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Conserved domains on  [gi|79326969|ref|NP_001031833|]
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Galactose oxidase/kelch repeat superfamily protein [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
21-278 3.48e-26

N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 107.93  E-value: 3.48e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969  21 EWTPLPvsgSRASARYKHAAVVVDEKLYIVGGSRNGRYLSDVQVFDLRSLTWSSLKlktesssadniqeDDGSSLREAFP 100
Cdd:COG3055   2 TWSSLP---DLPTPRSEAAAALLDGKVYVAGGLSGGSASNSFEVYDPATNTWSELA-------------PLPGPPRHHAA 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969 101 AISDhrmikwGNKLLLIGGHSKKSSDNMLV----RFiDLETHSCGVIdvfGNVPASRGGHSITLVGSRVLVFGGEDKNRR 176
Cdd:COG3055  66 AVAQ------DGKLYVFGGFTGANPSSTPLndvyVY-DPATNTWTKL---APMPTPRGGATALLLDGKIYVVGGWDDGGN 135

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969 177 LlNDLHVLHLETMTWdvvETKQTRPVPRFDHTAATHSDRYLLIFGGCSHSI----------------------------- 227
Cdd:COG3055 136 V-AWVEVYDPATGTW---TQLAPLPTPRDHLAAAVLPDGKILVIGGRNGSGfsntwttlaplptaraghaaavlggkilv 211

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 79326969 228 ------FYSDLHILDLQTMEWSQphvQGDVVTPRAGHAGITIDENWYIVGGGDNSTG 278
Cdd:COG3055 212 fggesgFSDEVEAYDPATNTWTA---LGELPTPRHGHAAVLTDGKVYVIGGETKPGV 265
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
399-502 6.48e-09

Uncharacterized protein, contains DUF3084 domain [Function unknown];


:

Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 57.60  E-value: 6.48e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969 399 RNRIDTIKEEKRALESSIAETQVENAKLREKIDEVNSSHTELSQELQSVEGQLISERSRCFKLEAQIAELQKALE--SGQ 476
Cdd:COG4372 100 QEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQalSEA 179

                        90       100
                ....*....|....*....|....*...
gi 79326969 477 SIEAEVEMLRRQ--RSASDEEEDGTVQR 502
Cdd:COG4372 180 EAEQALDELLKEanRNAEKEEELAEAEK 207
 
Name Accession Description Interval E-value
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
21-278 3.48e-26

N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 107.93  E-value: 3.48e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969  21 EWTPLPvsgSRASARYKHAAVVVDEKLYIVGGSRNGRYLSDVQVFDLRSLTWSSLKlktesssadniqeDDGSSLREAFP 100
Cdd:COG3055   2 TWSSLP---DLPTPRSEAAAALLDGKVYVAGGLSGGSASNSFEVYDPATNTWSELA-------------PLPGPPRHHAA 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969 101 AISDhrmikwGNKLLLIGGHSKKSSDNMLV----RFiDLETHSCGVIdvfGNVPASRGGHSITLVGSRVLVFGGEDKNRR 176
Cdd:COG3055  66 AVAQ------DGKLYVFGGFTGANPSSTPLndvyVY-DPATNTWTKL---APMPTPRGGATALLLDGKIYVVGGWDDGGN 135

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969 177 LlNDLHVLHLETMTWdvvETKQTRPVPRFDHTAATHSDRYLLIFGGCSHSI----------------------------- 227
Cdd:COG3055 136 V-AWVEVYDPATGTW---TQLAPLPTPRDHLAAAVLPDGKILVIGGRNGSGfsntwttlaplptaraghaaavlggkilv 211

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 79326969 228 ------FYSDLHILDLQTMEWSQphvQGDVVTPRAGHAGITIDENWYIVGGGDNSTG 278
Cdd:COG3055 212 fggesgFSDEVEAYDPATNTWTA---LGELPTPRHGHAAVLTDGKVYVIGGETKPGV 265
Kelch_1 pfam01344
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 34-75 4.25e-10

Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six copies of the motif. It has been shown that Swiss:Q04652 is related to Galactose Oxidase for which a structure has been solved. The kelch motif forms a beta sheet. Several of these sheets associate to form a beta propeller structure as found in pfam00064, pfam00400 and pfam00415.


Pssm-ID: 396078 [Multi-domain]  Cd Length: 46  Bit Score: 54.93  E-value: 4.25e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 79326969    34 ARYKHAAVVVDEKLYIVGGSRNGRYLSDVQVFDLRSLTWSSL 75
Cdd:pfam01344   1 RRSGAGVVVVGGKIYVIGGFDGNQSLNSVEVYDPETNTWSKL 42
PLN02193 PLN02193
nitrile-specifier protein
 147-336 4.47e-09

nitrile-specifier protein


Pssm-ID: 177844 [Multi-domain]  Cd Length: 470  Bit Score: 58.81  E-value: 4.47e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969  147 GNVPASRGGHSITLVGSRVLVFGGE-DKNRRLLNDLHVLHLETMTWDVveTKQTRPVP-------RFDHTAAThsdryLL 218
Cdd:PLN02193 160 GEGPGLRCSHGIAQVGNKIYSFGGEfTPNQPIDKHLYVFDLETRTWSI--SPATGDVPhlsclgvRMVSIGST-----LY 232

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969  219 IFGGCSHSIFYSDLHILDLQTMEWS--QPHVQGDvvTPRAGHAGITIDENWYIVgGGDNSTGCLETL-VLNMSKLVW-ST 294
Cdd:PLN02193 233 VFGGRDASRQYNGFYSFDTTTNEWKllTPVEEGP--TPRSFHSMAADEENVYVF-GGVSATARLKTLdSYNIVDKKWfHC 309

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 79326969  295 STHVEARHPLASEGLSVCSASVFgenilVAFgGYNGKYNNDI 336
Cdd:PLN02193 310 STPGDSFSIRGGAGLEVVQGKVW-----VVY-GFNGCEVDDV 345
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
399-502 6.48e-09

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 57.60  E-value: 6.48e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969 399 RNRIDTIKEEKRALESSIAETQVENAKLREKIDEVNSSHTELSQELQSVEGQLISERSRCFKLEAQIAELQKALE--SGQ 476
Cdd:COG4372 100 QEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQalSEA 179

                        90       100
                ....*....|....*....|....*...
gi 79326969 477 SIEAEVEMLRRQ--RSASDEEEDGTVQR 502
Cdd:COG4372 180 EAEQALDELLKEanRNAEKEEELAEAEK 207
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 399-497 2.80e-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: 46.97  E-value: 2.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969    399 RNRIDTIKEEKRALESSIAETQVENAKLREKIDEVNSSHTELSQELQSVEGQLISERSRCFKLEAQIAELQKALESGQSI 478
Cdd:TIGR02168  238 REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQ 317

                           90
                   ....*....|....*....
gi 79326969    479 EAEVEmLRRQRSASDEEED 497
Cdd:TIGR02168  318 LEELE-AQLEELESKLDEL 335
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
395-494 3.14e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.60  E-value: 3.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969  395 ERDIRNRIDTIKEEKRALESSIAETQVENA---KLREKIDEVNSSHTElsQELQSVEGQLISERSRCFKLEAQIAELQKA 471
Cdd:PRK03918 611 EKELEREEKELKKLEEELDKAFEELAETEKrleELRKELEELEKKYSE--EEYEELREEYLELSRELAGLRAELEELEKR 688

                         90       100
                 ....*....|....*....|...
gi 79326969  472 LEsgqSIEAEVEMLRRQRSASDE 494
Cdd:PRK03918 689 RE---EIKKTLEKLKEELEEREK 708
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 409-487 9.36e-05

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 45.17  E-value: 9.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969    409 KRALESSIAETQVENAKLREKIDEVNSSHTELSQELQSVEGQLISE---RSRCFK----LEAQIAELQKALESGQSIEAE 481
Cdd:pfam01576  210 KRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEEtaqKNNALKkireLEAQISELQEDLESERAARNK 289


                   ....*.
gi 79326969    482 VEMLRR 487
Cdd:pfam01576  290 AEKQRR 295
Kelch smart00612
Kelch domain;
46-75 4.40e-04

Kelch domain;


Pssm-ID: 128874 [Multi-domain]  Cd Length: 47  Bit Score: 37.92  E-value: 4.40e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 79326969     46 KLYIVGGSRNGRYLSDVQVFDLRSLTWSSL 75
Cdd:smart00612   1 KIYVVGGFDGGQRLKSVEVYDPETNKWTPL 30
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 397-488 7.82e-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: 41.54  E-value: 7.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969    397 DIRNRIDTIKEEKRALESSIAETQV----ENAKLREK-------IDEVNSSHTELSQELQSVEGQLISERSRCFKLEAQI 465
Cdd:smart00787 176 KLRDRKDALEEELRQLKQLEDELEDcdptELDRAKEKlkkllqeIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEI 255

                           90       100
                   ....*....|....*....|....
gi 79326969    466 AELQKALESGQSIEA-EVEMLRRQ 488
Cdd:smart00787 256 AEAEKKLEQCRGFTFkEIEKLKEQ 279
 
Name Accession Description Interval E-value
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
21-278 3.48e-26

N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 107.93  E-value: 3.48e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969  21 EWTPLPvsgSRASARYKHAAVVVDEKLYIVGGSRNGRYLSDVQVFDLRSLTWSSLKlktesssadniqeDDGSSLREAFP 100
Cdd:COG3055   2 TWSSLP---DLPTPRSEAAAALLDGKVYVAGGLSGGSASNSFEVYDPATNTWSELA-------------PLPGPPRHHAA 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969 101 AISDhrmikwGNKLLLIGGHSKKSSDNMLV----RFiDLETHSCGVIdvfGNVPASRGGHSITLVGSRVLVFGGEDKNRR 176
Cdd:COG3055  66 AVAQ------DGKLYVFGGFTGANPSSTPLndvyVY-DPATNTWTKL---APMPTPRGGATALLLDGKIYVVGGWDDGGN 135

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969 177 LlNDLHVLHLETMTWdvvETKQTRPVPRFDHTAATHSDRYLLIFGGCSHSI----------------------------- 227
Cdd:COG3055 136 V-AWVEVYDPATGTW---TQLAPLPTPRDHLAAAVLPDGKILVIGGRNGSGfsntwttlaplptaraghaaavlggkilv 211

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 79326969 228 ------FYSDLHILDLQTMEWSQphvQGDVVTPRAGHAGITIDENWYIVGGGDNSTG 278
Cdd:COG3055 212 fggesgFSDEVEAYDPATNTWTA---LGELPTPRHGHAAVLTDGKVYVIGGETKPGV 265
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
111-338 2.35e-21

N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 94.07  E-value: 2.35e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969 111 GNKLLLIGGHSKKSSDNMLVRFiDLETHSCGVIDVFgnvPASRGGHSITLV-GSRVLVFGGEDKN---RRLLNDLHVLHL 186
Cdd:COG3055  22 DGKVYVAGGLSGGSASNSFEVY-DPATNTWSELAPL---PGPPRHHAAAVAqDGKLYVFGGFTGAnpsSTPLNDVYVYDP 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969 187 ETMTWdvvETKQTRPVPRFDHTAATHSDRyLLIFGGCSHSIFYSDLHILDLQTMEWSQphvQGDVVTPRAGHAGITIDEN 266
Cdd:COG3055  98 ATNTW---TKLAPMPTPRGGATALLLDGK-IYVVGGWDDGGNVAWVEVYDPATGTWTQ---LAPLPTPRDHLAAAVLPDG 170

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 79326969 267 WYIVGGGDNSTGcletlvlnmSKLVWSTSthveARHPLASEGLsvcSASVFGENILVaFGGYNGkYNNDIFV 338
Cdd:COG3055 171 KILVIGGRNGSG---------FSNTWTTL----APLPTARAGH---AAAVLGGKILV-FGGESG-FSDEVEA 224
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
16-224 8.16e-20

N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 89.44  E-value: 8.16e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969  16 NLAHDEWTPLPVSgsrASARYKHAAVVVDEKLYIVGGSRNGRYLSDVQVFDLRSLTWSSLKlktesssadniqedDGSSL 95
Cdd:COG3055  96 DPATNTWTKLAPM---PTPRGGATALLLDGKIYVVGGWDDGGNVAWVEVYDPATGTWTQLA--------------PLPTP 158

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969  96 REAFPAIsdhrmIKWGNKLLLIGGHSKKSSDNmlvRFIDLETHscgvidvfgnvPASRGGHSITLVGSRVLVFGGEDKNr 175
Cdd:COG3055 159 RDHLAAA-----VLPDGKILVIGGRNGSGFSN---TWTTLAPL-----------PTARAGHAAAVLGGKILVFGGESGF- 218

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 79326969 176 rlLNDLHVLHLETMTWDVVETKqtrPVPRFDHTAATHSDRyLLIFGGCS 224
Cdd:COG3055 219 --SDEVEAYDPATNTWTALGEL---PTPRHGHAAVLTDGK-VYVIGGET 261
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
147-337 1.15e-19

N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 89.06  E-value: 1.15e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969 147 GNVPASRGGHSITLVGSRVLVFGGEDKNRrLLNDLHVLHLETMTWdvvETKQTRPVPRFDHTAATHSDRYLLIFGGCS-- 224
Cdd:COG3055   7 PDLPTPRSEAAAALLDGKVYVAGGLSGGS-ASNSFEVYDPATNTW---SELAPLPGPPRHHAAAVAQDGKLYVFGGFTga 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969 225 --HSIFYSDLHILDLQTMEWSQphvQGDVVTPRAGHAGITIDENWYIVGGGDNSTGCLETLVLNMSKLVWSTSTHVearh 302
Cdd:COG3055  83 npSSTPLNDVYVYDPATNTWTK---LAPMPTPRGGATALLLDGKIYVVGGWDDGGNVAWVEVYDPATGTWTQLAPL---- 155

                       170       180       190
                ....*....|....*....|....*....|....*
gi 79326969 303 PLASEGLsvcSASVFGENILVAFGGYNGKYNNDIF 337
Cdd:COG3055 156 PTPRDHL---AAAVLPDGKILVIGGRNGSGFSNTW 187
Kelch_1 pfam01344
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 34-75 4.25e-10

Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six copies of the motif. It has been shown that Swiss:Q04652 is related to Galactose Oxidase for which a structure has been solved. The kelch motif forms a beta sheet. Several of these sheets associate to form a beta propeller structure as found in pfam00064, pfam00400 and pfam00415.


Pssm-ID: 396078 [Multi-domain]  Cd Length: 46  Bit Score: 54.93  E-value: 4.25e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 79326969    34 ARYKHAAVVVDEKLYIVGGSRNGRYLSDVQVFDLRSLTWSSL 75
Cdd:pfam01344   1 RRSGAGVVVVGGKIYVIGGFDGNQSLNSVEVYDPETNTWSKL 42
PLN02193 PLN02193
nitrile-specifier protein
 147-336 4.47e-09

nitrile-specifier protein


Pssm-ID: 177844 [Multi-domain]  Cd Length: 470  Bit Score: 58.81  E-value: 4.47e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969  147 GNVPASRGGHSITLVGSRVLVFGGE-DKNRRLLNDLHVLHLETMTWDVveTKQTRPVP-------RFDHTAAThsdryLL 218
Cdd:PLN02193 160 GEGPGLRCSHGIAQVGNKIYSFGGEfTPNQPIDKHLYVFDLETRTWSI--SPATGDVPhlsclgvRMVSIGST-----LY 232

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969  219 IFGGCSHSIFYSDLHILDLQTMEWS--QPHVQGDvvTPRAGHAGITIDENWYIVgGGDNSTGCLETL-VLNMSKLVW-ST 294
Cdd:PLN02193 233 VFGGRDASRQYNGFYSFDTTTNEWKllTPVEEGP--TPRSFHSMAADEENVYVF-GGVSATARLKTLdSYNIVDKKWfHC 309

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 79326969  295 STHVEARHPLASEGLSVCSASVFgenilVAFgGYNGKYNNDI 336
Cdd:PLN02193 310 STPGDSFSIRGGAGLEVVQGKVW-----VVY-GFNGCEVDDV 345
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
399-502 6.48e-09

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 57.60  E-value: 6.48e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969 399 RNRIDTIKEEKRALESSIAETQVENAKLREKIDEVNSSHTELSQELQSVEGQLISERSRCFKLEAQIAELQKALE--SGQ 476
Cdd:COG4372 100 QEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQalSEA 179

                        90       100
                ....*....|....*....|....*...
gi 79326969 477 SIEAEVEMLRRQ--RSASDEEEDGTVQR 502
Cdd:COG4372 180 EAEQALDELLKEanRNAEKEEELAEAEK 207
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
396-497 6.06e-08

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 54.91  E-value: 6.06e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969 396 RDIRNRIDTIKEEKRALESSIAETQVENAKLREKIDEVNSSHTELSQELQSVEGQLISERSRCFKLEAQIAELQKALESG 475
Cdd:COG4372  34 RKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEEL 113

                        90       100
                ....*....|....*....|....*.
gi 79326969 476 QS----IEAEVEMLRRQRSASDEEED 497
Cdd:COG4372 114 QEeleeLQKERQDLEQQRKQLEAQIA 139
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
396-495 2.00e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 52.98  E-value: 2.00e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969 396 RDIRNRIDTIKEEKRALESSIAETQVENAKLREKIDEVNSSHTELSQELQSVEGQLISERSRCFKLEAQIAELQKAL--- 472
Cdd:COG4372  48 EQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERqdl 127

                        90       100
                ....*....|....*....|....
gi 79326969 473 -ESGQSIEAEVEMLRRQRSASDEE 495
Cdd:COG4372 128 eQQRKQLEAQIAELQSEIAEREEE 151
PLN02153 PLN02153
epithiospecifier protein
 147-282 2.17e-07

epithiospecifier protein


Pssm-ID: 177814 [Multi-domain]  Cd Length: 341  Bit Score: 52.68  E-value: 2.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969  147 GNVPASRGGHSITLVGSRVLVFGGEDK-NRRLLNDLHVLHLETMTWDVVETKQTRPVPRFDHTAATHSDRYLLIFGGCSH 225
Cdd:PLN02153  17 GKGPGPRCSHGIAVVGDKLYSFGGELKpNEHIDKDLYVFDFNTHTWSIAPANGDVPRISCLGVRMVAVGTKLYIFGGRDE 96

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 79326969  226 SIFYSDLHILDLQTMEWSQPHVQGDVVTP--RAGHAgITIDENWYIVGGGDNSTGCLET 282
Cdd:PLN02153  97 KREFSDFYSYDTVKNEWTFLTKLDEEGGPeaRTFHS-MASDENHVYVFGGVSKGGLMKT 154
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 397-496 2.90e-07

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 51.46  E-value: 2.90e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969 397 DIRNRIDTIKEEKRALESSIAETQVENAKLREKIDEVNSSHTELSQELQSVEGQLisersrcFKLEAQIAELQKALESG- 475
Cdd:COG1579  14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEI-------EEVEARIKKYEEQLGNVr 86

                        90       100
                ....*....|....*....|....*.
gi 79326969 476 -----QSIEAEVEMLRRQRSASDEEE 496
Cdd:COG1579  87 nnkeyEALQKEIESLKRRISDLEDEI 112
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
396-496 5.78e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 51.83  E-value: 5.78e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969 396 RDIRNRIDTIKEEKRALESSIAETQVENAKLREKIDEVNSSHTELSQELQSVEGQLISERSRCFKLEAQIAELQKALesg 475
Cdd:COG4372  83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQL--- 159

                        90       100
                ....*....|....*....|.
gi 79326969 476 QSIEAEVEMLRRQRSASDEEE 496
Cdd:COG4372 160 ESLQEELAALEQELQALSEAE 180
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
396-489 1.56e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 50.92  E-value: 1.56e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969 396 RDIRNRIDTIKEEKRALESSIAETQVENAKLREKIDevnssHTELSQELQSVEGQLISERSRCFKLEAQIAELQKALESG 475
Cdd:COG4717  91 AELQEELEELEEELEELEAELEELREELEKLEKLLQ-----LLPLYQELEALEAELAELPERLEELEERLEELRELEEEL 165

                        90
                ....*....|....
gi 79326969 476 QSIEAEVEMLRRQR 489
Cdd:COG4717 166 EELEAELAELQEEL 179
Kelch_4 pfam13418
Galactose oxidase, central domain;
203-244 1.96e-06

Galactose oxidase, central domain;


Pssm-ID: 433191 [Multi-domain]  Cd Length: 49  Bit Score: 44.91  E-value: 1.96e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 79326969   203 PRFDHTAATHSDRYLLIFGGCS-HSIFYSDLHILDLQTMEWSQ 244
Cdd:pfam13418   1 PRAYHTSTSIPDDTIYLFGGEGeDGTLLSDLWVFDLSTNEWTR 43
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 396-482 4.28e-06

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 48.99  E-value: 4.28e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969 396 RDIRNRIDTIKEEKRALESSIAETQVENAKLREKIDEVNSSHTELSQELQSVEGQLISERSRCFKLEAQIAELQKALESG 475
Cdd:COG4942  23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102


                ....*..
gi 79326969 476 QSIEAEV 482
Cdd:COG4942 103 KEELAEL 109
Kelch_3 pfam13415
Galactose oxidase, central domain;
214-263 6.03e-06

Galactose oxidase, central domain;


Pssm-ID: 433188 [Multi-domain]  Cd Length: 49  Bit Score: 43.43  E-value: 6.03e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 79326969   214 DRYLLIFGGC--SHSIFYSDLHILDLQTMEWSQPhvqGDVVTPRAGHAGITI 263
Cdd:pfam13415   1 GDKLYIFGGLgfDGQTRLNDLYVYDLDTNTWTQI---GDLPPPRSGHSATYI 49
Kelch_6 pfam13964
Kelch motif;
155-204 6.47e-06

Kelch motif;


Pssm-ID: 404790 [Multi-domain]  Cd Length: 50  Bit Score: 43.48  E-value: 6.47e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 79326969   155 GHSITLVGSRVLVFGGEDKNRRLLNDLHVLHLETMTWDVVETKqtrPVPR 204
Cdd:pfam13964   4 FHSVVSVGGYIYVFGGYTNASPALNKLEVYNPLTKSWEELPPL---PTPR 50
PLN02153 PLN02153
epithiospecifier protein
 21-327 1.57e-05

epithiospecifier protein


Pssm-ID: 177814 [Multi-domain]  Cd Length: 341  Bit Score: 46.90  E-value: 1.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969   21 EWTPLPVSGSRASA-RYKHAAVVVDEKLYIVGG--SRNGRYLSDVQVFDLRSLTWSslklktesssadnIQEDDGSSlre 97
Cdd:PLN02153   8 GWIKVEQKGGKGPGpRCSHGIAVVGDKLYSFGGelKPNEHIDKDLYVFDFNTHTWS-------------IAPANGDV--- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969   98 afPAIS--DHRMIKWGNKLLLIGGHSKKSSDNMLVRF--IDLETHSCGVIDVFGNvPASRGGHSITLVGSRVLVFGGEDK 173
Cdd:PLN02153  72 --PRISclGVRMVAVGTKLYIFGGRDEKREFSDFYSYdtVKNEWTFLTKLDEEGG-PEARTFHSMASDENHVYVFGGVSK 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969  174 NRRLLNDLHVLHLEtmTWDVVETKQTR---PVPRFDHTA----ATHSDRYLLIFGGCSHSI------FYSD-LHILDLQT 239
Cdd:PLN02153 149 GGLMKTPERFRTIE--AYNIADGKWVQlpdPGENFEKRGgagfAVVQGKIWVVYGFATSILpggksdYESNaVQFFDPAS 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969  240 MEWSQPHVQGDVVTPRAGHAGITIDENWYIVGG-------GDNSTGCL--ETLVLNMSKLVWSTSThvEARHPLASEG-L 309
Cdd:PLN02153 227 GKWTEVETTGAKPSARSVFAHAVVGKYIIIFGGevwpdlkGHLGPGTLsnEGYALDTETLVWEKLG--ECGEPAMPRGwT 304

                        330
                 ....*....|....*...
gi 79326969  310 SVCSASVFGENILVAFGG 327
Cdd:PLN02153 305 AYTTATVYGKNGLLMHGG 322
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
390-495 1.63e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.20  E-value: 1.63e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969 390 GNSLPERDIRNRIDTIKEEKR------ALESSIAETQVENAKLREKIDEVNSSHTELSQELQSVEGQLISERSRCFKLEA 463
Cdd:COG4372   1 GDRLGEKVGKARLSLFGLRPKtgiliaALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEE 80

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 79326969 464 QIAELQKALESGQS----IEAEVEMLRRQRSASDEE 495
Cdd:COG4372  81 ELEELNEQLQAAQAelaqAQEELESLQEEAEELQEE 116
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 402-489 1.93e-05

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: 46.07  E-value: 1.93e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969 402 IDTIKEEKRALESSIAETQVENAKLREKIDEVNSSHTELSQELQSVEGQLISERSrcfKLEAQIAELQKALES-GQSIEA 480
Cdd:COG1579  98 IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELA---ELEAELEELEAEREElAAKIPP 174

                        90
                ....*....|...
gi 79326969 481 EV----EMLRRQR 489
Cdd:COG1579 175 ELlalyERIRKRK 187
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 396-503 2.79e-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: 2.79e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969 396 RDIRNRIDTIKEEKRALESSIAETQVENAKLREKIDEVNSSHTELSQELQSVEGQLISERSRCFKLEAQIAELQKALESG 475
Cdd:COG1196 277 EELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356

                        90       100
                ....*....|....*....|....*...
gi 79326969 476 QSIEAEVEMLRRQRSASDEEEDGTVQRQ 503
Cdd:COG1196 357 EAELAEAEEALLEAEAELAEAEEELEEL 384
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 399-497 2.80e-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: 46.97  E-value: 2.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969    399 RNRIDTIKEEKRALESSIAETQVENAKLREKIDEVNSSHTELSQELQSVEGQLISERSRCFKLEAQIAELQKALESGQSI 478
Cdd:TIGR02168  238 REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQ 317

                           90
                   ....*....|....*....
gi 79326969    479 EAEVEmLRRQRSASDEEED 497
Cdd:TIGR02168  318 LEELE-AQLEELESKLDEL 335
Kelch_4 pfam13418
Galactose oxidase, central domain;
153-197 3.03e-05

Galactose oxidase, central domain;


Pssm-ID: 433191 [Multi-domain]  Cd Length: 49  Bit Score: 41.44  E-value: 3.03e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 79326969   153 RGGHSITLVGS-RVLVFGGEDKNRRLLNDLHVLHLETMTWDVVETK 197
Cdd:pfam13418   2 RAYHTSTSIPDdTIYLFGGEGEDGTLLSDLWVFDLSTNEWTRLGSL 47
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
395-494 3.14e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.60  E-value: 3.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969  395 ERDIRNRIDTIKEEKRALESSIAETQVENA---KLREKIDEVNSSHTElsQELQSVEGQLISERSRCFKLEAQIAELQKA 471
Cdd:PRK03918 611 EKELEREEKELKKLEEELDKAFEELAETEKrleELRKELEELEKKYSE--EEYEELREEYLELSRELAGLRAELEELEKR 688

                         90       100
                 ....*....|....*....|...
gi 79326969  472 LEsgqSIEAEVEMLRRQRSASDE 494
Cdd:PRK03918 689 RE---EIKKTLEKLKEELEEREK 708
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 395-497 3.55e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 3.55e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969 395 ERDIR---NRIDTIKEEKRALESSIAETQVENAKLREKIDEVNSSHTELSQELQSVEGQLISERSRCFKLEAQIAELQKA 471
Cdd:COG1196 224 ELEAElllLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303

                        90       100
                ....*....|....*....|....*...
gi 79326969 472 LESGQ--SIEAEVEMLRRQRSASDEEED 497
Cdd:COG1196 304 IARLEerRRELEERLEELEEELAELEEE 331
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 396-498 3.63e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 45.91  E-value: 3.63e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969 396 RDIRNRIDTIKEEKRALESSIAETQVENAKLREKIDEVNSSHTELSQELQSVEGQLISERSRCFKLEAQIAELQKALesg 475
Cdd:COG4942 146 PARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEA--- 222

                        90       100
                ....*....|....*....|...
gi 79326969 476 QSIEAEVEMLRRQRSASDEEEDG 498
Cdd:COG4942 223 EELEALIARLEAEAAAAAERTPA 245
Kelch_5 pfam13854
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 33-69 4.02e-05

Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six copies of the motif. It has been shown that Swiss:Q04652 is related to Galactose Oxidase for which a structure has been solved. The kelch motif forms a beta sheet. Several of these sheets associate to form a beta propeller structure as found in pfam00064, pfam00400 and pfam00415.


Pssm-ID: 433528 [Multi-domain]  Cd Length: 41  Bit Score: 40.63  E-value: 4.02e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 79326969    33 SARYKHAAVVVDEKLYIVGG--SRNGRYLSDVQVFDLRS 69
Cdd:pfam13854   2 VPRYGHCAVTVGDYIYLYGGytGGEGQPSDDVYVLSLPT 40
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 395-497 4.88e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.08  E-value: 4.88e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969 395 ERDIRNRIDTIKEEKRALESSIAETQVENAKLREKIDEVNSSHTELSQELQSVEGQLISERSRCFKLEAQIAELQKALEs 474
Cdd:COG1196 290 EYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL- 368

                        90       100
                ....*....|....*....|...
gi 79326969 475 gqsiEAEVEMLRRQRSASDEEED 497
Cdd:COG1196 369 ----EAEAELAEAEEELEELAEE 387
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
386-508 7.11e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 45.39  E-value: 7.11e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969 386 LNGNGNSLPERDIRNRIDTIKEEKRALESSIAETQV---EN----AKLREKIDEVNSS-HTELSQELQSVEGQLISERSR 457
Cdd:COG3206 249 LGSGPDALPELLQSPVIQQLRAQLAELEAELAELSArytPNhpdvIALRAQIAALRAQlQQEAQRILASLEAELEALQAR 328

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 79326969 458 CFKLEAQIAELQKALESGQSIEAEVEMLRRQRSASDEEEDGTVQRQGSAGV 508
Cdd:COG3206 329 EASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARL 379
Kelch_4 pfam13418
Galactose oxidase, central domain;
34-75 7.42e-05

Galactose oxidase, central domain;


Pssm-ID: 433191 [Multi-domain]  Cd Length: 49  Bit Score: 40.29  E-value: 7.42e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 79326969    34 ARYKHAAVVV-DEKLYIVGG-SRNGRYLSDVQVFDLRSLTWSSL 75
Cdd:pfam13418   1 PRAYHTSTSIpDDTIYLFGGeGEDGTLLSDLWVFDLSTNEWTRL 44
Kelch_6 pfam13964
Kelch motif;
34-75 9.01e-05

Kelch motif;


Pssm-ID: 404790 [Multi-domain]  Cd Length: 50  Bit Score: 40.01  E-value: 9.01e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 79326969    34 ARYKHAAVVVDEKLYIVGG-SRNGRYLSDVQVFDLRSLTWSSL 75
Cdd:pfam13964   1 PRTFHSVVSVGGYIYVFGGyTNASPALNKLEVYNPLTKSWEEL 43
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 409-487 9.36e-05

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 45.17  E-value: 9.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969    409 KRALESSIAETQVENAKLREKIDEVNSSHTELSQELQSVEGQLISE---RSRCFK----LEAQIAELQKALESGQSIEAE 481
Cdd:pfam01576  210 KRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEEtaqKNNALKkireLEAQISELQEDLESERAARNK 289


                   ....*.
gi 79326969    482 VEMLRR 487
Cdd:pfam01576  290 AEKQRR 295
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
393-507 1.16e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.91  E-value: 1.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969  393 LPERDIRNRIDTIKEEKRALESsiAETQVENAKLR----EKIDEVNSSHTELSQELQSVEGQLisERSRCFKLEAQIAEL 468
Cdd:COG4913  218 LEEPDTFEAADALVEHFDDLER--AHEALEDAREQiellEPIRELAERYAAARERLAELEYLR--AALRLWFAQRRLELL 293

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 79326969  469 QKALESG----QSIEAEVEMLRRQRSASDEEEDG-TVQRQGSAG 507
Cdd:COG4913  294 EAELEELraelARLEAELERLEARLDALREELDElEAQIRGNGG 337
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 399-491 1.34e-04

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: 43.37  E-value: 1.34e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969 399 RNRIDTIKEEK--RALESSIAETQVENAKLREKIDEVNSSHTELSQELQSVEGQLISERSRcfkLEAQIAELQKALEsgq 476
Cdd:COG1579  79 EEQLGNVRNNKeyEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAE---LEEKKAELDEELA--- 152

                        90
                ....*....|....*
gi 79326969 477 SIEAEVEMLRRQRSA 491
Cdd:COG1579 153 ELEAELEELEAEREE 167
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 400-473 1.50e-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: 44.63  E-value: 1.50e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 79326969   400 NRIDTIKEEKRALESSIAETQVENAKLREKIDEVNSSHTELSQELQSVEGQLISERSRCFK--LEAQIAELQKALE 473
Cdd:TIGR04523 496 KELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKenLEKEIDEKNKEIE 571
Kelch_2 pfam07646
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 35-76 1.54e-04

Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six copies of the motif. It has been shown that Swiss:Q04652 is related to Galactose Oxidase for which a structure has been solved. The kelch motif forms a beta sheet. Several of these sheets associate to form a beta propeller structure as found in pfam00064, pfam00400 and pfam00415.


Pssm-ID: 462220 [Multi-domain]  Cd Length: 47  Bit Score: 39.24  E-value: 1.54e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 79326969    35 RYKHAAVVVDEKLYIVGGS--RNGRYLSDVQVFDLRSLTWSSLK 76
Cdd:pfam07646   2 RYPHASSVPGGKLYVVGGSdgLGDLSSSDVLVYDPETNVWTEVP 45
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 407-507 1.92e-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: 43.60  E-value: 1.92e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969 407 EEKRALESSIAETQVENAKLREKIDEVNSSHTELSQELQSVEGQLISERSRCFKLEAQIAELQKALESGQSIEAEVEMLR 486
Cdd:COG4942  20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99

                        90       100
                ....*....|....*....|.
gi 79326969 487 RQRSASDEEEDGTVQRQGSAG 507
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQP 120
Kelch_3 pfam13415
Galactose oxidase, central domain;
162-212 1.99e-04

Galactose oxidase, central domain;


Pssm-ID: 433188 [Multi-domain]  Cd Length: 49  Bit Score: 39.20  E-value: 1.99e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 79326969   162 GSRVLVFGGEDKNRR-LLNDLHVLHLETMTWDVVETKqtrPVPRFDHTAATH 212
Cdd:pfam13415   1 GDKLYIFGGLGFDGQtRLNDLYVYDLDTNTWTQIGDL---PPPRSGHSATYI 49
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
395-486 2.00e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.28  E-value: 2.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969  395 ERDIRNRIDTIKEEKRALESSIAETQVENAKLREKIDEVNSSH----------TELSQELQSVEGQLISERSRCFKLEAQ 464
Cdd:PRK03918 188 TENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVkeleelkeeiEELEKELESLEGSKRKLEEKIRELEER 267

                         90       100
                 ....*....|....*....|..
gi 79326969  465 IAELQKALESGQSIEAEVEMLR 486
Cdd:PRK03918 268 IEELKKEIEELEEKVKELKELK 289
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 404-497 2.14e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 2.14e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969 404 TIKEEKRALESS-----IAETQVENAKLREKIDEVNSSHTELSQELQSVEGQLISERSRCFKLEAQIAELQKAL-ESGQS 477
Cdd:COG1196 217 ELKEELKELEAEllllkLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEyELLAE 296

                        90       100
                ....*....|....*....|
gi 79326969 478 IEAEVEMLRRQRSASDEEED 497
Cdd:COG1196 297 LARLEQDIARLEERRRELEE 316
PHA03098 PHA03098
kelch-like protein; Provisional
 35-293 2.21e-04

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 43.99  E-value: 2.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969   35 RYKHAAVVVDEKLYIVGGS-RNGRYLSDVQVFDLRSLTWSSLKlktesssadniqedDGSSLREaFPAISDHRmikwgNK 113
Cdd:PHA03098 285 VYCFGSVVLNNVIYFIGGMnKNNLSVNSVVSYDTKTKSWNKVP--------------ELIYPRK-NPGVTVFN-----NR 344

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969  114 LLLIGGhskkSSDNMLVRFIDLETHSCGVIDVFGNVPASRGGHSITLVGSRVLVFGGEDKNRRLLNDLHVLHLETMTWDv 193
Cdd:PHA03098 345 IYVIGG----IYNSISLNTVESWKPGESKWREEPPLIFPRYNPCVVNVNNLIYVIGGISKNDELLKTVECFSLNTNKWS- 419

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969  194 veTKQTRPVPRFDHTAATHsDRYLLIFGGCSHS---IFYSDLHILDLQTMEWsqpHVQGDVVTPRAGHAGITIDENWYIV 270
Cdd:PHA03098 420 --KGSPLPISHYGGCAIYH-DGKIYVIGGISYIdniKVYNIVESYNPVTNKW---TELSSLNFPRINASLCIFNNKIYVV 493

                        250       260
                 ....*....|....*....|...
gi 79326969  271 GGGDNSTGCLETLVLNMSKLVWS 293
Cdd:PHA03098 494 GGDKYEYYINEIEVYDDKTNTWT 516
PHA03098 PHA03098
kelch-like protein; Provisional
 35-194 2.77e-04

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 43.60  E-value: 2.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969   35 RYKHAAVVVDEKLYIVGG-SRNGRYLSDVQVFDLRSLTWSSLklktessSADNIQEDDGSslreafpAISDHRMIkwgnk 113
Cdd:PHA03098 380 RYNPCVVNVNNLIYVIGGiSKNDELLKTVECFSLNTNKWSKG-------SPLPISHYGGC-------AIYHDGKI----- 440

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969  114 lLLIGGHSKKSSDNMLVRFIDLETHSCGVIDVFG-NVPasRGGHSITLVGSRVLVFGGeDKNRRLLNDLHVLHLETMTWD 192
Cdd:PHA03098 441 -YVIGGISYIDNIKVYNIVESYNPVTNKWTELSSlNFP--RINASLCIFNNKIYVVGG-DKYEYYINEIEVYDDKTNTWT 516


                 ..
gi 79326969  193 VV 194
Cdd:PHA03098 517 LF 518
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 381-480 4.25e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.51  E-value: 4.25e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969 381 PANPTLNGNGNSLpeRDIRNRIDTIKEEKRALESSIAETQVENAKLREKIDEVNSSHTELSQELQSVEgQLISERSRcfK 460
Cdd:COG3883  13 FADPQIQAKQKEL--SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAE-AEIEERRE--E 87

                        90       100
                ....*....|....*....|
gi 79326969 461 LEAQIAELQKALESGQSIEA 480
Cdd:COG3883  88 LGERARALYRSGGSVSYLDV 107
Kelch smart00612
Kelch domain;
46-75 4.40e-04

Kelch domain;


Pssm-ID: 128874 [Multi-domain]  Cd Length: 47  Bit Score: 37.92  E-value: 4.40e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 79326969     46 KLYIVGGSRNGRYLSDVQVFDLRSLTWSSL 75
Cdd:smart00612   1 KIYVVGGFDGGQRLKSVEVYDPETNKWTPL 30
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 397-511 4.90e-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: 43.13  E-value: 4.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969    397 DIRNRIDTIKEE--------------KRALESSIAETQVENAKLREKIDEVNSSHTELSQELQSVEGQL-------ISER 455
Cdd:TIGR02169  389 DYREKLEKLKREinelkreldrlqeeLQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLeqlaadlSKYE 468

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 79326969    456 SRCFKLEAQIAELQKALESGQSieaEVEMLRRQRSASDEEEDG-----TVQRQGSAGVWGL 511
Cdd:TIGR02169  469 QELYDLKEEYDRVEKELSKLQR---ELAEAEAQARASEERVRGgraveEVLKASIQGVHGT 526
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 394-482 5.44e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.74  E-value: 5.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969    394 PERDIRNRIDTIKEEKRALESSIAETQVENAKLREKIDEVNSSHTELSQELQSVEGQLISERSRCFKLEAQIAELQKALE 473
Cdd:TIGR02168  867 LIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLS 946


                   ....*....
gi 79326969    474 SGQSIEAEV 482
Cdd:TIGR02168  947 EEYSLTLEE 955
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
398-502 5.53e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 42.70  E-value: 5.53e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969 398 IRNRIDTIKEEkraLESsiAETQVENAKLREKIDEVNSSHTELSQELQSVEGQLISERSRCFKLEAQIAELQKALESGQS 477
Cdd:COG3206 180 LEEQLPELRKE---LEE--AEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPD 254

                        90       100       110
                ....*....|....*....|....*....|.
gi 79326969 478 IEAEV------EMLRRQRSASDEEEDGTVQR 502
Cdd:COG3206 255 ALPELlqspviQQLRAQLAELEAELAELSAR 285
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 387-497 5.54e-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: 42.57  E-value: 5.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969   387 NGNGNSLPERDIRNRiDTIKEEKRALESSIAETQVENAKLREKID-------EVNSSHTELSQELQSVEGQLISERSRCF 459
Cdd:pfam07888  54 NRQREKEKERYKRDR-EQWERQRRELESRVAELKEELRQSREKHEeleekykELSASSEELSEEKDALLAQRAAHEARIR 132

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 79326969   460 KLEAQIAEL-QKALEsgqsIEAEVEMLR-RQRSA----SDEEED 497
Cdd:pfam07888 133 ELEEDIKTLtQRVLE----RETELERMKeRAKKAgaqrKEEEAE 172
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 408-488 5.62e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.12  E-value: 5.62e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969 408 EKRALESSIAETQVENAKLREKIDEVNSSHTELSQELQSVEGQLIsersrcfKLEAQIAELQKALESGQS-IEAEVEMLR 486
Cdd:COG3883  17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELE-------ALQAEIDKLQAEIAEAEAeIEERREELG 89


                ..
gi 79326969 487 RQ 488
Cdd:COG3883  90 ER 91
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 396-503 6.18e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 42.75  E-value: 6.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969    396 RDIRNRIDTIKEEKRALESSIAETQVE-------NAKLREKIDEVNSSHTELSQELQSVEGQLISERSRCFKLEAQIAEL 468
Cdd:TIGR02169  698 RRIENRLDELSQELSDASRKIGEIEKEieqleqeEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKL 777

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 79326969    469 QKALEsgqSIEAEVEMLR-RQRSASDEEEDGTVQRQ 503
Cdd:TIGR02169  778 EEALN---DLEARLSHSRiPEIQAELSKLEEEVSRI 810
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 397-497 6.22e-04

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: 41.45  E-value: 6.22e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969 397 DIRNRIDTIKEEKRALESSIAETQVENAKLREKIDEVNSSH--TELSQELQSVEG--QLISERSRCF-----KLEAQIAE 467
Cdd:COG1579  49 AAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKeyEALQKEIESLKRriSDLEDEILELmerieELEEELAE 128

                        90       100       110
                ....*....|....*....|....*....|.
gi 79326969 468 LQKALESGQS-IEAEVEMLRRQRSASDEEED 497
Cdd:COG1579 129 LEAELAELEAeLEEKKAELDEELAELEAELE 159
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
399-506 6.74e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.59  E-value: 6.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969  399 RNRIDTIKEEKRALESSIAETQVENAKLREKIDEVNSSHTELsQELQSVEGQLISERSrcfkLEAQIAELQKALESGQSI 478
Cdd:COG4913  609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAL-QRLAEYSWDEIDVAS----AEREIAELEAELERLDAS 683

                         90       100
                 ....*....|....*....|....*...
gi 79326969  479 EAEVEMLRRQRSASDEEEDGTVQRQGSA 506
Cdd:COG4913  684 SDDLAALEEQLEELEAELEELEEELDEL 711
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 397-488 7.82e-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: 41.54  E-value: 7.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969    397 DIRNRIDTIKEEKRALESSIAETQV----ENAKLREK-------IDEVNSSHTELSQELQSVEGQLISERSRCFKLEAQI 465
Cdd:smart00787 176 KLRDRKDALEEELRQLKQLEDELEDcdptELDRAKEKlkkllqeIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEI 255

                           90       100
                   ....*....|....*....|....
gi 79326969    466 AELQKALESGQSIEA-EVEMLRRQ 488
Cdd:smart00787 256 AEAEKKLEQCRGFTFkEIEKLKEQ 279
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 413-504 7.86e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.35  E-value: 7.86e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969    413 ESSIAETQVENAKLREKIDEVNSSHTELSQELQSVEGQLISERSRCFKLEAQIAELQKAL----ESGQSIEAEVEML-RR 487
Cdd:TIGR02168  669 NSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQIsalrKDLARLEAEVEQLeER 748

                           90
                   ....*....|....*..
gi 79326969    488 QRSASDEEEDGTVQRQG 504
Cdd:TIGR02168  749 IAQLSKELTELEAEIEE 765
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
392-489 7.96e-04

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 41.43  E-value: 7.96e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969 392 SLPERDIRNRIDTIKEEKRALESSIAETQVENAKLREKIDEVNSSHTELSQELQsvegQLISERSrcfKLEAQIAEL--- 468
Cdd:COG1340   7 SSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQ----ELREKRD---ELNEKVKELkee 79

                        90       100
                ....*....|....*....|..
gi 79326969 469 -QKALESGQSIEAEVEMLRRQR 489
Cdd:COG1340  80 rDELNEKLNELREELDELRKEL 101
ZapB COG3074
Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome ...
 399-451 8.74e-04

Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442308 [Multi-domain]  Cd Length: 79  Bit Score: 38.03  E-value: 8.74e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 79326969 399 RNRIDTIKEEKRALESSIAETQVENAKLREKIDEVNSSHTELSQELQSVEGQL 451
Cdd:COG3074  24 QMEVEELKEKNEELEQENEELQSENEELQSENEQLKTENAEWQERIRSLLGKI 76
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 391-482 9.31e-04

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 41.99  E-value: 9.31e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969 391 NSLPE--RDIRNRIDTIKEEKRALESS--------IAETQVENAKLREKIDEVNS---SHTELSQELQSVEGQLISERSR 457
Cdd:COG0542 407 DSKPEelDELERRLEQLEIEKEALKKEqdeasferLAELRDELAELEEELEALKArweAEKELIEEIQELKEELEQRYGK 486

                        90       100
                ....*....|....*....|....*
gi 79326969 458 CFKLEAQIAELQKALESGQSIEAEV 482
Cdd:COG0542 487 IPELEKELAELEEELAELAPLLREE 511
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
395-488 9.67e-04

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 41.05  E-value: 9.67e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969 395 ERDIRNRIDTIKEEKRALE------SSIAETQVENAKLREKIDEVNSSHTELSQELQSVEGQLISERSRCFKLEAQIAEL 468
Cdd:COG1340 135 EKELVEKIKELEKELEKAKkaleknEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADEL 214

                        90       100
                ....*....|....*....|
gi 79326969 469 QKALesgQSIEAEVEMLRRQ 488
Cdd:COG1340 215 HKEI---VEAQEKADELHEE 231
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 386-494 1.17e-03

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: 41.42  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969   386 LNGNGNSLPER--DIRNRIDTIKEEKRALESSIAETQVENAKLREKIDEVNSSHTELSQELQSVEGQLISERSRCFKLEA 463
Cdd:pfam07888 134 LEEDIKTLTQRvlERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQD 213

                          90       100       110
                  ....*....|....*....|....*....|.
gi 79326969   464 QIAELQKALESGQSIEAEVEMLRRQRSASDE 494
Cdd:pfam07888 214 TITTLTQKLTTAHRKEAENEALLEELRSLQE 244
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
 402-490 1.27e-03

TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.


Pssm-ID: 462316 [Multi-domain]  Cd Length: 129  Bit Score: 39.16  E-value: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969   402 IDTIKEEKRALESSIAETQVENAKLREKID---------------EVNSsHTELSQELQSVEGQLISERSRCFKLEAQIA 466
Cdd:pfam07926   3 LSSLQSEIKRLKEEAADAEAQLQKLQEDLEkqaeiareaqqnyerELVL-HAEDIKALQALREELNELKAEIAELKAEAE 81

                          90       100
                  ....*....|....*....|....*
gi 79326969   467 ELQKALESGQ-SIEAEVEMLRRQRS 490
Cdd:pfam07926  82 SAKAELEESEeSWEEQKKELEKELS 106
Filament pfam00038
Intermediate filament protein;
396-495 1.32e-03

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 41.06  E-value: 1.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969   396 RDIRNRIDTIKEEKRALESSIAETQVENAKLREK--IDEVNSSHTELSQ---ELQSVEGQLISERSRCFKLEAQIAELQK 470
Cdd:pfam00038 173 AEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAArnGDALRSAKEEITElrrTIQSLEIELQSLKKQKASLERQLAETEE 252

                          90       100
                  ....*....|....*....|....*
gi 79326969   471 ALesgqsiEAEVEMLRRQRSASDEE 495
Cdd:pfam00038 253 RY------ELQLADYQELISELEAE 271
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 397-495 1.37e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.58  E-value: 1.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969    397 DIRNRIDTIKEEKRALESSIAETQVENAKLREKIDEVNSSHTELSQELQSVE---GQLISERSRCFK-----------LE 462
Cdd:TIGR02168  772 EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRerlESLERRIAATERrledleeqieeLS 851

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 79326969    463 AQIAELQKALESGQS----IEAEVEMLRRQRSASDEE 495
Cdd:TIGR02168  852 EDIESLAAEIEELEElieeLESELEALLNERASLEEA 888
Kelch_2 pfam07646
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 153-194 1.53e-03

Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six copies of the motif. It has been shown that Swiss:Q04652 is related to Galactose Oxidase for which a structure has been solved. The kelch motif forms a beta sheet. Several of these sheets associate to form a beta propeller structure as found in pfam00064, pfam00400 and pfam00415.


Pssm-ID: 462220 [Multi-domain]  Cd Length: 47  Bit Score: 36.55  E-value: 1.53e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 79326969   153 RGGHSITLVGSRVLVFGGEDKNRRL-LNDLHVLHLETMTWDVV 194
Cdd:pfam07646   2 RYPHASSVPGGKLYVVGGSDGLGDLsSSDVLVYDPETNVWTEV 44
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
399-497 1.78e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.18  E-value: 1.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969  399 RNRIDTIKEEKRALESSIAETQVENAKLREKIDEVNSSHTELSQELQSVEgqliSERSRCFKLEAQIAELQKAlesgqsi 478
Cdd:PRK02224 536 RERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELK----ERIESLERIRTLLAAIADA------- 604

                         90
                 ....*....|....*....
gi 79326969  479 EAEVEMLRRQRSASDEEED 497
Cdd:PRK02224 605 EDEIERLREKREALAELND 623
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
395-490 1.81e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 1.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969  395 ERDIRNRIDTIKEEKRALESSIAETQVENAKLREKIDEVNS------SHTELSQELQSVEGQLISERSRCFKLEAQIAEL 468
Cdd:PRK03918 247 LESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkekaeEYIKLSEFYEEYLDELREIEKRLSRLEEEINGI 326

                         90       100
                 ....*....|....*....|..
gi 79326969  469 QKALESGQSIEAEVEMLRRQRS 490
Cdd:PRK03918 327 EERIKELEEKEERLEELKKKLK 348
COG4223 COG4223
Uncharacterized conserved protein [Function unknown];
398-487 2.11e-03

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443367 [Multi-domain]  Cd Length: 259  Bit Score: 40.03  E-value: 2.11e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969 398 IRNRIDTIKEE------KRALESSIAETQVENAKLREKIDEVNSShtELSQELQSVEGQLISE----RSRCFKLEAQIA- 466
Cdd:COG4223  19 LEQRLAALEAApaaaaaTAALEARLAALRAALAAAREAVAAAAAA--ALEARLAALEAKAAAPeaeaAAAARAAALALAa 96

                        90       100
                ....*....|....*....|..
gi 79326969 467 -ELQKALESGQSIEAEVEMLRR 487
Cdd:COG4223  97 aALRAAVERGQPFAAELAALEA 118
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 396-495 2.21e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.91  E-value: 2.21e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969 396 RDIRNRIDTIKE-------EKRALESSIAETQVENAKLREKIDEVNSSHtelsqELQSVEGQLISERSRCFKLEAQIAEL 468
Cdd:COG1579  41 AALEARLEAAKTeledlekEIKRLELEIEEVEARIKKYEEQLGNVRNNK-----EYEALQKEIESLKRRISDLEDEILEL 115

                        90       100
                ....*....|....*....|....*..
gi 79326969 469 QKALEsgqSIEAEVEMLRRQRSASDEE 495
Cdd:COG1579 116 MERIE---ELEEELAELEAELAELEAE 139
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 404-493 2.46e-03

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 40.44  E-value: 2.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969   404 TIKEEKRALessiaetQVENAKLREKIDEVNS-------SHTELSQeLQSVEGQLISE-----------RSRCFKLEAQI 465
Cdd:pfam05622  25 LLQEEKNSL-------QQENKKLQERLDQLESgddsgtpGGKKYLL-LQKQLEQLQEEnfrletarddyRIKCEELEKEV 96

                          90       100       110
                  ....*....|....*....|....*....|..
gi 79326969   466 AELQKALESGQSIEAEVEMLRRQ----RSASD 493
Cdd:pfam05622  97 LELQHRNEELTSLAEEAQALKDEmdilRESSD 128
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 395-503 2.70e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.43  E-value: 2.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969    395 ERDIRNRIDTIKEEKRALESSIAETQVENAKLREKIDEVNSSHTELSQELQSVEGQLISERSRCFKLEAQIAELQKALES 474
Cdd:TIGR02168  693 IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE 772

                           90       100       110
                   ....*....|....*....|....*....|.
gi 79326969    475 GQS--IEAEVEMLRRQRSASDEEEDGTVQRQ 503
Cdd:TIGR02168  773 AEEelAEAEAEIEELEAQIEQLKEELKALRE 803
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 411-497 2.74e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.13  E-value: 2.74e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969 411 ALESSIAETQVENAKLREKIDEVNSSHTELSQELQSVEGQLisersrcFKLEAQIAELQKALesgQSIEAEVEMLRRQRS 490
Cdd:COG4942  17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQL-------AALERRIAALARRI---RALEQELAALEAELA 86


                ....*..
gi 79326969 491 ASDEEED 497
Cdd:COG4942  87 ELEKEIA 93
PRK01156 PRK01156
chromosome segregation protein; Provisional
 396-493 2.80e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 40.66  E-value: 2.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969  396 RDIRNRIDTIKEEKRALES---SIAETQVENAKLREKID---EVNSSHTELSQELQSVEGQLISE--------------R 455
Cdd:PRK01156 629 NNLNNKYNEIQENKILIEKlrgKIDNYKKQIAEIDSIIPdlkEITSRINDIEDNLKKSRKALDDAkanrarlestieilR 708

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 79326969  456 SRCFKLEAQIAELQKALESGQSIEAEVEMLRRQRSASD 493
Cdd:PRK01156 709 TRINELSDRINDINETLESMKKIKKAIGDLKRLREAFD 746
DUF724 pfam05266
Protein of unknown function (DUF724); This family contains several uncharacterized proteins ...
 398-474 3.07e-03

Protein of unknown function (DUF724); This family contains several uncharacterized proteins found in Arabidopsis thaliana and other plants. This region is often found associated with Agenet domains and may contain coiled-coil.


Pssm-ID: 428400 [Multi-domain]  Cd Length: 188  Bit Score: 38.79  E-value: 3.07e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 79326969   398 IRNRIDTIKEEKRALESSIAETQVENAKLREKIDEVNSSHTELSQELQSVEGQLISERSRCFKLEAQIAELQKALES 474
Cdd:pfam05266 100 LKDRQTKLLEELKKLEKKIAEEESEKRKLEEEIDELEKKILELERQLALAKEKKEAADKEIARLKSEAEKLEQEIQD 176
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 397-503 3.80e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.04  E-value: 3.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969    397 DIRNRIDTIKEEKRALESSIAETQVENAKLREKIDEVNSSHTELSQELQSVEGQLISERSRCFKLEAQIAELQKALEsgq 476
Cdd:TIGR02168  355 SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE--- 431

                           90       100
                   ....*....|....*....|....*..
gi 79326969    477 siEAEVEMLRRQRSASDEEEDGTVQRQ 503
Cdd:TIGR02168  432 --EAELKELQAELEELEEELEELQEEL 456
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 402-474 5.10e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 39.62  E-value: 5.10e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 79326969   402 IDTIKEEKRALESSIAETQVENAKLREKIDEVNSSHTELSQELQSVEGQLISERSRCFKLEAQIAELQKALES 474
Cdd:TIGR04523 386 IKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKN 458
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
387-486 5.30e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.64  E-value: 5.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969  387 NGNGNSLPER--DIRNRIDTIKEEKRALESSIAETQVENAKLREKIDEVNSSHTELSQ-------ELQSVEGQLISERSR 457
Cdd:PRK02224 341 NEEAESLREDadDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRErfgdapvDLGNAEDFLEELREE 420

                         90       100
                 ....*....|....*....|....*....
gi 79326969  458 CFKLEAQIAELQKALESGQSIEAEVEMLR 486
Cdd:PRK02224 421 RDELREREAELEATLRTARERVEEAEALL 449
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
395-495 5.99e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.51  E-value: 5.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969  395 ERDIRN----RIDTIKEEKRALESSIAETQVENAKLREKIDEVNSSH-------TELSQELQSVEGQLISERSRC----F 459
Cdd:COG4913  329 EAQIRGnggdRLEQLEREIERLERELEERERRRARLEALLAALGLPLpasaeefAALRAEAAALLEALEEELEALeealA 408

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 79326969  460 KLEAQIAELQKALEsgqSIEAEVEMLRRQRSASDEE 495
Cdd:COG4913  409 EAEAALRDLRRELR---ELEAEIASLERRKSNIPAR 441
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
396-490 6.11e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 38.74  E-value: 6.11e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969 396 RDIRNRIDTIKEEKRALESSIAETQVE----NAKLREKIDEVNS-------------SHTELSQELQ------------- 445
Cdd:COG1340  53 KELREEAQELREKRDELNEKVKELKEErdelNEKLNELREELDElrkelaelnkaggSIDKLRKEIErlewrqqtevlsp 132

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 79326969 446 SVEGQLISERSRcfkLEAQIAELQKALESGQSI---EAEVEMLRRQRS 490
Cdd:COG1340 133 EEEKELVEKIKE---LEKELEKAKKALEKNEKLkelRAELKELRKEAE 177
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
399-498 7.47e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.25  E-value: 7.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969  399 RNRIDTIKEEKRALESSIAETQVENAKLREKIDEVNSSHTELSQELQSVEGQLISERSRCFKLEAQIAELQKALEsgqSI 478
Cdd:PRK02224 250 REELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDE---EL 326

                         90       100
                 ....*....|....*....|
gi 79326969  479 EAEVEMLRRQRSASDEEEDG 498
Cdd:PRK02224 327 RDRLEECRVAAQAHNEEAES 346
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
399-506 7.55e-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: 7.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969  399 RNRIDTIKEEKRALESSIAETQVENAKLREKIDevnsshtELSQELQSVEGQLISErsrcfkLEAQIAELQKALES---- 474
Cdd:COG4913  294 EAELEELRAELARLEAELERLEARLDALREELD-------ELEAQIRGNGGDRLEQ------LEREIERLERELEErerr 360

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 79326969  475 -----------GQSIEAEVEMLRRQRSASDEEEDGTVQRQGSA 506
Cdd:COG4913  361 rarleallaalGLPLPASAEEFAALRAEAAALLEALEEELEAL 403
Kelch_1 pfam01344
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 203-244 8.28e-03

Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six copies of the motif. It has been shown that Swiss:Q04652 is related to Galactose Oxidase for which a structure has been solved. The kelch motif forms a beta sheet. Several of these sheets associate to form a beta propeller structure as found in pfam00064, pfam00400 and pfam00415.


Pssm-ID: 396078 [Multi-domain]  Cd Length: 46  Bit Score: 34.51  E-value: 8.28e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 79326969   203 PRFDHTAATHsDRYLLIFGGCSHSIFYSDLHILDLQTMEWSQ 244
Cdd:pfam01344   1 RRSGAGVVVV-GGKIYVIGGFDGNQSLNSVEVYDPETNTWSK 41
DUF4472 pfam14739
Domain of unknown function (DUF4472); This family is specific to the Chordates. Some members ...
 407-497 9.22e-03

Domain of unknown function (DUF4472); This family is specific to the Chordates. Some members also carry Kinesin-motor domains at their N-terminus, Kinesin, pfam00225.


Pssm-ID: 464291 [Multi-domain]  Cd Length: 107  Bit Score: 36.13  E-value: 9.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79326969   407 EEKRALESSIAETQVENAKLREKIDEVNSshtELSQELQSVEGQLISERSRCFKLEAQIAELQKAL----ESGQSIEAEV 482
Cdd:pfam14739   3 EEKLQISKALVDLQIENNKLREQYEAEKF---ELKNKLLNLENRVLELELRLEKAAEEIQDLRERLreleDDRRELAEEF 79

                          90
                  ....*....|....*....
gi 79326969   483 EMLRR----QRSASDEEED 497
Cdd:pfam14739  80 VALKKnyqaLSKELEAEVA 98
 
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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