NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|18400511|ref|NP_566492|]
View 

structural maintenance of chromosomes domain protein [Arabidopsis thaliana]

Protein Classification

coiled-coil domain-containing protein( domain architecture ID 1000037)

coiled-coil domain-containing protein contains a region with alpha-helical coiled-coil sequence signatures that is being annotated by a variety of protein family models, not necessarily indicating family membership

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
EnvC super family cl34844
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
70-252 2.77e-07

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


The actual alignment was detected with superfamily member COG4942:

Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 51.69  E-value: 2.77e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511  70 LEDRLAAQNQDVQGLladNQRLAAthvaLKQELEVAQHELQRIMHYIDSLRAEEEIMMREMYDKSMRSEMEL-------- 141
Cdd:COG4942  60 LERRIAALARRIRAL---EQELAA----LEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALllspedfl 132
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511 142 ---REVDAMRAEIQKIRADIKEFTSGRQELTSQVHLMTQDLARLTADLQQIPTLTAEIENTKQELQRARAAIDYEKKGYA 218
Cdd:COG4942 133 davRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELA 212
                       170       180       190
                ....*....|....*....|....*....|....
gi 18400511 219 ENYEHGKIMEHKLVAMARELEKLRAEIANSETSA 252
Cdd:COG4942 213 AELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
 
Name Accession Description Interval E-value
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
70-252 2.77e-07

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: 51.69  E-value: 2.77e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511  70 LEDRLAAQNQDVQGLladNQRLAAthvaLKQELEVAQHELQRIMHYIDSLRAEEEIMMREMYDKSMRSEMEL-------- 141
Cdd:COG4942  60 LERRIAALARRIRAL---EQELAA----LEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALllspedfl 132
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511 142 ---REVDAMRAEIQKIRADIKEFTSGRQELTSQVHLMTQDLARLTADLQQIPTLTAEIENTKQELQRARAAIDYEKKGYA 218
Cdd:COG4942 133 davRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELA 212
                       170       180       190
                ....*....|....*....|....*....|....
gi 18400511 219 ENYEHGKIMEHKLVAMARELEKLRAEIANSETSA 252
Cdd:COG4942 213 AELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
89-250 1.47e-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: 50.07  E-value: 1.47e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511     89 QRLAATHVALKQELEVAQHELQRIMHYIDSLRAEEEIMMREMYDKSMRSEMELREVDAMRAEIQKIRADIKEFTSGRQEL 168
Cdd:TIGR02169  677 QRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENV 756
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511    169 TSQVHLMTQDLARLTADL----------------QQIPTLTAEIENTKQELQRARAAI-----DYEKKGYAENYEHGKIM 227
Cdd:TIGR02169  757 KSELKELEARIEELEEDLhkleealndlearlshSRIPEIQAELSKLEEEVSRIEARLreieqKLNRLTLEKEYLEKEIQ 836
                          170       180
                   ....*....|....*....|....*..
gi 18400511    228 EhkLVAMARELE----KLRAEIANSET 250
Cdd:TIGR02169  837 E--LQEQRIDLKeqikSIEKEIENLNG 861
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
70-251 4.69e-05

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: 45.10  E-value: 4.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511    70 LEDRLAAQNQDVQGLLADNQRLAathvalkQELEVAQHELQRIMHYIDSLRAEEEIMMREMYDKSMRSEMELREVDAMRA 149
Cdd:pfam05483 273 LEEKTKLQDENLKELIEKKDHLT-------KELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKA 345
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511   150 EIQKIRADIKEFTSGRQEL-----------TSQVHLMTQDLARLTADLQQIPTLTAEIENTKQELQRARA---AIDYEKK 215
Cdd:pfam05483 346 AHSFVVTEFEATTCSLEELlrteqqrleknEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAedeKLLDEKK 425
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 18400511   216 GYAENYEHGKIMEHKLV----AMARELEKLRAEIANSETS 251
Cdd:pfam05483 426 QFEKIAEELKGKEQELIfllqAREKEIHDLEIQLTAIKTS 465
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
68-202 1.35e-04

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 43.08  E-value: 1.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511     68 SILEDRLAAQNQDVQGLLADNQRLAATHVALKQELEVAQHELqrimhyiDSLR-AEEEImmrEMYDKSmrsemelrEVDA 146
Cdd:smart00787 147 EGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEEL-------RQLKqLEDEL---EDCDPT--------ELDR 208
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 18400511    147 MRAEIQKIRADIKEFTSGRQELTSQVHLMTQDLARLTADLQQIPTLTAEIENTKQE 202
Cdd:smart00787 209 AKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQ 264
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
102-249 7.86e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 7.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511  102 LEVAQHELQRIMHYIDSLRAE-EEIMMREMYDKSMRSEME------LREVDA-------MRAEIQKIRADIKEFTSGRQE 167
Cdd:PRK03918 160 YENAYKNLGEVIKEIKRRIERlEKFIKRTENIEELIKEKEkeleevLREINEisselpeLREELEKLEKEVKELEELKEE 239
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511  168 LTS---QVHLMTQDLARLTADLQQIPTLTAEIENTKQELQRARAAIDyEKKGYAENYEH-GKIMEHKLVAMAR---ELEK 240
Cdd:PRK03918 240 IEElekELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKlSEFYEEYLDELREiekRLSR 318

                 ....*....
gi 18400511  241 LRAEIANSE 249
Cdd:PRK03918 319 LEEEINGIE 327
 
Name Accession Description Interval E-value
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
70-252 2.77e-07

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: 51.69  E-value: 2.77e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511  70 LEDRLAAQNQDVQGLladNQRLAAthvaLKQELEVAQHELQRIMHYIDSLRAEEEIMMREMYDKSMRSEMEL-------- 141
Cdd:COG4942  60 LERRIAALARRIRAL---EQELAA----LEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALllspedfl 132
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511 142 ---REVDAMRAEIQKIRADIKEFTSGRQELTSQVHLMTQDLARLTADLQQIPTLTAEIENTKQELQRARAAIDYEKKGYA 218
Cdd:COG4942 133 davRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELA 212
                       170       180       190
                ....*....|....*....|....*....|....
gi 18400511 219 ENYEHGKIMEHKLVAMARELEKLRAEIANSETSA 252
Cdd:COG4942 213 AELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
89-250 1.47e-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: 50.07  E-value: 1.47e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511     89 QRLAATHVALKQELEVAQHELQRIMHYIDSLRAEEEIMMREMYDKSMRSEMELREVDAMRAEIQKIRADIKEFTSGRQEL 168
Cdd:TIGR02169  677 QRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENV 756
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511    169 TSQVHLMTQDLARLTADL----------------QQIPTLTAEIENTKQELQRARAAI-----DYEKKGYAENYEHGKIM 227
Cdd:TIGR02169  757 KSELKELEARIEELEEDLhkleealndlearlshSRIPEIQAELSKLEEEVSRIEARLreieqKLNRLTLEKEYLEKEIQ 836
                          170       180
                   ....*....|....*....|....*..
gi 18400511    228 EhkLVAMARELE----KLRAEIANSET 250
Cdd:TIGR02169  837 E--LQEQRIDLKeqikSIEKEIENLNG 861
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
66-212 4.95e-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: 48.13  E-value: 4.95e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511     66 QFSILEDRLAAQNQDVQGLLADNQRLAATHVALKQELEVAQHELQRIMHYIDSLRAEEEIMMREM------YDKSMRSEM 139
Cdd:TIGR02168  811 ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELeallneRASLEEALA 890
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511    140 ELR-EVDAMRAEIQKIRADIKEFTSGRQELTSQVHLMTQDLARLTADLQQI-------------------PTLTAEIENT 199
Cdd:TIGR02168  891 LLRsELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLqerlseeysltleeaealeNKIEDDEEEA 970
                          170
                   ....*....|...
gi 18400511    200 KQELQRARAAIDY 212
Cdd:TIGR02168  971 RRRLKRLENKIKE 983
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
70-252 8.23e-06

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: 8.23e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511  70 LEDRLAAQNQDVQGLLADNQRLAATHVALKQELEVAQHELQRIMHYIDSLRAEEEIMMREMYDKSMRSEMELREVDAMRA 149
Cdd:COG1196 237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE 316
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511 150 EIQKIRADIKEFTSGRQELTSQVHLMTQDLARLTADLQQIptLTAEIENTKQELQRARAAIDYEKKGYAENYEHGKIMEH 229
Cdd:COG1196 317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA--EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
                       170       180
                ....*....|....*....|...
gi 18400511 230 KLVAMARELEKLRAEIANSETSA 252
Cdd:COG1196 395 AAELAAQLEELEEAEEALLERLE 417
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
70-250 1.41e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.97  E-value: 1.41e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511     70 LEDRLAAQNQDVQGLLADNQRLAATHVALKQELEVAQHELQRIMHYIDSLRAEEEIMMREMYDKSMRSEMELREVDAMRA 149
Cdd:TIGR02168  759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATER 838
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511    150 EIQKIRADIKEFTSGRQELTSQVHLMTQDLARLTADLQQiptLTAEIENTKQELQRARAAIDYEKKGYAEnyehgkiMEH 229
Cdd:TIGR02168  839 RLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEA---LLNERASLEEALALLRSELEELSEELRE-------LES 908
                          170       180
                   ....*....|....*....|.
gi 18400511    230 KLVAMARELEKLRAEIANSET 250
Cdd:TIGR02168  909 KRSELRRELEELREKLAQLEL 929
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
73-252 1.46e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.85  E-value: 1.46e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511  73 RLAAQNQDVQGLLADNQRLAATHVALKQELEVAQHELQRIMHYIDSLRAEEEIMMREMYDKSMRSEMELREVDAMRAEIQ 152
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511 153 KIRADIKEFTSGRQELTSQVHLMTQDLARLTADLQQiptLTAEIENTKQELQRARAAIDYEKKGYAENYEHGKIMEHKLV 232
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEE---AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
                       170       180
                ....*....|....*....|
gi 18400511 233 AMARELEKLRAEIANSETSA 252
Cdd:COG1196 390 EALRAAAELAAQLEELEEAE 409
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
70-247 1.99e-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: 1.99e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511     70 LEDRLAAQNQDVQGLLADNQRLAATHVALKQELEVAQHELQRIMHYIDSLRAEEEIMMREMYDKSMRSEMELREVDAMRA 149
Cdd:TIGR02168  780 AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA 859
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511    150 EIQKIRADIKEFTSGRQELTSQVHLMTQDLARLTADLQQIPTLTAEIENTKQELQRARAAidyekkgyaenyehgkiMEH 229
Cdd:TIGR02168  860 EIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEE-----------------LRE 922
                          170
                   ....*....|....*...
gi 18400511    230 KLVAMARELEKLRAEIAN 247
Cdd:TIGR02168  923 KLAQLELRLEGLEVRIDN 940
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
70-313 2.68e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 45.59  E-value: 2.68e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511  70 LEDRLAAQNQDVQGLLADNQRLAATHVALKQELEVAQHELQRIMHYIDSLRAEEEIMMREMYDKSMRSEME--------- 140
Cdd:COG3883  35 AQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYLdvllgsesf 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511 141 ---LREVDAMRAEIQKIRADIKEFTSGRQELTSQVHLMTQDLARLTADLQQIPTLTAEIENTKQELQRARAAIDYEKKGY 217
Cdd:COG3883 115 sdfLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAA 194
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511 218 AENYEHGKIMEHKLVAMARELEKLRAEIANSETSAYANGPVGNPGGVAYGGGYGNPEAGYPVNPYQPNYTMNPAQTGVVG 297
Cdd:COG3883 195 EAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGA 274
                       250
                ....*....|....*.
gi 18400511 298 YYPPPYGPQAAWAGGY 313
Cdd:COG3883 275 GAAAASAAGGGAGGAG 290
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
70-210 4.32e-05

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 44.15  E-value: 4.32e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511  70 LEDRLAAQNQDVQGLLADNQRLAATHVALKQELEVAQHELQRIMHYIDSLRAEEEIMMREMydKSMRSEMEL----REVD 145
Cdd:COG1579  22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL--GNVRNNKEYealqKEIE 99
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18400511 146 AMRAEIQKIRADIKEFTSGRQELTSQVHLMTQDLARLTADL----QQIPTLTAEIENTKQELQRARAAI 210
Cdd:COG1579 100 SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELeekkAELDEELAELEAELEELEAEREEL 168
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
70-251 4.69e-05

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: 45.10  E-value: 4.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511    70 LEDRLAAQNQDVQGLLADNQRLAathvalkQELEVAQHELQRIMHYIDSLRAEEEIMMREMYDKSMRSEMELREVDAMRA 149
Cdd:pfam05483 273 LEEKTKLQDENLKELIEKKDHLT-------KELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKA 345
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511   150 EIQKIRADIKEFTSGRQEL-----------TSQVHLMTQDLARLTADLQQIPTLTAEIENTKQELQRARA---AIDYEKK 215
Cdd:pfam05483 346 AHSFVVTEFEATTCSLEELlrteqqrleknEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAedeKLLDEKK 425
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 18400511   216 GYAENYEHGKIMEHKLV----AMARELEKLRAEIANSETS 251
Cdd:pfam05483 426 QFEKIAEELKGKEQELIfllqAREKEIHDLEIQLTAIKTS 465
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
70-250 5.02e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.91  E-value: 5.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511   70 LEDRLAAQNQDVQGLLADNQRLAATHVALKQELEVAQHELQRIMHYIDSLRAEEEImmremydksMRSEMELREVDAMRA 149
Cdd:COG4913  615 LEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREI---------AELEAELERLDASSD 685
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511  150 EIQKIRADIKEFTSGRQELTSQVHLMTQDLARLTADLQQIptlTAEIENTKQELQRARAAIDYEKKGYAENYEHGKIMEH 229
Cdd:COG4913  686 DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQA---EEELDELQDRLEAAEDLARLELRALLEERFAAALGDA 762
                        170       180
                 ....*....|....*....|....*
gi 18400511  230 KLVAMARELE----KLRAEIANSET 250
Cdd:COG4913  763 VERELRENLEeridALRARLNRAEE 787
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
80-254 9.81e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 9.81e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511  80 DVQGLLADNQRLAATHVALKQELEVAQHELQRIMHYIDSLRAEEEIMMREMYDKSMRSEMELREVDAMRAEIQKIRADIK 159
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA 305
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511 160 EFTSGRQELtsqvhlmTQDLARLTADLQQiptLTAEIENTKQELQRARAaidyEKKGYAENYEHGKIMEHKLVAMARELE 239
Cdd:COG1196 306 RLEERRREL-------EERLEELEEELAE---LEEELEELEEELEELEE----ELEEAEEELEEAEAELAEAEEALLEAE 371
                       170
                ....*....|....*
gi 18400511 240 KLRAEIANSETSAYA 254
Cdd:COG1196 372 AELAEAEEELEELAE 386
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
63-208 1.16e-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: 1.16e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511  63 LPPQFSILEDRLAAQNQDVQGLLADNQRLAATHVALKQELEVAQHELQRIMH--YIDSLRAEEEIMMREMYDKSMRSEME 140
Cdd:COG3206 210 LSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARYTPN 289
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18400511 141 LREVDAMRAEIQKIRADIK--------EFTSGRQELTSQVHLMTQDLARLTADLQQIPTLTAEIENTKQELQRARA 208
Cdd:COG3206 290 HPDVIALRAQIAALRAQLQqeaqrilaSLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARE 365
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
68-202 1.35e-04

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 43.08  E-value: 1.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511     68 SILEDRLAAQNQDVQGLLADNQRLAATHVALKQELEVAQHELqrimhyiDSLR-AEEEImmrEMYDKSmrsemelrEVDA 146
Cdd:smart00787 147 EGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEEL-------RQLKqLEDEL---EDCDPT--------ELDR 208
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 18400511    147 MRAEIQKIRADIKEFTSGRQELTSQVHLMTQDLARLTADLQQIPTLTAEIENTKQE 202
Cdd:smart00787 209 AKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQ 264
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
72-235 1.63e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.22  E-value: 1.63e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511  72 DRLAAQNQDVQGLLADNQRLAATHVALKQELEVAQHELQRIMHYIDSLRAEEEIM-----MREMYDKSMRSEMELREVDA 146
Cdd:COG4717  81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEaleaeLAELPERLEELEERLEELRE 160
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511 147 MRAEIQKIRADIKEFTSGRQELTSQVHLMT-QDLARLTADL----QQIPTLTAEIENTKQELQRARAAIDYEKKGYAENY 221
Cdd:COG4717 161 LEEELEELEAELAELQEELEELLEQLSLATeEELQDLAEELeelqQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240
                       170
                ....*....|....
gi 18400511 222 EHGKIMEHKLVAMA 235
Cdd:COG4717 241 LEERLKEARLLLLI 254
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
70-247 2.65e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.98  E-value: 2.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511   70 LEDRLAAQNQDVQGLLADNQRLAATHVALKQELEVAQHELQRImhyidSLRAEEEImmremydksmrsemeLREVDAMRA 149
Cdd:COG4913  293 LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGN-----GGDRLEQL---------------EREIERLER 352
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511  150 EIQKIRADIKEFtsgrQELTSQVHL-MTQDLARLTADLQQIPTLTAEIENTKQELQRARAAIDYEKKgyaenyehgkime 228
Cdd:COG4913  353 ELEERERRRARL----EALLAALGLpLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALR------------- 415
                        170
                 ....*....|....*....
gi 18400511  229 hklvAMARELEKLRAEIAN 247
Cdd:COG4913  416 ----DLRRELRELEAEIAS 430
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
73-220 2.70e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.20  E-value: 2.70e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511  73 RLAAQNQDVQGLLADNQRLAATHVALKQELEVAQHELQRIMHYIDSLraEEEIMMREMYDKSMRSEMELR--EVDAMRAE 150
Cdd:COG4372  39 ELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL--NEQLQAAQAELAQAQEELESLqeEAEELQEE 116
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511 151 IQKIRADIKEFTSGRQELTSQVHLMTQDLARLTADLQQiptLTAEIENTKQELQRARAAIDYEKKGYAEN 220
Cdd:COG4372 117 LEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKE---LEEQLESLQEELAALEQELQALSEAEAEQ 183
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
63-250 2.88e-04

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: 42.65  E-value: 2.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511     63 LPPQFSILEDRLAAQNQDVQGLLADNQRLAATHVALKQELEVAQHELQRIMHYIDSLRAEEEIMMREMYDKSMRSEMELR 142
Cdd:TIGR00618  210 TPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRA 289
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511    143 EVDAMRAEIQKIRADI-KEFTSGRQELTSQVHLMTQDLARLTADLQQiptlTAEIENTKQELQRARAAIDY------EKK 215
Cdd:TIGR00618  290 RKAAPLAAHIKAVTQIeQQAQRIHTELQSKMRSRAKLLMKRAAHVKQ----QSSIEEQRRLLQTLHSQEIHirdaheVAT 365
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 18400511    216 GYAENYEHGKIMEH--------------KLVAMARELEKLRAEIANSET 250
Cdd:TIGR00618  366 SIREISCQQHTLTQhihtlqqqkttltqKLQSLCKELDILQREQATIDT 414
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
68-250 4.84e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 4.84e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511  68 SILEDRLAAQNQDV-----QGLLADNQRLAATHVALKqELEVAQHELQRIMHYIDSLRAEEEIMMREMYdksmrsemELR 142
Cdd:COG4717  45 AMLLERLEKEADELfkpqgRKPELNLKELKELEEELK-EAEEKEEEYAELQEELEELEEELEELEAELE--------ELR 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511 143 EVDAMRAEIQKIRADIKEFTSGRQELTS---QVHLMTQDLARLTADLQQIPTLTAEIENTKQELQRARAAIDYEKkgyae 219
Cdd:COG4717 116 EELEKLEKLLQLLPLYQELEALEAELAElpeRLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLAT----- 190
                       170       180       190
                ....*....|....*....|....*....|.
gi 18400511 220 nyehgkimEHKLVAMARELEKLRAEIANSET 250
Cdd:COG4717 191 --------EEELQDLAEELEELQQRLAELEE 213
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
58-247 5.23e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 5.23e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511  58 VDARGLPPQFSILEDR-LAAQNQDVQGLLADNQRLAAthvalkqelevaQHELQRIMHYIDSLRAEEEIMMREMYDksmR 136
Cdd:COG4717 325 LAALGLPPDLSPEELLeLLDRIEELQELLREAEELEE------------ELQLEELEQEIAALLAEAGVEDEEELR---A 389
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511 137 SEMELREVDAMRAEIQKIRADIKEFTSGRQELtsqvhLMTQDLARLTADLQQIPTLTAEIENTKQELQRARAAIDYEKKG 216
Cdd:COG4717 390 ALEQAEEYQELKEELEELEEQLEELLGELEEL-----LEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQ 464
                       170       180       190
                ....*....|....*....|....*....|.
gi 18400511 217 YAEnyehgkimEHKLVAMARELEKLRAEIAN 247
Cdd:COG4717 465 LEE--------DGELAELLQELEELKAELRE 487
ADIP pfam11559
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ...
133-246 6.19e-04

Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.


Pssm-ID: 463295 [Multi-domain]  Cd Length: 151  Bit Score: 39.61  E-value: 6.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511   133 KSMRSEMELREvdAMRAEIQKIRADIKEFTSGRQELTSQVHLMTQDLARLTADLQQ----IPTLTAEIENTKQELQRARA 208
Cdd:pfam11559  45 QQRDRDLEFRE--SLNETIRTLEAEIERLQSKIERLKTQLEDLERELALLQAKERQlekkLKTLEQKLKNEKEELQRLKN 122
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 18400511   209 AIDYEKKGYAenyehgkimeHKLVAMARELEKLRAEIA 246
Cdd:pfam11559 123 ALQQIKTQFA----------HEVKKRDREIEKLKERLA 150
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
47-204 6.76e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.59  E-value: 6.76e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511     47 MIDDSREPQFRVDARGLPPQFSILEDRLAAQNQDVQGLLADNQRLAAthvaLKQELEVAQHELQrimHYIDSLRAEEE-- 124
Cdd:TIGR02169  787 RLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEK----EIQELQEQRIDLK---EQIKSIEKEIEnl 859
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511    125 -IMMREMYDKSMRSEMELREVDA----MRAEIQKIRADIKEFTSGRQELTSQVHLMTQDLARLTADLQQIPTLTAEIENT 199
Cdd:TIGR02169  860 nGKKEELEEELEELEAALRDLESrlgdLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDP 939

                   ....*
gi 18400511    200 KQELQ 204
Cdd:TIGR02169  940 KGEDE 944
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
69-246 7.64e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.44  E-value: 7.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511   69 ILEDRLAAQnqDVQGLLADNQRLAATHVALKQELEVAQHeLQRIM-HYIDSLRAEEEIMMREMYDKSMRSEMELREVDAM 147
Cdd:COG4913  217 MLEEPDTFE--AADALVEHFDDLERAHEALEDAREQIEL-LEPIReLAERYAAARERLAELEYLRAALRLWFAQRRLELL 293
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511  148 RAEIQKIRADIKEFTSGRQELTSQVHLMTQDLARLTADLQQIPT-----LTAEIENTKQELQRARAAidyekkgyAENYE 222
Cdd:COG4913  294 EAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGdrleqLEREIERLERELEERERR--------RARLE 365
                        170       180
                 ....*....|....*....|....*
gi 18400511  223 HG-KIMEHKLVAMARELEKLRAEIA 246
Cdd:COG4913  366 ALlAALGLPLPASAEEFAALRAEAA 390
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
102-249 7.86e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 7.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511  102 LEVAQHELQRIMHYIDSLRAE-EEIMMREMYDKSMRSEME------LREVDA-------MRAEIQKIRADIKEFTSGRQE 167
Cdd:PRK03918 160 YENAYKNLGEVIKEIKRRIERlEKFIKRTENIEELIKEKEkeleevLREINEisselpeLREELEKLEKEVKELEELKEE 239
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511  168 LTS---QVHLMTQDLARLTADLQQIPTLTAEIENTKQELQRARAAIDyEKKGYAENYEH-GKIMEHKLVAMAR---ELEK 240
Cdd:PRK03918 240 IEElekELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKlSEFYEEYLDELREiekRLSR 318

                 ....*....
gi 18400511  241 LRAEIANSE 249
Cdd:PRK03918 319 LEEEINGIE 327
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
133-249 9.14e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 9.14e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511 133 KSMRSEMELREVDAMRAEIQKIRADIkeftsgrQELTSQVHLMTQDLARLTADLQQiptLTAEIENTKQELQRARAAID- 211
Cdd:COG1196 216 RELKEELKELEAELLLLKLRELEAEL-------EELEAELEELEAELEELEAELAE---LEAELEELRLELEELELELEe 285
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 18400511 212 -----YEKKGYAENYEHGKIMEH-KLVAMARELEKLRAEIANSE 249
Cdd:COG1196 286 aqaeeYELLAELARLEQDIARLEeRRRELEERLEELEEELAELE 329
PRK01156 PRK01156
chromosome segregation protein; Provisional
70-249 1.51e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 40.27  E-value: 1.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511   70 LEDRLAAQNQDVQGLLADNQRLAATHVALKQELEVAQHELQRIMHYIDSLRAEEEIMMrEMYDKSMRSEMELREVDAMRA 149
Cdd:PRK01156 188 LEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELS-SLEDMKNRYESEIKTAESDLS 266
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511  150 EIQKIRADIKEFTSGRQELTS-QVHLMTQDLARLTADLQQIPTLTAEIENTKQELQRARAAI-----------DY-EKKG 216
Cdd:PRK01156 267 MELEKNNYYKELEERHMKIINdPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIkklsvlqkdynDYiKKKS 346
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 18400511  217 YAENYEHG----KIMEHKLVAMARELEKLRAEIANSE 249
Cdd:PRK01156 347 RYDDLNNQilelEGYEMDYNSYLKSIESLKKKIEEYS 383
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
66-247 1.55e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.43  E-value: 1.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511     66 QFSILEDRLAAQNQDVQGLLADNQRLAATHVALKQELEVAQHELQRIMHYIDSLRAEEEIMMREMYDKSMR-SEMELR-- 142
Cdd:TIGR02168  226 ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEiSRLEQQkq 305
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511    143 ----EVDAMRAEIQKIRADIKEFTSGRQELTSQVHLMTQDLARLTADLQ----QIPTLTAEIENTKQELQRARAAIDYEK 214
Cdd:TIGR02168  306 ilreRLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELEsleaELEELEAELEELESRLEELEEQLETLR 385
                          170       180       190
                   ....*....|....*....|....*....|...
gi 18400511    215 KGYAENYEHGKIMEHKLVAMARELEKLRAEIAN 247
Cdd:TIGR02168  386 SKVAQLELQIASLNNEIERLEARLERLEDRRER 418
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
55-258 1.56e-03

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: 40.44  E-value: 1.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511     55 QFRVDARGLPPQFSILEDRLAAQNQDVQGLLADNQRLAATHVALKQELEVAQHElqrimhyIDSLRAEEeimmREMYDKS 134
Cdd:TIGR02169  347 EERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKRE-------INELKREL----DRLQEEL 415
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511    135 MRSEMELREvdamraeiqkIRADIKEFTSGRQELTSQVHlmtqdlarltadlqqipTLTAEIENTKQELQRARA-AIDYE 213
Cdd:TIGR02169  416 QRLSEELAD----------LNAAIAGIEAKINELEEEKE-----------------DKALEIKKQEWKLEQLAAdLSKYE 468
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 18400511    214 KKGYAENYEHGKImEHKLVAMARELEKLRAEIANSETSAYANGPV 258
Cdd:TIGR02169  469 QELYDLKEEYDRV-EKELSKLQRELAEAEAQARASEERVRGGRAV 512
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
98-210 1.76e-03

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 39.74  E-value: 1.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511    98 LKQELEVAQHELQRIMHYIDSLRAEeeimMREMYDKsmrsemELREVDAMRAEIQKIRADIKEFTSGRQELTSQVHLMTQ 177
Cdd:pfam09787  52 LRQERDLLREEIQKLRGQIQQLRTE----LQELEAQ------QQEEAESSREQLQELEEQLATERSARREAEAELERLQE 121
                          90       100       110
                  ....*....|....*....|....*....|....
gi 18400511   178 DLARLTADL-QQIPTLTAEIENTKQELQRARAAI 210
Cdd:pfam09787 122 ELRYLEEELrRSKATLQSRIKDREAEIEKLRNQL 155
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
57-255 2.67e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.12  E-value: 2.67e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511  57 RVDARGLPPQFSILedrLAAQNQDVQGLLADNQRLAATHVALKQELEVAQHELQRIMHYIDSLRAEEEIMMREMYDKSMR 136
Cdd:COG4372  12 RLSLFGLRPKTGIL---IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQ 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511 137 SEMELREVDAMRAEIQKIRADIKEFTSGRQELTSQVHLMTQDLARLTADLQQIPTLTAEIENTKQELQRARAAIDYEKKG 216
Cdd:COG4372  89 LQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAA 168
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 18400511 217 YAENYEHGKIMEHKlvamaRELEKLRAEIANSETSAYAN 255
Cdd:COG4372 169 LEQELQALSEAEAE-----QALDELLKEANRNAEKEEEL 202
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
143-261 2.84e-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: 38.98  E-value: 2.84e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511 143 EVDAMRAEIQKIRADIKEFTSGRQELTSQVHLMTQDLARLTadlQQIPTLTAEIENTKQELQRARAAIdyekkgyaenye 222
Cdd:COG4942  21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALE---RRIAALARRIRALEQELAALEAEL------------ 85
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 18400511 223 hgKIMEHKLVAMARELEKLRAEIANSETSAYANGPVGNP 261
Cdd:COG4942  86 --AELEKEIAELRAELEAQKEELAELLRALYRLGRQPPL 122
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
109-254 3.10e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.37  E-value: 3.10e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511 109 LQRIMHYIdsLRAEEEIMMREMYDKSMR-SEMELREVDAMRAEIQKIRADIKEFtsgrQELTSQVHLMTQDLARLTADLQ 187
Cdd:COG4717  39 LLAFIRAM--LLERLEKEADELFKPQGRkPELNLKELKELEEELKEAEEKEEEY----AELQEELEELEEELEELEAELE 112
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18400511 188 QiptLTAEIENTKQELQRARAAIDYEK-----KGYAENYEHGKIMEHKLVAMARELEKLRAEIANSETSAYA 254
Cdd:COG4717 113 E---LREELEKLEKLLQLLPLYQELEAleaelAELPERLEELEERLEELRELEEELEELEAELAELQEELEE 181
PRK12758 PRK12758
DNA gyrase/topoisomerase IV subunit A;
98-222 3.14e-03

DNA gyrase/topoisomerase IV subunit A;


Pssm-ID: 237192 [Multi-domain]  Cd Length: 869  Bit Score: 39.22  E-value: 3.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511   98 LKQELEVAQHELQRIMHYiDSLraeEEIMMRE-MYDksmrsemELREVDAMRAEIQKIRADIKEFTSG-RQELTsqvhlm 175
Cdd:PRK12758 345 LKQELEIRLSELEEQWHF-ASL---EKIFIEErIYK-------EIEEAETWEAVIEAIDKGLEPFKKQfIREVT------ 407
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18400511  176 TQDLARLT--------------ADlQQIPTLTAEIENTKQELQR-ARAAIDYE---KKGYAENYE 222
Cdd:PRK12758 408 EDDIVRLTeikikriskfdsdkAD-ELIARLEAEIAEVKHHLAHlTDYAIAYFtnlKKKYGKGRE 471
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
97-312 4.11e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 38.66  E-value: 4.11e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511  97 ALKQELEVAQHELQRIMHYIDSLRAEEEIMMREMYDKSMRSEMELREVDAMRAEIQKIRADIKE------------FTSG 164
Cdd:COG3883  20 AKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEErreelgeraralYRSG 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511 165 R--------------QELTSQVHLMTQ--------------DLARLTADLQQIPTLTAEIENTKQELQRARAAIDYEKKG 216
Cdd:COG3883 100 GsvsyldvllgsesfSDFLDRLSALSKiadadadlleelkaDKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAE 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511 217 YAENYEHGKIMEHKLVAMARELEKLRAEIANSETSAYANGPVGNPGGVAYGGGYGNPEAGYPVNPYQPNYTMNPAQTGVV 296
Cdd:COG3883 180 QEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAA 259
                       250
                ....*....|....*.
gi 18400511 297 GYYPPPYGPQAAWAGG 312
Cdd:COG3883 260 GSAGAAGAAAGAAGAG 275
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
66-252 4.32e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 38.76  E-value: 4.32e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511  66 QFSILEDRLAAQNQDVQGLLADNQRLAATHVALKQELEVAQHELQRIMHYIDSL-----RAEEEIMMREMYDKSMRSEME 140
Cdd:COG1196 282 ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELeeeleELEEELEEAEEELEEAEAELA 361
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511 141 --LREVDAMRAEIQKIRADIKEFTSGRQELTSQVHLMTQDLARLTADLQQiptLTAEIENTKQELQRARAAIDYEKKGYA 218
Cdd:COG1196 362 eaEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEA---LLERLERLEEELEELEEALAELEEEEE 438
                       170       180       190
                ....*....|....*....|....*....|....
gi 18400511 219 ENYEHGKIMEHKLVAMARELEKLRAEIANSETSA 252
Cdd:COG1196 439 EEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
71-246 5.61e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 38.38  E-value: 5.61e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511  71 EDRLAAQNQDVQGLLADNQRLAATHVALKQELEVAQHELQRIMHYIDSLRAEEEIMMREmydksmrsemELREVDAMRAE 150
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE----------AEEELEELAEE 387
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511 151 IQKIRADIKEFTSGRQELTSQVHLMTQDLARLTADLQQiptLTAEIENTKQELQRARAAIDYEKKGYAENYEHGKIMEHK 230
Cdd:COG1196 388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE---LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEL 464
                       170
                ....*....|....*.
gi 18400511 231 LVAMARELEKLRAEIA 246
Cdd:COG1196 465 LAELLEEAALLEAALA 480
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
55-207 7.57e-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: 37.95  E-value: 7.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511    55 QFRVDARGLPPQFSILEDRLAAQNQDVQGLLADNQRLAATHVALKQE----LEVAQHELQRIMHYIDSLRA------EEE 124
Cdd:pfam07888  70 QWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEkdalLAQRAAHEARIRELEEDIKTltqrvlERE 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511   125 IMMREMYDKSMRSEMELREVDAMR-----------AEIQKIRADIKEFTSGRQELTSQVHLMTQDLARLTADLQQIPTLT 193
Cdd:pfam07888 150 TELERMKERAKKAGAQRKEEEAERkqlqaklqqteEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKE 229
                         170
                  ....*....|....
gi 18400511   194 AEIENTKQELQRAR 207
Cdd:pfam07888 230 AENEALLEELRSLQ 243
DUF445 pfam04286
Protein of unknown function (DUF445); Predicted to be a membrane protein.
87-203 9.25e-03

Protein of unknown function (DUF445); Predicted to be a membrane protein.


Pssm-ID: 427840 [Multi-domain]  Cd Length: 368  Bit Score: 37.61  E-value: 9.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400511    87 DNQRLAAthVALKQELEVAQHE------LQRIMHYIDSLRAEEEImmREMYDKSMRSEMELREVDAMRAE---------I 151
Cdd:pfam04286 121 DLAPLLG--KLLELLLAEGRHQallddlLDRLRDWLRSEEGKQRI--AEMIDEFLEEWGPLVALLGGIAEmilralsslL 196
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 18400511   152 QKIRADIKEFTsgRQELTSQVHlmtqdlaRLTADLQQIPTLTAEIENTKQEL 203
Cdd:pfam04286 197 DEVQADPDHPL--RLAFDRAVR-------ELITDLLNDPELRAEVEELKQKL 239
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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