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Conserved domains on  [gi|125628636|ref|NP_872313|]
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keratin, type II cytoskeletal 80 isoform K80 [Homo sapiens]

Protein Classification

intermediate filament family protein( domain architecture ID 705869)

intermediate filament (IF) family protein is a primordial component of the cytoskeleton and the nuclear envelope; such as type I keratins

CATH:  1.20.5.170
Gene Ontology:  GO:0005882
PubMed:  2183847|12596228|28101862

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
Filament super family cl25641
Intermediate filament protein;
82-393 7.80e-98

Intermediate filament protein;


The actual alignment was detected with superfamily member pfam00038:

Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 296.06  E-value: 7.80e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636   82 QEKEEMKALNDKFASLIGKVQALEQRNQLLETRWSFLQGQDSA-IFDLGHLYEEYQGRLQEELRKVSQERGQLEANLLQV 160
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAePSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636  161 LEKVEEFRIRYEDEISKRTDMEFTFVQLKKDLDAECLHRTELETKLKSLESFVELMKTIYEQELKDLAAQVKDVSVTVGM 240
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636  241 DSRCHIDLSGIVEEVKAQYDAVAARSLEEAEAYSRSQLEEQAARSAEYGSSLQSSRSEIADLNVRIQKLRSQILSVKSHC 320
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 125628636  321 LKLEENIKTAEEQGELAFQDAKTKLAQLEAALQQAKQDMARQLRKYQELMNVKLALDIEIATYRKLVEGEEGR 393
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
82-393 7.80e-98

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 296.06  E-value: 7.80e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636   82 QEKEEMKALNDKFASLIGKVQALEQRNQLLETRWSFLQGQDSA-IFDLGHLYEEYQGRLQEELRKVSQERGQLEANLLQV 160
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAePSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636  161 LEKVEEFRIRYEDEISKRTDMEFTFVQLKKDLDAECLHRTELETKLKSLESFVELMKTIYEQELKDLAAQVKDVSVTVGM 240
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636  241 DSRCHIDLSGIVEEVKAQYDAVAARSLEEAEAYSRSQLEEQAARSAEYGSSLQSSRSEIADLNVRIQKLRSQILSVKSHC 320
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 125628636  321 LKLEENIKTAEEQGELAFQDAKTKLAQLEAALQQAKQDMARQLRKYQELMNVKLALDIEIATYRKLVEGEEGR 393
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 85-375 6.03e-10

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: 61.61  E-value: 6.03e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636    85 EEMKALNDKFASLIGKVQALEQRNQLLETRWSFLQGQDSAIFDLGHLYEEYQGRLQEELRKVSQERGQLEANLLQVLEKV 164
Cdd:TIGR02168  684 EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEI 763

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636   165 EEFRIRYEDEISKRTDMEFTFVQLKKDLDAECLHRTELETKLKSLESFVELMKTIY---EQELKDLAAQVKDVSVTVGMD 241
Cdd:TIGR02168  764 EELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAanlRERLESLERRIAATERRLEDL 843

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636   242 SRCHIDLSGIVEEVKAQYDavaarSLEEAEAYSRSQLEE------------QAARSAEY--GSSLQSSRSEIADLNVRIQ 307
Cdd:TIGR02168  844 EEQIEELSEDIESLAAEIE-----ELEELIEELESELEAllnerasleealALLRSELEelSEELRELESKRSELRRELE 918

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 125628636   308 KLRSQILSVKSHC----LKLEENIKTAEEQGELAFQDAKTKLAQLEAALQQAKQDMARQLRKYQELMNVKLA 375
Cdd:TIGR02168  919 ELREKLAQLELRLegleVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLA 990
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 130-381 7.59e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.39  E-value: 7.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636 130 HLYEEYQGRLQEELRKVSQERGQLEANLLQVLEKVEEFR---IRYEDEISKRTDMEFTFV----QLKKDLDAECLHRTEL 202
Cdd:COG1196  235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRlelEELELELEEAQAEEYELLaelaRLEQDIARLEERRREL 314

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636 203 ETKLKSLESFVELMKTIYEQELKDLAAQVKDVsvtvgmdsrchIDLSGIVEEVKAQYDAVAARSLEEAEAYS-------- 274
Cdd:COG1196  315 EERLEELEEELAELEEELEELEEELEELEEEL-----------EEAEEELEEAEAELAEAEEALLEAEAELAeaeeelee 383

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636 275 -RSQLEEQAARSAEYGSSLQSSRSEIADLNVRIQKLRSQILSVKSHclklEENIKTAEEQGELAFQDAKTKLAQLEAALQ 353
Cdd:COG1196  384 lAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA----LAELEEEEEEEEEALEEAAEEEAELEEEEE 459

                        250       260
                 ....*....|....*....|....*...
gi 125628636 354 QAKQDMARQLRKYQELMNVKLALDIEIA 381
Cdd:COG1196  460 ALLELLAELLEEAALLEAALAELLEELA 487
PRK09039 PRK09039
peptidoglycan -binding protein;
221-361 3.95e-04

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 42.26  E-value: 3.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636 221 EQELKDLAAQVKDVSVTVGMDSRCHIDLSGIVEEVKAQYDAVAA-RS-LEEAEAYSRSQLEEQAARSAEYGSSL------ 292
Cdd:PRK09039  52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAeRSrLQALLAELAGAGAAAEGRAGELAQELdsekqv 131

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 125628636 293 -QSSRSEIADLNVRIQKLRSQILSvkshclkLEENIKTAEEQGelafQDAKTKLA----QLEAALQQAKQDMAR 361
Cdd:PRK09039 132 sARALAQVELLNQQIAALRRQLAA-------LEAALDASEKRD----RESQAKIAdlgrRLNVALAQRVQELNR 194
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
82-393 7.80e-98

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 296.06  E-value: 7.80e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636   82 QEKEEMKALNDKFASLIGKVQALEQRNQLLETRWSFLQGQDSA-IFDLGHLYEEYQGRLQEELRKVSQERGQLEANLLQV 160
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAePSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636  161 LEKVEEFRIRYEDEISKRTDMEFTFVQLKKDLDAECLHRTELETKLKSLESFVELMKTIYEQELKDLAAQVKDVSVTVGM 240
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636  241 DSRCHIDLSGIVEEVKAQYDAVAARSLEEAEAYSRSQLEEQAARSAEYGSSLQSSRSEIADLNVRIQKLRSQILSVKSHC 320
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 125628636  321 LKLEENIKTAEEQGELAFQDAKTKLAQLEAALQQAKQDMARQLRKYQELMNVKLALDIEIATYRKLVEGEEGR 393
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 85-375 6.03e-10

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: 61.61  E-value: 6.03e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636    85 EEMKALNDKFASLIGKVQALEQRNQLLETRWSFLQGQDSAIFDLGHLYEEYQGRLQEELRKVSQERGQLEANLLQVLEKV 164
Cdd:TIGR02168  684 EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEI 763

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636   165 EEFRIRYEDEISKRTDMEFTFVQLKKDLDAECLHRTELETKLKSLESFVELMKTIY---EQELKDLAAQVKDVSVTVGMD 241
Cdd:TIGR02168  764 EELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAanlRERLESLERRIAATERRLEDL 843

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636   242 SRCHIDLSGIVEEVKAQYDavaarSLEEAEAYSRSQLEE------------QAARSAEY--GSSLQSSRSEIADLNVRIQ 307
Cdd:TIGR02168  844 EEQIEELSEDIESLAAEIE-----ELEELIEELESELEAllnerasleealALLRSELEelSEELRELESKRSELRRELE 918

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 125628636   308 KLRSQILSVKSHC----LKLEENIKTAEEQGELAFQDAKTKLAQLEAALQQAKQDMARQLRKYQELMNVKLA 375
Cdd:TIGR02168  919 ELREKLAQLELRLegleVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLA 990
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 199-395 3.27e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.67  E-value: 3.27e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636   199 RTELETKLKSLESFVELMktiyeQELKDLAAQVKDVSVTVgmdsrchidLSGIVEEVKAQYDAvaarsLEEAEAYSRSQL 278
Cdd:TIGR02168  195 LNELERQLKSLERQAEKA-----ERYKELKAELRELELAL---------LVLRLEELREELEE-----LQEELKEAEEEL 255

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636   279 EEQAARSAEYGSSLQSSRSEIADLNVRIQKLRSQILSVKSHCLKLEENIKTAEEQGELAFQDAK---TKLAQLEAALQQA 355
Cdd:TIGR02168  256 EELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEeleAQLEELESKLDEL 335

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 125628636   356 KQDMARQLRKYQELMNVKLALDIEIATYRKLVEGEEGRMD 395
Cdd:TIGR02168  336 AEELAELEEKLEELKEELESLEAELEELEAELEELESRLE 375
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 130-381 7.59e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.39  E-value: 7.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636 130 HLYEEYQGRLQEELRKVSQERGQLEANLLQVLEKVEEFR---IRYEDEISKRTDMEFTFV----QLKKDLDAECLHRTEL 202
Cdd:COG1196  235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRlelEELELELEEAQAEEYELLaelaRLEQDIARLEERRREL 314

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636 203 ETKLKSLESFVELMKTIYEQELKDLAAQVKDVsvtvgmdsrchIDLSGIVEEVKAQYDAVAARSLEEAEAYS-------- 274
Cdd:COG1196  315 EERLEELEEELAELEEELEELEEELEELEEEL-----------EEAEEELEEAEAELAEAEEALLEAEAELAeaeeelee 383

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636 275 -RSQLEEQAARSAEYGSSLQSSRSEIADLNVRIQKLRSQILSVKSHclklEENIKTAEEQGELAFQDAKTKLAQLEAALQ 353
Cdd:COG1196  384 lAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA----LAELEEEEEEEEEALEEAAEEEAELEEEEE 459

                        250       260
                 ....*....|....*....|....*...
gi 125628636 354 QAKQDMARQLRKYQELMNVKLALDIEIA 381
Cdd:COG1196  460 ALLELLAELLEEAALLEAALAELLEELA 487
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 85-357 8.74e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 48.53  E-value: 8.74e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636    85 EEMKALNDKFASLIGKVQALEQRNQLLETRWSFLQGQDSAIFDLGHLYEEYQGRLQEELRkvsqergQLEANLLQVLEKV 164
Cdd:TIGR02169  681 ERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLE-------ELEEDLSSLEQEI 753

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636   165 EEFRIRYEDEISKRTDMEFTFVQLKKDLDAecLHRTELETKLKSLEsfvELMKTIyEQELKDLAAQVKDVSVTVGMDSRC 244
Cdd:TIGR02169  754 ENVKSELKELEARIEELEEDLHKLEEALND--LEARLSHSRIPEIQ---AELSKL-EEEVSRIEARLREIEQKLNRLTLE 827

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636   245 HIDLSGIVEEVKAQYDAvaarsLEEAEAYSRSQLEEQAARSAEYGSSLQSSRSEIADLNVRIQKLRSQILSVKSHCLKLE 324
Cdd:TIGR02169  828 KEYLEKEIQELQEQRID-----LKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELE 902

                          250       260       270
                   ....*....|....*....|....*....|...
gi 125628636   325 ENIKTAEEQGELAFQDAKTKLAQLEAALQQAKQ 357
Cdd:TIGR02169  903 RKIEELEAQIEKKRKRLSELKAKLEALEEELSE 935
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 131-388 1.66e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.24  E-value: 1.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636 131 LYEEYQGRLQEELRKVSQERGQLEANLLQVLEKVEEFRIRYEDEISKRTDMEFTFVQLKKDLDAECLHRTELETKLKSLE 210
Cdd:COG1196  243 ELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELE 322

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636 211 sfvelmktiyeQELKDLAAQvkdvsvtvgmdsrcHIDLSGIVEEVKAQYDAVAARsLEEAEAY---SRSQLEEQAARSAE 287
Cdd:COG1196  323 -----------EELAELEEE--------------LEELEEELEELEEELEEAEEE-LEEAEAElaeAEEALLEAEAELAE 376

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636 288 YGSSLQSSRSEIADLNVRIQKLRSQILSVKSHCLKLEENIKTAEEQGELAFQDAKTKLAQLEAALQQAKQDMARQLRKYQ 367
Cdd:COG1196  377 AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456

                        250       260
                 ....*....|....*....|.
gi 125628636 368 ELMNVKLALDIEIATYRKLVE 388
Cdd:COG1196  457 EEEALLELLAELLEEAALLEA 477
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 68-382 3.18e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.60  E-value: 3.18e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636    68 LDVKLDPAVQQLKNQEKEEMKALndKFASLIGKVQALEQrnQLLETRWSFLQGQDSAIfdlghlyEEYQGRLQEELRKVS 147
Cdd:TIGR02169  189 LDLIIDEKRQQLERLRREREKAE--RYQALLKEKREYEG--YELLKEKEALERQKEAI-------ERQLASLEEELEKLT 257

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636   148 QERGQLEANLLQVLEKVEEFriryEDEISKRTDMEFtfVQLKKDLDaeclhrtELETKLKSLESFVELmktiYEQELKDL 227
Cdd:TIGR02169  258 EEISELEKRLEEIEQLLEEL----NKKIKDLGEEEQ--LRVKEKIG-------ELEAEIASLERSIAE----KERELEDA 320

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636   228 AAQVkdvsvtvgmdsrchidlsgiveevkAQYDAVAARSLEEAEAYSRsQLEEQAARSAEYGSSLQSSRSEIADLNVRIQ 307
Cdd:TIGR02169  321 EERL-------------------------AKLEAEIDKLLAEIEELER-EIEEERKRRDKLTEEYAELKEELEDLRAELE 374

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 125628636   308 KL--RSQILSVKSHCLKlEENIKTAEEQGELAFQDAK--TKLAQLEAALQQAKQDMARQLRKYQELMNVKLALDIEIAT 382
Cdd:TIGR02169  375 EVdkEFAETRDELKDYR-EKLEKLKREINELKRELDRlqEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKK 452
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 147-371 3.76e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.20  E-value: 3.76e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636   147 SQERGQLEANLLQVLEKVEEFRIRYEDEISKRTDMEFTFVQLKKDLDAECLHRTELETKLKSLESFVEL---MKTIYEQE 223
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQleeRIAQLSKE 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636   224 LKDLAAQVKDVSVTVGMDSrchiDLSGIVEEVKAQYDAVAARSLEEAEAySRSQLEEQAARsaeygssLQSSRSEIADLN 303
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAE----EELAEAEAEIEELEAQIEQLKEELKA-LREALDELRAE-------LTLLNEEAANLR 823

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 125628636   304 VRIQKLRSQILSVKSHCLKLEENIKTAEEQGE---LAFQDAKTKLAQLEAALQ-------QAKQDMARQLRKYQELMN 371
Cdd:TIGR02168  824 ERLESLERRIAATERRLEDLEEQIEELSEDIEslaAEIEELEELIEELESELEallneraSLEEALALLRSELEELSE 901
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 84-311 8.08e-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: 45.05  E-value: 8.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636    84 KEEMKALNDKFASLIGKVQALEQRNQLLETRWSFLQGQDSAIFDLGHLYEEYQGRLQEELRKVSQERGQLEANLLQVLEK 163
Cdd:TIGR02168  280 EEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE 359

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636   164 VEEFRIRYEDEISKRTDMEF-------TFVQLKKDLDAECLHRTELETKLKSLESFVELMKTIYEQELKDLA-AQVKDVS 235
Cdd:TIGR02168  360 LEELEAELEELESRLEELEEqletlrsKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEeAELKELQ 439

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 125628636   236 VTVGmdsrchiDLSGIVEEVKAQYDAVAARSLEEAEAYSRSQLEEQAARsaeygSSLQSSRSEIADLNVRIQKLRS 311
Cdd:TIGR02168  440 AELE-------ELEEELEELQEELERLEEALEELREELEEAEQALDAAE-----RELAQLQARLDSLERLQENLEG 503
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 75-393 8.88e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.93  E-value: 8.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636  75 AVQQLKNQEKEEMKALNDKFASLIGKVQALEQRNQLLETRWSFLQGQDSAIFDLGHLYEEYQGRLQ---EELRKVSQERG 151
Cdd:COG1196  345 ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEallERLERLEEELE 424

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636 152 QLEANLLQVLEKVEEFRIRYEDEISKRTDMEFTFVQLKKDLDAECLHRTELETKLKSLESFVELMKTIY---EQELKDLA 228
Cdd:COG1196  425 ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLlllLEAEADYE 504

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636 229 AQVKDVSVTVGMDSRCHIDLSGIVE-EVKAQYDAVAARSLEEAEAYSRSQLEEQAARSAEYGSSLQSSRSEIADLNVriQ 307
Cdd:COG1196  505 GFLEGVKAALLLAGLRGLAGAVAVLiGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDK--I 582

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636 308 KLRSQILSVKSHCLKLEENIKTAEEQGELAFQDAKTKLAQLEAALQQAKQDMARQLRKYQELMNVKLALDIEIATYRKLV 387
Cdd:COG1196  583 RARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSL 662


                 ....*.
gi 125628636 388 EGEEGR 393
Cdd:COG1196  663 TGGSRR 668
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
127-365 9.80e-05

DNA repair ATPase RecN [Replication, recombination and repair];


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 44.68  E-value: 9.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636 127 DLGHLYEEYQGRLQEeLRKVSQERGQLEANLLQVLEKVEefRIRYE-DEISKrtdmeftfVQLKKDLDAEclhrteLETK 205
Cdd:COG0497  152 GLEELLEEYREAYRA-WRALKKELEELRADEAERARELD--LLRFQlEELEA--------AALQPGEEEE------LEEE 214

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636 206 LKSLESFVELMKTIYE--QELKDlaaqvKDVSVtVGMDSRCHIDLSGIVEeVKAQYDAVAARsLEEAEAysrsQLEEQAA 283
Cdd:COG0497  215 RRRLSNAEKLREALQEalEALSG-----GEGGA-LDLLGQALRALERLAE-YDPSLAELAER-LESALI----ELEEAAS 282

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636 284 RSAEYGSSLQSSRSEIADLNVRIQKLRSqiLSVKSHClKLEENIKTAEE-QGELA-FQDAKTKLAQLEAALQQAKQDM-- 359
Cdd:COG0497  283 ELRRYLDSLEFDPERLEEVEERLALLRR--LARKYGV-TVEELLAYAEElRAELAeLENSDERLEELEAELAEAEAELle 359


                 ....*..
gi 125628636 360 -ARQLRK 365
Cdd:COG0497  360 aAEKLSA 366
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 127-345 1.12e-04

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 45.04  E-value: 1.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636   127 DLGHLYEEYQGRLQEELRKVSQErgqleaNLLQVLE---KVEEFRIRYEDEISKRTDMEFTFVQLkkdldaeclHRTELE 203
Cdd:TIGR01612  664 ELSKIYEDDIDALYNELSSIVKE------NAIDNTEdkaKLDDLKSKIDKEYDKIQNMETATVEL---------HLSNIE 728

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636   204 TKLKSLES-FVELMKTIYEQELKDLAAQVKD-------VSVTVGMDSRCHIDLS---GIVEEVKAQY-DAVAARSLEEAE 271
Cdd:TIGR01612  729 NKKNELLDiIVEIKKHIHGEINKDLNKILEDfknkekeLSNKINDYAKEKDELNkykSKISEIKNHYnDQINIDNIKDED 808

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 125628636   272 AysrsqlEEQAARSAEYGSSLQSSRSEIADLNVRIQKLRSQILSVKSHCLKLEENIKTAEEQGELAFQDAKTKL 345
Cdd:TIGR01612  809 A------KQNYDKSKEYIKTISIKEDEIFKIINEMKFMKDDFLNKVDKFINFENNCKEKIDSEHEQFAELTNKI 876
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
221-404 1.86e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.85  E-value: 1.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636 221 EQELKDLAAQVKDVSVTVGMDSrchidLSGIVEEVKAQYDAVAARsLEEAEAySRSQLEEQAARSAEYGSSLQSS----- 295
Cdd:COG3206  195 EAALEEFRQKNGLVDLSEEAKL-----LLQQLSELESQLAEARAE-LAEAEA-RLAALRAQLGSGPDALPELLQSpviqq 267

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636 296 -RSEIADLNVR--------------IQKLRSQILSVKShclKLEENIKTAEEQGELAFQDAKTKLAQLEAALQQAKQDMA 360
Cdd:COG3206  268 lRAQLAELEAElaelsarytpnhpdVIALRAQIAALRA---QLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLA 344

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 125628636 361 RQLRKYQELMNVKLALDIEIATYRKLVE-----GEEGRMDSPSATVVSA 404
Cdd:COG3206  345 ELPELEAELRRLEREVEVARELYESLLQrleeaRLAEALTVGNVRVIDP 393
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
75-301 2.10e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.75  E-value: 2.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636   75 AVQQLKNQEK--EEMKALNDKFASLIGKVQALEQrnqLLETRWSFLQGQDSAifdlghLYEEYQGRLQEELRKVSQERGQ 152
Cdd:COG4913   243 ALEDAREQIEllEPIRELAERYAAARERLAELEY---LRAALRLWFAQRRLE------LLEAELEELRAELARLEAELER 313

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636  153 LEANLLQVLEKVEEFRIRYEDEISKRTDmeftfvQLKKDLDAECLHRTELETKLKSLESFVELMKTIYEQELKDLAAQVK 232
Cdd:COG4913   314 LEARLDALREELDELEAQIRGNGGDRLE------QLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRA 387

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 125628636  233 DVSVTVGmdsrchiDLSGIVEEVKAQYDAVAARS--LEEAEAYSRSQLEEQAARSAEYGSSLQSSRSEIAD 301
Cdd:COG4913   388 EAAALLE-------ALEEELEALEEALAEAEAALrdLRRELRELEAEIASLERRKSNIPARLLALRDALAE 451
PRK09039 PRK09039
peptidoglycan -binding protein;
221-361 3.95e-04

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 42.26  E-value: 3.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636 221 EQELKDLAAQVKDVSVTVGMDSRCHIDLSGIVEEVKAQYDAVAA-RS-LEEAEAYSRSQLEEQAARSAEYGSSL------ 292
Cdd:PRK09039  52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAeRSrLQALLAELAGAGAAAEGRAGELAQELdsekqv 131

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 125628636 293 -QSSRSEIADLNVRIQKLRSQILSvkshclkLEENIKTAEEQGelafQDAKTKLA----QLEAALQQAKQDMAR 361
Cdd:PRK09039 132 sARALAQVELLNQQIAALRRQLAA-------LEAALDASEKRD----RESQAKIAdlgrRLNVALAQRVQELNR 194
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 85-363 6.45e-04

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 42.22  E-value: 6.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636  85 EEMK-----ALNDKFASLI------GKVQaLEQRNQLLET----RWSFLQGQDSAIFDLGHLYEEYQGRLQEELRKVS-Q 148
Cdd:PRK05771   4 VRMKkvlivTLKSYKDEVLealhelGVVH-IEDLKEELSNerlrKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSvK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636 149 ERGQLEANLLQVLEKVEEFRIRYEDEISKrtdmeftfvqlkkdLDAEclhRTELETKLKSLESFVEL-MKTIYEQELKDL 227
Cdd:PRK05771  83 SLEELIKDVEEELEKIEKEIKELEEEISE--------------LENE---IKELEQEIERLEPWGNFdLDLSLLLGFKYV 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636 228 AAQVKDVSVTVGMDSRCHIDLSGIVEEVKA-QYDAVAARSLEEAEAYSRSQLEEQAARSAEYGSS------LQSSRSEIA 300
Cdd:PRK05771 146 SVFVGTVPEDKLEELKLESDVENVEYISTDkGYVYVVVVVLKELSDEVEEELKKLGFERLELEEEgtpselIREIKEELE 225

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 125628636 301 DLNVRIQKLRSQILSVKShclKLEENIKTAEEQGElafqdakTKLAQLEAALQQAKQDMARQL 363
Cdd:PRK05771 226 EIEKERESLLEELKELAK---KYLEELLALYEYLE-------IELERAEALSKFLKTDKTFAI 278
PRK11556 PRK11556
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
333-404 7.05e-04

MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;


Pssm-ID: 183194 [Multi-domain]  Cd Length: 415  Bit Score: 41.70  E-value: 7.05e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 125628636 333 QGELAFQDAKTKLAQLEAALQQAKQDMARqlrkYQELMNVKLALDIEIATYRKLVEGEEGRMDSPSATVVSA 404
Cdd:PRK11556 122 PFKVALAQAQGQLAKDQATLANARRDLAR----YQQLAKTNLVSRQELDAQQALVSETEGTIKADEASVASA 189
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 28-410 1.34e-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: 41.26  E-value: 1.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636    28 TSGWDSCRAPGPGFSSRSLTG-----CWSAGTISKVTVNPgllvPLDVKLDPAVQQLKNQEKEEMKALNDKFASLIGKVQ 102
Cdd:pfam15921   16 SSGITSNRGSSSPFFVSSIRGtiienTSSTGTFTQIPIFP----KYEVELDSPRKIIAYPGKEHIERVLEEYSHQVKDLQ 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636   103 A-LEQRNQLLETRWSFLQgqdSAIFDLGHLYEEYQ---GRLQEELRKVSQERGQLEANLLQVLEKVEEFRIRYEDEISkr 178
Cdd:pfam15921   92 RrLNESNELHEKQKFYLR---QSVIDLQTKLQEMQmerDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLE-- 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636   179 tDMEFTFVQLKKDLDAeclHRTELETKLKSLESFVELM-KTIYEQE------LKDLAAQVKdvSVTVGMDSRCHIdLSGI 251
Cdd:pfam15921  167 -DSNTQIEQLRKMMLS---HEGVLQEIRSILVDFEEASgKKIYEHDsmstmhFRSLGSAIS--KILRELDTEISY-LKGR 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636   252 VEEVKAQYDAVAARSLEEAEAYsrsqLEEQAARSAEYgssLQSSRSEIADLNVRIQKLRSQILSVKSHCLKLEENIKTAE 331
Cdd:pfam15921  240 IFPVEDQLEALKSESQNKIELL----LQQHQDRIEQL---ISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQN 312

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636   332 EQGELAFQDAKTKLAQLEAALQQAK---QDMARQLRKYQELMNVKLAldiEIATYRKLVEGEEGRMDSPSATVVSAVQSR 408
Cdd:pfam15921  313 SMYMRQLSDLESTVSQLRSELREAKrmyEDKIEELEKQLVLANSELT---EARTERDQFSQESGNLDDQLQKLLADLHKR 389


                   ..
gi 125628636   409 CK 410
Cdd:pfam15921  390 EK 391
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 261-367 1.50e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.52  E-value: 1.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636 261 AVAARSLEEAEAYSRSQLEEQAARSAEYGSSLQSSRSEIADLNVRIQKLRSQILSVKSHCLKLEENIKTAEEQgelaFQD 340
Cdd:COG4942   12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAE----LAE 87

                         90       100
                 ....*....|....*....|....*..
gi 125628636 341 AKTKLAQLEAALQQAKQDMARQLRKYQ 367
Cdd:COG4942   88 LEKEIAELRAELEAQKEELAELLRALY 114
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 77-367 2.24e-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: 40.49  E-value: 2.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636    77 QQLKNQEKEEMKALNDKFASLIGKVQALEQRNQLLETRWSFLQGQdsAIFDLGHLYEEYQGRLQeelrkVSQERGQLEAN 156
Cdd:pfam15921  306 EQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQ--LVLANSELTEARTERDQ-----FSQESGNLDDQ 378

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636   157 LLQVLEKVE--EFRIRYEDEISKR-----TDMEFTFVQLKKDLDAECLHRTELETKLKSLESFVELMktiYEQELKDLAA 229
Cdd:pfam15921  379 LQKLLADLHkrEKELSLEKEQNKRlwdrdTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQ---MERQMAAIQG 455

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636   230 QVKDV----SVTVGMDSRCHIdLSGIVEEVKAQydavaarsleeaeaysRSQLEEQAARSAEYGSSLQSSRSEIADLNVR 305
Cdd:pfam15921  456 KNESLekvsSLTAQLESTKEM-LRKVVEELTAK----------------KMTLESSERTVSDLTASLQEKERAIEATNAE 518

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 125628636   306 IQKLRSQIlsvkshCLKLEE--NIKTAEEQgelaFQDAKTKLAQLEaaLQQAKQDMARQLRKYQ 367
Cdd:pfam15921  519 ITKLRSRV------DLKLQElqHLKNEGDH----LRNVQTECEALK--LQMAEKDKVIEILRQQ 570
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 252-391 3.06e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.92  E-value: 3.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636 252 VEEVKAQYDAVAAR--SLEEAEAYSRSQLEEQAARSAEYGSSLQSSRSEIADLNVRIQKLRSQILSVKSHCLKLEENIKT 329
Cdd:COG1196  283 LEEAQAEEYELLAElaRLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 125628636 330 AEEQG---ELAFQDAKTKLAQLEAALQQAKQDMARQLRKYQELMNVKLALDIEIATYRKLVEGEE 391
Cdd:COG1196  363 AEEALleaEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE 427
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
78-356 3.15e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.05  E-value: 3.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636  78 QLKNQEKE------EMKALNDKFASLIGKVQALEQRNQLLETRWSFLQGqdsaifdlghlyeeyqgrLQEELRKVSQERG 151
Cdd:PRK03918 194 LIKEKEKEleevlrEINEISSELPELREELEKLEKEVKELEELKEEIEE------------------LEKELESLEGSKR 255

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636 152 QLEANLLQVLEKVEEFRIRYEDEISKRTDMEftfvQLKKDLDaECLHRTELETKLKSLESFVELMKTIYEQELKDLAAQV 231
Cdd:PRK03918 256 KLEEKIRELEERIEELKKEIEELEEKVKELK----ELKEKAE-EYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERI 330

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636 232 KDVSvtvGMDSRCHiDLSGIVEEVKaqydavaaRSLEEAEAYSRsQLEEQAARSAEygssLQSSRSEIADLNvrIQKLRS 311
Cdd:PRK03918 331 KELE---EKEERLE-ELKKKLKELE--------KRLEELEERHE-LYEEAKAKKEE----LERLKKRLTGLT--PEKLEK 391

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 125628636 312 QILSVKSHCLKLEENIKT-AEEQGELafqdaKTKLAQLEAALQQAK 356
Cdd:PRK03918 392 ELEELEKAKEEIEEEISKiTARIGEL-----KKEIKELKKAIEELK 432
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 272-368 3.36e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.43  E-value: 3.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636 272 AYSRSQLEEQAARSAEYGSSLQSSRSEIADLNVRIQKLRSQILSVKSHCLKLEENIKTAEEQgelafqdaktkLAQLEAA 351
Cdd:COG3883   12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAE-----------IAEAEAE 80

                         90
                 ....*....|....*..
gi 125628636 352 LQQAKQDMARQLRKYQE 368
Cdd:COG3883   81 IEERREELGERARALYR 97
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 136-372 3.45e-03

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


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 39.88  E-value: 3.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636  136 QGRLQEELrkvsQERGQLEANLLQVLEKVEEFRIRYEDEiskRTDMEFTFVQLKKDLDaeclhrtELETKLKSLESFVEL 215
Cdd:pfam07888  33 QNRLEECL----QERAELLQAQEAANRQREKEKERYKRD---REQWERQRRELESRVA-------ELKEELRQSREKHEE 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636  216 MKTIY--EQELKDLAAQVKDVSVTVGMDSRCHI----DLSGIVEEVKAQYDAVAARSLEEAEAYSRSQLEEQAARSAeYG 289
Cdd:pfam07888  99 LEEKYkeLSASSEELSEEKDALLAQRAAHEARIreleEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQ-LQ 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636  290 SSLQSSRSEIADLNVRIQKLRSQILSVKSHCLKLEENIKTAEEQGELAFQdaktKLAQLEAALQqakqdmarQLRKYQEL 369
Cdd:pfam07888 178 AKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHR----KEAENEALLE--------ELRSLQER 245


                  ...
gi 125628636  370 MNV 372
Cdd:pfam07888 246 LNA 248
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 252-395 3.86e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.92  E-value: 3.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636 252 VEEVKAQYDAVAARSLEEAEAYSRSQLEEQAARS--AEYGSSLQSSRSEIADLNVRIQKLRSQILSVKSHCLKLEENI-- 327
Cdd:COG1196  262 LAELEAELEELRLELEELELELEEAQAEEYELLAelARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELee 341

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 125628636 328 -----KTAEEQ---GELAFQDAKTKLAQLEAALQQAKQDMARQLRKYQELMNVKLALDIEIATYRKLVEGEEGRMD 395
Cdd:COG1196  342 leeelEEAEEEleeAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE 417
PRK11281 PRK11281
mechanosensitive channel MscK;
253-360 4.36e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 39.51  E-value: 4.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636  253 EEVKAQYDAVAARSLEEAEAYSRSQLEEQAARSAEygsSLQSSRSEIADLNVRIQKLRSQILSVKSHCLKLEENIKTAEE 332
Cdd:PRK11281   39 ADVQAQLDALNKQKLLEAEDKLVQQDLEQTLALLD---KIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETR 115

                          90       100       110
                  ....*....|....*....|....*....|
gi 125628636  333 Q--GELAFQDAKTKLAQLEAALQQAKQDMA 360
Cdd:PRK11281  116 EtlSTLSLRQLESRLAQTLDQLQNAQNDLA 145
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
67-215 4.62e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 39.46  E-value: 4.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636  67 PLDVKLDPAVQQLKNQEKEEMKALNDKFASLIGKVQALEQRNQLLETRwsfLQGQDSAIFdlghlyeeyqgRLQEELRKV 146
Cdd:COG2433  388 KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAE---LEEKDERIE-----------RLERELSEA 453

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 125628636 147 SQERGQleanllqvlekveefRIRYEDEISKRtdmEFTFVQLKKDLDAECLHRTELETKLKSLESFVEL 215
Cdd:COG2433  454 RSEERR---------------EIRKDREISRL---DREIERLERELEEERERIEELKRKLERLKELWKL 504
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 76-335 4.77e-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: 4.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636   76 VQQLKNQEkEEMKALNDKFASLIGKVQALEQ-----RNQLLETRWSFLQGQDSAIFDLGHLYEEYQGRLQEELRKVSQER 150
Cdd:pfam05483 512 TLELKKHQ-EDIINCKKQEERMLKQIENLEEkemnlRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMK 590

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636  151 gqLEANLLQVLEKVEEFRIRYEDEISKRTD-MEFTFVQLKKDLDAECLHRTELETKLKSLESFVELMKTIYEQELKD--- 226
Cdd:pfam05483 591 --ILENKCNNLKKQIENKNKNIEELHQENKaLKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDkki 668

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636  227 ----LAAQVKDVSVTVG--------MDSRCH---IDLSGIVEEVKAQYDAVaarsleeaeaysrsqLEEQAARSAEYGSS 291
Cdd:pfam05483 669 seekLLEEVEKAKAIADeavklqkeIDKRCQhkiAEMVALMEKHKHQYDKI---------------IEERDSELGLYKNK 733

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 125628636  292 LQSSRSEIADLNVRIQKLRSQILSVKSHC-LKLEENIKTAEEQGE 335
Cdd:pfam05483 734 EQEQSSAKAALEIELSNIKAELLSLKKQLeIEKEEKEKLKMEAKE 778
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
 268-351 5.97e-03

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 39.00  E-value: 5.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636 268 EEAEAYSRSQLEEQAARSAEYGSSLQSSRSEIADLNVRIQKLRSQILSVK-----------------SHCLKLEENIKTA 330
Cdd:PRK10636 534 KENNANSAQARKDQKRREAELRTQTQPLRKEIARLEKEMEKLNAQLAQAEeklgdselydqsrkaelTACLQQQASAKSG 613

                         90       100
                 ....*....|....*....|.
gi 125628636 331 EEQGELAFQDAKTKLAQLEAA 351
Cdd:PRK10636 614 LEECEMAWLEAQEQLEQMLLE 634
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 99-357 7.56e-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: 39.05  E-value: 7.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636    99 GKVQALEQRNQLLETRWSFLQGQDSAIFDLGHLYEEYQGRLQEELRKVSQERGQLEANLLQV------------------ 160
Cdd:pfam12128  241 PEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKrdelngelsaadaavakd 320

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636   161 ---LEKVEEFRIRYEDEiskrtDMEftfvQLKKDLDAECLHRTELETKLKSLESFVELMKTIyEQELKDLAAQVkdvsvt 237
Cdd:pfam12128  321 rseLEALEDQHGAFLDA-----DIE----TAAADQEQLPSWQSELENLEERLKALTGKHQDV-TAKYNRRRSKI------ 384

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636   238 vgmDSRCHIDLSGIVEEVKAQYD------AVAARSLEEAEAYSRSQLEEQAARSAEYGSSLQSSRSE------------- 298
Cdd:pfam12128  385 ---KEQNNRDIAGIKDKLAKIREardrqlAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGElklrlnqatatpe 461

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 125628636   299 ----IADLNVRIQKLRSQILSVKSHCLKL---EENIKTAEEQGELAFQDAKTKLAQLEAALQQAKQ 357
Cdd:pfam12128  462 lllqLENFDERIERAREEQEAANAEVERLqseLRQARKRRDQASEALRQASRRLEERQSALDELEL 527
PTZ00121 PTZ00121
MAEBL; Provisional
 100-344 9.11e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.58  E-value: 9.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636  100 KVQALEQRNQLLETRWSFLQGQDSAIFDLGHLYEEYQGRLQEELRKVSQERGQLEAnllqvLEKVEEFRIRYEDEISKRT 179
Cdd:PTZ00121 1569 AKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEE-----LKKAEEEKKKVEQLKKKEA 1643

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636  180 DMEFTFVQLKKDLDAECLHRTELETKLKSLESFVELMKTIYEQELKDLAAQVKDVSvtvgmDSRCHIDLSGIVEEVKAQY 259
Cdd:PTZ00121 1644 EEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAE-----EAKKAEELKKKEAEEKKKA 1718

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125628636  260 DAVaaRSLEEAEAYSRSQL---EEQAARSAEYGSSLQSSRSEIADLNVRIQKLRSQILSVKSHClkLEENIKTAEEQGEL 336
Cdd:PTZ00121 1719 EEL--KKAEEENKIKAEEAkkeAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAV--IEEELDEEDEKRRM 1794


                  ....*...
gi 125628636  337 AFqDAKTK 344
Cdd:PTZ00121 1795 EV-DKKIK 1801
 
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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