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Conserved domains on  [gi|1904926754|ref|NP_001373822|]
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golgin subfamily A member 8A isoform 1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GOLGA2L5 super family cl25923
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ...
 218-397 1.56e-31

Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein family remains unknown. This family of proteins is thought to be found in the Golgi apparatus of eukaryotes.


The actual alignment was detected with superfamily member pfam15070:

Pssm-ID: 464485 [Multi-domain]  Cd Length: 521  Bit Score: 128.64  E-value: 1.56e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754 218 QLKESLKEVQLERDQYAEQIKGERAQWQQRMRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKNQMAEPLPPDA--PAVS 295
Cdd:pfam15070   1 QLMESLKQLQTERDQYAENLKEEGAVWQQKMQQLSEQVRTLREEKERSVSQVQELETSLAELKNQAAVPPAEEEqpPAGP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754 296 SEVE------LQDLRKELERVAGELQAQVENNQCISLLNRGQKERLREQEERLQEQQERLREREKRL------------- 356
Cdd:pfam15070  81 SEEEqrlqeeAEQLQKELEALAGQLQAQVQDNEQLSRLNQEQEQRLLELERAAERWGEQAEDRKQILedmqsdratisra 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1904926754 357 --------QQLAEPQSDLEELKHEN---KSALQLEQQVK-ELQEKLGQVMETL 397
Cdd:pfam15070 161 lsqnrelkEQLAELQNGFVKLTNENmelTSALQSEQHVKkELAKKLGQLQEEL 213
GM130_C pfam19046
GM130 C-terminal binding motif; This entry represents the C-terminal motif from the GM130 ...
 558-603 1.59e-22

GM130 C-terminal binding motif; This entry represents the C-terminal motif from the GM130 protein that is bound by the GRASP65 PDZ domain pfam04495.


:

Pssm-ID: 465957  Cd Length: 46  Bit Score: 90.52  E-value: 1.59e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1904926754 558 SSQDNPTAQPVVQLLGEMQDHQEHPGLGSNCCVPCFCWAWLPRRRR 603
Cdd:pfam19046   1 SPPENPTAQQIMQLLPEIQNPQEHPGLGSNPCIPFFYRADENDEVK 46
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 78-440 8.44e-13

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 71.51  E-value: 8.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754  78 LNSRSIKISRLNDTIKSLKQQKKQVEHQLEEEKKANNEKQKAERELEGQIQRLNTEKKKLNTDLYHMKHSLRYFEEESKD 157
Cdd:COG1196   227 AELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIAR 306

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754 158 LAGRLQRSSQRIGELEWSLCAVAATQkkkpdgfssrskALLKRQLEQSIREQILLKGHVTQLKESLKEVQLERDQYAEQI 237
Cdd:COG1196   307 LEERRRELEERLEELEEELAELEEEL------------EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754 238 KGERAQWQQRMRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKNQMAEplppdapAVSSEVELQDLRKELERVAGELQAQ 317
Cdd:COG1196   375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE-------LEELEEALAELEEEEEEEEEALEEA 447

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754 318 VENNQCISLLNRGQKERLREQEERLQEQQERLREREKRLQQLAEPQSDLEELK--HENKSALQLEQQVKELQEKLGQVME 395
Cdd:COG1196   448 AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEadYEGFLEGVKAALLLAGLRGLAGAVA 527

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1904926754 396 TLTSAEKEPEAAVPASGTGGESSGLMDLLEEKADLREHVEKLELG 440
Cdd:COG1196   528 VLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAG 572
 
Name Accession Description Interval E-value
GOLGA2L5 pfam15070
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ...
 218-397 1.56e-31

Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein family remains unknown. This family of proteins is thought to be found in the Golgi apparatus of eukaryotes.


Pssm-ID: 464485 [Multi-domain]  Cd Length: 521  Bit Score: 128.64  E-value: 1.56e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754 218 QLKESLKEVQLERDQYAEQIKGERAQWQQRMRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKNQMAEPLPPDA--PAVS 295
Cdd:pfam15070   1 QLMESLKQLQTERDQYAENLKEEGAVWQQKMQQLSEQVRTLREEKERSVSQVQELETSLAELKNQAAVPPAEEEqpPAGP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754 296 SEVE------LQDLRKELERVAGELQAQVENNQCISLLNRGQKERLREQEERLQEQQERLREREKRL------------- 356
Cdd:pfam15070  81 SEEEqrlqeeAEQLQKELEALAGQLQAQVQDNEQLSRLNQEQEQRLLELERAAERWGEQAEDRKQILedmqsdratisra 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1904926754 357 --------QQLAEPQSDLEELKHEN---KSALQLEQQVK-ELQEKLGQVMETL 397
Cdd:pfam15070 161 lsqnrelkEQLAELQNGFVKLTNENmelTSALQSEQHVKkELAKKLGQLQEEL 213
GM130_C pfam19046
GM130 C-terminal binding motif; This entry represents the C-terminal motif from the GM130 ...
 558-603 1.59e-22

GM130 C-terminal binding motif; This entry represents the C-terminal motif from the GM130 protein that is bound by the GRASP65 PDZ domain pfam04495.


Pssm-ID: 465957  Cd Length: 46  Bit Score: 90.52  E-value: 1.59e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1904926754 558 SSQDNPTAQPVVQLLGEMQDHQEHPGLGSNCCVPCFCWAWLPRRRR 603
Cdd:pfam19046   1 SPPENPTAQQIMQLLPEIQNPQEHPGLGSNPCIPFFYRADENDEVK 46
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 78-440 8.44e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 71.51  E-value: 8.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754  78 LNSRSIKISRLNDTIKSLKQQKKQVEHQLEEEKKANNEKQKAERELEGQIQRLNTEKKKLNTDLYHMKHSLRYFEEESKD 157
Cdd:COG1196   227 AELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIAR 306

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754 158 LAGRLQRSSQRIGELEWSLCAVAATQkkkpdgfssrskALLKRQLEQSIREQILLKGHVTQLKESLKEVQLERDQYAEQI 237
Cdd:COG1196   307 LEERRRELEERLEELEEELAELEEEL------------EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754 238 KGERAQWQQRMRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKNQMAEplppdapAVSSEVELQDLRKELERVAGELQAQ 317
Cdd:COG1196   375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE-------LEELEEALAELEEEEEEEEEALEEA 447

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754 318 VENNQCISLLNRGQKERLREQEERLQEQQERLREREKRLQQLAEPQSDLEELK--HENKSALQLEQQVKELQEKLGQVME 395
Cdd:COG1196   448 AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEadYEGFLEGVKAALLLAGLRGLAGAVA 527

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1904926754 396 TLTSAEKEPEAAVPASGTGGESSGLMDLLEEKADLREHVEKLELG 440
Cdd:COG1196   528 VLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAG 572
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 78-439 2.37e-08

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: 57.37  E-value: 2.37e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754   78 LNSRSIKISRLNDTIKSLKQQKKQVEHQLEEEKKANnEKQKAERELE-----GQIQRLNTEKKKLNTDLYHMkhslryfE 152
Cdd:TIGR02168  181 LERTRENLDRLEDILNELERQLKSLERQAEKAERYK-ELKAELRELElallvLRLEELREELEELQEELKEA-------E 252

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754  153 EESKDLAGRLQRSSQRIGELEwslcavaatqkkkpDGFSSRSKALLKRQ--LEQSIREQILLKGHVTQLKESLKEVQLER 230
Cdd:TIGR02168  253 EELEELTAELQELEEKLEELR--------------LEVSELEEEIEELQkeLYALANEISRLEQQKQILRERLANLERQL 318

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754  231 DQYAEQIkgerAQWQQRMRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKNQMAEplppdapavsSEVELQDLRKELERV 310
Cdd:TIGR02168  319 EELEAQL----EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEE----------LESRLEELEEQLETL 384

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754  311 AGEL-----QAQVENNQCISLLNRGQKERLREQEERLQEQQERLREREKRLQQLAEPQSDLEELKHENKSAL-QLEQQVK 384
Cdd:TIGR02168  385 RSKVaqlelQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELeRLEEALE 464

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1904926754  385 ELQEKLGQVMETLTSAEKEPEAAvpasgtGGESSGLMDLLEEKADLREHVEKLEL 439
Cdd:TIGR02168  465 ELREELEEAEQALDAAERELAQL------QARLDSLERLQENLEGFSEGVKALLK 513
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 92-438 2.94e-08

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: 56.99  E-value: 2.94e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754   92 IKSLKQQKKQVEHQLEEEKKANNEKQKAERELEGQIQRLNTEKKKLNTDLYHMKHSLRYFEEESKDLAGRLQRSSQRIGE 171
Cdd:TIGR02168  679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754  172 LEWSLcAVAATQKKKPDGFSSRSKAL----------LKRQLEQSIREQILLKGHVTQLKESLKEVQLERDQYAEQIKGER 241
Cdd:TIGR02168  759 LEAEI-EELEERLEEAEEELAEAEAEieeleaqieqLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATE 837

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754  242 AQW---QQRMRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKNQMAeplppdapavSSEVELQDLRKELERVAGELQaqv 318
Cdd:TIGR02168  838 RRLedlEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERA----------SLEEALALLRSELEELSEELR--- 904

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754  319 ENNQCISLLNRGQKERLREQEERLQEQQERLREREKRLQQLAEPQSDLEE--LKHENK---SALQLEQQVKELQEKLGQV 393
Cdd:TIGR02168  905 ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEeaEALENKiedDEEEARRRLKRLENKIKEL 984

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 1904926754  394 METLTSAEKEPEAavpasgtggESSGLMDLLEEKADLREHVEKLE 438
Cdd:TIGR02168  985 GPVNLAAIEEYEE---------LKERYDFLTAQKEDLTEAKETLE 1020
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
84-438 2.97e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 50.45  E-value: 2.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754  84 KISRLNDTIKS---LKQQKKQVEHQLEEEKKANNEKQKAERELEGQIQRLNTEKKKLNTdlyhMKHSLRYFEEESKDLAG 160
Cdd:PRK03918  177 RIERLEKFIKRtenIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEE----LKEEIEELEKELESLEG 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754 161 RLQRSSQRIGELEWSLcavaATQKKKPDGFSSRSKALlkRQLEQSIREQILLKGHVTQLKESLKEVQLERDQYAEQIKGE 240
Cdd:PRK03918  253 SKRKLEEKIRELEERI----EELKKEIEELEEKVKEL--KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGI 326

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754 241 RAQWQQRmRKMSQEVCTLKEEKKHDTHRVEELERS-------------LSRLKNQMAEPLPPDAPAVSSEV-----ELQD 302
Cdd:PRK03918  327 EERIKEL-EEKEERLEELKKKLKELEKRLEELEERhelyeeakakkeeLERLKKRLTGLTPEKLEKELEELekakeEIEE 405

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754 303 LRKELERVAGELQAQV-ENNQCISLLNR--------GQKERLREQEERLQEQQERLREREKRLQQLAEPQSDLEELKHEN 373
Cdd:PRK03918  406 EISKITARIGELKKEIkELKKAIEELKKakgkcpvcGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELREL 485

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1904926754 374 KSALQLE----------QQVKELQEKLGQV-METLTSAEKEPEAAVPAS-GTGGESSGLMDLLEEKADLREHVEKLE 438
Cdd:PRK03918  486 EKVLKKEseliklkelaEQLKELEEKLKKYnLEELEKKAEEYEKLKEKLiKLKGEIKSLKKELEKLEELKKKLAELE 562
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 92-403 2.51e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.62  E-value: 2.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754  92 IKSLKQQKKQ----VEHQLEEEKKANNEKQKAERELEGQIQRLNTEKKKLNTDLyhmkhslRYFEEESKDLAGRLQRSSQ 167
Cdd:COG1196   202 LEPLERQAEKaeryRELKEELKELEAELLLLKLRELEAELEELEAELEELEAEL-------EELEAELAELEAELEELRL 274

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754 168 RIGELEWslcAVAATQKKKpdgfssrskALLKRQLEQSIREQILLKGHVTQLKESLKEVQLERDQYAEQIkgerAQWQQR 247
Cdd:COG1196   275 ELEELEL---ELEEAQAEE---------YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL----EELEEE 338

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754 248 MRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKNQMAEplppdapavssevELQDLRKELERVAGELQAQVENNQCISLL 327
Cdd:COG1196   339 LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE-------------AEEELEELAEELLEALRAAAELAAQLEEL 405

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1904926754 328 NRGQKERLREQEERLQEQQERLREREKRLQQLAEPQSDLEELKHENKSALQLEQQVKELQEKLGQVMETLTSAEKE 403
Cdd:COG1196   406 EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 73-461 1.95e-04

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 44.58  E-value: 1.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754   73 EQAAVLNSRSIKISRLNDTIKSLKQQKKQVEHQLEEEKKANNEKQKAERELEGQIQRLNTEKKKLNTDLYHmkhsLRYFE 152
Cdd:pfam02463  160 EEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLD----YLKLN 235

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754  153 EESKDLAGRLQRSSQRIGELEwslcavAATQKKKPDGFSSRSKalLKRQLEQSIREQILLKGHVTQLKESLKEVQLERDQ 232
Cdd:pfam02463  236 EERIDLLQELLRDEQEEIESS------KQEIEKEEEKLAQVLK--ENKEEEKEKKLQEEELKLLAKEEEELKSELLKLER 307

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754  233 YAEQIKGERAQWQQRMRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKNQMAEPLPPDAPAVSSEVELQDLRKELErvAG 312
Cdd:pfam02463  308 RKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLES--ER 385

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754  313 ELQAQVENNQCISLLNRGQKERLREQEERLQEQQERLREREKRLQQLAEPQSDLEELKhENKSALQLEQQVKELQEKLGQ 392
Cdd:pfam02463  386 LSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQ-GKLTEEKEELEKQELKLLKDE 464

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1904926754  393 VMETLTSAEKEPEAAVPASGTGGESSGLMDLLEEKADLREHVE--KLELGFIQYRRERCHQKVHRLLTEPG 461
Cdd:pfam02463  465 LELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSglKVLLALIKDGVGGRIISAHGRLGDLG 535
TOPEUc smart00435
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina ...
 71-173 1.52e-03

DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina virus topoisomerase, Variola virus topoisomerase, Shope fibroma virus topoisomeras


Pssm-ID: 214661 [Multi-domain]  Cd Length: 391  Bit Score: 41.18  E-value: 1.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754   71 CQEQAAVLNSRSIKISRLNDTIKSLKQQKKQVEHQLEEEKKANNEKQKAERELEGQIQRLNTEKKKLNtdlyhmkhslRY 150
Cdd:smart00435 265 CNHQRTVSKTHEKSMEKLQEKIKALKYQLKRLKKMILLFEMISDLKRKLKSKFERDNEKLDAEVKEKK----------KE 334

                           90       100
                   ....*....|....*....|...
gi 1904926754  151 FEEESKDLAgRLQRSSQRIGELE 173
Cdd:smart00435 335 KKKEEKKKK-QIERLEERIEKLE 356
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
72-320 1.62e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.59  E-value: 1.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754  72 QEQAAVLNSRSIKISRLNDTIKSLKQQKKQ-------VEHQLEEEKKANNEKQKAE--RELEGQIQRLNTEKKKLNTDLY 142
Cdd:PRK03918  448 EHRKELLEEYTAELKRIEKELKEIEEKERKlrkelreLEKVLKKESELIKLKELAEqlKELEEKLKKYNLEELEKKAEEY 527

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754 143 H-MKHSLRYFEEESKDLAGRLQRSSQRIGELEWSLCAVAATQKKKPD--------GFSSRSKALLK-RQLEQSIREQILL 212
Cdd:PRK03918  528 EkLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAEllkeleelGFESVEELEERlKELEPFYNEYLEL 607

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754 213 KGHVTQLKESLKEVQLERDQyAEQIKGERAQWQQRMRKMSQEVCTLKEEKKHDTHR-----VEELERSLSRLKNQMAepl 287
Cdd:PRK03918  608 KDAEKELEREEKELKKLEEE-LDKAFEELAETEKRLEELRKELEELEKKYSEEEYEelreeYLELSRELAGLRAELE--- 683

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1904926754 288 ppdapavssevELQDLRKELERVAGELQAQVEN 320
Cdd:PRK03918  684 -----------ELEKRREEIKKTLEKLKEELEE 705
 
Name Accession Description Interval E-value
GOLGA2L5 pfam15070
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ...
 218-397 1.56e-31

Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein family remains unknown. This family of proteins is thought to be found in the Golgi apparatus of eukaryotes.


Pssm-ID: 464485 [Multi-domain]  Cd Length: 521  Bit Score: 128.64  E-value: 1.56e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754 218 QLKESLKEVQLERDQYAEQIKGERAQWQQRMRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKNQMAEPLPPDA--PAVS 295
Cdd:pfam15070   1 QLMESLKQLQTERDQYAENLKEEGAVWQQKMQQLSEQVRTLREEKERSVSQVQELETSLAELKNQAAVPPAEEEqpPAGP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754 296 SEVE------LQDLRKELERVAGELQAQVENNQCISLLNRGQKERLREQEERLQEQQERLREREKRL------------- 356
Cdd:pfam15070  81 SEEEqrlqeeAEQLQKELEALAGQLQAQVQDNEQLSRLNQEQEQRLLELERAAERWGEQAEDRKQILedmqsdratisra 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1904926754 357 --------QQLAEPQSDLEELKHEN---KSALQLEQQVK-ELQEKLGQVMETL 397
Cdd:pfam15070 161 lsqnrelkEQLAELQNGFVKLTNENmelTSALQSEQHVKkELAKKLGQLQEEL 213
GM130_C pfam19046
GM130 C-terminal binding motif; This entry represents the C-terminal motif from the GM130 ...
 558-603 1.59e-22

GM130 C-terminal binding motif; This entry represents the C-terminal motif from the GM130 protein that is bound by the GRASP65 PDZ domain pfam04495.


Pssm-ID: 465957  Cd Length: 46  Bit Score: 90.52  E-value: 1.59e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1904926754 558 SSQDNPTAQPVVQLLGEMQDHQEHPGLGSNCCVPCFCWAWLPRRRR 603
Cdd:pfam19046   1 SPPENPTAQQIMQLLPEIQNPQEHPGLGSNPCIPFFYRADENDEVK 46
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 78-440 8.44e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 71.51  E-value: 8.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754  78 LNSRSIKISRLNDTIKSLKQQKKQVEHQLEEEKKANNEKQKAERELEGQIQRLNTEKKKLNTDLYHMKHSLRYFEEESKD 157
Cdd:COG1196   227 AELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIAR 306

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754 158 LAGRLQRSSQRIGELEWSLCAVAATQkkkpdgfssrskALLKRQLEQSIREQILLKGHVTQLKESLKEVQLERDQYAEQI 237
Cdd:COG1196   307 LEERRRELEERLEELEEELAELEEEL------------EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754 238 KGERAQWQQRMRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKNQMAEplppdapAVSSEVELQDLRKELERVAGELQAQ 317
Cdd:COG1196   375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE-------LEELEEALAELEEEEEEEEEALEEA 447

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754 318 VENNQCISLLNRGQKERLREQEERLQEQQERLREREKRLQQLAEPQSDLEELK--HENKSALQLEQQVKELQEKLGQVME 395
Cdd:COG1196   448 AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEadYEGFLEGVKAALLLAGLRGLAGAVA 527

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1904926754 396 TLTSAEKEPEAAVPASGTGGESSGLMDLLEEKADLREHVEKLELG 440
Cdd:COG1196   528 VLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAG 572
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 64-285 3.29e-10

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: 62.09  E-value: 3.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754  64 LHARQSPCQEQAAVLNSRSIKISRLNDTIKSLKQQKKQVEHQLEEEKKANNEKQKAERELEGQIQRLNTEKKKLNTDLYH 143
Cdd:COG4942    15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754 144 MKHSLryfEEESKDLAGRLqRSSQRIGELEWSLCAVAAtqkKKPDGFSSRSKAL--LKRQLEQSIREQILLKGHVTQLKE 221
Cdd:COG4942    95 LRAEL---EAQKEELAELL-RALYRLGRQPPLALLLSP---EDFLDAVRRLQYLkyLAPARREQAEELRADLAELAALRA 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1904926754 222 SLKEVQLERDQYAEQIKGERAQWQQRMRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKNQMAE 285
Cdd:COG4942   168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 78-439 2.37e-08

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: 57.37  E-value: 2.37e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754   78 LNSRSIKISRLNDTIKSLKQQKKQVEHQLEEEKKANnEKQKAERELE-----GQIQRLNTEKKKLNTDLYHMkhslryfE 152
Cdd:TIGR02168  181 LERTRENLDRLEDILNELERQLKSLERQAEKAERYK-ELKAELRELElallvLRLEELREELEELQEELKEA-------E 252

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754  153 EESKDLAGRLQRSSQRIGELEwslcavaatqkkkpDGFSSRSKALLKRQ--LEQSIREQILLKGHVTQLKESLKEVQLER 230
Cdd:TIGR02168  253 EELEELTAELQELEEKLEELR--------------LEVSELEEEIEELQkeLYALANEISRLEQQKQILRERLANLERQL 318

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754  231 DQYAEQIkgerAQWQQRMRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKNQMAEplppdapavsSEVELQDLRKELERV 310
Cdd:TIGR02168  319 EELEAQL----EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEE----------LESRLEELEEQLETL 384

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754  311 AGEL-----QAQVENNQCISLLNRGQKERLREQEERLQEQQERLREREKRLQQLAEPQSDLEELKHENKSAL-QLEQQVK 384
Cdd:TIGR02168  385 RSKVaqlelQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELeRLEEALE 464

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1904926754  385 ELQEKLGQVMETLTSAEKEPEAAvpasgtGGESSGLMDLLEEKADLREHVEKLEL 439
Cdd:TIGR02168  465 ELREELEEAEQALDAAERELAQL------QARLDSLERLQENLEGFSEGVKALLK 513
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 92-438 2.94e-08

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: 56.99  E-value: 2.94e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754   92 IKSLKQQKKQVEHQLEEEKKANNEKQKAERELEGQIQRLNTEKKKLNTDLYHMKHSLRYFEEESKDLAGRLQRSSQRIGE 171
Cdd:TIGR02168  679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754  172 LEWSLcAVAATQKKKPDGFSSRSKAL----------LKRQLEQSIREQILLKGHVTQLKESLKEVQLERDQYAEQIKGER 241
Cdd:TIGR02168  759 LEAEI-EELEERLEEAEEELAEAEAEieeleaqieqLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATE 837

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754  242 AQW---QQRMRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKNQMAeplppdapavSSEVELQDLRKELERVAGELQaqv 318
Cdd:TIGR02168  838 RRLedlEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERA----------SLEEALALLRSELEELSEELR--- 904

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754  319 ENNQCISLLNRGQKERLREQEERLQEQQERLREREKRLQQLAEPQSDLEE--LKHENK---SALQLEQQVKELQEKLGQV 393
Cdd:TIGR02168  905 ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEeaEALENKiedDEEEARRRLKRLENKIKEL 984

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 1904926754  394 METLTSAEKEPEAavpasgtggESSGLMDLLEEKADLREHVEKLE 438
Cdd:TIGR02168  985 GPVNLAAIEEYEE---------LKERYDFLTAQKEDLTEAKETLE 1020
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 84-407 2.17e-07

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: 54.30  E-value: 2.17e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754   84 KISRLNDTIKSLKQQKKQVE---HQLEEEKKANNEKQKAE-RELEGQIQRLNTEKKKLNTDLYHMkhslryfEEESKDLA 159
Cdd:TIGR02169  185 NIERLDLIIDEKRQQLERLRrerEKAERYQALLKEKREYEgYELLKEKEALERQKEAIERQLASL-------EEELEKLT 257

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754  160 GRLQRSSQRIGELEWSLCAVAATQKKKPDGFSSRSK---ALLKRQLEQSIREQILLKGHVTQLKESLKEVQLERDQY--- 233
Cdd:TIGR02169  258 EEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKekiGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLlae 337

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754  234 AEQIKGERAQWQQRMRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKnqmaeplppdapavsseVELQDLRKELERVAGE 313
Cdd:TIGR02169  338 IEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETR-----------------DELKDYREKLEKLKRE 400

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754  314 LQAqvennqcislLNRGQKERLREQEERLQEQQERLREREKRLQQLAEPQSDLEELKHENKSALQ-----------LEQQ 382
Cdd:TIGR02169  401 INE----------LKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWkleqlaadlskYEQE 470

                          330       340
                   ....*....|....*....|....*
gi 1904926754  383 VKELQEKLGQVMETLTSAEKEPEAA 407
Cdd:TIGR02169  471 LYDLKEEYDRVEKELSKLQRELAEA 495
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 84-438 6.73e-07

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: 52.76  E-value: 6.73e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754   84 KISRLNDTIKSLKQQKKQVEHQLEEEKKANNEKQKAERELEGQIQRLNTEKKKLNTDLYHMKHSLRYFEEESKDLAGRLQ 163
Cdd:TIGR02169  682 RLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELK 761

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754  164 RSSQRIGELEWSLCAVAAtQKKKPDGFSSRSKALLKRQLEQSIREQIL-LKGHVTQLKESLKEVQLERdQYAEQikgERA 242
Cdd:TIGR02169  762 ELEARIEELEEDLHKLEE-ALNDLEARLSHSRIPEIQAELSKLEEEVSrIEARLREIEQKLNRLTLEK-EYLEK---EIQ 836

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754  243 QWQQRMRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKNQMAEplppdapavsSEVELQDLRKELERVAGELQAQVENNQ 322
Cdd:TIGR02169  837 ELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRD----------LESRLGDLKKERDELEAQLRELERKIE 906

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754  323 CIsllnrgqKERLREQEERLQEQQERLREREKRLQQLAEPQSDLEELKHENKSALQLEQQVKELQEKLGQVMETLTSAEK 402
Cdd:TIGR02169  907 EL-------EAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQ 979

                          330       340       350
                   ....*....|....*....|....*....|....*.
gi 1904926754  403 EPEAAVPASGTGGESsgLMDLLEEKADLREHVEKLE 438
Cdd:TIGR02169  980 EYEEVLKRLDELKEK--RAKLEEERKAILERIEEYE 1013
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
84-438 2.97e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 50.45  E-value: 2.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754  84 KISRLNDTIKS---LKQQKKQVEHQLEEEKKANNEKQKAERELEGQIQRLNTEKKKLNTdlyhMKHSLRYFEEESKDLAG 160
Cdd:PRK03918  177 RIERLEKFIKRtenIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEE----LKEEIEELEKELESLEG 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754 161 RLQRSSQRIGELEWSLcavaATQKKKPDGFSSRSKALlkRQLEQSIREQILLKGHVTQLKESLKEVQLERDQYAEQIKGE 240
Cdd:PRK03918  253 SKRKLEEKIRELEERI----EELKKEIEELEEKVKEL--KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGI 326

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754 241 RAQWQQRmRKMSQEVCTLKEEKKHDTHRVEELERS-------------LSRLKNQMAEPLPPDAPAVSSEV-----ELQD 302
Cdd:PRK03918  327 EERIKEL-EEKEERLEELKKKLKELEKRLEELEERhelyeeakakkeeLERLKKRLTGLTPEKLEKELEELekakeEIEE 405

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754 303 LRKELERVAGELQAQV-ENNQCISLLNR--------GQKERLREQEERLQEQQERLREREKRLQQLAEPQSDLEELKHEN 373
Cdd:PRK03918  406 EISKITARIGELKKEIkELKKAIEELKKakgkcpvcGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELREL 485

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1904926754 374 KSALQLE----------QQVKELQEKLGQV-METLTSAEKEPEAAVPAS-GTGGESSGLMDLLEEKADLREHVEKLE 438
Cdd:PRK03918  486 EKVLKKEseliklkelaEQLKELEEKLKKYnLEELEKKAEEYEKLKEKLiKLKGEIKSLKKELEKLEELKKKLAELE 562
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 72-308 3.54e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.32  E-value: 3.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754  72 QEQAAVLNSRSIKISRLNDTIKSLKQQKKQVEHQLEEEKKANNEKQKAERELEGQIQRLNTEKKKLNTDLYHMKHSLRYF 151
Cdd:COG1196   270 EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA 349

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754 152 EEESKDLAGRLQRSSQRIGELEwslcAVAATQKKKPDGFSSRSKALLKRQLEQSIREQILLK--GHVTQLKESLKEVQLE 229
Cdd:COG1196   350 EEELEEAEAELAEAEEALLEAE----AELAEAEEELEELAEELLEALRAAAELAAQLEELEEaeEALLERLERLEEELEE 425

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1904926754 230 RDQYAEQIKGERAQWQQRMRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKNQMAEPLPPDAPAVSSEVELQDLRKELE 308
Cdd:COG1196   426 LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 84-309 2.32e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.74  E-value: 2.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754   84 KISRLNDTIKSLKQQKKQVEHQLEEEKKANNEKQKAERELEGQIQRLNTEKKKLNTDLYHMKHSLRYFEEESKDLAGRLQ 163
Cdd:TIGR02168  748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE 827

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754  164 RSSQRIGELEWSLCAVAATQKKKPDGFSSRSKALlkRQLEQSIREQIllkghvTQLKESLKEVQlERDQYAEQIKGERAQ 243
Cdd:TIGR02168  828 SLERRIAATERRLEDLEEQIEELSEDIESLAAEI--EELEELIEELE------SELEALLNERA-SLEEALALLRSELEE 898

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754  244 WQQRMRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKN-----------------QMAEPLPPDAPAVSSEVE--LQDLR 304
Cdd:TIGR02168  899 LSEELRELESKRSELRRELEELREKLAQLELRLEGLEVridnlqerlseeysltlEEAEALENKIEDDEEEARrrLKRLE 978


                   ....*
gi 1904926754  305 KELER 309
Cdd:TIGR02168  979 NKIKE 983
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 92-403 2.51e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.62  E-value: 2.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754  92 IKSLKQQKKQ----VEHQLEEEKKANNEKQKAERELEGQIQRLNTEKKKLNTDLyhmkhslRYFEEESKDLAGRLQRSSQ 167
Cdd:COG1196   202 LEPLERQAEKaeryRELKEELKELEAELLLLKLRELEAELEELEAELEELEAEL-------EELEAELAELEAELEELRL 274

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754 168 RIGELEWslcAVAATQKKKpdgfssrskALLKRQLEQSIREQILLKGHVTQLKESLKEVQLERDQYAEQIkgerAQWQQR 247
Cdd:COG1196   275 ELEELEL---ELEEAQAEE---------YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL----EELEEE 338

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754 248 MRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKNQMAEplppdapavssevELQDLRKELERVAGELQAQVENNQCISLL 327
Cdd:COG1196   339 LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE-------------AEEELEELAEELLEALRAAAELAAQLEEL 405

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1904926754 328 NRGQKERLREQEERLQEQQERLREREKRLQQLAEPQSDLEELKHENKSALQLEQQVKELQEKLGQVMETLTSAEKE 403
Cdd:COG1196   406 EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 84-389 3.21e-05

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 46.94  E-value: 3.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754  84 KISRLNDTIKSLKQQKKQVEHQLEEEKKANNEKQKAERELEGQIQRLNTEKKKLNTDLYHMKHSLRYFEEESKDLAGRLQ 163
Cdd:TIGR04523 336 IISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIK 415

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754 164 RSSQRIGELEWSLCAVAATQKKKPDGFSSRSKAllKRQLEQSIREqilLKGHVTQLKESLKEVQLErdqyAEQIKGERAQ 243
Cdd:TIGR04523 416 KLQQEKELLEKEIERLKETIIKNNSEIKDLTNQ--DSVKELIIKN---LDNTRESLETQLKVLSRS----INKIKQNLEQ 486

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754 244 WQQRMRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKNQM----AEPLPPDAPAVSSEVELQDLRKELERVAGELQAQvE 319
Cdd:TIGR04523 487 KQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIekleSEKKEKESKISDLEDELNKDDFELKKENLEKEID-E 565

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1904926754 320 NNQCISLLNRGQKerlreqeerlqEQQERLREREKRLQQLAEPQSDL-EELKHENKSALQLEQQVKELQEK 389
Cdd:TIGR04523 566 KNKEIEELKQTQK-----------SLKKKQEEKQELIDQKEKEKKDLiKEIEEKEKKISSLEKELEKAKKE 625
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 78-405 7.45e-05

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 45.78  E-value: 7.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754  78 LNSRSIKISRLN-----DTIKSLKQQKKQVEHQLEEEKKANNEKQKAERELEGQIQRLNTEKKKLNTDLYHMKHSLRYFE 152
Cdd:TIGR04523 290 LNQLKSEISDLNnqkeqDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQ 369

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754 153 EESKDLAGRLQRSSQRIGELEWSlcavaatqkkkpdgfssrskallKRQLEQSIREQillKGHVTQLKESLKEVQLERDQ 232
Cdd:TIGR04523 370 NEIEKLKKENQSYKQEIKNLESQ-----------------------INDLESKIQNQ---EKLNQQKDEQIKKLQQEKEL 423

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754 233 YAEQIKGERAQwqqrMRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKNQMAEPLppdAPAVSSEVELQDLRKELERVAG 312
Cdd:TIGR04523 424 LEKEIERLKET----IIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLS---RSINKIKQNLEQKQKELKSKEK 496

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754 313 ELQAQVENNqciSLLNRGQKERLREQEERLQEQQERLREREKRLQQLAEPQSDLEELKHENKSAlQLEQQVKELQEKLGQ 392
Cdd:TIGR04523 497 ELKKLNEEK---KELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKE-NLEKEIDEKNKEIEE 572

                         330
                  ....*....|...
gi 1904926754 393 VMETLTSAEKEPE 405
Cdd:TIGR04523 573 LKQTQKSLKKKQE 585
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
74-308 7.73e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 45.78  E-value: 7.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754  74 QAAVLNSRSIKISRLNDTIKSLKQQKKQVEHQLEEekkannekqkAERELEGqiqrlntekkklntdlYHMKHSLRYFEE 153
Cdd:COG3206   159 EAYLEQNLELRREEARKALEFLEEQLPELRKELEE----------AEAALEE----------------FRQKNGLVDLSE 212

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754 154 ESKDLAGRLQRSSQRIGELEWSLCAVAATQkkkpdgfssrskALLKRQLEQSIREQILLKGH--VTQLKESLKEVQLERD 231
Cdd:COG3206   213 EAKLLLQQLSELESQLAEARAELAEAEARL------------AALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELA 280

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754 232 QYAE----------QIKGERAQWQQRMRKMSQEVC-TLKEEKKHDTHRVEELERSLSRLKNQMAEplppdAPAVssEVEL 300
Cdd:COG3206   281 ELSArytpnhpdviALRAQIAALRAQLQQEAQRILaSLEAELEALQAREASLQAQLAQLEARLAE-----LPEL--EAEL 353


                  ....*...
gi 1904926754 301 QDLRKELE 308
Cdd:COG3206   354 RRLEREVE 361
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 64-372 7.85e-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: 45.83  E-value: 7.85e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754   64 LHARQSPCQEQAAVLNSRSIKISRLNDTIKSLKQQKKQVEHQLE--EEKKANN--EKQKAERELEGQIQRLNTEKKKLNt 139
Cdd:TIGR02169  704 LDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSslEQEIENVksELKELEARIEELEEDLHKLEEALN- 782

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754  140 DLYHM--KHSLRYFEEESKDLAGRLQRSSQRIGELEwslcavAATQKKKPDGFSSRSK--------ALLKRQLEQSIREQ 209
Cdd:TIGR02169  783 DLEARlsHSRIPEIQAELSKLEEEVSRIEARLREIE------QKLNRLTLEKEYLEKEiqelqeqrIDLKEQIKSIEKEI 856

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754  210 ILLKGHVTQLKESLKEVQLERDQYAEQ---IKGERAQWQQRMRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKNQMAE- 285
Cdd:TIGR02169  857 ENLNGKKEELEEELEELEAALRDLESRlgdLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEi 936

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754  286 --PLPPDAPAVSSEVELQDLRKELERVAGELQAQVE-NNQCISLLNRGQKERLREQEERL--QEQQErlrerekrlqQLA 360
Cdd:TIGR02169  937 edPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPvNMLAIQEYEEVLKRLDELKEKRAklEEERK----------AIL 1006

                          330
                   ....*....|..
gi 1904926754  361 EPQSDLEELKHE 372
Cdd:TIGR02169 1007 ERIEEYEKKKRE 1018
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 68-403 9.73e-05

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 45.40  E-value: 9.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754  68 QSPCQEQAAVLNSRSIKISRLNDTIKSLKQQKKQVEHQLEEEKKANNEKQKAERELEGQIQRLNTEKKK-LNTDLyhmKH 146
Cdd:TIGR04523 238 QQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQdWNKEL---KS 314

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754 147 SLRYFEEESKDLAGRLQRSSQRIGELEWSlcaVAATQKKKPDGFSSRSKalLKRQLEQSIREQILLKGHVTQLKESLKEV 226
Cdd:TIGR04523 315 ELKNQEKKLEEIQNQISQNNKIISQLNEQ---ISQLKKELTNSESENSE--KQRELEEKQNEIEKLKKENQSYKQEIKNL 389

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754 227 QLER---DQYAEQIKGERAQWQQRMRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKNQMAeplppdapavssevELQDL 303
Cdd:TIGR04523 390 ESQIndlESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDS--------------VKELI 455

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754 304 RKELERVAGELQAQvennqcISLLNRGQKERLREQEERLqeqqerlrerekrlQQLAEPQSDLEELKHENKsalQLEQQV 383
Cdd:TIGR04523 456 IKNLDNTRESLETQ------LKVLSRSINKIKQNLEQKQ--------------KELKSKEKELKKLNEEKK---ELEEKV 512

                         330       340
                  ....*....|....*....|
gi 1904926754 384 KELQEKLGQVMETLTSAEKE 403
Cdd:TIGR04523 513 KDLTKKISSLKEKIEKLESE 532
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 73-246 1.52e-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: 45.05  E-value: 1.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754   73 EQAAVLNSRSIKISRLNDTIKSLKQQKKQVEHQLEEEKKANNEKQKAER---ELEGQIQRLNTEKKKLNTDLYHMKHSLR 149
Cdd:TIGR02168  324 QLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESrleELEEQLETLRSKVAQLELQIASLNNEIE 403

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754  150 YFEEESKDLAGRLQRSSQRIGELEWSLcavaatqkkkpdgfSSRSKALLKRQLEQSIREQILLKGHVTQLKESLKEVQLE 229
Cdd:TIGR02168  404 RLEARLERLEDRRERLQQEIEELLKKL--------------EEAELKELQAELEELEEELEELQEELERLEEALEELREE 469

                          170
                   ....*....|....*..
gi 1904926754  230 RDQYAEQIKGERAQWQQ 246
Cdd:TIGR02168  470 LEEAEQALDAAERELAQ 486
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
78-405 1.81e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.67  E-value: 1.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754  78 LNSRSIKISRLNDTIKSLKQQKKQVEHQLEEEKKANNEKQKAERELEGQIQR-------------LNTEKKKLNTDLYHM 144
Cdd:PRK03918  233 LEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKElkelkekaeeyikLSEFYEEYLDELREI 312

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754 145 KHSLRYFEEESKDLAGRLQRSSQRIGELEWSLCAVAATQKKKPDGFSS-----RSKALLKRQLEQSIREQILLKGHVTQL 219
Cdd:PRK03918  313 EKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERhelyeEAKAKKEELERLKKRLTGLTPEKLEKE 392

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754 220 KESLKEVQLERDQYAEQIKGERAQWQQRMRKMSQEVCTLKEEKKH---------DTHRVEELER---SLSRLKNQMAEpl 287
Cdd:PRK03918  393 LEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgreltEEHRKELLEEytaELKRIEKELKE-- 470

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754 288 ppdapavsSEVELQDLRKELERVAGELQAQVENNQCISLLNRGQKERLREQEERLQEQQERLREREKRLQQLAEPQSDLE 367
Cdd:PRK03918  471 --------IEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIK 542

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1904926754 368 ELKHENKSALQLEQQVKELQEKLGQVMETLTSAEKEPE 405
Cdd:PRK03918  543 SLKKELEKLEELKKKLAELEKKLDELEEELAELLKELE 580
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 73-461 1.95e-04

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 44.58  E-value: 1.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754   73 EQAAVLNSRSIKISRLNDTIKSLKQQKKQVEHQLEEEKKANNEKQKAERELEGQIQRLNTEKKKLNTDLYHmkhsLRYFE 152
Cdd:pfam02463  160 EEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLD----YLKLN 235

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754  153 EESKDLAGRLQRSSQRIGELEwslcavAATQKKKPDGFSSRSKalLKRQLEQSIREQILLKGHVTQLKESLKEVQLERDQ 232
Cdd:pfam02463  236 EERIDLLQELLRDEQEEIESS------KQEIEKEEEKLAQVLK--ENKEEEKEKKLQEEELKLLAKEEEELKSELLKLER 307

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754  233 YAEQIKGERAQWQQRMRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKNQMAEPLPPDAPAVSSEVELQDLRKELErvAG 312
Cdd:pfam02463  308 RKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLES--ER 385

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754  313 ELQAQVENNQCISLLNRGQKERLREQEERLQEQQERLREREKRLQQLAEPQSDLEELKhENKSALQLEQQVKELQEKLGQ 392
Cdd:pfam02463  386 LSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQ-GKLTEEKEELEKQELKLLKDE 464

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1904926754  393 VMETLTSAEKEPEAAVPASGTGGESSGLMDLLEEKADLREHVE--KLELGFIQYRRERCHQKVHRLLTEPG 461
Cdd:pfam02463  465 LELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSglKVLLALIKDGVGGRIISAHGRLGDLG 535
PTZ00121 PTZ00121
MAEBL; Provisional
 86-415 5.17e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 5.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754   86 SRLNDTIKSLKQQKKQVEHQLEEEKKANNEKQKAERELEGQIQRLNTEKKKlntdlyhmkhslryfEEESKDLAGRLQRS 165
Cdd:PTZ00121  1521 AKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKK---------------AEEDKNMALRKAEE 1585

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754  166 SQRIGELEWSLCAVAATQKKKpdgfsSRSKALLKRQLEQSIREQILLKGHVTQLKESLKEVQLERDQYAEQIKgeRAQWQ 245
Cdd:PTZ00121  1586 AKKAEEARIEEVMKLYEEEKK-----MKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELK--KAEEE 1658

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754  246 QRMRKMSQEVCTLKEEKKHDTHRVEELErslsrlKNQMAEPLPPDAPAVSSEVELQDLRKELERVAGELQAQVENNQcis 325
Cdd:PTZ00121  1659 NKIKAAEEAKKAEEDKKKAEEAKKAEED------EKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENK--- 1729

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754  326 lLNRGQKERLREQEERLQEQQERLREREKRLQQLAEPQSDLEELKHENKSALqLEQQVKELQEKLGQVMETLTSAEKEPE 405
Cdd:PTZ00121  1730 -IKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAV-IEEELDEEDEKRRMEVDKKIKDIFDNF 1807

                          330
                   ....*....|
gi 1904926754  406 AAVPASGTGG 415
Cdd:PTZ00121  1808 ANIIEGGKEG 1817
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 189-439 6.48e-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: 6.48e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754  189 GFSSRSKALLKRQLE-QSIREQI-LLKGHVTQLKESLKEVQLERDQYAEQIKGERAQWQQRMRKMSQ---EVCTLKEEKK 263
Cdd:TIGR02168  664 GSAKTNSSILERRREiEELEEKIeELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISAlrkDLARLEAEVE 743

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754  264 HDTHRVEELERSLSRLKNQMAEPLPPDAPAVSSEVELQDLRKELERVAGELQAQVENNQCISllnRGQKERLREQEERLQ 343
Cdd:TIGR02168  744 QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREAL---DELRAELTLLNEEAA 820

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754  344 EQQERLREREKRL-----------QQLAEPQSDLEELKHE----NKSALQLEQQVKELQEKLGQVMETLTSAEKEPEAAv 408
Cdd:TIGR02168  821 NLRERLESLERRIaaterrledleEQIEELSEDIESLAAEieelEELIEELESELEALLNERASLEEALALLRSELEEL- 899

                          250       260       270
                   ....*....|....*....|....*....|.
gi 1904926754  409 pASGTGGESSGLMDLLEEKADLREHVEKLEL 439
Cdd:TIGR02168  900 -SEELRELESKRSELRRELEELREKLAQLEL 929
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 198-297 7.09e-04

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 42.76  E-value: 7.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754 198 LKRQLEQ-SIREQILLKGHVTQLKESLKEVQLERDQYAEQIKGERAQWQQRmRKMSQEVCTLKEEKKHDTHRVEELERSL 276
Cdd:COG0542   416 LERRLEQlEIEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAE-KELIEEIQELKEELEQRYGKIPELEKEL 494

                          90       100
                  ....*....|....*....|.
gi 1904926754 277 SRLKNQMAEPLPPDAPAVSSE 297
Cdd:COG0542   495 AELEEELAELAPLLREEVTEE 515
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 83-285 8.23e-04

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 42.31  E-value: 8.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754  83 IKISRLNDTIKSLKQQKKQVEHQLEEEKKANNEKQKAERELEGQIQRLNTEKKKLNTDLYHMKHSLRYFEEESKDLAGRL 162
Cdd:TIGR04523 454 LIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEK 533

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754 163 QRSSQRIGELEwslcavaaTQKKKPDgfSSRSKALLKRQLEQSIREQILLKGHVTQLKESLKEVQLERDQYAEQIKGERA 242
Cdd:TIGR04523 534 KEKESKISDLE--------DELNKDD--FELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIK 603

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1904926754 243 QWQQRMRKMSQ---EVCTLKEEKKhdthRVEELERSLSRLKNQMAE 285
Cdd:TIGR04523 604 EIEEKEKKISSlekELEKAKKENE----KLSSIIKNIKSKKNKLKQ 645
TOPEUc smart00435
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina ...
 71-173 1.52e-03

DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina virus topoisomerase, Variola virus topoisomerase, Shope fibroma virus topoisomeras


Pssm-ID: 214661 [Multi-domain]  Cd Length: 391  Bit Score: 41.18  E-value: 1.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754   71 CQEQAAVLNSRSIKISRLNDTIKSLKQQKKQVEHQLEEEKKANNEKQKAERELEGQIQRLNTEKKKLNtdlyhmkhslRY 150
Cdd:smart00435 265 CNHQRTVSKTHEKSMEKLQEKIKALKYQLKRLKKMILLFEMISDLKRKLKSKFERDNEKLDAEVKEKK----------KE 334

                           90       100
                   ....*....|....*....|...
gi 1904926754  151 FEEESKDLAgRLQRSSQRIGELE 173
Cdd:smart00435 335 KKKEEKKKK-QIERLEERIEKLE 356
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
72-320 1.62e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.59  E-value: 1.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754  72 QEQAAVLNSRSIKISRLNDTIKSLKQQKKQ-------VEHQLEEEKKANNEKQKAE--RELEGQIQRLNTEKKKLNTDLY 142
Cdd:PRK03918  448 EHRKELLEEYTAELKRIEKELKEIEEKERKlrkelreLEKVLKKESELIKLKELAEqlKELEEKLKKYNLEELEKKAEEY 527

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754 143 H-MKHSLRYFEEESKDLAGRLQRSSQRIGELEWSLCAVAATQKKKPD--------GFSSRSKALLK-RQLEQSIREQILL 212
Cdd:PRK03918  528 EkLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAEllkeleelGFESVEELEERlKELEPFYNEYLEL 607

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754 213 KGHVTQLKESLKEVQLERDQyAEQIKGERAQWQQRMRKMSQEVCTLKEEKKHDTHR-----VEELERSLSRLKNQMAepl 287
Cdd:PRK03918  608 KDAEKELEREEKELKKLEEE-LDKAFEELAETEKRLEELRKELEELEKKYSEEEYEelreeYLELSRELAGLRAELE--- 683

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1904926754 288 ppdapavssevELQDLRKELERVAGELQAQVEN 320
Cdd:PRK03918  684 -----------ELEKRREEIKKTLEKLKEELEE 705
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 72-301 1.84e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.97  E-value: 1.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754  72 QEQAAVLNSRSIKISRLNDTIKSLKQQKKQVEHQLEEEKKANNEKQKAERELEGQIQRLNTEKKKLNTDLyhmkhslryf 151
Cdd:COG3883    19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL---------- 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754 152 eeesKDLAGRLQRSSQRIGELEwslcavAATQKKKPDGFSSRSKAL--LKRQLEQSIREQILLKGHVTQLKESLKEVQLE 229
Cdd:COG3883    89 ----GERARALYRSGGSVSYLD------VLLGSESFSDFLDRLSALskIADADADLLEELKADKAELEAKKAELEAKLAE 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1904926754 230 RDQYAEQIKGERAQWQQRMRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKNQMAEPLPPDAPAVSSEVELQ 301
Cdd:COG3883   159 LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
73-405 1.95e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 1.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754  73 EQAAVLNSRSIKISRLNDTIKSLKQQKKQVEHQLEEEKKANNEKQKAeRELEGQIQRLNTEKK-----KLNTDLYHMKHS 147
Cdd:PRK03918  321 EEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEA-KAKKEELERLKKRLTgltpeKLEKELEELEKA 399

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754 148 LRYFEEESKDLAGRLQRSSQRIGELEWSLCAVAATQKKKPdgfssrskaLLKRQLEQSIREQILLKGHVtQLKESLKEVQ 227
Cdd:PRK03918  400 KEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCP---------VCGRELTEEHRKELLEEYTA-ELKRIEKELK 469

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754 228 ----LERDQYAEQIKGERAQWQQR----MRKMSQEVCTLKEE-KKHDTHRVEELERSLSRLKNQMAEpLPPDAPAVSSEV 298
Cdd:PRK03918  470 eieeKERKLRKELRELEKVLKKESelikLKELAEQLKELEEKlKKYNLEELEKKAEEYEKLKEKLIK-LKGEIKSLKKEL 548

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754 299 E-LQDLRKELERVAGELQAQvennqcisllnrgQKERLREQEERLQEQQERLREREKRLQQLAEPQSDLEELKHENKSAL 377
Cdd:PRK03918  549 EkLEELKKKLAELEKKLDEL-------------EEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELE 615

                         330       340
                  ....*....|....*....|....*...
gi 1904926754 378 QLEQQVKELQEKLGQVMETLTSAEKEPE 405
Cdd:PRK03918  616 REEKELKKLEEELDKAFEELAETEKRLE 643
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 212-388 1.97e-03

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 41.36  E-value: 1.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754  212 LKGHVTQLKESLKEVQLERDQYAEQIKGERAQWQQRMRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKNQMAEPLPPDA 291
Cdd:pfam12128  267 YKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQ 346

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754  292 ---PAVSSEVELQDLR-KELERVAGELQAQVENnqcisllnRGQKERLREQEERLQEQQERLREREKRLQQLAEPQSDLE 367
Cdd:pfam12128  347 eqlPSWQSELENLEERlKALTGKHQDVTAKYNR--------RRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQ 418

                          170       180
                   ....*....|....*....|.
gi 1904926754  368 ELkhENKSALQLEQQVKELQE 388
Cdd:pfam12128  419 AL--ESELREQLEAGKLEFNE 437
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 78-403 2.66e-03

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 40.87  E-value: 2.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754   78 LNSRSIKISRLNDTIKSLKQQ-KKQVEHQLEEEKKANNEKQKAErELEGQIQRLNTEKKKLNTDLYHMKHSLRYFEEESK 156
Cdd:pfam15921  421 LDDRNMEVQRLEALLKAMKSEcQGQMERQMAAIQGKNESLEKVS-SLTAQLESTKEMLRKVVEELTAKKMTLESSERTVS 499

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754  157 DLAGRLQRSSQrigelewslcAVAATQKKKPdgfSSRSKALLKRQLEQSIREQILLKGHVTQLKESLKEVQLERDQYAE- 235
Cdd:pfam15921  500 DLTASLQEKER----------AIEATNAEIT---KLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEi 566

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754  236 ---------QIKG-----------ERAQWQQRMRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKNQMAEPLPPDAPAVS 295
Cdd:pfam15921  567 lrqqienmtQLVGqhgrtagamqvEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLR 646

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754  296 SeveLQDLRKELERVAGELQaqvennQCISLLNRGQKERLREQEERLQEQQERLREREKRLQQLAEPQSDLEELK----- 370
Cdd:pfam15921  647 A---VKDIKQERDQLLNEVK------TSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRntlks 717

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 1904926754  371 ------HENKSALQLEQQVK-------ELQEKLGQVMETLTSAEKE 403
Cdd:pfam15921  718 megsdgHAMKVAMGMQKQITakrgqidALQSKIQFLEEAMTNANKE 763
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
99-405 3.41e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 3.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754  99 KKQVEHQLEEEKKANNEKQKAERELEGQIQRLNTEKKKLNTDL-------------------YHMKHSLRYFEEESKDLA 159
Cdd:PRK03918  386 PEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIeelkkakgkcpvcgrelteEHRKELLEEYTAELKRIE 465

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754 160 GRLQRSSQRIGELEWSLCAVAATQKKKPDGFSSRSKALLKRQLEQSI-------------------REQILLKGHVTQLK 220
Cdd:PRK03918  466 KELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLkkynleelekkaeeyeklkEKLIKLKGEIKSLK 545

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754 221 ESLKEvqlerdqyAEQIKGERAQWQQRMRKMSQEVCTL-KEEKKHDTHRVEELERSLSRLKNQMAEPLPpdapAVSSEVE 299
Cdd:PRK03918  546 KELEK--------LEELKKKLAELEKKLDELEEELAELlKELEELGFESVEELEERLKELEPFYNEYLE----LKDAEKE 613

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754 300 LQDLRKELERVAGELQAQVENnqcislLNRGQKERLREQEERLQEQQERLREREKRL-QQLAEPQSDLEELKHENKSALQ 378
Cdd:PRK03918  614 LEREEKELKKLEEELDKAFEE------LAETEKRLEELRKELEELEKKYSEEEYEELrEEYLELSRELAGLRAELEELEK 687

                         330       340
                  ....*....|....*....|....*..
gi 1904926754 379 LEQQVKELQEKLGQVMETLTSAEKEPE 405
Cdd:PRK03918  688 RREEIKKTLEKLKEELEEREKAKKELE 714
PRK00106 PRK00106
ribonuclease Y;
95-317 3.64e-03

ribonuclease Y;


Pssm-ID: 178867 [Multi-domain]  Cd Length: 535  Bit Score: 40.24  E-value: 3.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754  95 LKQQKKQVEHQL-EEEKKANNEKQKAERELEGQIQRLNTEKKKLNTD-LYHMKHSLRYFEEEskdLAGRLQRSSQRIGEL 172
Cdd:PRK00106   26 MKSAKEAAELTLlNAEQEAVNLRGKAERDAEHIKKTAKRESKALKKElLLEAKEEARKYREE---IEQEFKSERQELKQI 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754 173 EWSLCAVAATQKKKPDGFSSRSKALlkRQLEQSIREQillKGHVTqlkeslkevqlERDQYAEQIKGERAQWQQRMRKMS 252
Cdd:PRK00106  103 ESRLTERATSLDRKDENLSSKEKTL--ESKEQSLTDK---SKHID-----------EREEQVEKLEEQKKAELERVAALS 166

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1904926754 253 QEVC---TLKEEKKHDTH----RVEELERSLSRLKNQMAEPLppdapavssevelqdLRKELERVAGELQAQ 317
Cdd:PRK00106  167 QAEAreiILAETENKLTHeiatRIREAEREVKDRSDKMAKDL---------------LAQAMQRLAGEYVTE 223
PTZ00121 PTZ00121
MAEBL; Provisional
 86-403 4.80e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.12  E-value: 4.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754   86 SRLNDTIKSLKQQKKQVEH---QLEEEKKANNEKQKAERELEG-QIQRLNTEKKKLNTDLYHMKHSLRYFEEESKDLAGR 161
Cdd:PTZ00121  1443 AKKADEAKKKAEEAKKAEEakkKAEEAKKADEAKKKAEEAKKAdEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAK 1522

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754  162 LQRSSQRIGELEWSLCAVAATQKKKPDGFSSRS---KALLKRQLEQSIREQ-----------ILLKGHVTQLKESLKEVQ 227
Cdd:PTZ00121  1523 KADEAKKAEEAKKADEAKKAEEKKKADELKKAEelkKAEEKKKAEEAKKAEedknmalrkaeEAKKAEEARIEEVMKLYE 1602

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754  228 LERDQYAEQIKGE-----RAQWQQRMRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKNQMAEPLPPDAPAVSSEVELQD 302
Cdd:PTZ00121  1603 EEKKMKAEEAKKAeeakiKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKK 1682

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754  303 LRKELERVAGELQAQVENNQCISLLNRGQKERLREQEERLQEQQERLREREKRLQQLAEPQSDLEELKHENKSALQLEQQ 382
Cdd:PTZ00121  1683 AEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHL 1762

                          330       340
                   ....*....|....*....|.
gi 1904926754  383 VKELQEKLGQVMETLTSAEKE 403
Cdd:PTZ00121  1763 KKEEEKKAEEIRKEKEAVIEE 1783
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 78-261 6.12e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 39.53  E-value: 6.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754  78 LNSRSIKISRLNDTIKS-------LKQQKKQVEHQLEEE--KKANNEKQKAERE---LEGQIQRLNTEKKKLNTDLYHMK 145
Cdd:PRK05771   48 LRSLLTKLSEALDKLRSylpklnpLREEKKKVSVKSLEEliKDVEEELEKIEKEikeLEEEISELENEIKELEQEIERLE 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754 146 hSLRYFEEESKDL---------AGRLQRSSQRIGELEWSLC-------------AVAATQKKKPDgfsSRSKALLKRQLE 203
Cdd:PRK05771  128 -PWGNFDLDLSLLlgfkyvsvfVGTVPEDKLEELKLESDVEnveyistdkgyvyVVVVVLKELSD---EVEEELKKLGFE 203

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1904926754 204 qsiREQILLKGHVTQ----LKESLKEVQLERDQYAEQIKGERAQWQQRMRKMSQEVCTLKEE 261
Cdd:PRK05771  204 ---RLELEEEGTPSElireIKEELEEIEKERESLLEELKELAKKYLEELLALYEYLEIELER 262
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
195-390 7.50e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 39.23  E-value: 7.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754 195 KALLKRQLEQSIREQILLKGHVTQLKESLKEVQLERDQYAEQ-----IKGERAQWQQRMRKMSQEVCTLKEEKkhdthrv 269
Cdd:COG3206   163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKnglvdLSEEAKLLLQQLSELESQLAEARAEL------- 235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754 270 EELERSLSRLKNQMAEPlPPDAPAVSSEVELQDLRKELERVAGELQAQV-----ENNQCISLLNRGQKERLREQEERLQE 344
Cdd:COG3206   236 AEAEARLAALRAQLGSG-PDALPELLQSPVIQQLRAQLAELEAELAELSarytpNHPDVIALRAQIAALRAQLQQEAQRI 314

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1904926754 345 QQERLREREKRLQQLAEPQSDLEELKHENKSALQLEQQVKELQEKL 390
Cdd:COG3206   315 LASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREV 360
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 64-322 7.59e-03

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 39.32  E-value: 7.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754  64 LHARQSPCQEQAAVLNSRSIKISRLNDTI---KSLKQQKKQVEhqleeekKANNEKQKAERELEGQIQRLNTEKKKLNTD 140
Cdd:pfam05483 386 LQKKSSELEEMTKFKNNKEVELEELKKILaedEKLLDEKKQFE-------KIAEELKGKEQELIFLLQAREKEIHDLEIQ 458

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754 141 LYHMKHSLRYFEEESKDLAGRLQRSSQRIGELEWSLCAVAATQKKKPDGFSSRSKAL---------LKRQLEQSIREQIL 211
Cdd:pfam05483 459 LTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELkkhqediinCKKQEERMLKQIEN 538

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754 212 LKGHVTQLKESLKEVQLERDQYAEQIKGERAQWQQRMRKMSQEVCTLKEEKKHDTHRVEELERSLSRlKNQMAEPLPPDA 291
Cdd:pfam05483 539 LEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIEN-KNKNIEELHQEN 617

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1904926754 292 PAVSS------------EVELQDLRKELERVAGELQAQVENNQ 322
Cdd:pfam05483 618 KALKKkgsaenkqlnayEIKVNKLELELASAKQKFEEIIDNYQ 660
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 97-273 8.21e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 39.18  E-value: 8.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754   97 QQKKQVEHQLEEEKKANNEKQKAERELEGqiqrLNTEKKKLNTDLYHMKHSLRYFEEESK-------DLAGRLQRSSQRI 169
Cdd:TIGR00618  670 LPKELLASRQLALQKMQSEKEQLTYWKEM----LAQCQTLLRELETHIEEYDREFNEIENassslgsDLAAREDALNQSL 745

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754  170 GELE----WSLCAVAATQKKKpdgfSSRSKALLKR-----QLEQSIREQI-LLKGHVTQLKESLKEVQLERDQYA----- 234
Cdd:TIGR00618  746 KELMhqarTVLKARTEAHFNN----NEEVTAALQTgaelsHLAAEIQFFNrLREEDTHLLKTLEAEIGQEIPSDEdilnl 821

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1904926754  235 --EQIKGERAQWQQRMRKMSQEVCTLKEEKKHDTHRVEELE 273
Cdd:TIGR00618  822 qcETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLA 862
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
80-398 8.36e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.28  E-value: 8.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754  80 SRSIKISRLNDTIKSLKQQKKqvEHQLEEEKKANNEKQKAERE---LEGQIQRLNTEKKKLNTdlyhMKHSLRYFEEESK 156
Cdd:PRK03918  493 SELIKLKELAEQLKELEEKLK--KYNLEELEKKAEEYEKLKEKlikLKGEIKSLKKELEKLEE----LKKKLAELEKKLD 566

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754 157 DLAGRLQRSSQRIGELewslcavaatqkkkpdGFSSRSKALLK-RQLEQSIREQILLKGHVTQLKESLKEVQLERDQyAE 235
Cdd:PRK03918  567 ELEEELAELLKELEEL----------------GFESVEELEERlKELEPFYNEYLELKDAEKELEREEKELKKLEEE-LD 629

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754 236 QIKGERAQWQQRMRKMSQEVCTLKEEKKHDTHR-----VEELERSLSRLKNQMAEplppdapavsseveLQDLRKELERV 310
Cdd:PRK03918  630 KAFEELAETEKRLEELRKELEELEKKYSEEEYEelreeYLELSRELAGLRAELEE--------------LEKRREEIKKT 695

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754 311 AGELQAQvennqcisllnrgqkerlreqeerlqeqQERLREREKRLQQLAEPQSDLEELKHENKS--ALQLEQQVKELQE 388
Cdd:PRK03918  696 LEKLKEE----------------------------LEEREKAKKELEKLEKALERVEELREKVKKykALLKERALSKVGE 747

                         330
                  ....*....|
gi 1904926754 389 KLGQVMETLT 398
Cdd:PRK03918  748 IASEIFEELT 757
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 191-414 9.48e-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: 38.59  E-value: 9.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754 191 SSRSKALLKRQLEQSIREQILLKGHVTQLKESLKEVQLERDQYAEQIkgerAQWQQRMRKMSQEVCTLKEEKKHDTHRVE 270
Cdd:COG4942    18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRI----AALARRIRALEQELAALEAELAELEKEIA 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754 271 ELERSLSRLKNQMAEPL---------PPDAPAVSSEVELQDLRKE--LERVAGELQAQVE----NNQCISLLNRGQKERL 335
Cdd:COG4942    94 ELRAELEAQKEELAELLralyrlgrqPPLALLLSPEDFLDAVRRLqyLKYLAPARREQAEelraDLAELAALRAELEAER 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904926754 336 REQEERLQEQQERLREREKRLQQLAEPQSDLE-ELKHENKSALQLEQQVKELQEKLGQVMETLTSAEKEPEAAVPASGTG 414
Cdd:COG4942   174 AELEALLAELEEERAALEALKAERQKLLARLEkELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKG 253
 
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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