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Conserved domains on  [gi|31083099|ref|NP_851422|]
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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 31083099   218 QLKESLKEVQLERDQYAEQIKGERAQWQQRMRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKNQMAEPLPPDA--PAVS 295
Cdd:pfam15070   1 QLMESLKQLQTERDQYAENLKEEGAVWQQKMQQLSEQVRTLREEKERSVSQVQELETSLAELKNQAAVPPAEEEqpPAGP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099   296 SEVE------LQDLRKELERVAGELQAQVENNQCISLLNRGQKERLREQEERLQEQQERLREREKRL------------- 356
Cdd:pfam15070  81 SEEEqrlqeeAEQLQKELEALAGQLQAQVQDNEQLSRLNQEQEQRLLELERAAERWGEQAEDRKQILedmqsdratisra 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 31083099   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 31083099   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 31083099  78 LNSRSIKISRLNDTIKSLKQQKKQVEHQLEEEKKANNEKQKAERELEGQIQRLNTEKKKLNTDLYHMKHSLRYFEEESKD 157
Cdd:COG1196 227 AELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIAR 306
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099 158 LAGRLQRSSQRIGELEWSLCAVAATQkkkpdgfssrskALLKRQLEQSIREQILLKGHVTQLKESLKEVQLERDQYAEQI 237
Cdd:COG1196 307 LEERRRELEERLEELEEELAELEEEL------------EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099 238 KGERAQWQQRMRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKNQMAEplppdapAVSSEVELQDLRKELERVAGELQAQ 317
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE-------LEELEEALAELEEEEEEEEEALEEA 447
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099 318 VENNQCISLLNRGQKERLREQEERLQEQQERLREREKRLQQLAEPQSDLEELK--HENKSALQLEQQVKELQEKLGQVME 395
Cdd:COG1196 448 AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEadYEGFLEGVKAALLLAGLRGLAGAVA 527
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
gi 31083099 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 31083099   218 QLKESLKEVQLERDQYAEQIKGERAQWQQRMRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKNQMAEPLPPDA--PAVS 295
Cdd:pfam15070   1 QLMESLKQLQTERDQYAENLKEEGAVWQQKMQQLSEQVRTLREEKERSVSQVQELETSLAELKNQAAVPPAEEEqpPAGP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099   296 SEVE------LQDLRKELERVAGELQAQVENNQCISLLNRGQKERLREQEERLQEQQERLREREKRL------------- 356
Cdd:pfam15070  81 SEEEqrlqeeAEQLQKELEALAGQLQAQVQDNEQLSRLNQEQEQRLLELERAAERWGEQAEDRKQILedmqsdratisra 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 31083099   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 31083099   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 31083099  78 LNSRSIKISRLNDTIKSLKQQKKQVEHQLEEEKKANNEKQKAERELEGQIQRLNTEKKKLNTDLYHMKHSLRYFEEESKD 157
Cdd:COG1196 227 AELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIAR 306
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099 158 LAGRLQRSSQRIGELEWSLCAVAATQkkkpdgfssrskALLKRQLEQSIREQILLKGHVTQLKESLKEVQLERDQYAEQI 237
Cdd:COG1196 307 LEERRRELEERLEELEEELAELEEEL------------EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099 238 KGERAQWQQRMRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKNQMAEplppdapAVSSEVELQDLRKELERVAGELQAQ 317
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE-------LEELEEALAELEEEEEEEEEALEEA 447
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099 318 VENNQCISLLNRGQKERLREQEERLQEQQERLREREKRLQQLAEPQSDLEELK--HENKSALQLEQQVKELQEKLGQVME 395
Cdd:COG1196 448 AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEadYEGFLEGVKAALLLAGLRGLAGAVA 527
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
gi 31083099 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 31083099     78 LNSRSIKISRLNDTIKSLKQQKKQVEHQLEEEKKANnEKQKAERELE-----GQIQRLNTEKKKLNTDLYHMkhslryfE 152
Cdd:TIGR02168  181 LERTRENLDRLEDILNELERQLKSLERQAEKAERYK-ELKAELRELElallvLRLEELREELEELQEELKEA-------E 252
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099    153 EESKDLAGRLQRSSQRIGELEwslcavaatqkkkpDGFSSRSKALLKRQ--LEQSIREQILLKGHVTQLKESLKEVQLER 230
Cdd:TIGR02168  253 EELEELTAELQELEEKLEELR--------------LEVSELEEEIEELQkeLYALANEISRLEQQKQILRERLANLERQL 318
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099    231 DQYAEQIkgerAQWQQRMRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKNQMAEplppdapavsSEVELQDLRKELERV 310
Cdd:TIGR02168  319 EELEAQL----EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEE----------LESRLEELEEQLETL 384
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099    311 AGEL-----QAQVENNQCISLLNRGQKERLREQEERLQEQQERLREREKRLQQLAEPQSDLEELKHENKSAL-QLEQQVK 384
Cdd:TIGR02168  385 RSKVaqlelQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELeRLEEALE 464
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 31083099    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 31083099     92 IKSLKQQKKQVEHQLEEEKKANNEKQKAERELEGQIQRLNTEKKKLNTDLYHMKHSLRYFEEESKDLAGRLQRSSQRIGE 171
Cdd:TIGR02168  679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099    172 LEWSLcAVAATQKKKPDGFSSRSKAL----------LKRQLEQSIREQILLKGHVTQLKESLKEVQLERDQYAEQIKGER 241
Cdd:TIGR02168  759 LEAEI-EELEERLEEAEEELAEAEAEieeleaqieqLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATE 837
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099    242 AQW---QQRMRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKNQMAeplppdapavSSEVELQDLRKELERVAGELQaqv 318
Cdd:TIGR02168  838 RRLedlEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERA----------SLEEALALLRSELEELSEELR--- 904
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099    319 ENNQCISLLNRGQKERLREQEERLQEQQERLREREKRLQQLAEPQSDLEE--LKHENK---SALQLEQQVKELQEKLGQV 393
Cdd:TIGR02168  905 ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEeaEALENKiedDEEEARRRLKRLENKIKEL 984
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 31083099    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 31083099   84 KISRLNDTIKS---LKQQKKQVEHQLEEEKKANNEKQKAERELEGQIQRLNTEKKKLNTdlyhMKHSLRYFEEESKDLAG 160
Cdd:PRK03918 177 RIERLEKFIKRtenIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEE----LKEEIEELEKELESLEG 252
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099  161 RLQRSSQRIGELEWSLcavaATQKKKPDGFSSRSKALlkRQLEQSIREQILLKGHVTQLKESLKEVQLERDQYAEQIKGE 240
Cdd:PRK03918 253 SKRKLEEKIRELEERI----EELKKEIEELEEKVKEL--KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGI 326
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099  241 RAQWQQRmRKMSQEVCTLKEEKKHDTHRVEELERS-------------LSRLKNQMAEPLPPDAPAVSSEV-----ELQD 302
Cdd:PRK03918 327 EERIKEL-EEKEERLEELKKKLKELEKRLEELEERhelyeeakakkeeLERLKKRLTGLTPEKLEKELEELekakeEIEE 405
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099  303 LRKELERVAGELQAQV-ENNQCISLLNR--------GQKERLREQEERLQEQQERLREREKRLQQLAEPQSDLEELKHEN 373
Cdd:PRK03918 406 EISKITARIGELKKEIkELKKAIEELKKakgkcpvcGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELREL 485
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 31083099  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 31083099  92 IKSLKQQKKQ----VEHQLEEEKKANNEKQKAERELEGQIQRLNTEKKKLNTDLyhmkhslRYFEEESKDLAGRLQRSSQ 167
Cdd:COG1196 202 LEPLERQAEKaeryRELKEELKELEAELLLLKLRELEAELEELEAELEELEAEL-------EELEAELAELEAELEELRL 274
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099 168 RIGELEWslcAVAATQKKKpdgfssrskALLKRQLEQSIREQILLKGHVTQLKESLKEVQLERDQYAEQIkgerAQWQQR 247
Cdd:COG1196 275 ELEELEL---ELEEAQAEE---------YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL----EELEEE 338
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099 248 MRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKNQMAEplppdapavssevELQDLRKELERVAGELQAQVENNQCISLL 327
Cdd:COG1196 339 LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE-------------AEEELEELAEELLEALRAAAELAAQLEEL 405
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31083099 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 31083099     73 EQAAVLNSRSIKISRLNDTIKSLKQQKKQVEHQLEEEKKANNEKQKAERELEGQIQRLNTEKKKLNTDLYHmkhsLRYFE 152
Cdd:pfam02463  160 EEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLD----YLKLN 235
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099    153 EESKDLAGRLQRSSQRIGELEwslcavAATQKKKPDGFSSRSKalLKRQLEQSIREQILLKGHVTQLKESLKEVQLERDQ 232
Cdd:pfam02463  236 EERIDLLQELLRDEQEEIESS------KQEIEKEEEKLAQVLK--ENKEEEKEKKLQEEELKLLAKEEEELKSELLKLER 307
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099    233 YAEQIKGERAQWQQRMRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKNQMAEPLPPDAPAVSSEVELQDLRKELErvAG 312
Cdd:pfam02463  308 RKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLES--ER 385
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099    313 ELQAQVENNQCISLLNRGQKERLREQEERLQEQQERLREREKRLQQLAEPQSDLEELKhENKSALQLEQQVKELQEKLGQ 392
Cdd:pfam02463  386 LSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQ-GKLTEEKEELEKQELKLLKDE 464
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 31083099    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 31083099     71 CQEQAAVLNSRSIKISRLNDTIKSLKQQKKQVEHQLEEEKKANNEKQKAERELEGQIQRLNTEKKKLNtdlyhmkhslRY 150
Cdd:smart00435 265 CNHQRTVSKTHEKSMEKLQEKIKALKYQLKRLKKMILLFEMISDLKRKLKSKFERDNEKLDAEVKEKK----------KE 334
                           90       100
                   ....*....|....*....|...
gi 31083099    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 31083099   72 QEQAAVLNSRSIKISRLNDTIKSLKQQKKQ-------VEHQLEEEKKANNEKQKAE--RELEGQIQRLNTEKKKLNTDLY 142
Cdd:PRK03918 448 EHRKELLEEYTAELKRIEKELKEIEEKERKlrkelreLEKVLKKESELIKLKELAEqlKELEEKLKKYNLEELEKKAEEY 527
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099  143 H-MKHSLRYFEEESKDLAGRLQRSSQRIGELEWSLCAVAATQKKKPD--------GFSSRSKALLK-RQLEQSIREQILL 212
Cdd:PRK03918 528 EkLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAEllkeleelGFESVEELEERlKELEPFYNEYLEL 607
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099  213 KGHVTQLKESLKEVQLERDQyAEQIKGERAQWQQRMRKMSQEVCTLKEEKKHDTHR-----VEELERSLSRLKNQMAepl 287
Cdd:PRK03918 608 KDAEKELEREEKELKKLEEE-LDKAFEELAETEKRLEELRKELEELEKKYSEEEYEelreeYLELSRELAGLRAELE--- 683
                        250       260       270
                 ....*....|....*....|....*....|...
gi 31083099  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 31083099   218 QLKESLKEVQLERDQYAEQIKGERAQWQQRMRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKNQMAEPLPPDA--PAVS 295
Cdd:pfam15070   1 QLMESLKQLQTERDQYAENLKEEGAVWQQKMQQLSEQVRTLREEKERSVSQVQELETSLAELKNQAAVPPAEEEqpPAGP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099   296 SEVE------LQDLRKELERVAGELQAQVENNQCISLLNRGQKERLREQEERLQEQQERLREREKRL------------- 356
Cdd:pfam15070  81 SEEEqrlqeeAEQLQKELEALAGQLQAQVQDNEQLSRLNQEQEQRLLELERAAERWGEQAEDRKQILedmqsdratisra 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 31083099   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 31083099   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 31083099  78 LNSRSIKISRLNDTIKSLKQQKKQVEHQLEEEKKANNEKQKAERELEGQIQRLNTEKKKLNTDLYHMKHSLRYFEEESKD 157
Cdd:COG1196 227 AELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIAR 306
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099 158 LAGRLQRSSQRIGELEWSLCAVAATQkkkpdgfssrskALLKRQLEQSIREQILLKGHVTQLKESLKEVQLERDQYAEQI 237
Cdd:COG1196 307 LEERRRELEERLEELEEELAELEEEL------------EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099 238 KGERAQWQQRMRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKNQMAEplppdapAVSSEVELQDLRKELERVAGELQAQ 317
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE-------LEELEEALAELEEEEEEEEEALEEA 447
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099 318 VENNQCISLLNRGQKERLREQEERLQEQQERLREREKRLQQLAEPQSDLEELK--HENKSALQLEQQVKELQEKLGQVME 395
Cdd:COG1196 448 AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEadYEGFLEGVKAALLLAGLRGLAGAVA 527
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
gi 31083099 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 31083099  64 LHARQSPCQEQAAVLNSRSIKISRLNDTIKSLKQQKKQVEHQLEEEKKANNEKQKAERELEGQIQRLNTEKKKLNTDLYH 143
Cdd:COG4942  15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099 144 MKHSLryfEEESKDLAGRLqRSSQRIGELEWSLCAVAAtqkKKPDGFSSRSKAL--LKRQLEQSIREQILLKGHVTQLKE 221
Cdd:COG4942  95 LRAEL---EAQKEELAELL-RALYRLGRQPPLALLLSP---EDFLDAVRRLQYLkyLAPARREQAEELRADLAELAALRA 167
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 31083099 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 31083099     78 LNSRSIKISRLNDTIKSLKQQKKQVEHQLEEEKKANnEKQKAERELE-----GQIQRLNTEKKKLNTDLYHMkhslryfE 152
Cdd:TIGR02168  181 LERTRENLDRLEDILNELERQLKSLERQAEKAERYK-ELKAELRELElallvLRLEELREELEELQEELKEA-------E 252
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099    153 EESKDLAGRLQRSSQRIGELEwslcavaatqkkkpDGFSSRSKALLKRQ--LEQSIREQILLKGHVTQLKESLKEVQLER 230
Cdd:TIGR02168  253 EELEELTAELQELEEKLEELR--------------LEVSELEEEIEELQkeLYALANEISRLEQQKQILRERLANLERQL 318
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099    231 DQYAEQIkgerAQWQQRMRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKNQMAEplppdapavsSEVELQDLRKELERV 310
Cdd:TIGR02168  319 EELEAQL----EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEE----------LESRLEELEEQLETL 384
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099    311 AGEL-----QAQVENNQCISLLNRGQKERLREQEERLQEQQERLREREKRLQQLAEPQSDLEELKHENKSAL-QLEQQVK 384
Cdd:TIGR02168  385 RSKVaqlelQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELeRLEEALE 464
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 31083099    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 31083099     92 IKSLKQQKKQVEHQLEEEKKANNEKQKAERELEGQIQRLNTEKKKLNTDLYHMKHSLRYFEEESKDLAGRLQRSSQRIGE 171
Cdd:TIGR02168  679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099    172 LEWSLcAVAATQKKKPDGFSSRSKAL----------LKRQLEQSIREQILLKGHVTQLKESLKEVQLERDQYAEQIKGER 241
Cdd:TIGR02168  759 LEAEI-EELEERLEEAEEELAEAEAEieeleaqieqLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATE 837
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099    242 AQW---QQRMRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKNQMAeplppdapavSSEVELQDLRKELERVAGELQaqv 318
Cdd:TIGR02168  838 RRLedlEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERA----------SLEEALALLRSELEELSEELR--- 904
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099    319 ENNQCISLLNRGQKERLREQEERLQEQQERLREREKRLQQLAEPQSDLEE--LKHENK---SALQLEQQVKELQEKLGQV 393
Cdd:TIGR02168  905 ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEeaEALENKiedDEEEARRRLKRLENKIKEL 984
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 31083099    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 31083099     84 KISRLNDTIKSLKQQKKQVE---HQLEEEKKANNEKQKAE-RELEGQIQRLNTEKKKLNTDLYHMkhslryfEEESKDLA 159
Cdd:TIGR02169  185 NIERLDLIIDEKRQQLERLRrerEKAERYQALLKEKREYEgYELLKEKEALERQKEAIERQLASL-------EEELEKLT 257
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099    160 GRLQRSSQRIGELEWSLCAVAATQKKKPDGFSSRSK---ALLKRQLEQSIREQILLKGHVTQLKESLKEVQLERDQY--- 233
Cdd:TIGR02169  258 EEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKekiGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLlae 337
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099    234 AEQIKGERAQWQQRMRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKnqmaeplppdapavsseVELQDLRKELERVAGE 313
Cdd:TIGR02169  338 IEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETR-----------------DELKDYREKLEKLKRE 400
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099    314 LQAqvennqcislLNRGQKERLREQEERLQEQQERLREREKRLQQLAEPQSDLEELKHENKSALQ-----------LEQQ 382
Cdd:TIGR02169  401 INE----------LKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWkleqlaadlskYEQE 470
                          330       340
                   ....*....|....*....|....*
gi 31083099    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 31083099     84 KISRLNDTIKSLKQQKKQVEHQLEEEKKANNEKQKAERELEGQIQRLNTEKKKLNTDLYHMKHSLRYFEEESKDLAGRLQ 163
Cdd:TIGR02169  682 RLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELK 761
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099    164 RSSQRIGELEWSLCAVAAtQKKKPDGFSSRSKALLKRQLEQSIREQIL-LKGHVTQLKESLKEVQLERdQYAEQikgERA 242
Cdd:TIGR02169  762 ELEARIEELEEDLHKLEE-ALNDLEARLSHSRIPEIQAELSKLEEEVSrIEARLREIEQKLNRLTLEK-EYLEK---EIQ 836
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099    243 QWQQRMRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKNQMAEplppdapavsSEVELQDLRKELERVAGELQAQVENNQ 322
Cdd:TIGR02169  837 ELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRD----------LESRLGDLKKERDELEAQLRELERKIE 906
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099    323 CIsllnrgqKERLREQEERLQEQQERLREREKRLQQLAEPQSDLEELKHENKSALQLEQQVKELQEKLGQVMETLTSAEK 402
Cdd:TIGR02169  907 EL-------EAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQ 979
                          330       340       350
                   ....*....|....*....|....*....|....*.
gi 31083099    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 31083099   84 KISRLNDTIKS---LKQQKKQVEHQLEEEKKANNEKQKAERELEGQIQRLNTEKKKLNTdlyhMKHSLRYFEEESKDLAG 160
Cdd:PRK03918 177 RIERLEKFIKRtenIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEE----LKEEIEELEKELESLEG 252
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099  161 RLQRSSQRIGELEWSLcavaATQKKKPDGFSSRSKALlkRQLEQSIREQILLKGHVTQLKESLKEVQLERDQYAEQIKGE 240
Cdd:PRK03918 253 SKRKLEEKIRELEERI----EELKKEIEELEEKVKEL--KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGI 326
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099  241 RAQWQQRmRKMSQEVCTLKEEKKHDTHRVEELERS-------------LSRLKNQMAEPLPPDAPAVSSEV-----ELQD 302
Cdd:PRK03918 327 EERIKEL-EEKEERLEELKKKLKELEKRLEELEERhelyeeakakkeeLERLKKRLTGLTPEKLEKELEELekakeEIEE 405
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099  303 LRKELERVAGELQAQV-ENNQCISLLNR--------GQKERLREQEERLQEQQERLREREKRLQQLAEPQSDLEELKHEN 373
Cdd:PRK03918 406 EISKITARIGELKKEIkELKKAIEELKKakgkcpvcGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELREL 485
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 31083099  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 31083099  72 QEQAAVLNSRSIKISRLNDTIKSLKQQKKQVEHQLEEEKKANNEKQKAERELEGQIQRLNTEKKKLNTDLYHMKHSLRYF 151
Cdd:COG1196 270 EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA 349
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099 152 EEESKDLAGRLQRSSQRIGELEwslcAVAATQKKKPDGFSSRSKALLKRQLEQSIREQILLK--GHVTQLKESLKEVQLE 229
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAE----AELAEAEEELEELAEELLEALRAAAELAAQLEELEEaeEALLERLERLEEELEE 425
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 31083099 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 31083099     84 KISRLNDTIKSLKQQKKQVEHQLEEEKKANNEKQKAERELEGQIQRLNTEKKKLNTDLYHMKHSLRYFEEESKDLAGRLQ 163
Cdd:TIGR02168  748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE 827
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099    164 RSSQRIGELEWSLCAVAATQKKKPDGFSSRSKALlkRQLEQSIREQIllkghvTQLKESLKEVQlERDQYAEQIKGERAQ 243
Cdd:TIGR02168  828 SLERRIAATERRLEDLEEQIEELSEDIESLAAEI--EELEELIEELE------SELEALLNERA-SLEEALALLRSELEE 898
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099    244 WQQRMRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKN-----------------QMAEPLPPDAPAVSSEVE--LQDLR 304
Cdd:TIGR02168  899 LSEELRELESKRSELRRELEELREKLAQLELRLEGLEVridnlqerlseeysltlEEAEALENKIEDDEEEARrrLKRLE 978

                   ....*
gi 31083099    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 31083099  92 IKSLKQQKKQ----VEHQLEEEKKANNEKQKAERELEGQIQRLNTEKKKLNTDLyhmkhslRYFEEESKDLAGRLQRSSQ 167
Cdd:COG1196 202 LEPLERQAEKaeryRELKEELKELEAELLLLKLRELEAELEELEAELEELEAEL-------EELEAELAELEAELEELRL 274
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099 168 RIGELEWslcAVAATQKKKpdgfssrskALLKRQLEQSIREQILLKGHVTQLKESLKEVQLERDQYAEQIkgerAQWQQR 247
Cdd:COG1196 275 ELEELEL---ELEEAQAEE---------YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL----EELEEE 338
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099 248 MRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKNQMAEplppdapavssevELQDLRKELERVAGELQAQVENNQCISLL 327
Cdd:COG1196 339 LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE-------------AEEELEELAEELLEALRAAAELAAQLEEL 405
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31083099 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 31083099    84 KISRLNDTIKSLKQQKKQVEHQLEEEKKANNEKQKAERELEGQIQRLNTEKKKLNTDLYHMKHSLRYFEEESKDLAGRLQ 163
Cdd:TIGR04523 336 IISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIK 415
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099   164 RSSQRIGELEWSLCAVAATQKKKPDGFSSRSKAllKRQLEQSIREqilLKGHVTQLKESLKEVQLErdqyAEQIKGERAQ 243
Cdd:TIGR04523 416 KLQQEKELLEKEIERLKETIIKNNSEIKDLTNQ--DSVKELIIKN---LDNTRESLETQLKVLSRS----INKIKQNLEQ 486
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099   244 WQQRMRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKNQM----AEPLPPDAPAVSSEVELQDLRKELERVAGELQAQvE 319
Cdd:TIGR04523 487 KQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIekleSEKKEKESKISDLEDELNKDDFELKKENLEKEID-E 565
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 31083099   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 31083099    78 LNSRSIKISRLN-----DTIKSLKQQKKQVEHQLEEEKKANNEKQKAERELEGQIQRLNTEKKKLNTDLYHMKHSLRYFE 152
Cdd:TIGR04523 290 LNQLKSEISDLNnqkeqDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQ 369
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099   153 EESKDLAGRLQRSSQRIGELEWSlcavaatqkkkpdgfssrskallKRQLEQSIREQillKGHVTQLKESLKEVQLERDQ 232
Cdd:TIGR04523 370 NEIEKLKKENQSYKQEIKNLESQ-----------------------INDLESKIQNQ---EKLNQQKDEQIKKLQQEKEL 423
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099   233 YAEQIKGERAQwqqrMRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKNQMAEPLppdAPAVSSEVELQDLRKELERVAG 312
Cdd:TIGR04523 424 LEKEIERLKET----IIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLS---RSINKIKQNLEQKQKELKSKEK 496
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099   313 ELQAQVENNqciSLLNRGQKERLREQEERLQEQQERLREREKRLQQLAEPQSDLEELKHENKSAlQLEQQVKELQEKLGQ 392
Cdd:TIGR04523 497 ELKKLNEEK---KELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKE-NLEKEIDEKNKEIEE 572
                         330
                  ....*....|...
gi 31083099   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 31083099  74 QAAVLNSRSIKISRLNDTIKSLKQQKKQVEHQLEEekkannekqkAERELEGqiqrlntekkklntdlYHMKHSLRYFEE 153
Cdd:COG3206 159 EAYLEQNLELRREEARKALEFLEEQLPELRKELEE----------AEAALEE----------------FRQKNGLVDLSE 212
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099 154 ESKDLAGRLQRSSQRIGELEWSLCAVAATQkkkpdgfssrskALLKRQLEQSIREQILLKGH--VTQLKESLKEVQLERD 231
Cdd:COG3206 213 EAKLLLQQLSELESQLAEARAELAEAEARL------------AALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELA 280
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099 232 QYAE----------QIKGERAQWQQRMRKMSQEVC-TLKEEKKHDTHRVEELERSLSRLKNQMAEplppdAPAVssEVEL 300
Cdd:COG3206 281 ELSArytpnhpdviALRAQIAALRAQLQQEAQRILaSLEAELEALQAREASLQAQLAQLEARLAE-----LPEL--EAEL 353

                ....*...
gi 31083099 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 31083099     64 LHARQSPCQEQAAVLNSRSIKISRLNDTIKSLKQQKKQVEHQLE--EEKKANN--EKQKAERELEGQIQRLNTEKKKLNt 139
Cdd:TIGR02169  704 LDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSslEQEIENVksELKELEARIEELEEDLHKLEEALN- 782
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099    140 DLYHM--KHSLRYFEEESKDLAGRLQRSSQRIGELEwslcavAATQKKKPDGFSSRSK--------ALLKRQLEQSIREQ 209
Cdd:TIGR02169  783 DLEARlsHSRIPEIQAELSKLEEEVSRIEARLREIE------QKLNRLTLEKEYLEKEiqelqeqrIDLKEQIKSIEKEI 856
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099    210 ILLKGHVTQLKESLKEVQLERDQYAEQ---IKGERAQWQQRMRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKNQMAE- 285
Cdd:TIGR02169  857 ENLNGKKEELEEELEELEAALRDLESRlgdLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEi 936
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099    286 --PLPPDAPAVSSEVELQDLRKELERVAGELQAQVE-NNQCISLLNRGQKERLREQEERL--QEQQErlrerekrlqQLA 360
Cdd:TIGR02169  937 edPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPvNMLAIQEYEEVLKRLDELKEKRAklEEERK----------AIL 1006
                          330
                   ....*....|..
gi 31083099    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 31083099    68 QSPCQEQAAVLNSRSIKISRLNDTIKSLKQQKKQVEHQLEEEKKANNEKQKAERELEGQIQRLNTEKKK-LNTDLyhmKH 146
Cdd:TIGR04523 238 QQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQdWNKEL---KS 314
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099   147 SLRYFEEESKDLAGRLQRSSQRIGELEWSlcaVAATQKKKPDGFSSRSKalLKRQLEQSIREQILLKGHVTQLKESLKEV 226
Cdd:TIGR04523 315 ELKNQEKKLEEIQNQISQNNKIISQLNEQ---ISQLKKELTNSESENSE--KQRELEEKQNEIEKLKKENQSYKQEIKNL 389
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099   227 QLER---DQYAEQIKGERAQWQQRMRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKNQMAeplppdapavssevELQDL 303
Cdd:TIGR04523 390 ESQIndlESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDS--------------VKELI 455
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099   304 RKELERVAGELQAQvennqcISLLNRGQKERLREQEERLqeqqerlrerekrlQQLAEPQSDLEELKHENKsalQLEQQV 383
Cdd:TIGR04523 456 IKNLDNTRESLETQ------LKVLSRSINKIKQNLEQKQ--------------KELKSKEKELKKLNEEKK---ELEEKV 512
                         330       340
                  ....*....|....*....|
gi 31083099   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 31083099     73 EQAAVLNSRSIKISRLNDTIKSLKQQKKQVEHQLEEEKKANNEKQKAER---ELEGQIQRLNTEKKKLNTDLYHMKHSLR 149
Cdd:TIGR02168  324 QLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESrleELEEQLETLRSKVAQLELQIASLNNEIE 403
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099    150 YFEEESKDLAGRLQRSSQRIGELEWSLcavaatqkkkpdgfSSRSKALLKRQLEQSIREQILLKGHVTQLKESLKEVQLE 229
Cdd:TIGR02168  404 RLEARLERLEDRRERLQQEIEELLKKL--------------EEAELKELQAELEELEEELEELQEELERLEEALEELREE 469
                          170
                   ....*....|....*..
gi 31083099    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 31083099   78 LNSRSIKISRLNDTIKSLKQQKKQVEHQLEEEKKANNEKQKAERELEGQIQR-------------LNTEKKKLNTDLYHM 144
Cdd:PRK03918 233 LEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKElkelkekaeeyikLSEFYEEYLDELREI 312
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099  145 KHSLRYFEEESKDLAGRLQRSSQRIGELEWSLCAVAATQKKKPDGFSS-----RSKALLKRQLEQSIREQILLKGHVTQL 219
Cdd:PRK03918 313 EKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERhelyeEAKAKKEELERLKKRLTGLTPEKLEKE 392
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099  220 KESLKEVQLERDQYAEQIKGERAQWQQRMRKMSQEVCTLKEEKKH---------DTHRVEELER---SLSRLKNQMAEpl 287
Cdd:PRK03918 393 LEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgreltEEHRKELLEEytaELKRIEKELKE-- 470
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099  288 ppdapavsSEVELQDLRKELERVAGELQAQVENNQCISLLNRGQKERLREQEERLQEQQERLREREKRLQQLAEPQSDLE 367
Cdd:PRK03918 471 --------IEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIK 542
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 31083099  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 31083099     73 EQAAVLNSRSIKISRLNDTIKSLKQQKKQVEHQLEEEKKANNEKQKAERELEGQIQRLNTEKKKLNTDLYHmkhsLRYFE 152
Cdd:pfam02463  160 EEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLD----YLKLN 235
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099    153 EESKDLAGRLQRSSQRIGELEwslcavAATQKKKPDGFSSRSKalLKRQLEQSIREQILLKGHVTQLKESLKEVQLERDQ 232
Cdd:pfam02463  236 EERIDLLQELLRDEQEEIESS------KQEIEKEEEKLAQVLK--ENKEEEKEKKLQEEELKLLAKEEEELKSELLKLER 307
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099    233 YAEQIKGERAQWQQRMRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKNQMAEPLPPDAPAVSSEVELQDLRKELErvAG 312
Cdd:pfam02463  308 RKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLES--ER 385
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099    313 ELQAQVENNQCISLLNRGQKERLREQEERLQEQQERLREREKRLQQLAEPQSDLEELKhENKSALQLEQQVKELQEKLGQ 392
Cdd:pfam02463  386 LSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQ-GKLTEEKEELEKQELKLLKDE 464
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 31083099    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 31083099    86 SRLNDTIKSLKQQKKQVEHQLEEEKKANNEKQKAERELEGQIQRLNTEKKKlntdlyhmkhslryfEEESKDLAGRLQRS 165
Cdd:PTZ00121 1521 AKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKK---------------AEEDKNMALRKAEE 1585
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099   166 SQRIGELEWSLCAVAATQKKKpdgfsSRSKALLKRQLEQSIREQILLKGHVTQLKESLKEVQLERDQYAEQIKgeRAQWQ 245
Cdd:PTZ00121 1586 AKKAEEARIEEVMKLYEEEKK-----MKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELK--KAEEE 1658
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099   246 QRMRKMSQEVCTLKEEKKHDTHRVEELErslsrlKNQMAEPLPPDAPAVSSEVELQDLRKELERVAGELQAQVENNQcis 325
Cdd:PTZ00121 1659 NKIKAAEEAKKAEEDKKKAEEAKKAEED------EKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENK--- 1729
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099   326 lLNRGQKERLREQEERLQEQQERLREREKRLQQLAEPQSDLEELKHENKSALqLEQQVKELQEKLGQVMETLTSAEKEPE 405
Cdd:PTZ00121 1730 -IKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAV-IEEELDEEDEKRRMEVDKKIKDIFDNF 1807
                         330
                  ....*....|
gi 31083099   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 31083099    189 GFSSRSKALLKRQLE-QSIREQI-LLKGHVTQLKESLKEVQLERDQYAEQIKGERAQWQQRMRKMSQ---EVCTLKEEKK 263
Cdd:TIGR02168  664 GSAKTNSSILERRREiEELEEKIeELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISAlrkDLARLEAEVE 743
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099    264 HDTHRVEELERSLSRLKNQMAEPLPPDAPAVSSEVELQDLRKELERVAGELQAQVENNQCISllnRGQKERLREQEERLQ 343
Cdd:TIGR02168  744 QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREAL---DELRAELTLLNEEAA 820
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099    344 EQQERLREREKRL-----------QQLAEPQSDLEELKHE----NKSALQLEQQVKELQEKLGQVMETLTSAEKEPEAAv 408
Cdd:TIGR02168  821 NLRERLESLERRIaaterrledleEQIEELSEDIESLAAEieelEELIEELESELEALLNERASLEEALALLRSELEEL- 899
                          250       260       270
                   ....*....|....*....|....*....|.
gi 31083099    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 31083099 198 LKRQLEQ-SIREQILLKGHVTQLKESLKEVQLERDQYAEQIKGERAQWQQRmRKMSQEVCTLKEEKKHDTHRVEELERSL 276
Cdd:COG0542 416 LERRLEQlEIEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAE-KELIEEIQELKEELEQRYGKIPELEKEL 494
                        90       100
                ....*....|....*....|.
gi 31083099 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 31083099    83 IKISRLNDTIKSLKQQKKQVEHQLEEEKKANNEKQKAERELEGQIQRLNTEKKKLNTDLYHMKHSLRYFEEESKDLAGRL 162
Cdd:TIGR04523 454 LIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEK 533
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099   163 QRSSQRIGELEwslcavaaTQKKKPDgfSSRSKALLKRQLEQSIREQILLKGHVTQLKESLKEVQLERDQYAEQIKGERA 242
Cdd:TIGR04523 534 KEKESKISDLE--------DELNKDD--FELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIK 603
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 31083099   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 31083099     71 CQEQAAVLNSRSIKISRLNDTIKSLKQQKKQVEHQLEEEKKANNEKQKAERELEGQIQRLNTEKKKLNtdlyhmkhslRY 150
Cdd:smart00435 265 CNHQRTVSKTHEKSMEKLQEKIKALKYQLKRLKKMILLFEMISDLKRKLKSKFERDNEKLDAEVKEKK----------KE 334
                           90       100
                   ....*....|....*....|...
gi 31083099    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 31083099   72 QEQAAVLNSRSIKISRLNDTIKSLKQQKKQ-------VEHQLEEEKKANNEKQKAE--RELEGQIQRLNTEKKKLNTDLY 142
Cdd:PRK03918 448 EHRKELLEEYTAELKRIEKELKEIEEKERKlrkelreLEKVLKKESELIKLKELAEqlKELEEKLKKYNLEELEKKAEEY 527
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099  143 H-MKHSLRYFEEESKDLAGRLQRSSQRIGELEWSLCAVAATQKKKPD--------GFSSRSKALLK-RQLEQSIREQILL 212
Cdd:PRK03918 528 EkLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAEllkeleelGFESVEELEERlKELEPFYNEYLEL 607
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099  213 KGHVTQLKESLKEVQLERDQyAEQIKGERAQWQQRMRKMSQEVCTLKEEKKHDTHR-----VEELERSLSRLKNQMAepl 287
Cdd:PRK03918 608 KDAEKELEREEKELKKLEEE-LDKAFEELAETEKRLEELRKELEELEKKYSEEEYEelreeYLELSRELAGLRAELE--- 683
                        250       260       270
                 ....*....|....*....|....*....|...
gi 31083099  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 31083099  72 QEQAAVLNSRSIKISRLNDTIKSLKQQKKQVEHQLEEEKKANNEKQKAERELEGQIQRLNTEKKKLNTDLyhmkhslryf 151
Cdd:COG3883  19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL---------- 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099 152 eeesKDLAGRLQRSSQRIGELEwslcavAATQKKKPDGFSSRSKAL--LKRQLEQSIREQILLKGHVTQLKESLKEVQLE 229
Cdd:COG3883  89 ----GERARALYRSGGSVSYLD------VLLGSESFSDFLDRLSALskIADADADLLEELKADKAELEAKKAELEAKLAE 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 31083099 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 31083099   73 EQAAVLNSRSIKISRLNDTIKSLKQQKKQVEHQLEEEKKANNEKQKAeRELEGQIQRLNTEKK-----KLNTDLYHMKHS 147
Cdd:PRK03918 321 EEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEA-KAKKEELERLKKRLTgltpeKLEKELEELEKA 399
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099  148 LRYFEEESKDLAGRLQRSSQRIGELEWSLCAVAATQKKKPdgfssrskaLLKRQLEQSIREQILLKGHVtQLKESLKEVQ 227
Cdd:PRK03918 400 KEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCP---------VCGRELTEEHRKELLEEYTA-ELKRIEKELK 469
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099  228 ----LERDQYAEQIKGERAQWQQR----MRKMSQEVCTLKEE-KKHDTHRVEELERSLSRLKNQMAEpLPPDAPAVSSEV 298
Cdd:PRK03918 470 eieeKERKLRKELRELEKVLKKESelikLKELAEQLKELEEKlKKYNLEELEKKAEEYEKLKEKLIK-LKGEIKSLKKEL 548
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099  299 E-LQDLRKELERVAGELQAQvennqcisllnrgQKERLREQEERLQEQQERLREREKRLQQLAEPQSDLEELKHENKSAL 377
Cdd:PRK03918 549 EkLEELKKKLAELEKKLDEL-------------EEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELE 615
                        330       340
                 ....*....|....*....|....*...
gi 31083099  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 31083099    212 LKGHVTQLKESLKEVQLERDQYAEQIKGERAQWQQRMRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKNQMAEPLPPDA 291
Cdd:pfam12128  267 YKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQ 346
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099    292 ---PAVSSEVELQDLR-KELERVAGELQAQVENnqcisllnRGQKERLREQEERLQEQQERLREREKRLQQLAEPQSDLE 367
Cdd:pfam12128  347 eqlPSWQSELENLEERlKALTGKHQDVTAKYNR--------RRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQ 418
                          170       180
                   ....*....|....*....|.
gi 31083099    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 31083099     78 LNSRSIKISRLNDTIKSLKQQ-KKQVEHQLEEEKKANNEKQKAErELEGQIQRLNTEKKKLNTDLYHMKHSLRYFEEESK 156
Cdd:pfam15921  421 LDDRNMEVQRLEALLKAMKSEcQGQMERQMAAIQGKNESLEKVS-SLTAQLESTKEMLRKVVEELTAKKMTLESSERTVS 499
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099    157 DLAGRLQRSSQrigelewslcAVAATQKKKPdgfSSRSKALLKRQLEQSIREQILLKGHVTQLKESLKEVQLERDQYAE- 235
Cdd:pfam15921  500 DLTASLQEKER----------AIEATNAEIT---KLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEi 566
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099    236 ---------QIKG-----------ERAQWQQRMRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKNQMAEPLPPDAPAVS 295
Cdd:pfam15921  567 lrqqienmtQLVGqhgrtagamqvEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLR 646
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099    296 SeveLQDLRKELERVAGELQaqvennQCISLLNRGQKERLREQEERLQEQQERLREREKRLQQLAEPQSDLEELK----- 370
Cdd:pfam15921  647 A---VKDIKQERDQLLNEVK------TSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRntlks 717
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 31083099    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 31083099   99 KKQVEHQLEEEKKANNEKQKAERELEGQIQRLNTEKKKLNTDL-------------------YHMKHSLRYFEEESKDLA 159
Cdd:PRK03918 386 PEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIeelkkakgkcpvcgrelteEHRKELLEEYTAELKRIE 465
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099  160 GRLQRSSQRIGELEWSLCAVAATQKKKPDGFSSRSKALLKRQLEQSI-------------------REQILLKGHVTQLK 220
Cdd:PRK03918 466 KELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLkkynleelekkaeeyeklkEKLIKLKGEIKSLK 545
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099  221 ESLKEvqlerdqyAEQIKGERAQWQQRMRKMSQEVCTL-KEEKKHDTHRVEELERSLSRLKNQMAEPLPpdapAVSSEVE 299
Cdd:PRK03918 546 KELEK--------LEELKKKLAELEKKLDELEEELAELlKELEELGFESVEELEERLKELEPFYNEYLE----LKDAEKE 613
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099  300 LQDLRKELERVAGELQAQVENnqcislLNRGQKERLREQEERLQEQQERLREREKRL-QQLAEPQSDLEELKHENKSALQ 378
Cdd:PRK03918 614 LEREEKELKKLEEELDKAFEE------LAETEKRLEELRKELEELEKKYSEEEYEELrEEYLELSRELAGLRAELEELEK 687
                        330       340
                 ....*....|....*....|....*..
gi 31083099  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 31083099   95 LKQQKKQVEHQL-EEEKKANNEKQKAERELEGQIQRLNTEKKKLNTD-LYHMKHSLRYFEEEskdLAGRLQRSSQRIGEL 172
Cdd:PRK00106  26 MKSAKEAAELTLlNAEQEAVNLRGKAERDAEHIKKTAKRESKALKKElLLEAKEEARKYREE---IEQEFKSERQELKQI 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099  173 EWSLCAVAATQKKKPDGFSSRSKALlkRQLEQSIREQillKGHVTqlkeslkevqlERDQYAEQIKGERAQWQQRMRKMS 252
Cdd:PRK00106 103 ESRLTERATSLDRKDENLSSKEKTL--ESKEQSLTDK---SKHID-----------EREEQVEKLEEQKKAELERVAALS 166
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 31083099  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 31083099    86 SRLNDTIKSLKQQKKQVEH---QLEEEKKANNEKQKAERELEG-QIQRLNTEKKKLNTDLYHMKHSLRYFEEESKDLAGR 161
Cdd:PTZ00121 1443 AKKADEAKKKAEEAKKAEEakkKAEEAKKADEAKKKAEEAKKAdEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAK 1522
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099   162 LQRSSQRIGELEWSLCAVAATQKKKPDGFSSRS---KALLKRQLEQSIREQ-----------ILLKGHVTQLKESLKEVQ 227
Cdd:PTZ00121 1523 KADEAKKAEEAKKADEAKKAEEKKKADELKKAEelkKAEEKKKAEEAKKAEedknmalrkaeEAKKAEEARIEEVMKLYE 1602
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099   228 LERDQYAEQIKGE-----RAQWQQRMRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKNQMAEPLPPDAPAVSSEVELQD 302
Cdd:PTZ00121 1603 EEKKMKAEEAKKAeeakiKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKK 1682
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099   303 LRKELERVAGELQAQVENNQCISLLNRGQKERLREQEERLQEQQERLREREKRLQQLAEPQSDLEELKHENKSALQLEQQ 382
Cdd:PTZ00121 1683 AEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHL 1762
                         330       340
                  ....*....|....*....|.
gi 31083099   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 31083099   78 LNSRSIKISRLNDTIKS-------LKQQKKQVEHQLEEE--KKANNEKQKAERE---LEGQIQRLNTEKKKLNTDLYHMK 145
Cdd:PRK05771  48 LRSLLTKLSEALDKLRSylpklnpLREEKKKVSVKSLEEliKDVEEELEKIEKEikeLEEEISELENEIKELEQEIERLE 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099  146 hSLRYFEEESKDL---------AGRLQRSSQRIGELEWSLC-------------AVAATQKKKPDgfsSRSKALLKRQLE 203
Cdd:PRK05771 128 -PWGNFDLDLSLLlgfkyvsvfVGTVPEDKLEELKLESDVEnveyistdkgyvyVVVVVLKELSD---EVEEELKKLGFE 203
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 31083099  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 31083099 195 KALLKRQLEQSIREQILLKGHVTQLKESLKEVQLERDQYAEQ-----IKGERAQWQQRMRKMSQEVCTLKEEKkhdthrv 269
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKnglvdLSEEAKLLLQQLSELESQLAEARAEL------- 235
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099 270 EELERSLSRLKNQMAEPlPPDAPAVSSEVELQDLRKELERVAGELQAQV-----ENNQCISLLNRGQKERLREQEERLQE 344
Cdd:COG3206 236 AEAEARLAALRAQLGSG-PDALPELLQSPVIQQLRAQLAELEAELAELSarytpNHPDVIALRAQIAALRAQLQQEAQRI 314
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 31083099 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 31083099    64 LHARQSPCQEQAAVLNSRSIKISRLNDTI---KSLKQQKKQVEhqleeekKANNEKQKAERELEGQIQRLNTEKKKLNTD 140
Cdd:pfam05483 386 LQKKSSELEEMTKFKNNKEVELEELKKILaedEKLLDEKKQFE-------KIAEELKGKEQELIFLLQAREKEIHDLEIQ 458
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099   141 LYHMKHSLRYFEEESKDLAGRLQRSSQRIGELEWSLCAVAATQKKKPDGFSSRSKAL---------LKRQLEQSIREQIL 211
Cdd:pfam05483 459 LTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELkkhqediinCKKQEERMLKQIEN 538
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099   212 LKGHVTQLKESLKEVQLERDQYAEQIKGERAQWQQRMRKMSQEVCTLKEEKKHDTHRVEELERSLSRlKNQMAEPLPPDA 291
Cdd:pfam05483 539 LEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIEN-KNKNIEELHQEN 617
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 31083099   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 31083099     97 QQKKQVEHQLEEEKKANNEKQKAERELEGqiqrLNTEKKKLNTDLYHMKHSLRYFEEESK-------DLAGRLQRSSQRI 169
Cdd:TIGR00618  670 LPKELLASRQLALQKMQSEKEQLTYWKEM----LAQCQTLLRELETHIEEYDREFNEIENassslgsDLAAREDALNQSL 745
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099    170 GELE----WSLCAVAATQKKKpdgfSSRSKALLKR-----QLEQSIREQI-LLKGHVTQLKESLKEVQLERDQYA----- 234
Cdd:TIGR00618  746 KELMhqarTVLKARTEAHFNN----NEEVTAALQTgaelsHLAAEIQFFNrLREEDTHLLKTLEAEIGQEIPSDEdilnl 821
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 31083099    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 31083099   80 SRSIKISRLNDTIKSLKQQKKqvEHQLEEEKKANNEKQKAERE---LEGQIQRLNTEKKKLNTdlyhMKHSLRYFEEESK 156
Cdd:PRK03918 493 SELIKLKELAEQLKELEEKLK--KYNLEELEKKAEEYEKLKEKlikLKGEIKSLKKELEKLEE----LKKKLAELEKKLD 566
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099  157 DLAGRLQRSSQRIGELewslcavaatqkkkpdGFSSRSKALLK-RQLEQSIREQILLKGHVTQLKESLKEVQLERDQyAE 235
Cdd:PRK03918 567 ELEEELAELLKELEEL----------------GFESVEELEERlKELEPFYNEYLELKDAEKELEREEKELKKLEEE-LD 629
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099  236 QIKGERAQWQQRMRKMSQEVCTLKEEKKHDTHR-----VEELERSLSRLKNQMAEplppdapavsseveLQDLRKELERV 310
Cdd:PRK03918 630 KAFEELAETEKRLEELRKELEELEKKYSEEEYEelreeYLELSRELAGLRAELEE--------------LEKRREEIKKT 695
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099  311 AGELQAQvennqcisllnrgqkerlreqeerlqeqQERLREREKRLQQLAEPQSDLEELKHENKS--ALQLEQQVKELQE 388
Cdd:PRK03918 696 LEKLKEE----------------------------LEEREKAKKELEKLEKALERVEELREKVKKykALLKERALSKVGE 747
                        330
                 ....*....|
gi 31083099  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 31083099 191 SSRSKALLKRQLEQSIREQILLKGHVTQLKESLKEVQLERDQYAEQIkgerAQWQQRMRKMSQEVCTLKEEKKHDTHRVE 270
Cdd:COG4942  18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRI----AALARRIRALEQELAALEAELAELEKEIA 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099 271 ELERSLSRLKNQMAEPL---------PPDAPAVSSEVELQDLRKE--LERVAGELQAQVE----NNQCISLLNRGQKERL 335
Cdd:COG4942  94 ELRAELEAQKEELAELLralyrlgrqPPLALLLSPEDFLDAVRRLqyLKYLAPARREQAEelraDLAELAALRAELEAER 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31083099 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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