NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|160333332|ref|NP_081687|]
View 

protein Spindly [Mus musculus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
COG4913 super family cl25907
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
18-195 2.94e-08

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


The actual alignment was detected with superfamily member COG4913:

Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 56.85  E-value: 2.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333332   18 ERLKAAHYGLQLLERQTELQSQLDKCHEE---MMITAEKYNQEKHAL-----QREVELKSRMLDSLSCECEALKQQ---- 85
Cdd:COG4913   235 DDLERAHEALEDAREQIELLEPIRELAERyaaARERLAELEYLRAALrlwfaQRRLELLEAELEELRAELARLEAElerl 314
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333332   86 ------QKAQLEQLEVQLHRSHRQEVSDLKNKLENLKVELDEARLGEKQLKQKLDLQGELLAHKSEELRLLSEQ--RVLS 157
Cdd:COG4913   315 earldaLREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEaaALLE 394
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 160333332  158 SMSSELLALETELTAAEGVKNALKEEVNELQYKQEQLE 195
Cdd:COG4913   395 ALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
 
Name Accession Description Interval E-value
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
18-195 2.94e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 56.85  E-value: 2.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333332   18 ERLKAAHYGLQLLERQTELQSQLDKCHEE---MMITAEKYNQEKHAL-----QREVELKSRMLDSLSCECEALKQQ---- 85
Cdd:COG4913   235 DDLERAHEALEDAREQIELLEPIRELAERyaaARERLAELEYLRAALrlwfaQRRLELLEAELEELRAELARLEAElerl 314
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333332   86 ------QKAQLEQLEVQLHRSHRQEVSDLKNKLENLKVELDEARLGEKQLKQKLDLQGELLAHKSEELRLLSEQ--RVLS 157
Cdd:COG4913   315 earldaLREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEaaALLE 394
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 160333332  158 SMSSELLALETELTAAEGVKNALKEEVNELQYKQEQLE 195
Cdd:COG4913   395 ALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
35-353 3.06e-07

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: 53.91  E-value: 3.06e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333332    35 ELQSQLDKCHEEMMiTAEKYnQEKHALQREVELKSRMLDslscecealKQQQKAQLEQLEVQLHRShRQEVSDLKNKLEN 114
Cdd:TIGR02168  197 ELERQLKSLERQAE-KAERY-KELKAELRELELALLVLR---------LEELREELEELQEELKEA-EEELEELTAELQE 264
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333332   115 LKVELDEARLGEKQLKQKL-DLQGELLAHKSE----ELRLLSEQRVLSSMSSELLALETELTAAEGVKNALKEEVNELQY 189
Cdd:TIGR02168  265 LEEKLEELRLEVSELEEEIeELQKELYALANEisrlEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEE 344
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333332   190 KQEQLECLNTSLLHQVDRLKeekeerereavsyyNALEKARVENQDLQVQLGHALQQAADPNSKGNSLFAEVEDRRVAME 269
Cdd:TIGR02168  345 KLEELKEELESLEAELEELE--------------AELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLE 410
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333332   270 rQLNLMKDKYQSLKKQN--AFTRDQMNKMKLQISTLLRMRGSQTE-----FEQQERLFAMIEQKNGEIKHLLGEINKLEK 342
Cdd:TIGR02168  411 -RLEDRRERLQQEIEELlkKLEEAELKELQAELEELEEELEELQEelerlEEALEELREELEEAEQALDAAERELAQLQA 489
                          330
                   ....*....|.
gi 160333332   343 FKNLYESMESR 353
Cdd:TIGR02168  490 RLDSLERLQEN 500
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
18-318 1.81e-04

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: 44.72  E-value: 1.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333332    18 ERLKAAHYGLQLLERQTelqSQLDKCHEEMMITAEKYNQEKHALQREVELKSRMLDSL----------SCECEALKQQQK 87
Cdd:pfam15921  482 EELTAKKMTLESSERTV---SDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLknegdhlrnvQTECEALKLQMA 558
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333332    88 AQLEQLEV---------QLHRSHRQEVSDLKNKLENLKVELDEARLGEKQ---LKQKLDLQGELLAHKSEELRLlSEQRV 155
Cdd:pfam15921  559 EKDKVIEIlrqqienmtQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEfkiLKDKKDAKIRELEARVSDLEL-EKVKL 637
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333332   156 LSSMSSELLALETELTAAEGVKNALKEEVNELQYKQEQLECLNTSLLHQVDRLKEEKEEREREAVSYYNALEKARVENQD 235
Cdd:pfam15921  638 VNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKS 717
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333332   236 LQVQLGHALQQAADPNSKGNSLFAEVEdrrvAMERQLNLMKDKYQSLKKQNAFTRDQMNKMKLQISTLL----RMRGSQT 311
Cdd:pfam15921  718 MEGSDGHAMKVAMGMQKQITAKRGQID----ALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVAteknKMAGELE 793

                   ....*..
gi 160333332   312 EFEQQER 318
Cdd:pfam15921  794 VLRSQER 800
PRK09039 PRK09039
peptidoglycan -binding protein;
61-208 5.81e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 39.18  E-value: 5.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333332  61 LQREVELKSRMLDSLSCECEAL----------KQQQKAQLEQLEVQLhRSHRQEVSDLKNKLENLKVELDEARLGEKQLK 130
Cdd:PRK09039  44 LSREISGKDSALDRLNSQIAELadllslerqgNQDLQDSVANLRASL-SAAEAERSRLQALLAELAGAGAAAEGRAGELA 122
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 160333332 131 QKLDLQGELLAHKSEELRLLSEQrvlssmsseLLALETELTAAEGVKNALKEEVNELQYKQEQL-ECLNTSLLHQVDRL 208
Cdd:PRK09039 123 QELDSEKQVSARALAQVELLNQQ---------IAALRRQLAALEAALDASEKRDRESQAKIADLgRRLNVALAQRVQEL 192
 
Name Accession Description Interval E-value
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
18-195 2.94e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 56.85  E-value: 2.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333332   18 ERLKAAHYGLQLLERQTELQSQLDKCHEE---MMITAEKYNQEKHAL-----QREVELKSRMLDSLSCECEALKQQ---- 85
Cdd:COG4913   235 DDLERAHEALEDAREQIELLEPIRELAERyaaARERLAELEYLRAALrlwfaQRRLELLEAELEELRAELARLEAElerl 314
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333332   86 ------QKAQLEQLEVQLHRSHRQEVSDLKNKLENLKVELDEARLGEKQLKQKLDLQGELLAHKSEELRLLSEQ--RVLS 157
Cdd:COG4913   315 earldaLREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEaaALLE 394
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 160333332  158 SMSSELLALETELTAAEGVKNALKEEVNELQYKQEQLE 195
Cdd:COG4913   395 ALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
34-318 7.22e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.71  E-value: 7.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333332  34 TELQSQLDKCHEEMmITAEKYNQEKHALQ-REVELKSRMLDSLSCECEALKQQ---QKAQLEQLEVQLhRSHRQEVSDLK 109
Cdd:COG1196  196 GELERQLEPLERQA-EKAERYRELKEELKeLEAELLLLKLRELEAELEELEAEleeLEAELEELEAEL-AELEAELEELR 273
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333332 110 NKLENLKVELDEARLGEKQLKQKLDLQGELLAHKSEELRLLSEQrvLSSMSSELLALETELTAAEGVKNALKEEVNELQY 189
Cdd:COG1196  274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER--LEELEEELAELEEELEELEEELEELEEELEEAEE 351
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333332 190 KQEQLECLNTSLLHQVDRLKEEKEEREREAVSYYNALEKARVENQDLQVQLGHALQQAADPNSKGNSLFAEVEDRRVAME 269
Cdd:COG1196  352 ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA 431
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 160333332 270 RQLNLMKDKYQSLKKQNAFTRDQMNKMKLQISTLLRMRGSQTEFEQQER 318
Cdd:COG1196  432 ELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALA 480
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
35-353 3.06e-07

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: 53.91  E-value: 3.06e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333332    35 ELQSQLDKCHEEMMiTAEKYnQEKHALQREVELKSRMLDslscecealKQQQKAQLEQLEVQLHRShRQEVSDLKNKLEN 114
Cdd:TIGR02168  197 ELERQLKSLERQAE-KAERY-KELKAELRELELALLVLR---------LEELREELEELQEELKEA-EEELEELTAELQE 264
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333332   115 LKVELDEARLGEKQLKQKL-DLQGELLAHKSE----ELRLLSEQRVLSSMSSELLALETELTAAEGVKNALKEEVNELQY 189
Cdd:TIGR02168  265 LEEKLEELRLEVSELEEEIeELQKELYALANEisrlEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEE 344
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333332   190 KQEQLECLNTSLLHQVDRLKeekeerereavsyyNALEKARVENQDLQVQLGHALQQAADPNSKGNSLFAEVEDRRVAME 269
Cdd:TIGR02168  345 KLEELKEELESLEAELEELE--------------AELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLE 410
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333332   270 rQLNLMKDKYQSLKKQN--AFTRDQMNKMKLQISTLLRMRGSQTE-----FEQQERLFAMIEQKNGEIKHLLGEINKLEK 342
Cdd:TIGR02168  411 -RLEDRRERLQQEIEELlkKLEEAELKELQAELEELEEELEELQEelerlEEALEELREELEEAEQALDAAERELAQLQA 489
                          330
                   ....*....|.
gi 160333332   343 FKNLYESMESR 353
Cdd:TIGR02168  490 RLDSLERLQEN 500
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
27-304 8.36e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 52.38  E-value: 8.36e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333332    27 LQLLERQTELQSQLDKCHEEMmitaEKYNQEKHALQREVELKSRMLDSLSCECEALKQQQ---KAQLEQLEVQLhRSHRQ 103
Cdd:TIGR02169  677 QRLRERLEGLKRELSSLQSEL----RRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEeklKERLEELEEDL-SSLEQ 751
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333332   104 EVSDLKNKLENLKVELDEARLGEKQLKQKL-DLQGELLAHKSEEL-RLLSEQR-VLSSMSSELLALETELTAAEGVKNAL 180
Cdd:TIGR02169  752 EIENVKSELKELEARIEELEEDLHKLEEALnDLEARLSHSRIPEIqAELSKLEeEVSRIEARLREIEQKLNRLTLEKEYL 831
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333332   181 KEEVNELQYKQEQLECLNTSLLHQVDRLKEEKEEREREavsyynaLEKARVENQDLQVQLGHalqqaadpnskgnsLFAE 260
Cdd:TIGR02169  832 EKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE-------LEELEAALRDLESRLGD--------------LKKE 890
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 160333332   261 VEDrrvaMERQLNLMKDKYQSLKKQNAFTRDQMNKMKLQISTLL 304
Cdd:TIGR02169  891 RDE----LEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALE 930
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
50-249 3.62e-06

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: 49.38  E-value: 3.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333332  50 TAEKYNQEKHALQREVELKSRMLDSLscecEALKQQQKAQLEQLEVQLHRShRQEVSDLKNKLENLKVELDEARLGEKQL 129
Cdd:COG4942   21 AAAEAEAELEQLQQEIAELEKELAAL----KKEEKALLKQLAALERRIAAL-ARRIRALEQELAALEAELAELEKEIAEL 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333332 130 KQKLDLQGELLAHKSEELRLLSEQRVLSSM--SSELLALETELTAAEGVKNALKEEVNELQYKQEQLECLNTSLLHQVDR 207
Cdd:COG4942   96 RAELEAQKEELAELLRALYRLGRQPPLALLlsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 160333332 208 LKEEKEEREREAvsyyNALEKARVENQDLQVQLGHALQQAAD 249
Cdd:COG4942  176 LEALLAELEEER----AALEALKAERQKLLARLEKELAELAA 213
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
18-318 1.81e-04

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: 44.72  E-value: 1.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333332    18 ERLKAAHYGLQLLERQTelqSQLDKCHEEMMITAEKYNQEKHALQREVELKSRMLDSL----------SCECEALKQQQK 87
Cdd:pfam15921  482 EELTAKKMTLESSERTV---SDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLknegdhlrnvQTECEALKLQMA 558
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333332    88 AQLEQLEV---------QLHRSHRQEVSDLKNKLENLKVELDEARLGEKQ---LKQKLDLQGELLAHKSEELRLlSEQRV 155
Cdd:pfam15921  559 EKDKVIEIlrqqienmtQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEfkiLKDKKDAKIRELEARVSDLEL-EKVKL 637
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333332   156 LSSMSSELLALETELTAAEGVKNALKEEVNELQYKQEQLECLNTSLLHQVDRLKEEKEEREREAVSYYNALEKARVENQD 235
Cdd:pfam15921  638 VNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKS 717
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333332   236 LQVQLGHALQQAADPNSKGNSLFAEVEdrrvAMERQLNLMKDKYQSLKKQNAFTRDQMNKMKLQISTLL----RMRGSQT 311
Cdd:pfam15921  718 MEGSDGHAMKVAMGMQKQITAKRGQID----ALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVAteknKMAGELE 793

                   ....*..
gi 160333332   312 EFEQQER 318
Cdd:pfam15921  794 VLRSQER 800
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1-240 3.48e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.89  E-value: 3.48e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333332     1 MEADITNLRNKLKECEDERLKAAHYGLQLLERQTELQSQLDKCHEEMmitaEKYNQEKHALQREVELKSRMLDSLSCECE 80
Cdd:TIGR02168  724 LSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERL----EEAEEELAEAEAEIEELEAQIEQLKEELK 799
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333332    81 ALKQQQKAQLEQLevqlhRSHRQEVSDLKNKLENLKVELDEARLGEKQLKQKLD---LQGELLAHKSEELRLLSEQrvls 157
Cdd:TIGR02168  800 ALREALDELRAEL-----TLLNEEAANLRERLESLERRIAATERRLEDLEEQIEelsEDIESLAAEIEELEELIEE---- 870
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333332   158 smssellaLETELTAAEGVKNALKEEVNELQYKQEQLECLNTSLLHQVDRLKEEKEEREREAVSYYNALEKARVENQDLQ 237
Cdd:TIGR02168  871 --------LESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQ 942

                   ...
gi 160333332   238 VQL 240
Cdd:TIGR02168  943 ERL 945
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
96-285 9.62e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 9.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333332   96 QLHRSHrQEVSDLKNKLENLK--VELDEARLGEKQLKQKLDLQGELLAHKSEELRLLSEQRVLSSMSSELLALETELTAA 173
Cdd:COG4913   236 DLERAH-EALEDAREQIELLEpiRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERL 314
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333332  174 EGVKNALKEEVNEL--QYKQEQLECLNtSLLHQVDRLKEEKEEREREAVSYYNALEKARVENQDLQVQLGHALQQAADPN 251
Cdd:COG4913   315 EARLDALREELDELeaQIRGNGGDRLE-QLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALL 393
                         170       180       190
                  ....*....|....*....|....*....|....
gi 160333332  252 SKGNSLFAEVEDRRVAMERQLNLMKDKYQSLKKQ 285
Cdd:COG4913   394 EALEEELEALEEALAEAEAALRDLRRELRELEAE 427
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
5-208 1.15e-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: 41.98  E-value: 1.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333332     5 ITNLRNKLKECEDERLKaahyglqLLERQTELQSQLDKCHEEMMItAEKYNQEKHALQREVELKSRM----LDSLSCECE 80
Cdd:TIGR02169  793 IPEIQAELSKLEEEVSR-------IEARLREIEQKLNRLTLEKEY-LEKEIQELQEQRIDLKEQIKSiekeIENLNGKKE 864
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333332    81 ALKQQQK---AQLEQLEVQL------HRSHRQEVSDLKNKLENLKVELDEARLGEKQLKQKLDLQGELLAH----KSEEL 147
Cdd:TIGR02169  865 ELEEELEeleAALRDLESRLgdlkkeRDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEiedpKGEDE 944
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 160333332   148 RLLSEQRVLSSMSSELLALETELTAAEGVKNALKEE-------VNELQYKQEQLECLNTSLLHQVDRL 208
Cdd:TIGR02169  945 EIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEyeevlkrLDELKEKRAKLEEERKAILERIEEY 1012
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
5-188 3.72e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.39  E-value: 3.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333332   5 ITNLRNKLKECED--ERLKAAH-------YGLQLLERQTELQSQLDKCHEEMMITAEKYNQEKHALQREVELKSRMLDSL 75
Cdd:COG3206  184 LPELRKELEEAEAalEEFRQKNglvdlseEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSP 263
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333332  76 scECEALKQQ---QKAQLEQLEVQLHRSHRQeVSDLKNKLENLKVELDEARlgeKQLKQKLDLQGELLAHKSEELR---- 148
Cdd:COG3206  264 --VIQQLRAQlaeLEAELAELSARYTPNHPD-VIALRAQIAALRAQLQQEA---QRILASLEAELEALQAREASLQaqla 337
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 160333332 149 -LLSEQRVLSSMSSELLALETELTAAEGVKNALKEEVNELQ 188
Cdd:COG3206  338 qLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEAR 378
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
87-267 4.00e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 4.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333332   87 KAQLEQLEVQLHRShRQEVSDLKNKLENLKVELDearlgekQLKQKLDLQGELLAHKSEELRLLSEQRVLSSM------- 159
Cdd:COG4913   609 RAKLAALEAELAEL-EEELAEAEERLEALEAELD-------ALQERREALQRLAEYSWDEIDVASAEREIAELeaelerl 680
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333332  160 ---SSELLALETELTAAEGVKNALKEEVNELQYKQEQLECLNTSLLHQVDRLKEEKEEREREAVSYYNALEKARVEN--- 233
Cdd:COG4913   681 dasSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAalg 760
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 160333332  234 ----QDLQVQLGHALQQAadpNSKGNSLFAEVEDRRVA 267
Cdd:COG4913   761 daveRELRENLEERIDAL---RARLNRAEEELERAMRA 795
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
28-175 5.37e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 39.84  E-value: 5.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333332  28 QLLERQTElqSQLDKCHEEMMITAEKYNQEKHALQREVELKSRMLDSLSCECEALKQQ---QKAQLEQLEVQLHRSHRQ- 103
Cdd:COG2433  380 EALEELIE--KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAEleeKDERIERLERELSEARSEe 457
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333332 104 --------EVSDLKNKLENLKVELDEARLGEKQLKQKLDLQGELlaHKSEELRLLSEQRVLSSMSSE-LLALETELTAAE 174
Cdd:COG2433  458 rreirkdrEISRLDREIERLERELEEERERIEELKRKLERLKEL--WKLEHSGELVPVKVVEKFTKEaIRRLEEEYGLKE 535

                 .
gi 160333332 175 G 175
Cdd:COG2433  536 G 536
PRK09039 PRK09039
peptidoglycan -binding protein;
61-208 5.81e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 39.18  E-value: 5.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333332  61 LQREVELKSRMLDSLSCECEAL----------KQQQKAQLEQLEVQLhRSHRQEVSDLKNKLENLKVELDEARLGEKQLK 130
Cdd:PRK09039  44 LSREISGKDSALDRLNSQIAELadllslerqgNQDLQDSVANLRASL-SAAEAERSRLQALLAELAGAGAAAEGRAGELA 122
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 160333332 131 QKLDLQGELLAHKSEELRLLSEQrvlssmsseLLALETELTAAEGVKNALKEEVNELQYKQEQL-ECLNTSLLHQVDRL 208
Cdd:PRK09039 123 QELDSEKQVSARALAQVELLNQQ---------IAALRRQLAALEAALDASEKRDRESQAKIADLgRRLNVALAQRVQEL 192
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
2-230 7.70e-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: 39.28  E-value: 7.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333332     2 EADITNLRNKLKECEDERLKAAHYGLQLLERQTELQSQLDKCHEEMMITAEKYNQEKHALQREVELKSRMLDSLSCECEA 81
Cdd:TIGR02169  190 DLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEE 269
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333332    82 LKQQqkaqLEQLEVQLHRSHRQEVSDLKNKLENLKVELDEARLGEKQLKQKL-DLQGELLAHKSEELRLLSE----QRVL 156
Cdd:TIGR02169  270 IEQL----LEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELeDAEERLAKLEAEIDKLLAEieelEREI 345
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333332   157 SSMSSELLALETELTAAEGVKNALKEEVNELQYK-----------QEQLECLNT---SLLHQVDRLKEEKEEREREAVSY 222
Cdd:TIGR02169  346 EEERKRRDKLTEEYAELKEELEDLRAELEEVDKEfaetrdelkdyREKLEKLKReinELKRELDRLQEELQRLSEELADL 425

                   ....*...
gi 160333332   223 YNALEKAR 230
Cdd:TIGR02169  426 NAAIAGIE 433
 
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