NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1622953243|ref|XP_028706780|]
View 

cell cycle progression protein 1 isoform X5 [Macaca mulatta]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PTZ00121 super family cl31754
MAEBL; Provisional
273-583 6.80e-08

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 56.69  E-value: 6.80e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243  273 QKRQQLVRKIHEDELNDMKDYLSQCQQEQESFVDYKSLKENLARCWTLT--EAEKMSFETQKTNLATENQYLRISLEKEE 350
Cdd:PTZ00121  1591 EARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKkkEAEEKKKAEELKKAEEENKIKAAEEAKKA 1670
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243  351 KALSSLQEELNKLREQIRILEDKGT-STELVRENQKLKQHLEEEKQKKHSFLSQRETLLAEAKMLKRELERERLVTTALR 429
Cdd:PTZ00121  1671 EEDKKKAEEAKKAEEDEKKAAEALKkEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAK 1750
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243  430 GELQQLSG-SQLHGKSDSPNVYTEKKEIAVLRERLSElerkltfeqqrSDLWERLYVEAKDQSGKQETDGKKKGGRGNHR 508
Cdd:PTZ00121  1751 KDEEEKKKiAHLKKEEEKKAEEIRKEKEAVIEEELDE-----------EDEKRRMEVDKKIKDIFDNFANIIEGGKEGNL 1819
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622953243  509 AKNKSKETFLGSVKETFDA---MKNSTKEFVRHHKEKIKQAKEAVKENlkkfSDSVKSTFrHFKDTTKNIFDEKGNKR 583
Cdd:PTZ00121  1820 VINDSKEMEDSAIKEVADSknmQLEEADAFEKHKFNKNNENGEDGNKE----ADFNKEKD-LKEDDEEEIEEADEIEK 1892
PLN02328 super family cl33466
lysine-specific histone demethylase 1 homolog
108-263 8.44e-04

lysine-specific histone demethylase 1 homolog


The actual alignment was detected with superfamily member PLN02328:

Pssm-ID: 215187 [Multi-domain]  Cd Length: 808  Bit Score: 43.06  E-value: 8.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243 108 TLEPPKLEEIGNQevVIVEEAQSSEDFNMGSSSSSQYTFCQPETErwweklwkiPECIWGWDDQLKHHVPSQLTFQVFSS 187
Cdd:PLN02328    5 TKEPEDPADNVND--VVSEASSPETDLSLSPSQSEQNIENDGQNS---------PETQSPLTELQPSPLPPNTTLDAPVS 73
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622953243 188 QPSDDESSSDETSNQPSPAFRRRRARKKtvstsESEDRLVAEQETEPSkeLSKRQFSSGLNKCVILALVIAISMGF 263
Cdd:PLN02328   74 DSQGDESSSEQQPQNPNSTEPAPPPKKR-----RRRKRFFTEINANPA--FRRHRVRGGLGKEVDVEALIAISVGF 142
 
Name Accession Description Interval E-value
PTZ00121 PTZ00121
MAEBL; Provisional
273-583 6.80e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 56.69  E-value: 6.80e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243  273 QKRQQLVRKIHEDELNDMKDYLSQCQQEQESFVDYKSLKENLARCWTLT--EAEKMSFETQKTNLATENQYLRISLEKEE 350
Cdd:PTZ00121  1591 EARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKkkEAEEKKKAEELKKAEEENKIKAAEEAKKA 1670
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243  351 KALSSLQEELNKLREQIRILEDKGT-STELVRENQKLKQHLEEEKQKKHSFLSQRETLLAEAKMLKRELERERLVTTALR 429
Cdd:PTZ00121  1671 EEDKKKAEEAKKAEEDEKKAAEALKkEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAK 1750
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243  430 GELQQLSG-SQLHGKSDSPNVYTEKKEIAVLRERLSElerkltfeqqrSDLWERLYVEAKDQSGKQETDGKKKGGRGNHR 508
Cdd:PTZ00121  1751 KDEEEKKKiAHLKKEEEKKAEEIRKEKEAVIEEELDE-----------EDEKRRMEVDKKIKDIFDNFANIIEGGKEGNL 1819
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622953243  509 AKNKSKETFLGSVKETFDA---MKNSTKEFVRHHKEKIKQAKEAVKENlkkfSDSVKSTFrHFKDTTKNIFDEKGNKR 583
Cdd:PTZ00121  1820 VINDSKEMEDSAIKEVADSknmQLEEADAFEKHKFNKNNENGEDGNKE----ADFNKEKD-LKEDDEEEIEEADEIEK 1892
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
322-549 1.34e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.25  E-value: 1.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243 322 EAEKMSFETQKTNLATENQYLRISLEKEEKALSSLQEELNKLREQI-RILEDKGTSTELVRENQKLKQHLEEEKQKKHSF 400
Cdd:COG1196   252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELaRLEQDIARLEERRRELEERLEELEEELAELEEE 331
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243 401 LSQRETLLAEAKMLKRELERERlvtTALRGELQQLsgsqlhgksdspnvytEKKEIAVLRERLSELERKLTFEQQRSDLW 480
Cdd:COG1196   332 LEELEEELEELEEELEEAEEEL---EEAEAELAEA----------------EEALLEAEAELAEAEEELEELAEELLEAL 392
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622953243 481 ERLYVEAKDQSGKQETDGKKKGGRGNHRAKNKSKETFLGSVKETFDAMKNSTKEFVRHHKEKIKQAKEA 549
Cdd:COG1196   393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
294-554 9.03e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.67  E-value: 9.03e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243  294 LSQCQQEQESfvDYKSLKENLARcwTLTEAEKMsfETQKTNLATENQYLRISLEKEEKALSSLQEELNKLREQIRILEDk 373
Cdd:TIGR02168  682 LEEKIEELEE--KIAELEKALAE--LRKELEEL--EEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK- 754
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243  374 gTSTELVRENQKLKQHLEEEKQKKHSFLSQRETLLAEAKMLKRELERERLVTTALRGELQQLSGS----QLHGKSDSPNV 449
Cdd:TIGR02168  755 -ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEaanlRERLESLERRI 833
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243  450 YTEKKEIAVLRERLSELERKLTF-EQQRSDLWERLYVEAKDQSGKQETDGKKKGGRGNHRAKNKSKETFLGSVKETFDAM 528
Cdd:TIGR02168  834 AATERRLEDLEEQIEELSEDIESlAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSEL 913
                          250       260
                   ....*....|....*....|....*.
gi 1622953243  529 KNSTKEfVRHHKEKIKQAKEAVKENL 554
Cdd:TIGR02168  914 RRELEE-LREKLAQLELRLEGLEVRI 938
PLN02328 PLN02328
lysine-specific histone demethylase 1 homolog
108-263 8.44e-04

lysine-specific histone demethylase 1 homolog


Pssm-ID: 215187 [Multi-domain]  Cd Length: 808  Bit Score: 43.06  E-value: 8.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243 108 TLEPPKLEEIGNQevVIVEEAQSSEDFNMGSSSSSQYTFCQPETErwweklwkiPECIWGWDDQLKHHVPSQLTFQVFSS 187
Cdd:PLN02328    5 TKEPEDPADNVND--VVSEASSPETDLSLSPSQSEQNIENDGQNS---------PETQSPLTELQPSPLPPNTTLDAPVS 73
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622953243 188 QPSDDESSSDETSNQPSPAFRRRRARKKtvstsESEDRLVAEQETEPSkeLSKRQFSSGLNKCVILALVIAISMGF 263
Cdd:PLN02328   74 DSQGDESSSEQQPQNPNSTEPAPPPKKR-----RRRKRFFTEINANPA--FRRHRVRGGLGKEVDVEALIAISVGF 142
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
337-501 3.82e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 40.88  E-value: 3.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243 337 TENQYLR--ISLEKEEKALS--SLQEELNKLrEQIRILEDKgtsTELVRENQKLKQhLEEEKQKKHSFLSQRETLLAEAK 412
Cdd:pfam17380 266 TENEFLNqlLHIVQHQKAVSerQQQEKFEKM-EQERLRQEK---EEKAREVERRRK-LEEAEKARQAEMDRQAAIYAEQE 340
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243 413 MLKRELERE--RLVTTALRGELQQLsgsqlhgksdspnvytEKKEIAVLRERLSELERkLTFEQQRSDLWERLYVEAKDQ 490
Cdd:pfam17380 341 RMAMEREREleRIRQEERKRELERI----------------RQEEIAMEISRMRELER-LQMERQQKNERVRQELEAARK 403
                         170
                  ....*....|.
gi 1622953243 491 SGKQETDGKKK 501
Cdd:pfam17380 404 VKILEEERQRK 414
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
272-486 6.55e-03

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: 39.62  E-value: 6.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243  272 IQKRQQLVRKIHEDELND----MKDYLSQCQQEQESFVD-YKSLKENlARcwtlTEAEKMSFE-------TQKTNLATEn 339
Cdd:smart00787  79 ISEGRDLFKEIEEETLINnpplFKEYFSASPDVKLLMDKqFQLVKTF-AR----LEAKKMWYEwrmklleGLKEGLDEN- 152
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243  340 qylRISLEKEEKALSSLQEELNKLREQIRILEDkgtstELVRENQKLKQHLEEEKQKKHSFLSQretLLAEAKMLKRELE 419
Cdd:smart00787 153 ---LEGLKEDYKLLMKELELLNSIKPKLRDRKD-----ALEEELRQLKQLEDELEDCDPTELDR---AKEKLKKLLQEIM 221
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622953243  420 RERLVTTALRGELQQLSGsqlhgksdspNVYTEKKEIAVLRERLSELERKLtfeqQRSDLWERLYVE 486
Cdd:smart00787 222 IKVKKLEELEEELQELES----------KIEDLTNKKSELNTEIAEAEKKL----EQCRGFTFKEIE 274
 
Name Accession Description Interval E-value
PTZ00121 PTZ00121
MAEBL; Provisional
273-583 6.80e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 56.69  E-value: 6.80e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243  273 QKRQQLVRKIHEDELNDMKDYLSQCQQEQESFVDYKSLKENLARCWTLT--EAEKMSFETQKTNLATENQYLRISLEKEE 350
Cdd:PTZ00121  1591 EARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKkkEAEEKKKAEELKKAEEENKIKAAEEAKKA 1670
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243  351 KALSSLQEELNKLREQIRILEDKGT-STELVRENQKLKQHLEEEKQKKHSFLSQRETLLAEAKMLKRELERERLVTTALR 429
Cdd:PTZ00121  1671 EEDKKKAEEAKKAEEDEKKAAEALKkEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAK 1750
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243  430 GELQQLSG-SQLHGKSDSPNVYTEKKEIAVLRERLSElerkltfeqqrSDLWERLYVEAKDQSGKQETDGKKKGGRGNHR 508
Cdd:PTZ00121  1751 KDEEEKKKiAHLKKEEEKKAEEIRKEKEAVIEEELDE-----------EDEKRRMEVDKKIKDIFDNFANIIEGGKEGNL 1819
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622953243  509 AKNKSKETFLGSVKETFDA---MKNSTKEFVRHHKEKIKQAKEAVKENlkkfSDSVKSTFrHFKDTTKNIFDEKGNKR 583
Cdd:PTZ00121  1820 VINDSKEMEDSAIKEVADSknmQLEEADAFEKHKFNKNNENGEDGNKE----ADFNKEKD-LKEDDEEEIEEADEIEK 1892
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
322-549 1.34e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.25  E-value: 1.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243 322 EAEKMSFETQKTNLATENQYLRISLEKEEKALSSLQEELNKLREQI-RILEDKGTSTELVRENQKLKQHLEEEKQKKHSF 400
Cdd:COG1196   252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELaRLEQDIARLEERRRELEERLEELEEELAELEEE 331
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243 401 LSQRETLLAEAKMLKRELERERlvtTALRGELQQLsgsqlhgksdspnvytEKKEIAVLRERLSELERKLTFEQQRSDLW 480
Cdd:COG1196   332 LEELEEELEELEEELEEAEEEL---EEAEAELAEA----------------EEALLEAEAELAEAEEELEELAEELLEAL 392
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622953243 481 ERLYVEAKDQSGKQETDGKKKGGRGNHRAKNKSKETFLGSVKETFDAMKNSTKEFVRHHKEKIKQAKEA 549
Cdd:COG1196   393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
347-470 6.84e-06

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 49.47  E-value: 6.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243 347 EKEEKALSSLQEELNKLREQIRiledkgtstELVRENQKLKQHLEEEKQKkhsfLSQRETLLAEAKMLKRELERERLVTT 426
Cdd:COG2433   402 EHEERELTEEEEEIRRLEEQVE---------RLEAEVEELEAELEEKDER----IERLERELSEARSEERREIRKDREIS 468
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1622953243 427 ALRGELQQLsgsqlhgksdspnvyteKKEIAVLRERLSELERKL 470
Cdd:COG2433   469 RLDREIERL-----------------ERELEEERERIEELKRKL 495
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
294-554 9.03e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.67  E-value: 9.03e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243  294 LSQCQQEQESfvDYKSLKENLARcwTLTEAEKMsfETQKTNLATENQYLRISLEKEEKALSSLQEELNKLREQIRILEDk 373
Cdd:TIGR02168  682 LEEKIEELEE--KIAELEKALAE--LRKELEEL--EEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK- 754
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243  374 gTSTELVRENQKLKQHLEEEKQKKHSFLSQRETLLAEAKMLKRELERERLVTTALRGELQQLSGS----QLHGKSDSPNV 449
Cdd:TIGR02168  755 -ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEaanlRERLESLERRI 833
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243  450 YTEKKEIAVLRERLSELERKLTF-EQQRSDLWERLYVEAKDQSGKQETDGKKKGGRGNHRAKNKSKETFLGSVKETFDAM 528
Cdd:TIGR02168  834 AATERRLEDLEEQIEELSEDIESlAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSEL 913
                          250       260
                   ....*....|....*....|....*.
gi 1622953243  529 KNSTKEfVRHHKEKIKQAKEAVKENL 554
Cdd:TIGR02168  914 RRELEE-LREKLAQLELRLEGLEVRI 938
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
338-490 1.01e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.00  E-value: 1.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243 338 ENQYLRISLEKEEKALSSLQEELNKLREQIRILEDKGTSTELVRENQKLKQHLEEEKQKKHSF---LSQRETLLAEAKML 414
Cdd:COG4717    89 EYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELeerLEELRELEEELEEL 168
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622953243 415 KRELERERlvtTALRGELQQLSGSQLHGKSDSPNVYTE-KKEIAVLRERLSELERKLTFEQQRSDLWERLYVEAKDQ 490
Cdd:COG4717   169 EAELAELQ---EELEELLEQLSLATEEELQDLAEELEElQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
338-435 1.15e-05

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 49.09  E-value: 1.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243 338 ENQYLRISLEKEEKALSSLQEELNKLREQIRILEDKgtSTELVRENQKLKQHLEEEKQKKHS-FLSQRE--TLLAEAKML 414
Cdd:COG2433   400 EKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAE--LEEKDERIERLERELSEARSEERReIRKDREisRLDREIERL 477
                          90       100
                  ....*....|....*....|.
gi 1622953243 415 KRELERERLVTTALRGELQQL 435
Cdd:COG2433   478 ERELEEERERIEELKRKLERL 498
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
274-482 1.26e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 48.91  E-value: 1.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243  274 KRQQLVRKIHEDELNdMKDYLSQCQQEQESFVDYKSLKENLARCWTLTEAEKMSFETQKTNLATENQYLRISLEKEEKAL 353
Cdd:TIGR02169  302 EIASLERSIAEKERE-LEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEF 380
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243  354 SSLQEELNKLREQIRILEDKgtSTELVRENQKlkqhLEEEKQKKHSFLSQRETLLAEAKMLKRELERERLVT----TALR 429
Cdd:TIGR02169  381 AETRDELKDYREKLEKLKRE--INELKRELDR----LQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKaleiKKQE 454
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1622953243  430 GELQQLSGSQlhgKSDSPNVYTEKKEIAVLRERLSELERKLTFEQQRSDLWER 482
Cdd:TIGR02169  455 WKLEQLAADL---SKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEE 504
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
339-476 1.33e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 48.86  E-value: 1.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243 339 NQYLRISLEKE----EKALSSLQEELNKLREQIRILEDKgtstelvrenqklkqhLEEEKQKKHSFLSQRETLLAEAKM- 413
Cdd:COG3206   159 EAYLEQNLELRreeaRKALEFLEEQLPELRKELEEAEAA----------------LEEFRQKNGLVDLSEEAKLLLQQLs 222
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622953243 414 -LKRELERERLVTTALRGELQQLSgSQLHGKSDSPNVYTEKKEIAVLRERLSELERKLTFEQQR 476
Cdd:COG3206   223 eLESQLAEARAELAEAEARLAALR-AQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSAR 285
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
273-587 8.23e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.20  E-value: 8.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243  273 QKRQQLVRKIHEDELNDMKDYLSQCQQEQESFvdyKSLKENLARCWTLTEAEKMSFETQKTNLATENQYLRISLEKEEKA 352
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEELAEAEAEIEEL---EAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243  353 LSSLQEELNKLREQIRILEDKGTSTELVRENQKLKQHLEEEKQKKHSFL-SQRETLLAEAKMLKRELERERLVTTALRGE 431
Cdd:TIGR02168  833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNErASLEEALALLRSELEELSEELRELESKRSE 912
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243  432 LQQLSGSQlhgksdspnvyteKKEIAVLRERLSELErkLTFEQQRSDLWERLYVEAKDQSGKQET-DGKKKGGRGN-HRA 509
Cdd:TIGR02168  913 LRRELEEL-------------REKLAQLELRLEGLE--VRIDNLQERLSEEYSLTLEEAEALENKiEDDEEEARRRlKRL 977
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243  510 KNKSKEtfLGSVkeTFDAM-----KNSTKEFVRHHKEKIKQAKEAVKENLKKFSDSVKSTfrhFKDTTKNIfdekgNKRF 584
Cdd:TIGR02168  978 ENKIKE--LGPV--NLAAIeeyeeLKERYDFLTAQKEDLTEAKETLEEAIEEIDREARER---FKDTFDQV-----NENF 1045

                   ...
gi 1622953243  585 GAT 587
Cdd:TIGR02168 1046 QRV 1048
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
284-559 1.24e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 45.83  E-value: 1.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243  284 EDELNDMKDYLsqcQQEQESFVDYKSLKENL--ARCWTLTeAEKMSFETQKTNLATENQYLRISLEKEEKALSSLQEELN 361
Cdd:TIGR02169  193 IDEKRQQLERL---RREREKAERYQALLKEKreYEGYELL-KEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLE 268
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243  362 KLRE--------------------QIRILEDKGTSTELVRENQKLKQHLEEEKQKKHSFLSQRETLLAEAKMLKRELERE 421
Cdd:TIGR02169  269 EIEQlleelnkkikdlgeeeqlrvKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEE 348
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243  422 RLVTTALRGELQQLSGSQLHGKSDspnVYTEKKEIAVLRERLSELERKLtfeqqrSDLWERLYVEAKDQSGKQETDGKKK 501
Cdd:TIGR02169  349 RKRRDKLTEEYAELKEELEDLRAE---LEEVDKEFAETRDELKDYREKL------EKLKREINELKRELDRLQEELQRLS 419
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622953243  502 GGRGNHRAKNKSKEtflGSVKEtFDAMKNSTKEFVRHHKEKIKQAKEAVKENLKKFSD 559
Cdd:TIGR02169  420 EELADLNAAIAGIE---AKINE-LEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYD 473
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
285-562 1.44e-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: 45.43  E-value: 1.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243  285 DELNDMKDYLSQCQQEQESFVD-YKSLKENLARC---WTLTEAEKMSFETQKTNLATENQYLRISLEKEEKALSSLQEEL 360
Cdd:TIGR02168  232 LRLEELREELEELQEELKEAEEeLEELTAELQELeekLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERL 311
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243  361 NKLREQI-----RILEDKGTSTELVRENQKLKQHLEEEKQKKHSFLSQRETLLAEAKMLKRELERERLVTTALRGELQQL 435
Cdd:TIGR02168  312 ANLERQLeeleaQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQL 391
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243  436 SGSQlhgksdspnvYTEKKEIAVLRERLSELERKLTFEQQRSDLWERLYVEAKDQSGKQETDGKKKgGRGNHRAKNKSKE 515
Cdd:TIGR02168  392 ELQI----------ASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEE-ELEELQEELERLE 460
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1622953243  516 TFLGSVKETFDAMKNSTKEFVRHHKEKIKQAK--EAVKENLKKFSDSVK 562
Cdd:TIGR02168  461 EALEELREELEEAEQALDAAERELAQLQARLDslERLQENLEGFSEGVK 509
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
270-490 1.99e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.93  E-value: 1.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243 270 IQIQKRQQLVRKIHEDELNDMKDYLSQCQQEQESFVDYKSLKENLARcwTLTEAEKMSFETQKTNLATENQYLRIS---L 346
Cdd:COG1196   298 ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEE--ELEEAEEELEEAEAELAEAEEALLEAEaelA 375
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243 347 EKEEKALSSLQEELNKLREQIriledkgtstELVRENQKLKQHLEEEKQKKHSFLSQRETLLAEAKMLKRELERERLVTT 426
Cdd:COG1196   376 EAEEELEELAEELLEALRAAA----------ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622953243 427 ALRGELQQLSGSQLHGKSDspnVYTEKKEIAVLRERLSELERKLtfEQQRSDLWERLYVEAKDQ 490
Cdd:COG1196   446 EAAEEEAELEEEEEALLEL---LAELLEEAALLEAALAELLEEL--AEAAARLLLLLEAEADYE 504
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
292-552 3.70e-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: 44.29  E-value: 3.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243  292 DYLSQCQQEQESFVDYKSLKENLARCWT-LTEAEKMSFE-TQKTNLATEnqylriSLEKEEKALSSLQEELNKLREQIRI 369
Cdd:TIGR02169  668 FSRSEPAELQRLRERLEGLKRELSSLQSeLRRIENRLDElSQELSDASR------KIGEIEKEIEQLEQEEEKLKERLEE 741
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243  370 LEDKGTSTELVRENQKLK-QHLEEEKQKKHSFLSQRETLLAEakmLKRELERERLVTtaLRGELQQLsgsqlhgksdspn 448
Cdd:TIGR02169  742 LEEDLSSLEQEIENVKSElKELEARIEELEEDLHKLEEALND---LEARLSHSRIPE--IQAELSKL------------- 803
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243  449 vyteKKEIAVLRERLSELERKLTFEQQRSDLWERLYVEAKDQsgKQETDGKKKGGRGNHRAKNKSKETFLGSVKETFDAM 528
Cdd:TIGR02169  804 ----EEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQ--RIDLKEQIKSIEKEIENLNGKKEELEEELEELEAAL 877
                          250       260       270
                   ....*....|....*....|....*....|
gi 1622953243  529 KNSTKEF------VRHHKEKIKQAKEAVKE 552
Cdd:TIGR02169  878 RDLESRLgdlkkeRDELEAQLRELERKIEE 907
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
273-423 8.26e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 8.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243 273 QKRQQLVRKIHEDELNDMKDYLSQCQQEQESFVDYKSLKENLARcwTLTEAEKMSFETQKTNLATENQYLRISLEKEEKA 352
Cdd:COG4717   370 QEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEE--LLGELEELLEALDEEELEEELEELEEELEELEEE 447
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622953243 353 LSSLQEELNKLREQIRILEDKGTSTELVRENQKLKQHLEEEkQKKHSFLSQRETLLAEAkmlKRELERERL 423
Cdd:COG4717   448 LEELREELAELEAELEQLEEDGELAELLQELEELKAELREL-AEEWAALKLALELLEEA---REEYREERL 514
PLN02328 PLN02328
lysine-specific histone demethylase 1 homolog
108-263 8.44e-04

lysine-specific histone demethylase 1 homolog


Pssm-ID: 215187 [Multi-domain]  Cd Length: 808  Bit Score: 43.06  E-value: 8.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243 108 TLEPPKLEEIGNQevVIVEEAQSSEDFNMGSSSSSQYTFCQPETErwweklwkiPECIWGWDDQLKHHVPSQLTFQVFSS 187
Cdd:PLN02328    5 TKEPEDPADNVND--VVSEASSPETDLSLSPSQSEQNIENDGQNS---------PETQSPLTELQPSPLPPNTTLDAPVS 73
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622953243 188 QPSDDESSSDETSNQPSPAFRRRRARKKtvstsESEDRLVAEQETEPSkeLSKRQFSSGLNKCVILALVIAISMGF 263
Cdd:PLN02328   74 DSQGDESSSEQQPQNPNSTEPAPPPKKR-----RRRKRFFTEINANPA--FRRHRVRGGLGKEVDVEALIAISVGF 142
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
333-556 1.03e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243 333 TNLATENQYLRISLEKEEKALSSLQEELNKLREQIRILEDKgtstelVRENQKLKqhleeEKQKKHSFLSQ-RETLLAEA 411
Cdd:PRK03918  241 EELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEK------VKELKELK-----EKAEEYIKLSEfYEEYLDEL 309
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243 412 KMLKRELERERLVTTALRGELQQLSgsqlhgksdspnvyTEKKEIAVLRERLSELERKLtfeqQRSDLWERLYVEAKDQS 491
Cdd:PRK03918  310 REIEKRLSRLEEEINGIEERIKELE--------------EKEERLEELKKKLKELEKRL----EELEERHELYEEAKAKK 371
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622953243 492 GKQETDGKKKGGRGNHRAKNKSKEtfLGSVKETFDAMKNSTKEFVRHHKEKIKQAKEAVKEnLKK 556
Cdd:PRK03918  372 EELERLKKRLTGLTPEKLEKELEE--LEKAKEEIEEEISKITARIGELKKEIKELKKAIEE-LKK 433
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
271-471 1.08e-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: 42.74  E-value: 1.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243  271 QIQKRQQLVRKiHEDELNDMKDYLSQCQQEqesfvdYKSLKENLARC-WTLTEAEKMSFETQKTNLATENQYLRIS--LE 347
Cdd:TIGR02168  783 EIEELEAQIEQ-LKEELKALREALDELRAE------LTLLNEEAANLrERLESLERRIAATERRLEDLEEQIEELSedIE 855
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243  348 KEEKALSSLQEELNKLREQIRILEDKGTSTELVRENQKLKQHLEEEKQKKHSflSQRETLLAEAKMLKRELERERLVTTA 427
Cdd:TIGR02168  856 SLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE--SKRSELRRELEELREKLAQLELRLEG 933
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1622953243  428 LRGELQQLSGS-----QLHGKSDSPNVYTEKKEIAVLRERLSELERKLT 471
Cdd:TIGR02168  934 LEVRIDNLQERlseeySLTLEEAEALENKIEDDEEEARRRLKRLENKIK 982
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
325-475 1.51e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.93  E-value: 1.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243 325 KMSFETQKTNLATENQYLRISLEKEEKALSSLQEELNKLREQIRIL----EDKGTSTELVRENQKLKQhLEEEKQKKHSF 400
Cdd:COG3206   163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVdlseEAKLLLQQLSELESQLAE-ARAELAEAEAR 241
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243 401 LSQRETLLAEAKMLKRELERERLVTtALRGELQQLSgSQLHGKS-----DSPNVYTEKKEIAVLRERLSELERKLTFEQQ 475
Cdd:COG3206   242 LAALRAQLGSGPDALPELLQSPVIQ-QLRAQLAELE-AELAELSarytpNHPDVIALRAQIAALRAQLQQEAQRILASLE 319
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
353-489 2.97e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.44  E-value: 2.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243  353 LSSLQEELNKLREQIRILEDKGTSTELVRENQKLKQHLEEEKQKKHSFLSQRETLLAEAKM---------LKRELERERL 423
Cdd:COG4913    237 LERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELeelraelarLEAELERLEA 316
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622953243  424 VTTALRGELQQLsgSQLHGKSDSPNVYTEKKEIAVLRERLSELERKLT-FEQQRSDLWERLYVEAKD 489
Cdd:COG4913    317 RLDALREELDEL--EAQIRGNGGDRLEQLEREIERLERELEERERRRArLEALLAALGLPLPASAEE 381
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
340-490 2.97e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 2.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243 340 QYLRISLEKEEK-------ALSSLQEELNKLREQIRILEDKgtSTELVRENQKLKQHLEEEKQKKHSFLSQRETLLAEAK 412
Cdd:COG1196   214 RYRELKEELKELeaellllKLRELEAELEELEAELEELEAE--LEELEAELAELEAELEELRLELEELELELEEAQAEEY 291
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622953243 413 MLKRELERERLVTTALRGELQQLSGSQLHgksdspnvytEKKEIAVLRERLSELERKLTFEQQRSDLWERLYVEAKDQ 490
Cdd:COG1196   292 ELLAELARLEQDIARLEERRRELEERLEE----------LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE 359
COG5022 COG5022
Myosin heavy chain [General function prediction only];
271-477 3.36e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 41.22  E-value: 3.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243  271 QIQKRQQLVRKI---HEDELNDMKDYLSQCQQEQESFV-DYKSLKENLARcwtLTEA-EKMSFETQKTNLATENQYLrIS 345
Cdd:COG5022    883 QLQELKIDVKSIsslKLVNLELESEIIELKKSLSSDLIeNLEFKTELIAR---LKKLlNNIDLEEGPSIEYVKLPEL-NK 958
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243  346 LEKEEKALSSLQEELNKLREQiriledkgtSTELVRENQKLKQHLEEEKQKKHSFLSQRETLLAEAKMLKrELERERLVT 425
Cdd:COG5022    959 LHEVESKLKETSEEYEDLLKK---------STILVREGNKANSELKNFKKELAELSKQYGALQESTKQLK-ELPVEVAEL 1028
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243  426 TAL-------RGELQQLSGSQ-LHGKSDSPNVYTEKKEIAVLRERLSELERKLTFEQQRS 477
Cdd:COG5022   1029 QSAskiisseSTELSILKPLQkLKGLLLLENNQLQARYKALKLRRENSLLDDKQLYQLES 1088
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
337-501 3.82e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 40.88  E-value: 3.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243 337 TENQYLR--ISLEKEEKALS--SLQEELNKLrEQIRILEDKgtsTELVRENQKLKQhLEEEKQKKHSFLSQRETLLAEAK 412
Cdd:pfam17380 266 TENEFLNqlLHIVQHQKAVSerQQQEKFEKM-EQERLRQEK---EEKAREVERRRK-LEEAEKARQAEMDRQAAIYAEQE 340
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243 413 MLKRELERE--RLVTTALRGELQQLsgsqlhgksdspnvytEKKEIAVLRERLSELERkLTFEQQRSDLWERLYVEAKDQ 490
Cdd:pfam17380 341 RMAMEREREleRIRQEERKRELERI----------------RQEEIAMEISRMRELER-LQMERQQKNERVRQELEAARK 403
                         170
                  ....*....|.
gi 1622953243 491 SGKQETDGKKK 501
Cdd:pfam17380 404 VKILEEERQRK 414
GvpP COG4980
Gas vesicle protein YhaH [General function prediction only];
520-578 4.00e-03

Gas vesicle protein YhaH [General function prediction only];


Pssm-ID: 444004 [Multi-domain]  Cd Length: 106  Bit Score: 37.64  E-value: 4.00e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622953243 520 SVKETFDAMKNSTKEFVRHHKEKIKQAKEAVKENLKKFSDSVKSTFRHFKDTTKNIFDE 578
Cdd:COG4980    35 KLKDKADDLKDKAEDLKDELKEKASELSEEAKEKLDELIEEIKEKIEELKEEVEPKIEE 93
PTZ00121 PTZ00121
MAEBL; Provisional
274-589 5.27e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 5.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243  274 KRQQLVRKIHEDELNDMKDYLSQCQQEQESfvdyksLKENLARCWTLTEAEKMSFETQKTNLATENQYLRISLEKEEKAL 353
Cdd:PTZ00121  1546 KKADELKKAEELKKAEEKKKAEEAKKAEED------KNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAK 1619
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243  354 SSLQEELNKLREQIRILEDKGTSTELVRENQKLKQHLEEEKQKKHSFLSQRETLLAEAKMLKRELERERLVTTALRGELQ 433
Cdd:PTZ00121  1620 IKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAE 1699
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243  434 qlsgsqlhgksdspnvytEKKEIAVLRERLSELERKLtfEQQRSDlwERLYVEAKDQSGKQETDGKKKGGRGNHRAKNKS 513
Cdd:PTZ00121  1700 ------------------EAKKAEELKKKEAEEKKKA--EELKKA--EEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKK 1757
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622953243  514 KETFLGsvketfdamKNSTKEFVRHHKEKIKQAKEAVKENLKKFSDSVKSTFRHFKDTTKNIFD--EKGNKRFGATKE 589
Cdd:PTZ00121  1758 KIAHLK---------KEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEggKEGNLVINDSKE 1826
PRK10246 PRK10246
exonuclease subunit SbcC; Provisional
273-471 5.96e-03

exonuclease subunit SbcC; Provisional


Pssm-ID: 182330 [Multi-domain]  Cd Length: 1047  Bit Score: 40.17  E-value: 5.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243  273 QKRQQLvrKIHEDELNDMKdylSQCQQEQE--SFVDYKSLKENLARCWTLTEAEKMSFETQKTNLATENQYLRISLEKEE 350
Cdd:PRK10246   465 EMRQRY--KEKTQQLADVK---TICEQEARikDLEAQRAQLQAGQPCPLCGSTSHPAVEAYQALEPGVNQSRLDALEKEV 539
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243  351 KAL----SSLQEELNKLREQIRILEDKGTSteLVRENQKLKQHLE-----------------------EEKQKKHSFLSQ 403
Cdd:PRK10246   540 KKLgeegAALRGQLDALTKQLQRDESEAQS--LRQEEQALTQQWQavcaslnitlqpqddiqpwldaqEEHERQLRLLSQ 617
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243  404 RETL---LAEAKMLKRELERERLVT-TALRGELQQLS---------GSQLHGKSDSPNVYTEKK-EIAVLRERLSELERK 469
Cdd:PRK10246   618 RHELqgqIAAHNQQIIQYQQQIEQRqQQLLTALAGYAltlpqedeeASWLATRQQEAQSWQQRQnELTALQNRIQQLTPL 697

                   ..
gi 1622953243  470 LT 471
Cdd:PRK10246   698 LE 699
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
281-409 6.36e-03

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 38.73  E-value: 6.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243 281 KIHEDELNDMKDYLSQCQQEQESfvDYKSLKENLArcwtltEAEKMSFETQKT--NLATENQYLRISLEKEEKALSSLQE 358
Cdd:pfam13851   4 KNHEKAFNEIKNYYNDITRNNLE--LIKSLKEEIA------ELKKKEERNEKLmsEIQQENKRLTEPLQKAQEEVEELRK 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1622953243 359 EL---NKLREQIRILEDKGTSTElvRENQKLKQHLEEEKQKKHSFLSQRETLLA 409
Cdd:pfam13851  76 QLenyEKDKQSLKNLKARLKVLE--KELKDLKWEHEVLEQRFEKVERERDELYD 127
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
343-490 6.44e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 6.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243 343 RISLEKEEKALSSLQEELNKLREQIRILEDKGTSTELVRENQKLKQHLEEEKQKkhsflsQRETLLAEAKMLKRELERER 422
Cdd:COG1196   662 LTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEE------RLEEELEEEALEEQLEAERE 735
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243 423 LVTTALRGELQQLSGSQLHGKSDSPNVYTEKKEIAVLRERLSEL---------------ERKLTFEQQRSDLwerlyVEA 487
Cdd:COG1196   736 ELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALgpvnllaieeyeeleERYDFLSEQREDL-----EEA 810

                  ...
gi 1622953243 488 KDQ 490
Cdd:COG1196   811 RET 813
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
272-486 6.55e-03

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: 39.62  E-value: 6.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243  272 IQKRQQLVRKIHEDELND----MKDYLSQCQQEQESFVD-YKSLKENlARcwtlTEAEKMSFE-------TQKTNLATEn 339
Cdd:smart00787  79 ISEGRDLFKEIEEETLINnpplFKEYFSASPDVKLLMDKqFQLVKTF-AR----LEAKKMWYEwrmklleGLKEGLDEN- 152
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243  340 qylRISLEKEEKALSSLQEELNKLREQIRILEDkgtstELVRENQKLKQHLEEEKQKKHSFLSQretLLAEAKMLKRELE 419
Cdd:smart00787 153 ---LEGLKEDYKLLMKELELLNSIKPKLRDRKD-----ALEEELRQLKQLEDELEDCDPTELDR---AKEKLKKLLQEIM 221
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622953243  420 RERLVTTALRGELQQLSGsqlhgksdspNVYTEKKEIAVLRERLSELERKLtfeqQRSDLWERLYVE 486
Cdd:smart00787 222 IKVKKLEELEEELQELES----------KIEDLTNKKSELNTEIAEAEKKL----EQCRGFTFKEIE 274
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
346-488 7.43e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.90  E-value: 7.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243  346 LEKEEKALSSLQEELNKLREQIRILEDKG-TSTELVRENQKLKQHLEEEK-----QKKHSFL-SQRETLLA---EAKMLK 415
Cdd:COG4913    612 LAALEAELAELEEELAEAEERLEALEAELdALQERREALQRLAEYSWDEIdvasaEREIAELeAELERLDAssdDLAALE 691
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622953243  416 RELERERLVTTALRGELQQLSGSQLhgksdspnvyTEKKEIAVLRERLSELERKLTFEQQRSDLWERLYVEAK 488
Cdd:COG4913    692 EQLEELEAELEELEEELDELKGEIG----------RLEKELEQAEEELDELQDRLEAAEDLARLELRALLEER 754
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
345-501 8.10e-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: 39.36  E-value: 8.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243 345 SLEKEEKALSSLQEELNKLREQIRILEDKgtSTELVRENQKLKQHLEEEKQKKHSFLSQRETLLAEAKMLKRELERERLV 424
Cdd:COG4942    21 AAAEAEAELEQLQQEIAELEKELAALKKE--EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243 425 TTALRGEL-QQLSGSQLHGKSDSPNV-------------------YTE--KKEIAVLRERLSELERKLTFEQQRSDLWER 482
Cdd:COG4942    99 LEAQKEELaELLRALYRLGRQPPLALllspedfldavrrlqylkyLAParREQAEELRADLAELAALRAELEAERAELEA 178
                         170
                  ....*....|....*....
gi 1622953243 483 LYVEAKDQSGKQETDGKKK 501
Cdd:COG4942   179 LLAELEEERAALEALKAER 197
PRK12705 PRK12705
hypothetical protein; Provisional
251-412 8.49e-03

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 39.69  E-value: 8.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243 251 VILALVIAISMGFghFYGtiQIQKRQQLVRKIHEDELNDMKDYLSQCQQEQESFVDYKSLKENLARCWTLTEAEKMSFET 330
Cdd:PRK12705    8 VILLLLIGLLLGV--LVV--LLKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243 331 QKTNLATENQYLRIS--------LEKEEKALSSLQEELNKLREQIR-ILEDKGTSTELVRENQ---KLKQHLEEEKQKKH 398
Cdd:PRK12705   84 ERLVQKEEQLDARAEkldnlenqLEEREKALSARELELEELEKQLDnELYRVAGLTPEQARKLllkLLDAELEEEKAQRV 163
                         170
                  ....*....|....
gi 1622953243 399 SFLSQRETLLAEAK 412
Cdd:PRK12705  164 KKIEEEADLEAERK 177
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
271-440 8.82e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.12  E-value: 8.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243 271 QIQKRQQLVRKIHEdELNDMKDYLSQCQQEQESF-VDYKSLKENLARcwtlTEAEKMSFETQKTNLATENQYLRISLEKE 349
Cdd:COG4372    74 ELEQLEEELEELNE-QLQAAQAELAQAQEELESLqEEAEELQEELEE----LQKERQDLEQQRKQLEAQIAELQSEIAER 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953243 350 EKALSSLQEELNKLREQIRILEDKGTSTELVRENQKLKQHLEEEKQKKHSFLSQRETLLAEAKMLKRELERERLVTTALR 429
Cdd:COG4372   149 EEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLE 228
                         170
                  ....*....|.
gi 1622953243 430 GELQQLSGSQL 440
Cdd:COG4372   229 AKLGLALSALL 239
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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