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Conserved domains on  [gi|767965678|ref|XP_011518313|]
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EF-hand calcium-binding domain-containing protein 4A isoform X7 [Homo sapiens]

Protein Classification

Graphical summary

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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]; ...
 223-388 2.01e-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: 56.87  E-value: 2.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965678 223 RQRAVRTLwARLQRERPEL---LGSFEDVLIRASACLEEAARERDGLEQALRRRESEHEREVRALYE---ETEQLREQSR 296
Cdd:COG1196  311 RRELEERL-EELEEELAELeeeLEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEaeeELEELAEELL 389

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965678 297 RPPSQNFARGERRSRLELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQAQNSQLWRAHEALRTQLEGAQEQIRRLE 376
Cdd:COG1196  390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469

                        170
                 ....*....|..
gi 767965678 377 SEARGRQEQTQR 388
Cdd:COG1196  470 EEAALLEAALAE 481
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 223-388 2.01e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.87  E-value: 2.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965678 223 RQRAVRTLwARLQRERPEL---LGSFEDVLIRASACLEEAARERDGLEQALRRRESEHEREVRALYE---ETEQLREQSR 296
Cdd:COG1196  311 RRELEERL-EELEEELAELeeeLEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEaeeELEELAEELL 389

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965678 297 RPPSQNFARGERRSRLELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQAQNSQLWRAHEALRTQLEGAQEQIRRLE 376
Cdd:COG1196  390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469

                        170
                 ....*....|..
gi 767965678 377 SEARGRQEQTQR 388
Cdd:COG1196  470 EEAALLEAALAE 481
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 223-388 1.71e-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: 50.83  E-value: 1.71e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965678   223 RQRAVRTLWARLQRERPELLG---SFEDVLIRASACLEEAARERDGLEQALRrreseherevrALYEETEQLREQSRRPP 299
Cdd:TIGR02168  741 EVEQLEERIAQLSKELTELEAeieELEERLEEAEEELAEAEAEIEELEAQIE-----------QLKEELKALREALDELR 809

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965678   300 SQNFARGERRSRLELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQAQNSQLWRAHEALRTQLEGAQEQIRRLE--- 376
Cdd:TIGR02168  810 AELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEeal 889

                          170
                   ....*....|..
gi 767965678   377 SEARGRQEQTQR 388
Cdd:TIGR02168  890 ALLRSELEELSE 901
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
 309-379 1.56e-05

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: 44.55  E-value: 1.56e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767965678  309 RSRLELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQ-------AQNSQLWRAHEALRTQLEGAQEQIRRLESEA 379
Cdd:pfam07926   3 LSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQqnyerelVLHAEDIKALQALREELNELKAEIAELKAEA 80
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
225-393 4.59e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.72  E-value: 4.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965678 225 RAVRTLWARLQR---ERPELLGS--FEDVLIRA-SACLEEAARERDGLEQALRRRESEHErevrALYEETEQLREQSRRP 298
Cdd:PRK02224 279 EEVRDLRERLEEleeERDDLLAEagLDDADAEAvEARREELEDRDEELRDRLEECRVAAQ----AHNEEAESLREDADDL 354

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965678 299 PSQNFARGERRSRLELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQAQNSQLWRAHEALRTQLEGAQEQIRRLE-- 376
Cdd:PRK02224 355 EERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEat 434

                        170
                 ....*....|....*...
gi 767965678 377 -SEARGRQEQTQRCRGTG 393
Cdd:PRK02224 435 lRTARERVEEAEALLEAG 452
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 312-380 1.45e-03

Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.


Pssm-ID: 439196 [Multi-domain]  Cd Length: 91  Bit Score: 37.93  E-value: 1.45e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767965678 312 LELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQAQNSQLWRAHEALRTQLEGAQEQIRRLESEAR 380
Cdd:cd22887    2 LESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEEND 70
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 223-388 2.01e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.87  E-value: 2.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965678 223 RQRAVRTLwARLQRERPEL---LGSFEDVLIRASACLEEAARERDGLEQALRRRESEHEREVRALYE---ETEQLREQSR 296
Cdd:COG1196  311 RRELEERL-EELEEELAELeeeLEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEaeeELEELAEELL 389

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965678 297 RPPSQNFARGERRSRLELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQAQNSQLWRAHEALRTQLEGAQEQIRRLE 376
Cdd:COG1196  390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469

                        170
                 ....*....|..
gi 767965678 377 SEARGRQEQTQR 388
Cdd:COG1196  470 EEAALLEAALAE 481
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
232-390 2.15e-08

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 56.06  E-value: 2.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965678 232 ARLQRERPEL--LGSFEDVLIRA-SACLEEAARERDGLEQALRrreseherevrALYEETEQLREQSRRPPSQNFARGER 308
Cdd:COG4372    6 EKVGKARLSLfgLRPKTGILIAAlSEQLRKALFELDKLQEELE-----------QLREELEQAREELEQLEEELEQARSE 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965678 309 RSRLELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQAQNSQLWRAHEALRTQLEGAQEQIRRLESEARGRQEQTQR 388
Cdd:COG4372   75 LEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKE 154


                 ..
gi 767965678 389 CR 390
Cdd:COG4372  155 LE 156
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 225-390 2.88e-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: 2.88e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965678 225 RAVRTLWARLQRERPELlgsfEDVLIRASACLEEAARERDGLEQALRRRESEHEREVRALYEETEQLREQSRRppsqnfa 304
Cdd:COG1196  235 RELEAELEELEAELEEL----EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD------- 303

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965678 305 rgerRSRLELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQAQNSQLWRAHEALRTQLEGAQEQIRRLESEARGRQE 384
Cdd:COG1196  304 ----IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379


                 ....*.
gi 767965678 385 QTQRCR 390
Cdd:COG1196  380 ELEELA 385
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 232-385 1.04e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.56  E-value: 1.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965678 232 ARLQRERPELLGSfEDVLIRASACLEEAARERDGLEQALRRRESEHEREVRALYEETEQLREQSRrppsQNFARGERRSR 311
Cdd:COG1196  344 EELEEAEEELEEA-EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE----AEEALLERLER 418

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767965678 312 LELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQAQNSQLWRAHEALRTQLEGAQEQIRRLESEARGRQEQ 385
Cdd:COG1196  419 LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR 492
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
231-388 2.18e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 53.23  E-value: 2.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965678 231 WARLQRERPELlgsfEDVLIRASACLEEAARERDGLEQALRRReseherevrALYEETEQLREQSRRPPSQ---NFARGE 307
Cdd:COG4717   90 YAELQEELEEL----EEELEELEAELEELREELEKLEKLLQLL---------PLYQELEALEAELAELPERleeLEERLE 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965678 308 RRSRLELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQAQN-SQLWRAHEALRTQLEGAQEQIRRLESEARGRQEQT 386
Cdd:COG4717  157 ELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEElEELQQRLAELEEELEEAQEELEELEEELEQLENEL 236


                 ..
gi 767965678 387 QR 388
Cdd:COG4717  237 EA 238
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 223-388 1.71e-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: 50.83  E-value: 1.71e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965678   223 RQRAVRTLWARLQRERPELLG---SFEDVLIRASACLEEAARERDGLEQALRrreseherevrALYEETEQLREQSRRPP 299
Cdd:TIGR02168  741 EVEQLEERIAQLSKELTELEAeieELEERLEEAEEELAEAEAEIEELEAQIE-----------QLKEELKALREALDELR 809

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965678   300 SQNFARGERRSRLELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQAQNSQLWRAHEALRTQLEGAQEQIRRLE--- 376
Cdd:TIGR02168  810 AELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEeal 889

                          170
                   ....*....|..
gi 767965678   377 SEARGRQEQTQR 388
Cdd:TIGR02168  890 ALLRSELEELSE 901
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
256-390 4.00e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.53  E-value: 4.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965678  256 LEEAARERDGLEQALRrreseherevrALYEETEQLREQSRrppsQNFARGERRSRLElELQSREQDLERAGLRQRELEQ 335
Cdd:COG4913   612 LAALEAELAELEEELA-----------EAEERLEALEAELD----ALQERREALQRLA-EYSWDEIDVASAEREIAELEA 675

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965678  336 QLHA-----QAAEHLEAQAQnsQLWRAHEALRTQLEGAQEQIRRLESEARGRQEQTQRCR 390
Cdd:COG4913   676 ELERldassDDLAALEEQLE--ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQ 733
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 222-388 5.92e-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: 48.90  E-value: 5.92e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965678   222 SRQRAVRTLWARLQRerpellgsFEDVLIRASACLEEAARERDGLEQA---LRRRESEHEREVRALYEETEQLREQSRRP 298
Cdd:TIGR02168  674 ERRREIEELEEKIEE--------LEEKIAELEKALAELRKELEELEEEleqLRKELEELSRQISALRKDLARLEAEVEQL 745

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965678   299 PSQNFARGERRSRLELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQAQNSQLWRAHEALRTQL----EGAQEQIRR 374
Cdd:TIGR02168  746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELtllnEEAANLRER 825

                          170
                   ....*....|....
gi 767965678   375 LESEARGRQEQTQR 388
Cdd:TIGR02168  826 LESLERRIAATERR 839
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
 309-379 1.56e-05

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: 44.55  E-value: 1.56e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767965678  309 RSRLELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQ-------AQNSQLWRAHEALRTQLEGAQEQIRRLESEA 379
Cdd:pfam07926   3 LSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQqnyerelVLHAEDIKALQALREELNELKAEIAELKAEA 80
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 223-391 2.34e-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: 2.34e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965678   223 RQRAVRTLWARLQRERPELLGSFEDV---LIRASACLEEAARERDGLEQALRRRESEHEREVRALYEETEQLREQSRRpp 299
Cdd:TIGR02168  310 RLANLERQLEELEAQLEELESKLDELaeeLAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK-- 387

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965678   300 sqNFARGERRSRLELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQAQNSQ------------LWRAHEALRTQLEG 367
Cdd:TIGR02168  388 --VAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQaeleeleeeleeLQEELERLEEALEE 465

                          170       180
                   ....*....|....*....|....
gi 767965678   368 AQEQIRRLESEARGRQEQTQRCRG 391
Cdd:TIGR02168  466 LREELEEAEQALDAAERELAQLQA 489
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 222-388 2.85e-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: 2.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965678 222 SRQRAVRTLWARLQRERpELLGSFEDVLIRASACLEEAARERDGLEQALRRRESEHEREVRALYEETEQLREQSRrppsQ 301
Cdd:COG1196  257 ELEAELAELEAELEELR-LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE----E 331

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965678 302 NFARGERRSRLELELQSREQDLERAglrQRELEQ---QLHAQAAEHLEAQAQNSQLWRAHEALRTQLEGAQEQIRRLESE 378
Cdd:COG1196  332 LEELEEELEELEEELEEAEEELEEA---EAELAEaeeALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408

                        170
                 ....*....|
gi 767965678 379 ARGRQEQTQR 388
Cdd:COG1196  409 EEALLERLER 418
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
240-390 3.33e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.45  E-value: 3.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965678  240 ELLGSFEDvLIRASACLEEAARERDGLEQAlrrreseherevRALYEETEQLREQsrrppsqnfargerrsRLELELQSR 319
Cdd:COG4913   229 ALVEHFDD-LERAHEALEDAREQIELLEPI------------RELAERYAAARER----------------LAELEYLRA 279

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767965678  320 EQDLERAGLRQRELEQQLHAQAAEHLEAQAQNSQLWRAHEALRTQLEGAQEQIR--------RLESEARGRQEQTQRCR 390
Cdd:COG4913   280 ALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRgnggdrleQLEREIERLERELEERE 358
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
286-390 3.47e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 46.30  E-value: 3.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965678 286 EETEQLREQSRRPPSQNfargERRSRLELELQSREQDLERAGLRQRELEQQLhaqaaEHLEAQAQNSQLWRAHEALRTQL 365
Cdd:COG4717   71 KELKELEEELKEAEEKE----EEYAELQEELEELEEELEELEAELEELREEL-----EKLEKLLQLLPLYQELEALEAEL 141

                         90       100
                 ....*....|....*....|....*
gi 767965678 366 EGAQEQIRRLESEARGRQEQTQRCR 390
Cdd:COG4717  142 AELPERLEELEERLEELRELEEELE 166
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
223-378 4.99e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.06  E-value: 4.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965678  223 RQRAVRTLWARLQRERpELLGSFEDVLIRASACLEEAARERDGLEQALRRREseherevralYEETEQLREQSRRppsqn 302
Cdd:COG4913   286 AQRRLELLEAELEELR-AELARLEAELERLEARLDALREELDELEAQIRGNG----------GDRLEQLEREIER----- 349

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965678  303 faRGERRSRLELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQAQNSQLWRAHE----ALRTQLEGAQEQIRRLESE 378
Cdd:COG4913   350 --LERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEealaEAEAALRDLRRELRELEAE 427
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
249-390 5.21e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.06  E-value: 5.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965678  249 LIRASACLEEAARERDGLEQALRRRESEHEREVRALYEETEQLREQSrrppsqnfarGERRSRLELELQSREQDLERAGL 328
Cdd:COG4913   290 LELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNG----------GDRLEQLEREIERLERELEERER 359

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767965678  329 RQRELEQQ---LHAQAAEHLEAQAQNSQLWRAH-EALRTQLEGAQEQIRRLESEARGRQEQTQRCR 390
Cdd:COG4913   360 RRARLEALlaaLGLPLPASAEEFAALRAEAAALlEALEEELEALEEALAEAEAALRDLRRELRELE 425
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
256-385 9.18e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.29  E-value: 9.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965678  256 LEEAARERDGLEQALRRRESEHEREVrALYEETEQLREQSRRPPSQNFARGERRSRLELELQSREQDLERAGLRQRELEQ 335
Cdd:COG4913   663 VASAEREIAELEAELERLDASSDDLA-ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAED 741

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767965678  336 ----QLHAQAAEHLEAQAQNSQLWRAHEALRTQLEGAQEQIRRLESEARGRQEQ 385
Cdd:COG4913   742 larlELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRA 795
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 231-380 9.19e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 45.06  E-value: 9.19e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965678   231 WARLQRERPELLGSFEDVLIRASAC---LEEAARERDGLEQALRRRESEHEREVRALyEETEQLREQSRRPPSQNFARG- 306
Cdd:TIGR02169  725 IEQLEQEEEKLKERLEELEEDLSSLeqeIENVKSELKELEARIEELEEDLHKLEEAL-NDLEARLSHSRIPEIQAELSKl 803

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767965678   307 -ERRSRLELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQAQNSQLWRAHEALRTQLEGAQEQIRRLESEAR 380
Cdd:TIGR02169  804 eEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALR 878
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 257-388 2.72e-04

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 40.67  E-value: 2.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965678  257 EEAARERDGLEQALRRreseherevraLYEETEQLREQSRRppSQNFARG--ERRSRLELE---LQSREQDLERAglrQR 331
Cdd:pfam20492   2 EEAEREKQELEERLKQ-----------YEEETKKAQEELEE--SEETAEEleEERRQAEEEaerLEQKRQEAEEE---KE 65

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767965678  332 ELEQQLHAQAAEhleaqaqnsqlwraHEALRTQLEGAQEQIRRLESEARGRQEQTQR 388
Cdd:pfam20492  66 RLEESAEMEAEE--------------KEQLEAELAEAQEEIARLEEEVERKEEEARR 108
TIGR04376 TIGR04376
TIGR04376 family protein; Members of this protein family resemble TIGR04375 and, more ...
 289-388 2.87e-04

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: 41.90  E-value: 2.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965678  289 EQLREQSrrppsqnfargERRSRLELELQSREQDLERAGLRQRELEQQLH--------------AQAAEHLEAQ--AQNS 352
Cdd:TIGR04376  31 EQLREQE-----------EDTLRLITDLQRQEKRLEDEILATAQEIQRWHeriekakaagrldlAEAAQEREAAllRQGN 99

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 767965678  353 QLWRAHEALRTQLEGAQE-----QIRRLESEARGRQEQTQR 388
Cdd:TIGR04376 100 QLWGQMQGLKERIQQSQEllrqiQQRRQEVQAKAAEAQAAQ 140
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 192-376 4.00e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 4.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965678 192 LDEEEEEEERFHTVLEQLGVAPVLGNSRPPSRQRAVRTLWARLQRERPELlgsfeDVLIRASACLEEAARERDGLEQALR 271
Cdd:COG1196  604 VASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEG-----EGGSAGGSLTGGSRRELLAALLEAE 678

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965678 272 RRESEHEREVRALYEETEQLREQSRRppsQNFARGERRSRLELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQAQN 351
Cdd:COG1196  679 AELEELAERLAEEELELEEALLAEEE---EERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEE 755

                        170       180
                 ....*....|....*....|....*
gi 767965678 352 SQLWRAHEALRTQLEGAQEQIRRLE 376
Cdd:COG1196  756 LPEPPDLEELERELERLEREIEALG 780
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
225-393 4.59e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.72  E-value: 4.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965678 225 RAVRTLWARLQR---ERPELLGS--FEDVLIRA-SACLEEAARERDGLEQALRRRESEHErevrALYEETEQLREQSRRP 298
Cdd:PRK02224 279 EEVRDLRERLEEleeERDDLLAEagLDDADAEAvEARREELEDRDEELRDRLEECRVAAQ----AHNEEAESLREDADDL 354

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965678 299 PSQNFARGERRSRLELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQAQNSQLWRAHEALRTQLEGAQEQIRRLE-- 376
Cdd:PRK02224 355 EERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEat 434

                        170
                 ....*....|....*...
gi 767965678 377 -SEARGRQEQTQRCRGTG 393
Cdd:PRK02224 435 lRTARERVEEAEALLEAG 452
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
256-385 5.35e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.20  E-value: 5.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965678 256 LEEAARERDGLEQALRRRESEHEREVRALYEETEQLRE-QSRRPPSQNF--ARGERRSRLELELQSREQDLERAGLRQRE 332
Cdd:COG4372   54 LEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAaQAELAQAQEEleSLQEEAEELQEELEELQKERQDLEQQRKQ 133

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767965678 333 LEQQLHAQAAEHLEAQAQNSQlwraheaLRTQLEGAQEQIRRLESEARGRQEQ 385
Cdd:COG4372  134 LEAQIAELQSEIAEREEELKE-------LEEQLESLQEELAALEQELQALSEA 179
MscS_porin pfam12795
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...
 286-388 6.01e-04

Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.


Pssm-ID: 432790 [Multi-domain]  Cd Length: 238  Bit Score: 41.52  E-value: 6.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965678  286 EETEQLREQSRRPPSQnfARGERRSRLELELQSREQDLER-AGLRQRELEQQLHAQAAEHLEAQAQNSQLWRAHEALRTQ 364
Cdd:pfam12795  37 QRAAAYQKALDDAPAE--LRELRQELAALQAKAEAAPKEIlASLSLEELEQRLLQTSAQLQELQNQLAQLNSQLIELQTR 114

                          90       100
                  ....*....|....*....|....
gi 767965678  365 LEGAQEQIrrleSEARGRQEQTQR 388
Cdd:pfam12795 115 PERAQQQL----SEARQRLQQIRN 134
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
256-380 6.26e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.81  E-value: 6.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965678 256 LEEAARERDGLEQALRRRESEHErevrALYEETEQLREQSRRPPSQNFARGERRSRLELELQSREQDLERAGLRQRELEQ 335
Cdd:COG4372  103 LESLQEEAEELQEELEELQKERQ----DLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSE 178

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 767965678 336 QLHAQAAEHLEAQAQNSQLWRAHEALRTQLEGAQEQIRRLESEAR 380
Cdd:COG4372  179 AEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEA 223
Taxilin pfam09728
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ...
 317-371 6.96e-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: 41.48  E-value: 6.96e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767965678  317 QSREQDLERAgLRQRELEQQLH----AQAAEHLEAQAQNSQLWRAHEaLRTQLEGAQEQ 371
Cdd:pfam09728 148 ELRELHFEKL-LKTKELEVQLAeaklQQATEEEEKKAQEKEVAKARE-LKAQVQTLSET 204
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 312-380 1.45e-03

Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.


Pssm-ID: 439196 [Multi-domain]  Cd Length: 91  Bit Score: 37.93  E-value: 1.45e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767965678 312 LELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQAQNSQLWRAHEALRTQLEGAQEQIRRLESEAR 380
Cdd:cd22887    2 LESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEEND 70
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 289-388 1.60e-03

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: 1.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965678 289 EQLREQSRRppsqnfAR-----GERRSRLELELQSREqdLERAGLRQRELEQQLHAQAAEHLEAQAQNSQLWRAHEALRT 363
Cdd:COG1196  203 EPLERQAEK------AEryrelKEELKELEAELLLLK--LRELEAELEELEAELEELEAELEELEAELAELEAELEELRL 274

                         90       100
                 ....*....|....*....|....*...
gi 767965678 364 QLEGAQEQIRRL---ESEARGRQEQTQR 388
Cdd:COG1196  275 ELEELELELEEAqaeEYELLAELARLEQ 302
UPF0242 pfam06785
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ...
 284-380 1.73e-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: 39.42  E-value: 1.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965678  284 LYEETEQLREQSRRPPSQ---NFA--------RGERRSRLELELQSREQDLERAGLRQRELEQQLHA----------QAA 342
Cdd:pfam06785  63 EKFEKSFLEEKEAKLTELdaeGFKileetleeLQSEEERLEEELSQKEEELRRLTEENQQLQIQLQQisqdfaefrlESE 142

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 767965678  343 EHLEAQAQNSQLWRAH-EALRTQLEGAQEQIRRLESEAR 380
Cdd:pfam06785 143 EQLAEKQLLINEYQQTiEEQRSVLEKRQDQIENLESKVR 181
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
285-390 2.42e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 2.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965678 285 YEETEQLREQSRRPPSQNFARGERRSRLELELQSREQDLERAGLRQRELEQ--QLHAQAAEHLEAQAQNSQL---WRAHE 359
Cdd:COG4717   73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAELAELperLEELE 152

                         90       100       110
                 ....*....|....*....|....*....|.
gi 767965678 360 ALRTQLEGAQEQIRRLESEARGRQEQTQRCR 390
Cdd:COG4717  153 ERLEELRELEEELEELEAELAELQEELEELL 183
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
205-374 4.13e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 4.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965678 205 VLEQLGVAPVLGNSRPP---SRQRAVRTLWARL-----QRERPELLGSFEDVLIRASACLEEAARERDGLEQALRRRESE 276
Cdd:COG4717  324 LLAALGLPPDLSPEELLellDRIEELQELLREAeeleeELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEE 403

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965678 277 HEREVRALYEETEQLREQSRRPPSQNFArgERRSRLELELQSREQDLERAGLRQRELEQQLHA-----------QAAEHL 345
Cdd:COG4717  404 LEELEEQLEELLGELEELLEALDEEELE--EELEELEEELEELEEELEELREELAELEAELEQleedgelaellQELEEL 481

                        170       180       190
                 ....*....|....*....|....*....|
gi 767965678 346 EAQ-AQNSQLWRAHEALRTQLEGAQEQIRR 374
Cdd:COG4717  482 KAElRELAEEWAALKLALELLEEAREEYRE 511
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 222-388 5.71e-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: 39.27  E-value: 5.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965678   222 SRQRAVRTLWARLQRERPELlgsfEDVLIRASACLEEAARERDGLEQALRRRESEHEREVRALYEETEQLREQSRRPPSQ 301
Cdd:TIGR02168  260 AELQELEEKLEELRLEVSEL----EEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDEL 335

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965678   302 NF---ARGERRSRLELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQAQNSQLWRAHEALRTQLEGAQEQIRRLESE 378
Cdd:TIGR02168  336 AEelaELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDR 415

                          170
                   ....*....|
gi 767965678   379 aRGRQEQTQR 388
Cdd:TIGR02168  416 -RERLQQEIE 424
Nuf2_DHR10-like pfam18595
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ...
 307-388 6.27e-03

Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This domain was identified as MazG related domain also designated as Designed helical repeat protein 10 (DHR10) that actually adopts a coiled-coil structure. Nuf2 is part of the Ndc80 complex, which binds to the spindle and is required for chromosome segregation and spindle checkpoint activity.


Pssm-ID: 465814 [Multi-domain]  Cd Length: 117  Bit Score: 36.41  E-value: 6.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965678  307 ERRSRlelELQSR-------EQDLERAG----------LRQRELEQQLHAQAAEHLEAQAQNSQLWRAHEALRTQLEGAQ 369
Cdd:pfam18595  15 ERKAR---ELQAKidalqvvEKDLRSCIklleeieaelAKLEEAKKKLKELRDALEEKEIELRELERREERLQRQLENAQ 91

                          90
                  ....*....|....*....
gi 767965678  370 EQIRRLESEARGRQEQTQR 388
Cdd:pfam18595  92 EKLERLREQAEEKREAAQA 110
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 314-388 6.32e-03

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: 38.37  E-value: 6.32e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767965678 314 LELQSREQDLERAGLRQRELEQQLhaqaaEHLEAQAQNSQlwRAHEALRTQLEGAQEQIRRLESEARGRQEQTQR 388
Cdd:COG1579   10 LDLQELDSELDRLEHRLKELPAEL-----AELEDELAALE--ARLEAAKTELEDLEKEIKRLELEIEEVEARIKK 77
PRK09039 PRK09039
peptidoglycan -binding protein;
309-387 6.53e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 38.79  E-value: 6.53e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767965678 309 RSRLELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQAQNSQLWRAHEALRTQLEGAQEQIRrlESEARGRQEQTQ 387
Cdd:PRK09039  97 RSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVSARALAQVELLNQQIAALRRQLAALEAALD--ASEKRDRESQAK 173
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 232-385 7.64e-03

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: 37.98  E-value: 7.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965678 232 ARLQRERPELLGSFEDVLIRASACLEEAARERDGLEQALRRREseherevrALYEETEQLREQSRRppSQNFARGERrsr 311
Cdd:COG1579   23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLE--------LEIEEVEARIKKYEE--QLGNVRNNK--- 89

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767965678 312 lelELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQAQNSQLWRAHEALRTQLEGAQEQIRRLESEARGRQEQ 385
Cdd:COG1579   90 ---EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEE 160
MscS_porin pfam12795
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...
 266-385 7.91e-03

Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.


Pssm-ID: 432790 [Multi-domain]  Cd Length: 238  Bit Score: 38.05  E-value: 7.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965678  266 LEQALRRRESEHEREVRALYEETEQLREQSRRP---PSQNFARGERRSRLELELQS---REQDLERAGLRQRELEQQLHA 339
Cdd:pfam12795  83 LEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPeraQQQLSEARQRLQQIRNRLNGpapPGEPLSEAQRWALQAELAALK 162

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 767965678  340 QAAEHLE-AQAQNSQLWrahEALRTQLEGAQEQIRRLESEARGRQEQ 385
Cdd:pfam12795 163 AQIDMLEqELLSNNNRQ---DLLKARRDLLTLRIQRLEQQLQALQEL 206
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 222-384 9.89e-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: 38.50  E-value: 9.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965678   222 SRQRAVRTLWARLQRERPELLGSFEDVLIRASAC---LEEAARERDGLEQALRRRESEHEREVRALYEETEQLREQSRRP 298
Cdd:TIGR02168  803 EALDELRAELTLLNEEAANLRERLESLERRIAATerrLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNER 882

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965678   299 PSQNFARGERRSRLElELQSREQDLERaglRQRELEQQLHAQAAEhleaqaqnsqlwraHEALRTQLEGAQEQIRRLESE 378
Cdd:TIGR02168  883 ASLEEALALLRSELE-ELSEELRELES---KRSELRRELEELREK--------------LAQLELRLEGLEVRIDNLQER 944


                   ....*.
gi 767965678   379 ARGRQE 384
Cdd:TIGR02168  945 LSEEYS 950
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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