NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|767965694|ref|XP_011518321|]
View 

EF-hand calcium-binding domain-containing protein 4A isoform X9 [Homo sapiens]

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
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 225-430 2.82e-08

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.48  E-value: 2.82e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965694 225 RAVRTLWARLQRERPELlgsfEDVLIRASACLEEAARERDGLEQALRRRESEHEREVRALYEETEQLREQSRRppsqnfa 304
Cdd:COG1196  235 RELEAELEELEAELEEL----EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD------- 303

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965694 305 rgerRSRLELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQAQNSQLWRAHEALRTQLEGAQEQIRRLESEARGRQE 384
Cdd:COG1196  304 ----IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 767965694 385 QTQRDVVAVSRNMQKEKVSLLRQLELLRELNTRLRDDRDACEARRA 430
Cdd:COG1196  380 ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 225-430 2.82e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.48  E-value: 2.82e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965694 225 RAVRTLWARLQRERPELlgsfEDVLIRASACLEEAARERDGLEQALRRRESEHEREVRALYEETEQLREQSRRppsqnfa 304
Cdd:COG1196  235 RELEAELEELEAELEEL----EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD------- 303

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965694 305 rgerRSRLELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQAQNSQLWRAHEALRTQLEGAQEQIRRLESEARGRQE 384
Cdd:COG1196  304 ----IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 767965694 385 QTQRDVVAVSRNMQKEKVSLLRQLELLRELNTRLRDDRDACEARRA 430
Cdd:COG1196  380 ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 222-443 1.21e-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: 48.13  E-value: 1.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965694   222 SRQRAVRTLWARLQRerpellgsFEDVLIRASACLEEAARERDGLEQA---LRRRESEHEREVRALYEETEQLREQSRRP 298
Cdd:TIGR02168  674 ERRREIEELEEKIEE--------LEEKIAELEKALAELRKELEELEEEleqLRKELEELSRQISALRKDLARLEAEVEQL 745

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965694   299 PSQNFARGERRSRLELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQAQNSQLWRAHEALRTQL----EGAQEQIRR 374
Cdd:TIGR02168  746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELtllnEEAANLRER 825

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767965694   375 LESEAR--GRQEQTQRDVVAVSRNMQKEKVSLLRQLELLRELNTRLRDDRDACEARRAGSSCRKALTTARL 443
Cdd:TIGR02168  826 LESLERriAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSEL 896
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
 309-379 2.00e-04

TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.


Pssm-ID: 462316 [Multi-domain]  Cd Length: 129  Bit Score: 41.09  E-value: 2.00e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767965694  309 RSRLELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQ-------AQNSQLWRAHEALRTQLEGAQEQIRRLESEA 379
Cdd:pfam07926   3 LSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQqnyerelVLHAEDIKALQALREELNELKAEIAELKAEA 80
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
233-388 5.52e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.25  E-value: 5.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965694 233 RLQRERPELLGS--FEDVLIRA-SACLEEAARERDGLEQALRRRESEHErevrALYEETEQLREQSRRPPSQNFARGERR 309
Cdd:PRK02224 290 ELEEERDDLLAEagLDDADAEAvEARREELEDRDEELRDRLEECRVAAQ----AHNEEAESLREDADDLEERAEELREEA 365

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965694 310 SRLELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQAQNSQLWRAHEALRTQLEGAQEQIRRLE---SEARGRQEQT 386
Cdd:PRK02224 366 AELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEatlRTARERVEEA 445


                 ..
gi 767965694 387 QR 388
Cdd:PRK02224 446 EA 447
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 225-430 2.82e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.48  E-value: 2.82e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965694 225 RAVRTLWARLQRERPELlgsfEDVLIRASACLEEAARERDGLEQALRRRESEHEREVRALYEETEQLREQSRRppsqnfa 304
Cdd:COG1196  235 RELEAELEELEAELEEL----EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD------- 303

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965694 305 rgerRSRLELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQAQNSQLWRAHEALRTQLEGAQEQIRRLESEARGRQE 384
Cdd:COG1196  304 ----IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 767965694 385 QTQRDVVAVSRNMQKEKVSLLRQLELLRELNTRLRDDRDACEARRA 430
Cdd:COG1196  380 ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 223-402 7.62e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.94  E-value: 7.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965694 223 RQRAVRTLWARLQRERPELLGSFEDVLIRASACLEEAARERDGLEQALRRRESEHEREVRALYEETEQLREQSRRppSQN 302
Cdd:COG1196  320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA--AAE 397

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965694 303 FArgERRSRLELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQAQNSQLWRAHEALRTQLEGAQEQIRRLESEARGR 382
Cdd:COG1196  398 LA--AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL 475

                        170       180
                 ....*....|....*....|
gi 767965694 383 QEQTQRDVVAVSRNMQKEKV 402
Cdd:COG1196  476 EAALAELLEELAEAAARLLL 495
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
286-388 1.72e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 49.90  E-value: 1.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965694 286 EETEQLREQSRRPPSQNFARGERRSRLELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQAQNSQLWRAHEALRTQL 365
Cdd:COG4372   52 EELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQR 131

                         90       100
                 ....*....|....*....|...
gi 767965694 366 EGAQEQIRRLESEARGRQEQTQR 388
Cdd:COG4372  132 KQLEAQIAELQSEIAEREEELKE 154
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 222-443 1.21e-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: 48.13  E-value: 1.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965694   222 SRQRAVRTLWARLQRerpellgsFEDVLIRASACLEEAARERDGLEQA---LRRRESEHEREVRALYEETEQLREQSRRP 298
Cdd:TIGR02168  674 ERRREIEELEEKIEE--------LEEKIAELEKALAELRKELEELEEEleqLRKELEELSRQISALRKDLARLEAEVEQL 745

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965694   299 PSQNFARGERRSRLELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQAQNSQLWRAHEALRTQL----EGAQEQIRR 374
Cdd:TIGR02168  746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELtllnEEAANLRER 825

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767965694   375 LESEAR--GRQEQTQRDVVAVSRNMQKEKVSLLRQLELLRELNTRLRDDRDACEARRAGSSCRKALTTARL 443
Cdd:TIGR02168  826 LESLERriAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSEL 896
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 223-388 2.57e-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: 2.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965694   223 RQRAVRTLWARLQRERPELLG---SFEDVLIRASACLEEAARERDGLEQALRRRESEHEREVRALYEETEQLRE------ 293
Cdd:TIGR02168  741 EVEQLEERIAQLSKELTELEAeieELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLlneeaa 820

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965694   294 --QSRRPPSQNFARGERRSRLELELQSREQDLERAGL-----RQRELEQQLHAQAAEHLEAQAQNSQlwrAHEALRTQLE 366
Cdd:TIGR02168  821 nlRERLESLERRIAATERRLEDLEEQIEELSEDIESLaaeieELEELIEELESELEALLNERASLEE---ALALLRSELE 897

                          170       180
                   ....*....|....*....|..
gi 767965694   367 GAQEQIRRLESEARGRQEQTQR 388
Cdd:TIGR02168  898 ELSEELRELESKRSELRRELEE 919
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
231-403 6.70e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.53  E-value: 6.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965694 231 WARLQRERPELlgsfEDVLIRASACLEEAARERDGLEQALRRReseherevrALYEETEQLREQSRRPPSQnFARGERRs 310
Cdd:COG4717   90 YAELQEELEEL----EEELEELEAELEELREELEKLEKLLQLL---------PLYQELEALEAELAELPER-LEELEER- 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965694 311 rlELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQAQN-SQLWRAHEALRTQLEGAQEQIRRLESEARGRQEQTQRD 389
Cdd:COG4717  155 --LEELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL 232

                        170
                 ....*....|....
gi 767965694 390 VVAVSRNMQKEKVS 403
Cdd:COG4717  233 ENELEAAALEERLK 246
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 223-464 8.21e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 8.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965694 223 RQRAVRTLWARLQRERPELLGSFEDVLIRASACLEEAARERDGLEQALRRRESEHEREVRALYEETEQLREQSRRPpSQN 302
Cdd:COG1196  352 ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE-EAL 430

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965694 303 FARGERRSRLELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQAQNSQLWRAHEALRTQLEGAQEQIRRLESEARGR 382
Cdd:COG1196  431 AELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGV 510

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965694 383 QEQTQRD-------VVAVSRNMQKEKVSLLRQLELLRELNTRLRDDRDAcEARRAGSSCRKALTTARLPGPTCCCCCCWA 455
Cdd:COG1196  511 KAALLLAglrglagAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVA-AAAIEYLKAAKAGRATFLPLDKIRARAALA 589


                 ....*....
gi 767965694 456 RPPRRGSGH 464
Cdd:COG1196  590 AALARGAIG 598
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
 309-379 2.00e-04

TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.


Pssm-ID: 462316 [Multi-domain]  Cd Length: 129  Bit Score: 41.09  E-value: 2.00e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767965694  309 RSRLELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQ-------AQNSQLWRAHEALRTQLEGAQEQIRRLESEA 379
Cdd:pfam07926   3 LSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQqnyerelVLHAEDIKALQALREELNELKAEIAELKAEA 80
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
256-389 2.55e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.75  E-value: 2.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965694  256 LEEAARERDGLEQALRRRESEHEREVrALYEETEQLREQSRRPPSQNFARGERRSRLELELQSREQDLERAGLRQRELEQ 335
Cdd:COG4913   663 VASAEREIAELEAELERLDASSDDLA-ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAED 741

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767965694  336 ----QLHAQAAEHLEAQAQNSQLWRAHEALRTQLEGAQEQIRRLESEARGRQEQTQRD 389
Cdd:COG4913   742 larlELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNRE 799
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 231-401 2.98e-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: 43.52  E-value: 2.98e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965694   231 WARLQRERPELLGSFEDVLIRASAC---LEEAARERDGLEQALRRRESEHEREVRALyEETEQLREQSRRPPSQNFARG- 306
Cdd:TIGR02169  725 IEQLEQEEEKLKERLEELEEDLSSLeqeIENVKSELKELEARIEELEEDLHKLEEAL-NDLEARLSHSRIPEIQAELSKl 803

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965694   307 -ERRSRLELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQAQNSQLWRAHEALRTQLEGAQEQIRRLESEAR---GR 382
Cdd:TIGR02169  804 eEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRdleSR 883

                          170
                   ....*....|....*....
gi 767965694   383 QEQTQRDVvavsRNMQKEK 401
Cdd:TIGR02169  884 LGDLKKER----DELEAQL 898
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
223-377 3.63e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 3.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965694  223 RQRAVRTLWARLQRERpELLGSFEDVLIRASACLEEAARERDGLEQALRRRESEHEREVRALYEETEQLREQsRRPPSQN 302
Cdd:COG4913   286 AQRRLELLEAELEELR-AELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEE-RERRRAR 363

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767965694  303 FArgERRSRLELELQSREQDLERAglrQRELEQQLHAQAAEHLEAQAQNSQLWRAHEALRTQLEGAQEQIRRLES 377
Cdd:COG4913   364 LE--ALLAALGLPLPASAEEFAAL---RAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
Taxilin pfam09728
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ...
 317-371 8.72e-04

Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.


Pssm-ID: 462861 [Multi-domain]  Cd Length: 302  Bit Score: 41.09  E-value: 8.72e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767965694  317 QSREQDLERAgLRQRELEQQLH----AQAAEHLEAQAQNSQLWRAHEaLRTQLEGAQEQ 371
Cdd:pfam09728 148 ELRELHFEKL-LKTKELEVQLAeaklQQATEEEEKKAQEKEVAKARE-LKAQVQTLSET 204
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
240-388 9.68e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.82  E-value: 9.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965694  240 ELLGSFEDvLIRASACLEEAARERDGLEQAlrrreseherevRALYEETEQLREQsrrppsqnfargerrsRLELELQSR 319
Cdd:COG4913   229 ALVEHFDD-LERAHEALEDAREQIELLEPI------------RELAERYAAARER----------------LAELEYLRA 279

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767965694  320 EQDLERAGLRQRELEQQLHAQAAEHLEAQAQNSQLWRAHEALRTQLEGAQEQIR--------RLESEARGRQEQTQR 388
Cdd:COG4913   280 ALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRgnggdrleQLEREIERLERELEE 356
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 192-376 1.21e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 1.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965694 192 LDEEEEEEERFHTVLEQLGVAPVLGNSRPPSRQRAVRTLWARLQRERPELlgsfeDVLIRASACLEEAARERDGLEQALR 271
Cdd:COG1196  604 VASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEG-----EGGSAGGSLTGGSRRELLAALLEAE 678

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965694 272 RRESEHEREVRALYEETEQLREQSRRppsQNFARGERRSRLELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQAQN 351
Cdd:COG1196  679 AELEELAERLAEEELELEEALLAEEE---EERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEE 755

                        170       180
                 ....*....|....*....|....*
gi 767965694 352 SQLWRAHEALRTQLEGAQEQIRRLE 376
Cdd:COG1196  756 LPEPPDLEELERELERLEREIEALG 780
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 234-392 1.77e-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: 40.81  E-value: 1.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965694   234 LQRERPELLGSFEDVLIRASACLEEAARERDGLEQaLRRRESEHEREVRALYEETEQLREQSRRPPSQNFARGERRSRLE 313
Cdd:TIGR02168  808 LRAELTLLNEEAANLRERLESLERRIAATERRLED-LEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLE 886

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767965694   314 LELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQAQNSQlwraheaLRTQLEGAQEQIRRLESEARGRQEQTQRDVVA 392
Cdd:TIGR02168  887 EALALLRSELEELSEELRELESKRSELRRELEELREKLAQ-------LELRLEGLEVRIDNLQERLSEEYSLTLEEAEA 958
TIGR04376 TIGR04376
TIGR04376 family protein; Members of this protein family resemble TIGR04375 and, more ...
 289-388 1.98e-03

TIGR04376 family protein; Members of this protein family resemble TIGR04375 and, more distantly, to phage shock protein A (PspA). Members are restricted to the Cyanobacteria.


Pssm-ID: 275169  Cd Length: 189  Bit Score: 39.21  E-value: 1.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965694  289 EQLREQSrrppsqnfargERRSRLELELQSREQDLERAGLRQRELEQQLH--------------AQAAEHLEAQ--AQNS 352
Cdd:TIGR04376  31 EQLREQE-----------EDTLRLITDLQRQEKRLEDEILATAQEIQRWHeriekakaagrldlAEAAQEREAAllRQGN 99

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 767965694  353 QLWRAHEALRTQLEGAQE-----QIRRLESEARGRQEQTQR 388
Cdd:TIGR04376 100 QLWGQMQGLKERIQQSQEllrqiQQRRQEVQAKAAEAQAAQ 140
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 307-442 2.37e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 2.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965694 307 ERRSRLELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQAQNSQLWRAHEALRTQLEGAQEQIRR----LESEARGR 382
Cdd:COG1196  253 AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEleeeLAELEEEL 332

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965694 383 QEQTQRDVVAVSRNMQKEKVSLLRQLELLRELNTRLRDDRDACEARRAGSSCRKALTTAR 442
Cdd:COG1196  333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
256-392 2.42e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.27  E-value: 2.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965694 256 LEEAARERDGLEQALRrreseherevrALYEETEQLREQSRRPPSQNFARGERRSRLELELQSREQDLERAGLRQRELEQ 335
Cdd:COG4372   54 LEQAREELEQLEEELE-----------QARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQK 122

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767965694 336 QLHAQAAEHLEAQAQNSQLWRAH-------EALRTQLEGAQEQIRRLESEARGRQEQTQRDVVA 392
Cdd:COG4372  123 ERQDLEQQRKQLEAQIAELQSEIaereeelKELEEQLESLQEELAALEQELQALSEAEAEQALD 186
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 312-385 4.04e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.92  E-value: 4.04e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767965694 312 LELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQAQNSQLWRAHEALRTQLEGAQEQIRRLESEARGRQEQ 385
Cdd:COG1196  216 RELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAE 289
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 307-398 5.31e-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: 5.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965694 307 ERRSRLELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQAQNSQLWRAHEALRTQLEGAQEQIRRLESEARGRQEQT 386
Cdd:COG4942   27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106

                         90
                 ....*....|..
gi 767965694 387 QRDVVAVSRNMQ 398
Cdd:COG4942  107 AELLRALYRLGR 118
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
256-442 5.49e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.51  E-value: 5.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965694  256 LEEAARERDGLEQALRRRESEHEREVrALYEETEQLREQSRRPPSQNFARGERRSrLELELQSREQDLERagLRQ----- 330
Cdd:COG4913   612 LAALEAELAELEEELAEAEERLEALE-AELDALQERREALQRLAEYSWDEIDVAS-AEREIAELEAELER--LDAssddl 687

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965694  331 RELEQQLHAQAAEHLEAQAQNSQLWRAhealRTQLEGAQEQIRRLESEARGRQEQTQRDVVAVSRNMQKEKVSLLRQLEL 410
Cdd:COG4913   688 AALEEQLEELEAELEELEEELDELKGE----IGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAV 763

                         170       180       190
                  ....*....|....*....|....*....|..
gi 767965694  411 LRELNTRLRDDRDACEARRAGssCRKALTTAR 442
Cdd:COG4913   764 ERELRENLEERIDALRARLNR--AEEELERAM 793
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
233-388 5.52e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.25  E-value: 5.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965694 233 RLQRERPELLGS--FEDVLIRA-SACLEEAARERDGLEQALRRRESEHErevrALYEETEQLREQSRRPPSQNFARGERR 309
Cdd:PRK02224 290 ELEEERDDLLAEagLDDADAEAvEARREELEDRDEELRDRLEECRVAAQ----AHNEEAESLREDADDLEERAEELREEA 365

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965694 310 SRLELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQAQNSQLWRAHEALRTQLEGAQEQIRRLE---SEARGRQEQT 386
Cdd:PRK02224 366 AELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEatlRTARERVEEA 445


                 ..
gi 767965694 387 QR 388
Cdd:PRK02224 446 EA 447
PTZ00121 PTZ00121
MAEBL; Provisional
 240-437 7.56e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.97  E-value: 7.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965694  240 ELLGSFEDVLIRASACLEEAARERDGLEQALRRRESEHEREVRALYEETEQLR-EQSRRPPSQNFARGERRsrleLELQS 318
Cdd:PTZ00121 1095 EAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKaEDAKRVEIARKAEDARK----AEEAR 1170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965694  319 REQDLERA-----GLRQRELEQQLHAQAAEHLEAQAQNSQLWRAHEALRTQLEGAQEQIRRLEsEARGRQEQTQRDVVAV 393
Cdd:PTZ00121 1171 KAEDAKKAeaarkAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAE-EAKKDAEEAKKAEEER 1249

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 767965694  394 SRNMQKEKVSLLRQLELLRELNTRLRDDRDACEARRAgSSCRKA 437
Cdd:PTZ00121 1250 NNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKA-EEKKKA 1292
UPF0242 pfam06785
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ...
 284-380 7.70e-03

Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal transmembrane region and a C-terminal coiled-coil.


Pssm-ID: 429117 [Multi-domain]  Cd Length: 194  Bit Score: 37.49  E-value: 7.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965694  284 LYEETEQLREQSRRPPSQ---NFA--------RGERRSRLELELQSREQDLERAGLRQRELEQQLHA----------QAA 342
Cdd:pfam06785  63 EKFEKSFLEEKEAKLTELdaeGFKileetleeLQSEEERLEEELSQKEEELRRLTEENQQLQIQLQQisqdfaefrlESE 142

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 767965694  343 EHLEAQAQNSQLWRAH-EALRTQLEGAQEQIRRLESEAR 380
Cdd:pfam06785 143 EQLAEKQLLINEYQQTiEEQRSVLEKRQDQIENLESKVR 181
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 244-430 8.20e-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: 38.90  E-value: 8.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965694   244 SFEDVLIRASACLEEAARERDGLEQALRRRESEHEREVRALYEETEQLREQSRrppsqnfargeRRSRLELELQSREQDL 323
Cdd:TIGR02169  671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEK-----------EIEQLEQEEEKLKERL 739

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965694   324 ERAGLRQRELEQQLHAQAAEHLEAQAQNSQLWRAHEALRTQLEG-----AQEQIRRLESEARgRQEQTQRDVVAVSRNMQ 398
Cdd:TIGR02169  740 EELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDlearlSHSRIPEIQAELS-KLEEEVSRIEARLREIE 818

                          170       180       190
                   ....*....|....*....|....*....|..
gi 767965694   399 KEKVSLLRQLELLRELNTRLRDDRDACEARRA 430
Cdd:TIGR02169  819 QKLNRLTLEKEYLEKEIQELQEQRIDLKEQIK 850
PRK12705 PRK12705
hypothetical protein; Provisional
 251-403 8.50e-03

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 38.54  E-value: 8.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965694 251 RASACLEEAARE-RDGLEQALRRRESEHEREVRALYEETEQLREQSRRPPSQNF-------ARGERRSRLELELQSREQD 322
Cdd:PRK12705  34 EAERILQEAQKEaEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVqkeeqldARAEKLDNLENQLEEREKA 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965694 323 LERA----GLRQRELEQQLhaQAAEHLEAQAQNSQLWRAHEAlRTQLEGAQEqIRRLESEARGRQEQTQRDVVAVSRNMQ 398
Cdd:PRK12705 114 LSARelelEELEKQLDNEL--YRVAGLTPEQARKLLLKLLDA-ELEEEKAQR-VKKIEEEADLEAERKAQNILAQAMQRI 189


                 ....*
gi 767965694 399 KEKVS 403
Cdd:PRK12705 190 ASETA 194
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 206-385 8.99e-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: 8.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965694 206 LEQLGVAPVLGNSRPPSRQRAVRTLWARLQRERPELLGSFEDVL---IRASACLEEAARERDGLEQALRRRESEHEREVR 282
Cdd:COG1196  579 LDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLlgrTLVAARLEAALRRAVTLAGRLREVTLEGEGGSA 658

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965694 283 ALYEETEQLREQSRRPpsqnfargERRSRLELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQAQNSQLwraHEALR 362
Cdd:COG1196  659 GGSLTGGSRRELLAAL--------LEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELE---EEALE 727

                        170       180
                 ....*....|....*....|...
gi 767965694 363 TQLEGAQEQIRRLESEARGRQEQ 385
Cdd:COG1196  728 EQLEAEREELLEELLEEEELLEE 750
 
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