATGKLL--RTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVR 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 413 SAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTV-FAGSSCNDIVCT--EQCVMSGHFDKKIRFWDIRSESVVREME-LL 488
Cdd:COG2319  209 SVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLtGHSGSVRSVAFSpdGRLLASGSADGTVRLWDLATGELLRTLTgHS 288
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 489 GKITALDLNPERTELLSCSRDDLLKIIDLRTNAIKQSFSAPgfkcGSDWTRVVFSPDGSYVAAGSADGSLYVWSVLTGKV 568
Cdd:COG2319  289 GGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGH----TGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGEL 364
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 158711749 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 3.59e-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: 194.09  E-value: 3.59e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 317 VFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWEAFGDKCEFkgSLSGSNAGITSIEFDSAGAYLLAASNDFASRIWTVD 396
Cdd:cd00200    4 TLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLR--TLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 397 DYRLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTvFAG----------SSCNDIVCteqcvmSGH 466
Cdd:cd00200   82 TGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTT-LRGhtdwvnsvafSPDGTFVA------SSS 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 467 FDKKIRFWDIRSESVVREMEL-LGKITALDLNPERTELLSCSRDDLLKIIDLRTNAIKQSFSAPgfkcgSDW-TRVVFSP 544
Cdd:cd00200  155 QDGTIKLWDLRTGKCVATLTGhTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGH-----ENGvNSVAFSP 229
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158711749 545 DGSYVAAGSADGSLYVWSVLTGKVEKVLSkQHSSSINAVAWAPSGLHVVSVDKGSRAVLWA 605
Cdd:cd00200  230 DGYLLASGSEDGTIRVWDLRTGECVQTLS-GHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
31-206 1.31e-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: 185.91  E-value: 1.31e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749   31 AFEEIILQYTKLLEKSDLHSVLTQKLQAEKHDVPNRHEISPGHDGAWNDSQLQEMAQLKMKHQEELTELHKKRGELAQLV 110
Cdd:pfam08614   1 AFLELIDAYNRLLDRTALLEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQLREELAELYRSRGELAQRL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749  111 IDLNNQMQQKDKEIQTNEAKIAECLQTISDLEADCLDLRTKLQDLEVANQTLKDEYDALQITFTALEEKLRKTTEENQEL 190
Cdd:pfam08614  81 VDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQDELVALQLQLNMAEEKLRKLEKENREL 160
                         170
                  ....*....|....*.
gi 158711749  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 2.46e-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: 114.20  E-value: 2.46e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 119 QKDKEIQTNEAKIAECLQTISDLEADCLDLRTKLQDLEVANQTLKDEYDALQITFTALEEKLRKTTEENQELVTRWMAEK 198
Cdd:cd22887    1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEENDELVERWMAKK 80
                         90
                 ....*....|.
gi 158711749 199 AQEANRLNAEN 209
Cdd:cd22887   81 QQEADKMNEAN 91
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
83-264 1.70e-09

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 59.92  E-value: 1.70e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749  83 QEMAQLKMKHQEELTELHKKRGELAQLvidlNNQMQQKDKEIQTNEAKIAECLQTISDLEADCLDLRTKLQDLEVANQTL 162
Cdd:COG4372   52 EELEQAREELEQLEEELEQARSELEQL----EEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDL 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 163 KDEYDALQITFTALEEKLRKTTEENQELVTRwMAEKAQEANRLNAENEKDSRRR-QARLQKELAEAAKEPLPVEQDDDIE 241
Cdd:COG4372  128 EQQRKQLEAQIAELQSEIAEREEELKELEEQ-LESLQEELAALEQELQALSEAEaEQALDELLKEANRNAEKEEELAEAE 206
                        170       180
                 ....*....|....*....|...
gi 158711749 242 VIVDETSDHTEETSPVRAISRAA 264
Cdd:COG4372  207 KLIESLPRELAEELLEAKDSLEA 229
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
316-350 8.76e-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: 48.46  E-value: 8.76e-08
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 158711749   316 YVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWE 350
Cdd:smart00320   6 KTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
316-350 2.32e-07

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 47.34  E-value: 2.32e-07
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 158711749  316 YVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWE 350
Cdd:pfam00400   5 KTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
114-266 8.50e-07

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: 52.37  E-value: 8.50e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749   114 NNQMQQKDKEIQTNEAKIAECLQTISDLEADCLDLRTKLQDLEVANQTLKDEYDALQITFTALEEKLRKTTEEnQELVTR 193
Cdd:TIGR02168  669 NSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE-VEQLEE 747
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158711749   194 WMAEKAQEANRLNAE-NEKDSRRRQARLQKELAEAAKEPLPVEQDDDIEVIVDETSDHTEETSPVRAISRAATK 266
Cdd:TIGR02168  748 RIAQLSKELTELEAEiEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAAN 821
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
325-561 3.19e-06

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 50.47  E-value: 3.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 325 VNAVQFSPGSRLLATGGMDRRVKLWEAF-----GDKCEFKGSLSGSNAGITSIEFDSAGAYLLAASN-DFASRIWTVDDY 398
Cdd:PLN00181 486 VCAIGFDRDGEFFATAGVNKKIKIFECEsiikdGRDIHYPVVELASRSKLSGICWNSYIKSQVASSNfEGVVQVWDVARS 565
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 399 RLRHTLTGHSGKVLSAKFL-LDNARIVSGSHDRTLKLWDLRSKVCIKTVfagSSCNDIVCTE------QCVMSGHFDKKI 471
Cdd:PLN00181 566 QLVTEMKEHEKRVWSIDYSsADPTLLASGSDDGSVKLWSINQGVSIGTI---KTKANICCVQfpsesgRSLAFGSADHKV 642
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 472 RFWDIRSE-----SVVREMELLGKITALDlnpeRTELLSCSRDDLLKIIDLRTNA--IKQS--FSAPGFKCGSDWTRVVF 542
Cdd:PLN00181 643 YYYDLRNPklplcTMIGHSKTVSYVRFVD----SSTLVSSSTDNTLKLWDLSMSIsgINETplHSFMGHTNVKNFVGLSV 718
                        250
                 ....*....|....*....
gi 158711749 543 SpDGsYVAAGSADGSLYVW 561
Cdd:PLN00181 719 S-DG-YIATGSETNEVFVY 735
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
46-230 1.75e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 44.65  E-value: 1.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749  46 SDLHSVLTQKLQAEKHDVPNRHEispghdgawndsqlQEMAQLK--MKHQEELTELHKKRGELAQLVIDLNNQMQQkdkE 123
Cdd:PRK02224 190 DQLKAQIEEKEEKDLHERLNGLE--------------SELAELDeeIERYEEQREQARETRDEADEVLEEHEERRE---E 252
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 124 IQTNEAKIAECLQTISDLEADCLDLRTKLQDLEVANQTLKDEYDAL--QITFTALE----EKLRKTTEENQELVTRWMAE 197
Cdd:PRK02224 253 LETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLlaEAGLDDADaeavEARREELEDRDEELRDRLEE 332
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 158711749 198 KAQEANRLN------AENEKDSRRRQARLQKELAEAAKE 230
Cdd:PRK02224 333 CRVAAQAHNeeaeslREDADDLEERAEELREEAAELESE 371
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
39-170 5.17e-04

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 42.31  E-value: 5.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749    39 YTKLLEKSDLHSVLTQKLQAEKHDVPNRHEISPGHDGAWNDSQLQEMAQLKMKHQEELTELHKKRGELAQLvidlNNQMQ 118
Cdd:smart00787 160 YKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRAKEKLKKLLQEIMIKVKKLEEL----EEELQ 235
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 158711749   119 QKDKEIQTNEAKIAECLQTISDLEADCLDLRtKLQDLEVAnqTLKDEYDALQ 170
Cdd:smart00787 236 ELESKIEDLTNKKSELNTEIAEAEKKLEQCR-GFTFKEIE--KLKEQLKLLQ 284
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
257-604 4.55e-59

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 202.83  E-value: 4.55e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 257 VRAISRAATKRLSQPAGGLLDSITNIFGRRSVSSIPVPQDVVDTHPASGKDVRVPTTAS----YVFDAHDGEVNAVQFSP 332
Cdd:COG2319   51 LAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATglllRTLTGHTGAVRSVAFSP 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 333 GSRLLATGGMDRRVKLWEAFGDKCEfkGSLSGSNAGITSIEFDSAGAYLLAASNDFASRIWTVDDYRLRHTLTGHSGKVL 412
Cdd:COG2319  131 DGKTLASGSADGTVRLWDLATGKLL--RTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVR 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 413 SAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTV-FAGSSCNDIVCT--EQCVMSGHFDKKIRFWDIRSESVVREME-LL 488
Cdd:COG2319  209 SVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLtGHSGSVRSVAFSpdGRLLASGSADGTVRLWDLATGELLRTLTgHS 288
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 489 GKITALDLNPERTELLSCSRDDLLKIIDLRTNAIKQSFSAPgfkcGSDWTRVVFSPDGSYVAAGSADGSLYVWSVLTGKV 568
Cdd:COG2319  289 GGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGH----TGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGEL 364
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 158711749 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 3.59e-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: 194.09  E-value: 3.59e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 317 VFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWEAFGDKCEFkgSLSGSNAGITSIEFDSAGAYLLAASNDFASRIWTVD 396
Cdd:cd00200    4 TLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLR--TLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 397 DYRLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTvFAG----------SSCNDIVCteqcvmSGH 466
Cdd:cd00200   82 TGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTT-LRGhtdwvnsvafSPDGTFVA------SSS 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 467 FDKKIRFWDIRSESVVREMEL-LGKITALDLNPERTELLSCSRDDLLKIIDLRTNAIKQSFSAPgfkcgSDW-TRVVFSP 544
Cdd:cd00200  155 QDGTIKLWDLRTGKCVATLTGhTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGH-----ENGvNSVAFSP 229
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158711749 545 DGSYVAAGSADGSLYVWSVLTGKVEKVLSkQHSSSINAVAWAPSGLHVVSVDKGSRAVLWA 605
Cdd:cd00200  230 DGYLLASGSEDGTIRVWDLRTGECVQTLS-GHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
31-206 1.31e-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: 185.91  E-value: 1.31e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749   31 AFEEIILQYTKLLEKSDLHSVLTQKLQAEKHDVPNRHEISPGHDGAWNDSQLQEMAQLKMKHQEELTELHKKRGELAQLV 110
Cdd:pfam08614   1 AFLELIDAYNRLLDRTALLEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQLREELAELYRSRGELAQRL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749  111 IDLNNQMQQKDKEIQTNEAKIAECLQTISDLEADCLDLRTKLQDLEVANQTLKDEYDALQITFTALEEKLRKTTEENQEL 190
Cdd:pfam08614  81 VDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQDELVALQLQLNMAEEKLRKLEKENREL 160
                         170
                  ....*....|....*.
gi 158711749  191 VTRWMAEKAQEANRLN 206
Cdd:pfam08614 161 VERWMKRKGQEAEAMN 176
WD40 COG2319
WD40 repeat [General function prediction only];
255-604 6.49e-54

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 188.97  E-value: 6.49e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 255 SPVRAISRAATKRLSQPAGGLLDSITNIFGRRSVSSIPVPQDVVDTHPASGKDVRV----PTTASYVFDAHDGEVNAVQF 330
Cdd:COG2319    7 AALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLldaaAGALLATLLGHTAAVLSVAF 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 331 SPGSRLLATGGMDRRVKLWEAFGDKCefKGSLSGSNAGITSIEFDSAGAYLLAASNDFASRIWTVDDYRLRHTLTGHSGK 410
Cdd:COG2319   87 SPDGRLLASASADGTVRLWDLATGLL--LRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGA 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 411 VLSAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTVFAGSSC-NDIVCT--EQCVMSGHFDKKIRFWDIRSESVVREMEL 487
Cdd:COG2319  165 VTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAvRSVAFSpdGKLLASGSADGTVRLWDLATGKLLRTLTG 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 488 -LGKITALDLNPERTELLSCSRDDLLKIIDLRTNAIKQSFSAPgfkcgSDW-TRVVFSPDGSYVAAGSADGSLYVWSVLT 565
Cdd:COG2319  245 hSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGH-----SGGvNSVAFSPDGKLLASGSDDGTVRLWDLAT 319
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 158711749 566 GKVEKVLsKQHSSSINAVAWAPSGLHVVSVDKGSRAVLW 604
Cdd:COG2319  320 GKLLRTL-TGHTGAVRSVAFSPDGKTLASGSDDGTVRLW 357
WD40 COG2319
WD40 repeat [General function prediction only];
316-563 6.67e-48

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 172.79  E-value: 6.67e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 316 YVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWEAFGDKCEFkgSLSGSNAGITSIEFDSAGAYLLAASNDFASRIWTV 395
Cdd:COG2319  156 RTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLR--TLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDL 233
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 396 DDYRLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTvFAGSSC--NDIVCT--EQCVMSGHFDKKI 471
Cdd:COG2319  234 ATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRT-LTGHSGgvNSVAFSpdGKLLASGSDDGTV 312
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 472 RFWDIRSESVVREME-LLGKITALDLNPERTELLSCSRDDLLKIIDLRTNAIKQSFSAPgfkcgSDW-TRVVFSPDGSYV 549
Cdd:COG2319  313 RLWDLATGKLLRTLTgHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGH-----TGAvTSVAFSPDGRTL 387
                        250
                 ....*....|....
gi 158711749 550 AAGSADGSLYVWSV 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 2.00e-38

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: 143.24  E-value: 2.00e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 316 YVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWEAFGDKCEFkgSLSGSNAGITSIEFDSAGAYLLAASNDFASRIWTV 395
Cdd:cd00200   87 RTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLT--TLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDL 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 396 DDYRLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTvfagsscndivcteqcvMSGHfdkkirfwd 475
Cdd:cd00200  165 RTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGT-----------------LRGH--------- 218
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 476 irsesvvremelLGKITALDLNPERTELLSCSRDDLLKIIDLRTNAIKQSFSAPGFKCGSdwtrVVFSPDGSYVAAGSAD 555
Cdd:cd00200  219 ------------ENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTS----LAWSPDGKRLASGSAD 282

                 ....*..
gi 158711749 556 GSLYVWS 562
Cdd:cd00200  283 GTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
317-519 1.33e-36

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 141.20  E-value: 1.33e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 317 VFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWEAFGDKCEFkgSLSGSNAGITSIEFDSAGAYLLAASNDFASRIWTVD 396
Cdd:COG2319  199 TLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLR--TLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLA 276
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 397 DYRLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTvFAG--SSCNDIVCT--EQCVMSGHFDKKIR 472
Cdd:COG2319  277 TGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRT-LTGhtGAVRSVAFSpdGKTLASGSDDGTVR 355
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 158711749 473 FWDIRSESVVREME-LLGKITALDLNPERTELLSCSRDDLLKIIDLRT 519
Cdd:COG2319  356 LWDLATGELLRTLTgHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
400-594 8.20e-35

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 133.23  E-value: 8.20e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 400 LRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTV----FAGSSCNDIVCTEQCVmSGHFDKKIRFWD 475
Cdd:cd00200    1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLkghtGPVRDVAASADGTYLA-SGSSDKTIRLWD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 476 IRSESVVREMEL-LGKITALDLNPERTELLSCSRDDLLKIIDLRTNAIKQSFSAPgfkcgSDWTR-VVFSPDGSYVAAGS 553
Cdd:cd00200   80 LETGECVRTLTGhTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGH-----TDWVNsVAFSPDGTFVASSS 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 158711749 554 ADGSLYVWSVLTGKVEKVLsKQHSSSINAVAWAPSGLHVVS 594
Cdd:cd00200  155 QDGTIKLWDLRTGKCVATL-TGHTGEVNSVAFSPDGEKLLS 194
WD40 COG2319
WD40 repeat [General function prediction only];
329-604 1.92e-34

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 135.04  E-value: 1.92e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 329 QFSPGSRLLATGGMDRRVKLWEAFGDKCEfkGSLSGSNAGITSIEFDSAGAYLLAASNDFASRIWTVDDYRLRHTLTGHS 408
Cdd:COG2319    1 ALSADGAALAAASADLALALLAAALGALL--LLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHT 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 409 GKVLSAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTVFA-GSSCNDIVCTE--QCVMSGHFDKKIRFWDIRSESVVREM 485
Cdd:COG2319   79 AAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGhTGAVRSVAFSPdgKTLASGSADGTVRLWDLATGKLLRTL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 486 EL-LGKITALDLNPERTELLSCSRDDLLKIIDLRTNAIKQSFSAPgfkcgSDW-TRVVFSPDGSYVAAGSADGSLYVWSV 563
Cdd:COG2319  159 TGhSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGH-----TGAvRSVAFSPDGKLLASGSADGTVRLWDL 233
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 158711749 564 LTGKVEKVLsKQHSSSINAVAWAPSGLHVVSVDKGSRAVLW 604
Cdd:COG2319  234 ATGKLLRTL-TGHSGSVRSVAFSPDGRLLASGSADGTVRLW 273
WD40 COG2319
WD40 repeat [General function prediction only];
316-478 9.49e-32

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 127.33  E-value: 9.49e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 316 YVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWEAFGDKCefKGSLSGSNAGITSIEFDSAGAYLLAASNDFASRIWTV 395
Cdd:COG2319  240 RTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGEL--LRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDL 317
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 396 DDYRLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTvFAGSScnDIVCT------EQCVMSGHFDK 469
Cdd:COG2319  318 ATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRT-LTGHT--GAVTSvafspdGRTLASGSADG 394

                 ....*....
gi 158711749 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 2.46e-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: 114.20  E-value: 2.46e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 119 QKDKEIQTNEAKIAECLQTISDLEADCLDLRTKLQDLEVANQTLKDEYDALQITFTALEEKLRKTTEENQELVTRWMAEK 198
Cdd:cd22887    1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEENDELVERWMAKK 80
                         90
                 ....*....|.
gi 158711749 199 AQEANRLNAEN 209
Cdd:cd22887   81 QQEADKMNEAN 91
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
83-264 1.70e-09

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 59.92  E-value: 1.70e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749  83 QEMAQLKMKHQEELTELHKKRGELAQLvidlNNQMQQKDKEIQTNEAKIAECLQTISDLEADCLDLRTKLQDLEVANQTL 162
Cdd:COG4372   52 EELEQAREELEQLEEELEQARSELEQL----EEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDL 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 163 KDEYDALQITFTALEEKLRKTTEENQELVTRwMAEKAQEANRLNAENEKDSRRR-QARLQKELAEAAKEPLPVEQDDDIE 241
Cdd:COG4372  128 EQQRKQLEAQIAELQSEIAEREEELKELEEQ-LESLQEELAALEQELQALSEAEaEQALDELLKEANRNAEKEEELAEAE 206
                        170       180
                 ....*....|....*....|...
gi 158711749 242 VIVDETSDHTEETSPVRAISRAA 264
Cdd:COG4372  207 KLIESLPRELAEELLEAKDSLEA 229
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
81-253 4.16e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.48  E-value: 4.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749  81 QLQEMAQLKMKHQEELTELHKKRGEL-------AQLVIDLNNQMQQKDKEIQTNEAKIAECLQTISDLEADCLDLRTKLQ 153
Cdd:COG1196  275 ELEELELELEEAQAEEYELLAELARLeqdiarlEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 154 DLEVANQTLKDEYDALQITFTALEEKLRKTTEENQELVTRWMAEKAQEANRlnAENEKDSRRRQARLQKELAEAAKEPLP 233
Cdd:COG1196  355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL--EEAEEALLERLERLEEELEELEEALAE 432
                        170       180
                 ....*....|....*....|
gi 158711749 234 VEQDDDIEVIVDETSDHTEE 253
Cdd:COG1196  433 LEEEEEEEEEALEEAAEEEA 452
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
316-350 8.76e-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: 48.46  E-value: 8.76e-08
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 158711749   316 YVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWE 350
Cdd:smart00320   6 KTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
79-230 8.97e-08

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: 53.39  E-value: 8.97e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749  79 DSQLQEMAQLKMKHQEELTELHKKRGELAQLVIDLNNQMQQKDKEIQTNEAKIAECLQTISDLEAdcldlrtKLQdlEVA 158
Cdd:COG1579   16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE-------QLG--NVR 86
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158711749 159 NQtlkDEYDALQITFTALEEKLRKTTEENQELVTRwmAEKAQ----EANRLNAENEKDSRRRQARLQKELAEAAKE 230
Cdd:COG1579   87 NN---KEYEALQKEIESLKRRISDLEDEILELMER--IEELEeelaELEAELAELEAELEEKKAELDEELAELEAE 157
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
399-436 1.56e-07

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 47.69  E-value: 1.56e-07
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 158711749   399 RLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWD 436
Cdd:smart00320   3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
93-238 1.92e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 54.00  E-value: 1.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749  93 QEELTELHKKRGELAQLVIDlnnQMQQKDKEIQTNEAKIAECLQTISDLEAdcldLRTKLQDLEVANQTLKDEYDAL--Q 170
Cdd:COG4717   52 EKEADELFKPQGRKPELNLK---ELKELEEELKEAEEKEEEYAELQEELEE----LEEELEELEAELEELREELEKLekL 124
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158711749 171 ITFTALEEKLRKTTEENQELVTRWMAEKAQEANRLNAENEKDSRRRQ-ARLQKELAEAAKEPLPVEQDD 238
Cdd:COG4717  125 LQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAElAELQEELEELLEQLSLATEEE 193
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
80-286 1.93e-07

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: 53.61  E-value: 1.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749  80 SQLQEMAQLKMKHQEELTELHKKRGELAQLVIDLNNQMQQKDKEIQTNEAKIAECLQTISDLEA---------------- 143
Cdd:COG4942   41 KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEelaellralyrlgrqp 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 144 ---------DCLDLRTKLQDLEVANQTLKDEYDALQITFTALEEKLRKTTEENQELVTRwMAEKAQEANRLNAEnEKDSR 214
Cdd:COG4942  121 plalllspeDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL-LAELEEERAALEAL-KAERQ 198
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158711749 215 RRQARLQKELAEAAKEPLPVEQDDD-----IEVIVDETSDHTEETSPVRAIsrAATKRLSQPAGGlldSITNIFGRR 286
Cdd:COG4942  199 KLLARLEKELAELAAELAELQQEAEelealIARLEAEAAAAAERTPAAGFA--ALKGKLPWPVSG---RVVRRFGER 270
WD40 pfam00400
WD domain, G-beta repeat;
316-350 2.32e-07

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 47.34  E-value: 2.32e-07
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 158711749  316 YVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWE 350
Cdd:pfam00400   5 KTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 pfam00400
WD domain, G-beta repeat;
399-436 4.35e-07

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 46.57  E-value: 4.35e-07
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 158711749  399 RLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWD 436
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
114-266 8.50e-07

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: 52.37  E-value: 8.50e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749   114 NNQMQQKDKEIQTNEAKIAECLQTISDLEADCLDLRTKLQDLEVANQTLKDEYDALQITFTALEEKLRKTTEEnQELVTR 193
Cdd:TIGR02168  669 NSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE-VEQLEE 747
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158711749   194 WMAEKAQEANRLNAE-NEKDSRRRQARLQKELAEAAKEPLPVEQDDDIEVIVDETSDHTEETSPVRAISRAATK 266
Cdd:TIGR02168  748 RIAQLSKELTELEAEiEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAAN 821
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
358-566 1.09e-06

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


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 50.08  E-value: 1.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 358 FKGSLSGSNAGITSIEFDSAGAYLLAASNDFASRIWTVDDYRLRHTLTGHSGKVLSAKFLLDNARI-VSGSHDRTLKLWD 436
Cdd:COG3391   17 ALAALAVAVAALGLGGGGPLLAAASGGVVGAAVGGGGVALLAGLGLGAAAVADADGADAGADGRRLyVANSGSGRVSVID 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 437 LRSKVCIKTVFAGSSCNDIVCTE---QCVMSGHFDKKIRFWDIRSESVVREMELLGKITALDLNPERTELLSCSRDD--- 510
Cdd:COG3391   97 LATGKVVATIPVGGGPRGLAVDPdggRLYVADSGNGRVSVIDTATGKVVATIPVGAGPHGIAVDPDGKRLYVANSGSntv 176
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158711749 511 --LLKIIDLRTNAIKQSFSApgfkcGSDWTRVVFSPDGS--YVA------AGSADGSLYVWSVLTG 566
Cdd:COG3391  177 svIVSVIDTATGKVVATIPV-----GGGPVGVAVSPDGRrlYVAnrgsntSNGGSNTVSVIDLATL 237
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
86-230 1.57e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.60  E-value: 1.57e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749    86 AQLKMKhQEELTELHKKRGELAQLVID-------LNNQMQQKDKEIQTNEAKIAECLQTISDLEADCLDLRTKLQDLEVA 158
Cdd:TIGR02168  260 AELQEL-EEKLEELRLEVSELEEEIEElqkelyaLANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEE 338
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158711749   159 NQTLKDEYDALQITFTALEEKLRKTTEENQELVTRWmAEKAQEANRLNAEnEKDSRRRQARLQKELAEAAKE 230
Cdd:TIGR02168  339 LAELEEKLEELKEELESLEAELEELEAELEELESRL-EELEEQLETLRSK-VAQLELQIASLNNEIERLEAR 408
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
83-230 2.79e-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: 50.44  E-value: 2.79e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749    83 QEMAQLkmkhQEELTELHKKRGELAQLVIDLNNQMQQKDKEIQTNEAKIAEclqtisdLEADCLDLRTKLQDLEVANQTL 162
Cdd:TIGR02168  747 ERIAQL----SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ-------LKEELKALREALDELRAELTLL 815
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158711749   163 KDEYDALQITFTALEEKLRKTTEENQELVTRWmAEKAQEANRLNAENEkDSRRRQARLQKELAEAAKE 230
Cdd:TIGR02168  816 NEEAANLRERLESLERRIAATERRLEDLEEQI-EELSEDIESLAAEIE-ELEELIEELESELEALLNE 881
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
325-561 3.19e-06

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 50.47  E-value: 3.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 325 VNAVQFSPGSRLLATGGMDRRVKLWEAF-----GDKCEFKGSLSGSNAGITSIEFDSAGAYLLAASN-DFASRIWTVDDY 398
Cdd:PLN00181 486 VCAIGFDRDGEFFATAGVNKKIKIFECEsiikdGRDIHYPVVELASRSKLSGICWNSYIKSQVASSNfEGVVQVWDVARS 565
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 399 RLRHTLTGHSGKVLSAKFL-LDNARIVSGSHDRTLKLWDLRSKVCIKTVfagSSCNDIVCTE------QCVMSGHFDKKI 471
Cdd:PLN00181 566 QLVTEMKEHEKRVWSIDYSsADPTLLASGSDDGSVKLWSINQGVSIGTI---KTKANICCVQfpsesgRSLAFGSADHKV 642
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 472 RFWDIRSE-----SVVREMELLGKITALDlnpeRTELLSCSRDDLLKIIDLRTNA--IKQS--FSAPGFKCGSDWTRVVF 542
Cdd:PLN00181 643 YYYDLRNPklplcTMIGHSKTVSYVRFVD----SSTLVSSSTDNTLKLWDLSMSIsgINETplHSFMGHTNVKNFVGLSV 718
                        250
                 ....*....|....*....
gi 158711749 543 SpDGsYVAAGSADGSLYVW 561
Cdd:PLN00181 719 S-DG-YIATGSETNEVFVY 735
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
83-221 4.33e-06

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: 49.79  E-value: 4.33e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749    83 QEMAQLKMKHQEELTELHKKRGELAQLVIDLNNQMQQKDKEIQTNEAKIAE-------CLQTISDLEADCLDLRTKLQD- 154
Cdd:pfam01576  204 QELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEetaqknnALKKIRELEAQISELQEDLESe 283
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158711749   155 ------LEVANQTLKDEYDALQitfTALEEKLrKTTEENQELVTRwmaeKAQEANRLNAENEKDSRRRQARLQ 221
Cdd:pfam01576  284 raarnkAEKQRRDLGEELEALK---TELEDTL-DTTAAQQELRSK----REQEVTELKKALEEETRSHEAQLQ 348
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
83-226 5.04e-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: 49.63  E-value: 5.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749   83 QEMAQLKMKHQEELTELHKKRGELAQ---LVIDLNNQMQQ--------------------------KDKEIQTNEAKIAE 133
Cdd:TIGR04523 253 TQLNQLKDEQNKIKKQLSEKQKELEQnnkKIKELEKQLNQlkseisdlnnqkeqdwnkelkselknQEKKLEEIQNQISQ 332
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749  134 CLQTISDLEADCLDLRTKLQDLEVANQTLKDEydalqitftaLEEK---LRKTTEENQelvtrwmaEKAQEANRLnaENE 210
Cdd:TIGR04523 333 NNKIISQLNEQISQLKKELTNSESENSEKQRE----------LEEKqneIEKLKKENQ--------SYKQEIKNL--ESQ 392
                         170
                  ....*....|....*.
gi 158711749  211 KDSRRRQARLQKELAE 226
Cdd:TIGR04523 393 INDLESKIQNQEKLNQ 408
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
83-230 5.21e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.55  E-value: 5.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749  83 QEMAQLKMKH-QEELTELHKKRGELAQLVIDLNNQMQQKDKEIQTNEAKIAECLQTISDLEADCLDLRTKLQDLEVANQT 161
Cdd:COG1196  227 AELLLLKLRElEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIAR 306
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158711749 162 LKDEYDALQITFTALEEKLRKTTEENQELVTR---WMAEKAQEANRLNAENEKDSRRRQARLQKELAEAAKE 230
Cdd:COG1196  307 LEERRRELEERLEELEEELAELEEELEELEEEleeLEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
48-230 6.68e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.00  E-value: 6.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749  48 LHSVLTQKLQAEKHDVPNRHeispGHDGAWNDSQLQEMaqlkmkhQEELTELHKKRGELAQLVidlnNQMQQKDKEIQTN 127
Cdd:COG4717   43 IRAMLLERLEKEADELFKPQ----GRKPELNLKELKEL-------EEELKEAEEKEEEYAELQ----EELEELEEELEEL 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 128 EAKIAECLQTISDLEA--DCLDLRTKLQDLEVANQTLKDEYDALQITFTALEEKLRKTTEENQELvTRWMAEKAQEANRL 205
Cdd:COG4717  108 EAELEELREELEKLEKllQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAEL-AELQEELEELLEQL 186
                        170       180
                 ....*....|....*....|....*...
gi 158711749 206 NAENE---KDSRRRQARLQKELAEAAKE 230
Cdd:COG4717  187 SLATEeelQDLAEELEELQQRLAELEEE 214
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
80-226 8.15e-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: 48.86  E-value: 8.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749   80 SQLQEMAQLKMKHQEELTELHKKRGELAQLVIDLNNQMQQKDKEIQTNEAKIAECLQTISDLEADCLDLRTKLQDLEVAN 159
Cdd:TIGR04523 370 NEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQD 449
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158711749  160 QTLKDEYDALQITFTALEEKLR------KTTEENQELVTRWMAEKAQEANRLNAENeKDSRRRQARLQKELAE 226
Cdd:TIGR04523 450 SVKELIIKNLDNTRESLETQLKvlsrsiNKIKQNLEQKQKELKSKEKELKKLNEEK-KELEEKVKDLTKKISS 521
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
31-249 9.62e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 48.91  E-value: 9.62e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749    31 AFEEIILQYTKLLEKSDLHSVLTQKLQAEKHDV----------PNRHEISPGhdgawnDSQLQEMAQLKMKHQEELTELH 100
Cdd:TIGR02169  191 LIIDEKRQQLERLRREREKAERYQALLKEKREYegyellkekeALERQKEAI------ERQLASLEEELEKLTEEISELE 264
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749   101 KKRGELAQLVIDLNNQMQQK-DKEIQTNEAKIAECLQTISDLEADCLDLRTKLQDLEVANQTLKDEYDALQITFTALEEK 179
Cdd:TIGR02169  265 KRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELERE 344
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158711749   180 LR-------KTTEENQELVTRwMAEKAQEANRLNAENeKDSRRRQARLQKELAEAAKE--PLPVEQDDDIEVIVDETSD 249
Cdd:TIGR02169  345 IEeerkrrdKLTEEYAELKEE-LEDLRAELEEVDKEF-AETRDELKDYREKLEKLKREinELKRELDRLQEELQRLSEE 421
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 158711749 321 HDGEVNAVQFSPGS-RLLATGGMDRRVKLWEAfgDKCEFKGSLSgSNAGITSIEFDSAGAYLLAasndFASRIWTVDDYR 399
Cdd:PLN00181 574 HEKRVWSIDYSSADpTLLASGSDDGSVKLWSI--NQGVSIGTIK-TKANICCVQFPSESGRSLA----FGSADHKVYYYD 646
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 158711749 400 LRH------TLTGHSGKVLSAKFLlDNARIVSGSHDRTLKLWDL 437
Cdd:PLN00181 647 LRNpklplcTMIGHSKTVSYVRFV-DSSTLVSSSTDNTLKLWDL 689
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
81-237 1.39e-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: 48.51  E-value: 1.39e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749    81 QLQEMAQLKMKHQEELTELHKKRGEL--------------AQLVIDLNNQMQQKDKEIQTNEAKIAECLQTISDLEADCL 146
Cdd:TIGR02168  324 QLEELESKLDELAEELAELEEKLEELkeelesleaeleelEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIE 403
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749   147 DLRTKLQDLEVANQTLKDEydalqitftaLEEKLRKTTEENQELVTRWMAEKAQEANRLNAENEkDSRRRQARLQKELAE 226
Cdd:TIGR02168  404 RLEARLERLEDRRERLQQE----------IEELLKKLEEAELKELQAELEELEEELEELQEELE-RLEEALEELREELEE 472
                          170
                   ....*....|.
gi 158711749   227 AAKEPLPVEQD 237
Cdd:TIGR02168  473 AEQALDAAERE 483
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
79-253 1.82e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.99  E-value: 1.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749   79 DSQLQEMAQLKMKHQEELTELHKKRGELAQLVIDLNNQMQQKD-KEIQTNEAKIAECLQTISDLEADCLDLRTKLQDLEV 157
Cdd:COG4913   294 EAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGL 373
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749  158 ANQTLKDEYDALQITFTALEEKLRKTTEENQELVTRWMAEKaqeanrlnaeneKDSRRRQARLQKELA--EAAKEPLPVE 235
Cdd:COG4913   374 PLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAAL------------RDLRRELRELEAEIAslERRKSNIPAR 441
                         170
                  ....*....|....*...
gi 158711749  236 QDDDIEVIVDETSDHTEE 253
Cdd:COG4913   442 LLALRDALAEALGLDEAE 459
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
84-232 3.45e-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: 3.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749  84 EMAQLKMKHQEELTELHKKRGELAQL---VIDLNNQMQQKDKEIQTNEAKIAECLQTISDLEADCLDLRTKLQDLEVANQ 160
Cdd:COG1196  268 ELEELRLELEELELELEEAQAEEYELlaeLARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELE 347
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 161 TLKDEYDALQITFTALEEKLRKTTEENQELVTRWMAEKAQEANRLNAENEK------------DSRRRQARLQKELAE-- 226
Cdd:COG1196  348 EAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELaaqleeleeaeeALLERLERLEEELEEle 427
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 158711749 227 --------------------------------AAKEPL 232
Cdd:COG1196  428 ealaeleeeeeeeeealeeaaeeeaeleeeeeALLELL 465
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
83-252 3.79e-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: 46.94  E-value: 3.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749   83 QEMAQLKMKHQEELTELHKKRGELAQLVIDLNNQMQQKD-----KEIQTNEAKIAECLQTISDLEADCLDLRTKLQDLEV 157
Cdd:TIGR04523 517 KKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKkenleKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEK 596
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749  158 ANQTLKDEYDALQITFTALEEKLRKTTEENQELvtrwmaekaqEANRLNAENEKDSRRRQARLQKELAEAAKEPLP--VE 235
Cdd:TIGR04523 597 EKKDLIKEIEEKEKKISSLEKELEKAKKENEKL----------SSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPeiIK 666
                         170
                  ....*....|....*..
gi 158711749  236 QDDDIEVIVDETSDHTE 252
Cdd:TIGR04523 667 KIKESKTKIDDIIELMK 683
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
81-238 4.18e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.60  E-value: 4.18e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749    81 QLQEMAQLKMKHQEELTELHKKRGELAQLVIDLNNQMQQKDKEIQTNEAKIAECLQTISDLEADCLDLRTKLQDLEVANQ 160
Cdd:TIGR02169  675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIE 754
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749   161 TLKDEYDALQITFTALEEKLRKTTEENQELVTRWMAEKAQEANRLNAENEKDSRRRQARLQ------------KELAEAA 228
Cdd:TIGR02169  755 NVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLReieqklnrltleKEYLEKE 834
                          170
                   ....*....|
gi 158711749   229 KEPLPVEQDD 238
Cdd:TIGR02169  835 IQELQEQRID 844
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
79-409 6.26e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 45.59  E-value: 6.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749  79 DSQLQEMAQLKMKHQEELTELHKKRGELAQLVIDLNNQMQQKDKEIQTNEAKIAECLQTISDLE---------------- 142
Cdd:COG3883   22 QKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERReelgeraralyrsggs 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 143 -------------ADCLDLRTKLQDLEVANQTLKDEYDALQITFTALEEKLRKTTEENQELVTRwMAEKAQEANRLNAEN 209
Cdd:COG3883  102 vsyldvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAE-LEAAKAELEAQQAEQ 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 210 EKdsRRRQARLQKELAEAAKEPLPVEQDDDIEVIVDETSDHTEETSPVRAISRAATKRLSQPAGGLLDSITNIFGRRSVS 289
Cdd:COG3883  181 EA--LLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAA 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 290 SIPVPQDVVDTHPASGKDVRVPTTASYVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWEAFGDKCEFKGSLSGSNAGI 369
Cdd:COG3883  259 AGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAVVGGASAGGGGGSGGGG 338
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 158711749 370 TSIEFDSAGAYLLAASNDFASRIWTVDDYRLRHTLTGHSG 409
Cdd:COG3883  339 GSSGGGSGGGGGGGGGGGGSSSGGGGGGVGLSVGGGYVGG 378
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
78-253 6.31e-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: 46.20  E-value: 6.31e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749    78 NDSQLQEmaqLKMKHQEELTELHKKRGELAQL---VIDLNNQMQQKDKEIQTNEAKIAECLQTISDLEADCLDLRTKLQD 154
Cdd:TIGR02168  801 LREALDE---LRAELTLLNEEAANLRERLESLerrIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEA 877
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749   155 L-------EVANQTLKDEYDALQITFTALEEKLRKTTEENQELvtrwMAEKAQEANRLN-AENEKDSRRRQARLQKELAE 226
Cdd:TIGR02168  878 LlneraslEEALALLRSELEELSEELRELESKRSELRRELEEL----REKLAQLELRLEgLEVRIDNLQERLSEEYSLTL 953
                          170       180
                   ....*....|....*....|....*..
gi 158711749   227 AAKEPLPVEQDDDIEVIVDETSDHTEE 253
Cdd:TIGR02168  954 EEAEALENKIEDDEEEARRRLKRLENK 980
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
101-270 8.68e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 45.14  E-value: 8.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 101 KKRGELAQLVIDLNNQMQQKDKEIQTNEAKIAECLQTISDLEADCLDLRTKLQDLEVANQTLKDEYDALQITFTALEEKL 180
Cdd:COG4942   20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 181 RKTTEENQELVTRW--MAEKAQEANRLNAENEKDSRRRQARLQ------KELAEAAKeplpvEQDDDIEVIVDETSDHTE 252
Cdd:COG4942  100 EAQKEELAELLRALyrLGRQPPLALLLSPEDFLDAVRRLQYLKylaparREQAEELR-----ADLAELAALRAELEAERA 174
                        170
                 ....*....|....*...
gi 158711749 253 ETSPVRAISRAATKRLSQ 270
Cdd:COG4942  175 ELEALLAELEEERAALEA 192
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
54-211 1.16e-04

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 45.42  E-value: 1.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749    54 QKLQAEKHDVPNRHE-ISPGHDGAWNDSQLQEMAQLKMKHQEELTELHKKRGELAQLVIDLNNQ---MQQKDKEIQTNEA 129
Cdd:TIGR00606  795 ERFQMELKDVERKIAqQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQiqhLKSKTNELKSEKL 874
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749   130 KIAECLQTISDLEADCLDLRTKLQDLEVANQTLKDEydalqitFTALEEKLRKTTEENQELVTRWMAEKAQEANRLNAEN 209
Cdd:TIGR00606  875 QIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQ-------DSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIK 947

                   ..
gi 158711749   210 EK 211
Cdd:TIGR00606  948 EK 949
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
43-215 1.24e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 45.44  E-value: 1.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749    43 LEKSDLHSVLtQKLQAEKHDVPNRHeispghdgAWNDSQLQEMAQLKMKHQEELTELHKKRGELAQLVIDLNNQMQQKDK 122
Cdd:TIGR02169  784 LEARLSHSRI-PEIQAELSKLEEEV--------SRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEK 854
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749   123 EIQTNEAKIAECLQTISDLEADCLDLRTKLQDLEVANQTLKDEYDALQITFTALEEKLRKTTEENQELvtrwmAEKAQEA 202
Cdd:TIGR02169  855 EIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSEL-----KAKLEAL 929
                          170
                   ....*....|...
gi 158711749   203 NRLNAENEKDSRR 215
Cdd:TIGR02169  930 EEELSEIEDPKGE 942
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
46-230 1.75e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 44.65  E-value: 1.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749  46 SDLHSVLTQKLQAEKHDVPNRHEispghdgawndsqlQEMAQLK--MKHQEELTELHKKRGELAQLVIDLNNQMQQkdkE 123
Cdd:PRK02224 190 DQLKAQIEEKEEKDLHERLNGLE--------------SELAELDeeIERYEEQREQARETRDEADEVLEEHEERRE---E 252
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 124 IQTNEAKIAECLQTISDLEADCLDLRTKLQDLEVANQTLKDEYDAL--QITFTALE----EKLRKTTEENQELVTRWMAE 197
Cdd:PRK02224 253 LETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLlaEAGLDDADaeavEARREELEDRDEELRDRLEE 332
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 158711749 198 KAQEANRLN------AENEKDSRRRQARLQKELAEAAKE 230
Cdd:PRK02224 333 CRVAAQAHNeeaeslREDADDLEERAEELREEAAELESE 371
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
42-232 2.17e-04

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 44.12  E-value: 2.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749   42 LLEKSDLHsvltQKLQAEKHDVPNRHEISPGHDGAWnDSQLQEMAQLKMKHQEELTELHKKRGELAQLVIDLNNQMQQKD 121
Cdd:pfam07888  40 LQERAELL----QAQEAANRQREKEKERYKRDREQW-ERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELS 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749  122 KEIQTNEAKIAECLQTISDLEADCLDLRTKLQDLEVANQTLKD--------------EYDALQITFTALEEKLRKTTEEN 187
Cdd:pfam07888 115 EEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKErakkagaqrkeeeaERKQLQAKLQQTEEELRSLSKEF 194
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 158711749  188 QELvTRWMAEKAQEANRLNAENEKDSRRRQARLQKELA-EAAKEPL 232
Cdd:pfam07888 195 QEL-RNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAEnEALLEEL 239
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
76-333 2.22e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.05  E-value: 2.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749  76 AWNDSQLQEMAQLKMKHQEELTELHKKRGELAQLVIDLNNQMQQKDKEIQTNEAKIAECLQTISDLEADCLDLRTKLQD- 154
Cdd:COG3883   12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEr 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 155 -------------LEV----------------------ANQTLKDEYDALQITFTALEEKLRKTTEENQELVTRwMAEKA 199
Cdd:COG3883   92 aralyrsggsvsyLDVllgsesfsdfldrlsalskiadADADLLEELKADKAELEAKKAELEAKLAELEALKAE-LEAAK 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 200 QEANRLNAENEKDSRRRQARLQKELAEAAKEPLPVEQDDDIEVIVDETSDHTEETSPVRAISRAATKRLSQPAGGLLDSI 279
Cdd:COG3883  171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAG 250
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 158711749 280 TNIFGRRSVSSIPVPQDVVDTHPASGKDVRVPTTASYVFDAHDGEVNAVQFSPG 333
Cdd:COG3883  251 AAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSG 304
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
93-270 2.58e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.14  E-value: 2.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749   93 QEELTELHKKRGELAQLVIDLNNQMQQKDKEIQTNEAKiAECLQTISDLEADCLDLRTKLQDLEVANQTLkDEYDALQIT 172
Cdd:COG4913   609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQER-REALQRLAEYSWDEIDVASAEREIAELEAEL-ERLDASSDD 686
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749  173 FTALEEKLRKTTEENQELVTRWmaEKAQEANRLNAENEKDSRRRQARLQKELAEAAKEPLPVEQDDdieviVDETSDHTE 252
Cdd:COG4913   687 LAALEEQLEELEAELEELEEEL--DELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL-----LEERFAAAL 759
                         170
                  ....*....|....*...
gi 158711749  253 ETSPVRAISRAATKRLSQ 270
Cdd:COG4913   760 GDAVERELRENLEERIDA 777
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
81-230 2.67e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.14  E-value: 2.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749   81 QLQEMAQLKMKHQEELTELHKKRGELAQLVID--------LNNQMQQKDKEIQTNEAKIAECLQTISDLEADCLDLR--- 149
Cdd:COG4913   253 LLEPIRELAERYAAARERLAELEYLRAALRLWfaqrrlelLEAELEELRAELARLEAELERLEARLDALREELDELEaqi 332
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749  150 ------------TKLQDLEVANQTLKDEYDALQITFTALEEKLRKTTEENQELVTRWMAEKAQEANRLNAENEK--DSRR 215
Cdd:COG4913   333 rgnggdrleqleREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEAlaEAEA 412
                         170
                  ....*....|....*
gi 158711749  216 RQARLQKELAEAAKE 230
Cdd:COG4913   413 ALRDLRRELRELEAE 427
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
538-562 2.82e-04

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 38.45  E-value: 2.82e-04
                           10        20
                   ....*....|....*....|....*
gi 158711749   538 TRVVFSPDGSYVAAGSADGSLYVWS 562
Cdd:smart00320  16 TSVAFSPDGKYLASGSDDGTIKLWD 40
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
80-227 3.91e-04

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


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 43.58  E-value: 3.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749   80 SQLQ-EMAQLKMKHQEELTELHKKRGELAQLV---IDLNNQMQQKDKEIQTNEAKIAECLQ--------TISDLEADCLD 147
Cdd:pfam05557  12 SQLQnEKKQMELEHKRARIELEKKASALKRQLdreSDRNQELQKRIRLLEKREAEAEEALReqaelnrlKKKYLEALNKK 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749  148 LRTKLQDLEVANQT---LKDEYDALQITFTALEEKLRKTTEENQELVTR--WMAEKAQEANRLNAENEKDsrrrqarlQK 222
Cdd:pfam05557  92 LNEKESQLADAREViscLKNELSELRRQIQRAELELQSTNSELEELQERldLLKAKASEAEQLRQNLEKQ--------QS 163

                  ....*
gi 158711749  223 ELAEA 227
Cdd:pfam05557 164 SLAEA 168
COG4946 COG4946
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown] ...
541-607 4.18e-04

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


Pssm-ID: 443973 [Multi-domain]  Cd Length: 1072  Bit Score: 43.49  E-value: 4.18e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158711749  541 VFSPDGSYVAAGSADGSLYVWSVLTGKVEKVLSKQHSSSINAVAWAPsglhvvsvDkgSRAVLWAQP 607
Cdd:COG4946   395 VWSPDGKKIAFTDNRGRLWVVDLASGKVRKVDTDGYGDGISDLAWSP--------D--SKWLAYSKP 451
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
80-230 4.22e-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: 43.52  E-value: 4.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749    80 SQLQEMAQLKMKHQEELTELHKKRGELAQLVIDLNNQMQQKDKEIQTNEAKIAECLQTISDLEADclDLRTKLQDLEVAN 159
Cdd:TIGR02169  723 KEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEAR--LSHSRIPEIQAEL 800
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158711749   160 QTLKDEYDALQITFTALEEKLRKTTEENQELvtRWMAEKAQEANRLNAENEKDSRRRQARLQKELAEAAKE 230
Cdd:TIGR02169  801 SKLEEEVSRIEARLREIEQKLNRLTLEKEYL--EKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE 869
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
79-270 5.03e-04

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 42.90  E-value: 5.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749  79 DSQLQEMAQLK------------MKHQEELTELHKKRGELAQLVIDLNN--------------QMQQK---------DKE 123
Cdd:PRK04778 178 EEEFSQFVELTesgdyveareilDQLEEELAALEQIMEEIPELLKELQTelpdqlqelkagyrELVEEgyhldhldiEKE 257
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 124 IQTNEAKIAECLQTISDLEadcldlrtkLQDLEVANQTLKDEYDALQITFTAlEEKLRKTTEENQELVTRwMAEKAQEAN 203
Cdd:PRK04778 258 IQDLKEQIDENLALLEELD---------LDEAEEKNEEIQERIDQLYDILER-EVKARKYVEKNSDTLPD-FLEHAKEQN 326
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158711749 204 R-LNAE----------NEKDSRRRQArLQKELAEAakeplpveqDDDIEVIVDETSDHTEETSPVRAISRAATKRLSQ 270
Cdd:PRK04778 327 KeLKEEidrvkqsytlNESELESVRQ-LEKQLESL---------EKQYDEITERIAEQEIAYSELQEELEEILKQLEE 394
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
39-170 5.17e-04

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 42.31  E-value: 5.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749    39 YTKLLEKSDLHSVLTQKLQAEKHDVPNRHEISPGHDGAWNDSQLQEMAQLKMKHQEELTELHKKRGELAQLvidlNNQMQ 118
Cdd:smart00787 160 YKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRAKEKLKKLLQEIMIKVKKLEEL----EEELQ 235
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 158711749   119 QKDKEIQTNEAKIAECLQTISDLEADCLDLRtKLQDLEVAnqTLKDEYDALQ 170
Cdd:smart00787 236 ELESKIEDLTNKKSELNTEIAEAEKKLEQCR-GFTFKEIE--KLKEQLKLLQ 284
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
79-189 5.18e-04

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 43.09  E-value: 5.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749   79 DSQLQEMAQLKMKHQEELTELHKKRGELAQLVIDLNNQMQQKDKEIQTNEAKIAECLQTISDLEADCLDLRTKLQDLEVA 158
Cdd:TIGR04523 327 QNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKL 406
                          90       100       110
                  ....*....|....*....|....*....|....
gi 158711749  159 NQTLKDEYDALQITFTALE---EKLRKTTEENQE 189
Cdd:TIGR04523 407 NQQKDEQIKKLQQEKELLEkeiERLKETIIKNNS 440
WD40 pfam00400
WD domain, G-beta repeat;
538-562 5.22e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 37.71  E-value: 5.22e-04
                          10        20
                  ....*....|....*....|....*
gi 158711749  538 TRVVFSPDGSYVAAGSADGSLYVWS 562
Cdd:pfam00400  15 TSLAFSPDGKLLASGSDDGTVKVWD 39
PTZ00420 PTZ00420
coronin; Provisional
369-526 5.92e-04

coronin; Provisional


Pssm-ID: 240412 [Multi-domain]  Cd Length: 568  Bit Score: 42.63  E-value: 5.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 369 ITSIEFDSAGaylLAASNDFASRIWTVDD------YRLRHT--------LTGHSGKVLSAKFLLDNARIV-SGSHDRTLK 433
Cdd:PTZ00420  24 ICSRVIDSCG---IACSSGFVAVPWEVEGggligaIRLENQmrkppvikLKGHTSSILDLQFNPCFSEILaSGSEDLTIR 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 434 LWDLRSKvciktvfaGSSCNDIVcTEQCVMSGH---------------------FDKKIRFWDIRSESVVREMELLGKIT 492
Cdd:PTZ00420 101 VWEIPHN--------DESVKEIK-DPQCILKGHkkkisiidwnpmnyyimcssgFDSFVNIWDIENEKRAFQINMPKKLS 171
                        170       180       190
                 ....*....|....*....|....*....|....
gi 158711749 493 ALDLNPERTELLSCSRDDLLKIIDLRTNAIKQSF 526
Cdd:PTZ00420 172 SLKWNIKGNLLSGTCVGKHMHIIDPRKQEIASSF 205
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
80-262 6.30e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.58  E-value: 6.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749  80 SQLQEMAQLKMKHQEELTELHKKRGELAQLVIDLNNQMQQKDKEIQTNEAKIAECLQTISDLEADCLDLRTKLQDLEVAN 159
Cdd:COG4372   87 EQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEEL 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 160 QTLKDEYDALQITFTALEEKLRKTTEENQELVTRWMAEKAQEANRLNAENEKDSRRRQARLQKELAEAAKEPLPVEQDDD 239
Cdd:COG4372  167 AALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEE 246
                        170       180
                 ....*....|....*....|...
gi 158711749 240 IEVIVDETSDHTEETSPVRAISR 262
Cdd:COG4372  247 DKEELLEEVILKEIEELELAILV 269
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
79-230 6.99e-04

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 42.70  E-value: 6.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749   79 DSQLQEMAQLKMKHQEELTELHKKRGELAQLVID---LNNQMQQKDKEIQTNEAKIAECLQTISDLEADCLDLRTKLQDL 155
Cdd:TIGR04523 464 ESLETQLKVLSRSINKIKQNLEQKQKELKSKEKElkkLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDL 543
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749  156 E---------VANQTLKDEYDALQITFTALEE---KLRKTTEENQELVtrwmAEKAQEANRLNAENEKDSrRRQARLQKE 223
Cdd:TIGR04523 544 EdelnkddfeLKKENLEKEIDEKNKEIEELKQtqkSLKKKQEEKQELI----DQKEKEKKDLIKEIEEKE-KKISSLEKE 618

                  ....*..
gi 158711749  224 LAEAAKE 230
Cdd:TIGR04523 619 LEKAKKE 625
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
86-270 7.77e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.06  E-value: 7.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749  86 AQLKMKHQEELTELHKKRGELAQLVIDLNNQMQQKDKEIQTNEAKIAECLQTISDLEADCLDLRTKLQDLEVANQTLKDE 165
Cdd:COG4942   19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 166 YDALQitfTALEEKLRK--TTEENQELVTRWMAEKAQEANR----LNAENEKDsRRRQARLQKELAE-AAKEPLPVEQDD 238
Cdd:COG4942   99 LEAQK---EELAELLRAlyRLGRQPPLALLLSPEDFLDAVRrlqyLKYLAPAR-REQAEELRADLAElAALRAELEAERA 174
                        170       180       190
                 ....*....|....*....|....*....|..
gi 158711749 239 DIEVIVDETSDHTEETSPVRAISRAATKRLSQ 270
Cdd:COG4942  175 ELEALLAELEEERAALEALKAERQKLLARLEK 206
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
81-188 9.06e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 9.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749  81 QLQEMAQLKMKHQEELTELHKKRGELAQLV---------IDLNNQMQQKDKEIQTNEAKIAECLQTISDLEADCL--DLR 149
Cdd:COG4717  396 EYQELKEELEELEEQLEELLGELEELLEALdeeeleeelEELEEELEELEEELEELREELAELEAELEQLEEDGElaELL 475
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 158711749 150 TKLQDLEVANQTLKDEYDALQITFTALEEKLRKTTEENQ 188
Cdd:COG4717  476 QELEELKAELRELAEEWAALKLALELLEEAREEYREERL 514
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
93-243 1.04e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.81  E-value: 1.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749  93 QEELTELHKKRGELAQLvidlNNQMQQKDKEIQTNEAKIAECLQTISDLEADCLDLRTKLQDLEVANQTLKDEYDALQIT 172
Cdd:COG4372   34 RKALFELDKLQEELEQL----REELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEE 109
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158711749 173 FTALEEKLRKTTEENQELVTRWMAEKAQEANRLNAENEKDSR-----RRQARLQKELAEAAKEPLPVEQDDDIEVI 243
Cdd:COG4372  110 AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEElkeleEQLESLQEELAALEQELQALSEAEAEQAL 185
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
80-230 1.30e-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: 41.93  E-value: 1.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749   80 SQLQEMAQLKMKHQEELT-ELHKKRGELAQLV---IDLNNQMQQKDKEIQTNEAKiaeclqtISDLEADCLDLRTKLQDL 155
Cdd:TIGR04523 228 NQLKDNIEKKQQEINEKTtEISNTQTQLNQLKdeqNKIKKQLSEKQKELEQNNKK-------IKELEKQLNQLKSEISDL 300
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749  156 -----EVANQTLKDEYDALQITFTALEEKLRKTTEENQELvTRWMAEKAQEANRLNAENEKdsrrrqarLQKELAEAAKE 230
Cdd:TIGR04523 301 nnqkeQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQL-NEQISQLKKELTNSESENSE--------KQRELEEKQNE 371
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
79-212 1.71e-03

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


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 40.82  E-value: 1.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749  79 DSQLQEMAQLKMKHQEELTElhKKRGELAQLVIDLNNQMQqkdKEIQTNEAKIAECLQTISDLEADCLDLRTKLQDLEVA 158
Cdd:cd22656   90 DSYYAEILELIDDLADATDD--EELEEAKKTIKALLDDLL---KEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKA 164
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 158711749 159 NQTLKDEYDALqITFTALEEKLRKTTEENQELVTRwMAEKAQEANRLNAENEKD 212
Cdd:cd22656  165 LKDLLTDEGGA-IARKEIKDLQKELEKLNEEYAAK-LKAKIDELKALIADDEAK 216
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
83-230 1.90e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.16  E-value: 1.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749  83 QEMAQLKMKH-----QEELTELHKKRGELAQLVIDLNNQMQQKDKEIQTNEAKIAECLQTISDLEADCL--DLRTKLQDL 155
Cdd:COG3206  196 AALEEFRQKNglvdlSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPViqQLRAQLAEL 275
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158711749 156 EVanqtlkdEYDALQITFTALEEKLRKTTEENQELvtrwMAEKAQEANRL--NAENEKDS-RRRQARLQKELAEAAKE 230
Cdd:COG3206  276 EA-------ELAELSARYTPNHPDVIALRAQIAAL----RAQLQQEAQRIlaSLEAELEAlQAREASLQAQLAQLEAR 342
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
315-350 2.10e-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: 40.40  E-value: 2.10e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 158711749 315 SYVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWE 350
Cdd:cd00200  254 VQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
82-238 2.22e-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: 2.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749   82 LQEMAQLkMKHQEELTELHKKRGELAQLViDLNNQMQQKDKEIQTNEAkiaecLQTISDLEADcldlRTKLQDLEVANQT 161
Cdd:COG4913   231 VEHFDDL-ERAHEALEDAREQIELLEPIR-ELAERYAAARERLAELEY-----LRAALRLWFA----QRRLELLEAELEE 299
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749  162 LKDEYDALQITFTALEEKLRKTTEENQELVTRWMAEKAQEANRL-----NAENEKDSRRRQARLQKELAEAAKEPLPVEQ 236
Cdd:COG4913   300 LRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLereieRLERELEERERRRARLEALLAALGLPLPASA 379

                  ..
gi 158711749  237 DD 238
Cdd:COG4913   380 EE 381
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
79-193 2.39e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.21  E-value: 2.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749    79 DSQLQEMAQLKMKHQEELTELHKKRGELAQLVIDLNNQMQQKDKEIQTNEAKIAE-------------CLQTISDLEADC 145
Cdd:TIGR02169  881 ESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEiedpkgedeeipeEELSLEDVQAEL 960
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 158711749   146 LDLRTKLQDLEVANQTLKDEYDALQITFTALEEKLRKTTEENQELVTR 193
Cdd:TIGR02169  961 QRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILER 1008
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
90-230 2.41e-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: 2.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749   90 MKHQEELTELHKKRGELAQLVIDLNN--QMQQKDKEIQTNEAKIAECLQTISDLEADCLDLRTKLQDLEVANQTLKDEYD 167
Cdd:COG4913   583 VKGNGTRHEKDDRRRIRSRYVLGFDNraKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEID 662
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158711749  168 --ALQITFTALEEKLRKTTEENQEL--VTRWMAEKAQEANRLNAEnEKDSRRRQARLQKELAEAAKE 230
Cdd:COG4913   663 vaSAEREIAELEAELERLDASSDDLaaLEEQLEELEAELEELEEE-LDELKGEIGRLEKELEQAEEE 728
TolB COG0823
Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, ...
534-604 2.90e-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: 2.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 534 GSDWTRV----------VFSPDGSYVA-AGSADGSLYVWSV-LTGKVEKVLSKqhssSINAVAWAPSGLHVV-SVDKGSR 600
Cdd:COG0823   64 GGEPRRLtfgggynaspSWSPDGKRLAfVSRSDGRFDIYVLdLDGGAPRRLTD----GPGSPSWSPDGRRIVfSSDRGGR 139

                 ....
gi 158711749 601 AVLW 604
Cdd:COG0823  140 PDLY 143
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
147-243 3.25e-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: 3.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 147 DLRTKLQDLEVANQTLKDEYD-ALQITFTALEEKLRKTTEENQELVTRWMAEKA--QEANRLNAENEKDSRRRQArLQKE 223
Cdd:COG0542  415 ELERRLEQLEIEKEALKKEQDeASFERLAELRDELAELEEELEALKARWEAEKEliEEIQELKEELEQRYGKIPE-LEKE 493
                         90       100
                 ....*....|....*....|....*...
gi 158711749 224 LAEA-----AKEPLPVEQ--DDDI-EVI 243
Cdd:COG0542  494 LAELeeelaELAPLLREEvtEEDIaEVV 521
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
79-253 3.45e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.89  E-value: 3.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749  79 DSQLQEMAQLKMKHQEELTELHKKRGELAQLVIDLNNQMQQKDKEIQTNEAKIAECLQTISDLEADCLDLRTKLQDLEVA 158
Cdd:COG4372   72 RSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEE 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 159 NQTLKDEYDALQITFTALEEKLRKTTEENQElvtRWMAEKAQEANRlNAENEKDSRRRQARLQKELAEAAKEPLPVEQDD 238
Cdd:COG4372  152 LKELEEQLESLQEELAALEQELQALSEAEAE---QALDELLKEANR-NAEKEEELAEAEKLIESLPRELAEELLEAKDSL 227
                        170
                 ....*....|....*
gi 158711749 239 DIEVIVDETSDHTEE 253
Cdd:COG4372  228 EAKLGLALSALLDAL 242
TolB COG0823
Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, ...
514-593 3.53e-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: 38.50  E-value: 3.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 514 IIDLRTNAIKQSFSAPGFKCGSDWtrvvfSPDGSYVAAGSADGS---LYVWSVLTGKVEKVLSKQHSSSinAVAWAPSGL 590
Cdd:COG0823   15 VVDLDGGEPRRLTNSPGIDTSPAW-----SPDGRRIAFTSDRGGgpqIYVVDADGGEPRRLTFGGGYNA--SPSWSPDGK 87

                 ...
gi 158711749 591 HVV 593
Cdd:COG0823   88 RLA 90
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
87-208 3.72e-03

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 39.79  E-value: 3.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749   87 QLKMKHQEELTELHKKRGELAQL---VIDLNNQMQQKDKEIQTNEAKIAECLQTISDLEADCLDLR-------TKLQDLE 156
Cdd:pfam15905 181 GMEGKLQVTQKNLEHSKGKVAQLeekLVSTEKEKIEEKSETEKLLEYITELSCVSEQVEKYKLDIAqleellkEKNDEIE 260
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 158711749  157 VANQTLKDEYDALQITFTALEEKLRKTTEENQELVTRwmaEKAQEANrLNAE 208
Cdd:pfam15905 261 SLKQSLEEKEQELSKQIKDLNEKCKLLESEKEELLRE---YEEKEQT-LNAE 308
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
82-230 4.19e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 39.51  E-value: 4.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749  82 LQEMAQLKMKHQEELTELHKKRGELAqlviDLNNQMQQKDKEIQTNEAKIAECLQtisdlEADcldlrtklqdlevanqT 161
Cdd:COG1340  152 AKKALEKNEKLKELRAELKELRKEAE----EIHKKIKELAEEAQELHEEMIELYK-----EAD----------------E 206
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158711749 162 LKDEYDALQITFTALEEKLRKTTEENQELVTRwMAEKAQEANRLNAENEKDSRRRQARLQKELAEAAKE 230
Cdd:COG1340  207 LRKEADELHKEIVEAQEKADELHEEIIELQKE-LRELRKELKKLRKKQRALKREKEKEELEEKAEEIFE 274
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
54-230 4.50e-03

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 40.03  E-value: 4.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749    54 QKLQAEKHDVPNRHEISpghdgawndsqlQEMAQLKMKH-QEELTELHKKRGELAQLVID-LNNQMQQKDKEIQTNEAKI 131
Cdd:TIGR00606  919 EKDQQEKEELISSKETS------------NKKAQDKVNDiKEKVKNIHGYMKDIENKIQDgKDDYLKQKETELNTVNAQL 986
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749   132 AECLQTISDLEAdclDLRTKLQDLEVANQT---LKDeydalQITFTALEEKLRKTTEE--------NQELVTRWMAE--K 198
Cdd:TIGR00606  987 EECEKHQEKINE---DMRLMRQDIDTQKIQerwLQD-----NLTLRKRENELKEVEEElkqhlkemGQMQVLQMKQEhqK 1058
                          170       180       190
                   ....*....|....*....|....*....|..
gi 158711749   199 AQEANRLNAENEKDSRRRQARLQKELAEAAKE 230
Cdd:TIGR00606 1059 LEENIDLIKRNHVLALGRQKGYEKEIKHFKKE 1090
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
81-186 5.23e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 5.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749  81 QLQEMAQLKMKHQEELTELHKKRGELAQLViDLNNQMQQKDKEIQTNEAKIAECLQTISDLEADCL-DLRTKLQDLEVAN 159
Cdd:COG4717  130 LYQELEALEAELAELPERLEELEERLEELR-ELEEELEELEAELAELQEELEELLEQLSLATEEELqDLAEELEELQQRL 208
                         90       100
                 ....*....|....*....|....*..
gi 158711749 160 QTLKDEYDALQITFTALEEKLRKTTEE 186
Cdd:COG4717  209 AELEEELEEAQEELEELEEELEQLENE 235
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
80-187 5.33e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 40.00  E-value: 5.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749   80 SQLQEMAQLKMKHQEELTELHKKRGELAQLVIDLNNQMQQKDKEIQTNEAKIaecLQTISDLEADCLDLRTKLQDLEVAN 159
Cdd:TIGR04523 204 SNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQL---NQLKDEQNKIKKQLSEKQKELEQNN 280
                          90       100
                  ....*....|....*....|....*...
gi 158711749  160 QTLKDEYDALQITFTALEEkLRKTTEEN 187
Cdd:TIGR04523 281 KKIKELEKQLNQLKSEISD-LNNQKEQD 307
46 PHA02562
endonuclease subunit; Provisional
79-244 5.76e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 39.61  E-value: 5.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749  79 DSQLQEMAQLKMKH---QEELTELHKKRGE-------LAQLVIDLNNQMQQKDKEIQ--TNEAKIAECLQTISDLEADCL 146
Cdd:PHA02562 223 DELVEEAKTIKAEIeelTDELLNLVMDIEDpsaalnkLNTAAAKIKSKIEQFQKVIKmyEKGGVCPTCTQQISEGPDRIT 302
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 147 DLRTK-------LQDLEVANQTLK---DEYDALQITFTALEEKLRKtteENQELVT-RWMAEKAQEA-NRLNAENeKDSR 214
Cdd:PHA02562 303 KIKDKlkelqhsLEKLDTAIDELEeimDEFNEQSKKLLELKNKIST---NKQSLITlVDKAKKVKAAiEELQAEF-VDNA 378
                        170       180       190
                 ....*....|....*....|....*....|
gi 158711749 215 RRQARLQKELAEAAKEPLPVEQDDDIEVIV 244
Cdd:PHA02562 379 EELAKLQDELDKIVKTKSELVKEKYHRGIV 408
PTZ00332 PTZ00332
paraflagellar rod protein; Provisional
10-226 7.38e-03

paraflagellar rod protein; Provisional


Pssm-ID: 240364 [Multi-domain]  Cd Length: 589  Bit Score: 39.18  E-value: 7.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749  10 FPRWKRHIAE-ELRRRDRLQRQAFEEIILQYTKLLEKS----DLH---SVLTQKLQAEK-HDVPNRHeispghdgawnDS 80
Cdd:PTZ00332 341 FEEVKRRIEEnDREEKRRVEYQQFLEVAGQHKKLLELTvyncDLAlrcTGLVEELVSEGcAAVKARH-----------DK 409
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749  81 QLQEMAQLKMK-HQEELTELHKKRGELAQLVIDLNNQMQQKDKEIQTNEAKIAECLQTI-------SDLEADCLDLRtkl 152
Cdd:PTZ00332 410 TNQDLAALRLQvHKEHLEYFRMLYLTLGSLIYKKEKRLEEIDRNIRTTHIQLEFCVETFdpnakkhADMKKELYKLR--- 486
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 153 QDLEVANQTLKDEYDALQITFTALEEKLRKT--------TEENQELVTRW--MAE-----KAQEANRLNAENEKDSRRRQ 217
Cdd:PTZ00332 487 QGVEEELAMLKEKQAQALEMFKESEEALDAAgiefvhpvDENNEEVLTRRskMVEyrshlAKQEEVKIAAEREEIKRARL 566

                 ....*....
gi 158711749 218 ARLQKELAE 226
Cdd:PTZ00332 567 LRSQGYRGE 575
Ge1_WD40 pfam16529
WD40 region of Ge1, enhancer of mRNA-decapping protein; Ge1_WD40 is the N-terminal region of ...
365-446 7.53e-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: 7.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749  365 SNAGITSIEFDSAGAYLLAASNDFASRIWTV-----DDYRLRHTLTGHSGKVLSAKFLLDNAR----------IVSGS-H 428
Cdd:pfam16529 185 EHSLLVDAAFSPDGTALATASLDGEVKFFQIylfdnRNPRCLHEWKPHDGKPLSSLFFLDNHKkppevqfwrfAITGAdN 264
                          90
                  ....*....|....*...
gi 158711749  429 DRTLKLWDLRSKVCIKTV 446
Cdd:pfam16529 265 NSELKLWSCESWTCLQTI 282
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
565-604 7.57e-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: 7.57e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 158711749   565 TGKVEKVLsKQHSSSINAVAWAPSGLHVVSVDKGSRAVLW 604
Cdd:smart00320   1 SGELLKTL-KGHTGPVTSVAFSPDGKYLASGSDDGTIKLW 39
Prefoldin_2 pfam01920
Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996.
93-190 8.31e-03

Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996.


Pssm-ID: 396482 [Multi-domain]  Cd Length: 102  Bit Score: 36.05  E-value: 8.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749   93 QEELTELHKKRGELAQlvidlnnqmQQKDKEIQTNEAKIAecLQTISDLEADcldlrTK----------LQDLEVANQTL 162
Cdd:pfam01920   1 INKFQQLQQQLQLLAQ---------QIKQLETQLKELELA--LEELELLDED-----TKvykligdvlvKQDKEEVKEQL 64
                          90       100
                  ....*....|....*....|....*...
gi 158711749  163 KDEYDALQITFTALEEKLRKTTEENQEL 190
Cdd:pfam01920  65 EERKETLEKEIKTLEKQLEKLEKELEEL 92
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
78-186 9.13e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.13  E-value: 9.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749   78 NDSQLQEMAQLKMKHQEELTELHKKRGELAQLVIDLNNQMQQKDKEIQTNEAKIAECLQTISDLEADCLDLRtkLQDLEV 157
Cdd:COG4913   683 SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEER--FAAALG 760
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 158711749  158 ANQT------LKDEYDALQITFTALEEKLRKTTEE 186
Cdd:COG4913   761 DAVErelrenLEERIDALRARLNRAEEELERAMRA 795
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
81-246 9.21e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.98  E-value: 9.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749  81 QLQEMAQLKMKHQEELTELHKKRG-------ELAQLVIDLNNQMQQKDKEIQT--NEAKIAECLQTISDLEADCldlrtK 151
Cdd:COG4717  306 ELQALPALEELEEEELEELLAALGlppdlspEELLELLDRIEELQELLREAEEleEELQLEELEQEIAALLAEA-----G 380
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158711749 152 LQDLE--VANQTLKDEYDALQITFTALEEKLRKTTEENQELVTRWMAEKAQEANRLNAENEKDSRRRQARLQKELAEAAK 229
Cdd:COG4717  381 VEDEEelRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEA 460
                        170
                 ....*....|....*..
gi 158711749 230 EPLPVEQDDDIEVIVDE 246
Cdd:COG4717  461 ELEQLEEDGELAELLQE 477
 
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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