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Conserved domains on  [gi|296452938|sp|Q9ULS5|]
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RecName: Full=Transmembrane and coiled-coil domain protein 3

Protein Classification

transmembrane and coiled-coil domain protein( domain architecture ID 11186040)

transmembrane and coiled-coil domain protein may be involved in the regulation of the proteolytic processing of the amyloid precursor protein (APP) possibly also implicating APOE

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Tmemb_cc2 pfam10267
Predicted transmembrane and coiled-coil 2 protein; This family of transmembrane coiled-coil ...
 64-463 0e+00

Predicted transmembrane and coiled-coil 2 protein; This family of transmembrane coiled-coil containing proteins is conserved from worms to humans. Its function is unknown.


:

Pssm-ID: 463036  Cd Length: 401  Bit Score: 598.94  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296452938   64 VKLTADSLKQKILKVTEQIKIEQTSRDGNVAEYLKLVNNADKQQAGRIKQVFEKKNQKSAHSIAQLQKKLEQYHRKLREI 143
Cdd:pfam10267   1 SRAAIEHLQQKILKIKEQIKIEQTARDENVAEYLKLANNADKQQLARIKQVFEKKNQKSAQNIAQLQKKLEQYHRRLKEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296452938  144 E---QNGASRSSKdiSKDHLKDIHRSLKDahvksrtaphCMESSKSGMPGVSLTPPVFVFNKSREFANLIRNKFGSADNI 220
Cdd:pfam10267  81 EngeQSSVTSHRQ--PKEVLRDVGQGLRD----------VGGNIRDGISGLSGGPPPTVFSKPREFAHLIKNKFGSADNI 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296452938  221 AHLKNSLEEFRPEASARAYGGS-ATIVNKPKYGSDDECSSGT--SGSADSNGNQSFGA----GGASTLDSQGKLAVILEE 293
Cdd:pfam10267 149 NSLKSSLETSHDEGGGRKLSGStFSTVTKPKYPSDDECSSSSveSISAGSNGNPPPHGadngGQQAESDSQNGLAAILEE 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296452938  294 LREIKDTQAQLAEDIEALKVQFKREYGFISQTLQEERYRYERLEDQLHDLTDLHQHETANLKQELASIEEKVAYQAYERS 373
Cdd:pfam10267 229 LQEIKEAQVQLEEKLERLKTQFKKEYKFLTQALQEERYRYERLEEQLNDLTELHQNEIANLKQELASMEEKVAYQSYERA 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296452938  374 RDIQEALESCQTRISKLELHQQEQQALQTDTV---NAKVLLGRCINVILAFMTVILVCVSTIAKFVSPMMKSRCHILGTF 450
Cdd:pfam10267 309 RDIQEALESCQTRISKMELQQQQQQLVQLEGLenaNARALLGKLINIVLAILTVILVLVSTAAKFVAPLLKTRLRILTTI 388

                         410
                  ....*....|...
gi 296452938  451 FAVTLLAIFCKNW 463
Cdd:pfam10267 389 LLVLLLIIFWKNW 401
 
Name Accession Description Interval E-value
Tmemb_cc2 pfam10267
Predicted transmembrane and coiled-coil 2 protein; This family of transmembrane coiled-coil ...
 64-463 0e+00

Predicted transmembrane and coiled-coil 2 protein; This family of transmembrane coiled-coil containing proteins is conserved from worms to humans. Its function is unknown.


Pssm-ID: 463036  Cd Length: 401  Bit Score: 598.94  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296452938   64 VKLTADSLKQKILKVTEQIKIEQTSRDGNVAEYLKLVNNADKQQAGRIKQVFEKKNQKSAHSIAQLQKKLEQYHRKLREI 143
Cdd:pfam10267   1 SRAAIEHLQQKILKIKEQIKIEQTARDENVAEYLKLANNADKQQLARIKQVFEKKNQKSAQNIAQLQKKLEQYHRRLKEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296452938  144 E---QNGASRSSKdiSKDHLKDIHRSLKDahvksrtaphCMESSKSGMPGVSLTPPVFVFNKSREFANLIRNKFGSADNI 220
Cdd:pfam10267  81 EngeQSSVTSHRQ--PKEVLRDVGQGLRD----------VGGNIRDGISGLSGGPPPTVFSKPREFAHLIKNKFGSADNI 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296452938  221 AHLKNSLEEFRPEASARAYGGS-ATIVNKPKYGSDDECSSGT--SGSADSNGNQSFGA----GGASTLDSQGKLAVILEE 293
Cdd:pfam10267 149 NSLKSSLETSHDEGGGRKLSGStFSTVTKPKYPSDDECSSSSveSISAGSNGNPPPHGadngGQQAESDSQNGLAAILEE 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296452938  294 LREIKDTQAQLAEDIEALKVQFKREYGFISQTLQEERYRYERLEDQLHDLTDLHQHETANLKQELASIEEKVAYQAYERS 373
Cdd:pfam10267 229 LQEIKEAQVQLEEKLERLKTQFKKEYKFLTQALQEERYRYERLEEQLNDLTELHQNEIANLKQELASMEEKVAYQSYERA 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296452938  374 RDIQEALESCQTRISKLELHQQEQQALQTDTV---NAKVLLGRCINVILAFMTVILVCVSTIAKFVSPMMKSRCHILGTF 450
Cdd:pfam10267 309 RDIQEALESCQTRISKMELQQQQQQLVQLEGLenaNARALLGKLINIVLAILTVILVLVSTAAKFVAPLLKTRLRILTTI 388

                         410
                  ....*....|...
gi 296452938  451 FAVTLLAIFCKNW 463
Cdd:pfam10267 389 LLVLLLIIFWKNW 401
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
282-407 1.53e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 51.07  E-value: 1.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296452938  282 DSQGKLAVILEELREIKDTQAQLAEDIEALKVQfkreygfiSQTLQEERYRYERLEDQLHDLTDL--HQHETANLKQELA 359
Cdd:COG4913   607 DNRAKLAALEAELAELEEELAEAEERLEALEAE--------LDALQERREALQRLAEYSWDEIDVasAEREIAELEAELE 678

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 296452938  360 SIE---------EKVAYQAYERSRDIQEALESCQTRISKLEL----HQQEQQALQTDTVNA 407
Cdd:COG4913   679 RLDassddlaalEEQLEELEAELEELEEELDELKGEIGRLEKeleqAEEELDELQDRLEAA 739
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 286-399 1.39e-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: 47.74  E-value: 1.39e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296452938   286 KLAVILEELREIKDT---QAQLAEDIEALKVQFKR-EYGFISQTLQEERYRYERLEDQLHDLTDLHQHETANLKQELASI 361
Cdd:TIGR02168  190 RLEDILNELERQLKSlerQAEKAERYKELKAELRElELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKL 269

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 296452938   362 EEKVAY--QAYERSRDIQEALESCQTRISKLELHQQEQQA 399
Cdd:TIGR02168  270 EELRLEvsELEEEIEELQKELYALANEISRLEQQKQILRE 309
 
Name Accession Description Interval E-value
Tmemb_cc2 pfam10267
Predicted transmembrane and coiled-coil 2 protein; This family of transmembrane coiled-coil ...
 64-463 0e+00

Predicted transmembrane and coiled-coil 2 protein; This family of transmembrane coiled-coil containing proteins is conserved from worms to humans. Its function is unknown.


Pssm-ID: 463036  Cd Length: 401  Bit Score: 598.94  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296452938   64 VKLTADSLKQKILKVTEQIKIEQTSRDGNVAEYLKLVNNADKQQAGRIKQVFEKKNQKSAHSIAQLQKKLEQYHRKLREI 143
Cdd:pfam10267   1 SRAAIEHLQQKILKIKEQIKIEQTARDENVAEYLKLANNADKQQLARIKQVFEKKNQKSAQNIAQLQKKLEQYHRRLKEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296452938  144 E---QNGASRSSKdiSKDHLKDIHRSLKDahvksrtaphCMESSKSGMPGVSLTPPVFVFNKSREFANLIRNKFGSADNI 220
Cdd:pfam10267  81 EngeQSSVTSHRQ--PKEVLRDVGQGLRD----------VGGNIRDGISGLSGGPPPTVFSKPREFAHLIKNKFGSADNI 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296452938  221 AHLKNSLEEFRPEASARAYGGS-ATIVNKPKYGSDDECSSGT--SGSADSNGNQSFGA----GGASTLDSQGKLAVILEE 293
Cdd:pfam10267 149 NSLKSSLETSHDEGGGRKLSGStFSTVTKPKYPSDDECSSSSveSISAGSNGNPPPHGadngGQQAESDSQNGLAAILEE 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296452938  294 LREIKDTQAQLAEDIEALKVQFKREYGFISQTLQEERYRYERLEDQLHDLTDLHQHETANLKQELASIEEKVAYQAYERS 373
Cdd:pfam10267 229 LQEIKEAQVQLEEKLERLKTQFKKEYKFLTQALQEERYRYERLEEQLNDLTELHQNEIANLKQELASMEEKVAYQSYERA 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296452938  374 RDIQEALESCQTRISKLELHQQEQQALQTDTV---NAKVLLGRCINVILAFMTVILVCVSTIAKFVSPMMKSRCHILGTF 450
Cdd:pfam10267 309 RDIQEALESCQTRISKMELQQQQQQLVQLEGLenaNARALLGKLINIVLAILTVILVLVSTAAKFVAPLLKTRLRILTTI 388

                         410
                  ....*....|...
gi 296452938  451 FAVTLLAIFCKNW 463
Cdd:pfam10267 389 LLVLLLIIFWKNW 401
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
282-407 1.53e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 51.07  E-value: 1.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296452938  282 DSQGKLAVILEELREIKDTQAQLAEDIEALKVQfkreygfiSQTLQEERYRYERLEDQLHDLTDL--HQHETANLKQELA 359
Cdd:COG4913   607 DNRAKLAALEAELAELEEELAEAEERLEALEAE--------LDALQERREALQRLAEYSWDEIDVasAEREIAELEAELE 678

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 296452938  360 SIE---------EKVAYQAYERSRDIQEALESCQTRISKLEL----HQQEQQALQTDTVNA 407
Cdd:COG4913   679 RLDassddlaalEEQLEELEAELEELEEELDELKGEIGRLEKeleqAEEELDELQDRLEAA 739
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
284-399 4.73e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.00  E-value: 4.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296452938 284 QGKLAVILEELREIKDTQAQLAEDIEALKVQFK-----REYGFISQTLQEERYRYERLEDQLHDLTDLHQH------ETA 352
Cdd:COG4717   94 QEELEELEEELEELEAELEELREELEKLEKLLQllplyQELEALEAELAELPERLEELEERLEELRELEEEleeleaELA 173

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 296452938 353 NLKQELASIEEKVAYQAYERSRDIQEALESCQTRISKLELHQQEQQA 399
Cdd:COG4717  174 ELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE 220
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 286-399 1.39e-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: 47.74  E-value: 1.39e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296452938   286 KLAVILEELREIKDT---QAQLAEDIEALKVQFKR-EYGFISQTLQEERYRYERLEDQLHDLTDLHQHETANLKQELASI 361
Cdd:TIGR02168  190 RLEDILNELERQLKSlerQAEKAERYKELKAELRElELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKL 269

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 296452938   362 EEKVAY--QAYERSRDIQEALESCQTRISKLELHQQEQQA 399
Cdd:TIGR02168  270 EELRLEvsELEEEIEELQKELYALANEISRLEQQKQILRE 309
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 286-399 1.65e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 1.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296452938 286 KLAVILEELREIKDTQAQLAEDIEALKVQFKR---EYGFISQTLQEERYRYERLEDQLHDLtdlhQHETANLKQELASIE 362
Cdd:COG1196  226 EAELLLLKLRELEAELEELEAELEELEAELEEleaELAELEAELEELRLELEELELELEEA----QAEEYELLAELARLE 301

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 296452938 363 EKVAYQAyERSRDIQEALESCQTRISKLELHQQEQQA 399
Cdd:COG1196  302 QDIARLE-ERRRELEERLEELEEELAELEEELEELEE 337
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 286-399 1.97e-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: 39.91  E-value: 1.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296452938 286 KLAVILEELREIKDTQAQLAEDIEALKVQF-----------------KREYGFISQTLQEERYRYERLEDQL------HD 342
Cdd:COG1579   11 DLQELDSELDRLEHRLKELPAELAELEDELaalearleaakteledlEKEIKRLELEIEEVEARIKKYEEQLgnvrnnKE 90

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 296452938 343 LTDLhQHETANLKQELASIEEKVAyQAYERSRDIQEALESCQTRISKLELHQQEQQA 399
Cdd:COG1579   91 YEAL-QKEIESLKRRISDLEDEIL-ELMERIEELEEELAELEAELAELEAELEEKKA 145
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 284-403 2.24e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.82  E-value: 2.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296452938   284 QGKLAVILEELREIKDTQAQLAEDIEALKVQFKREYGFISQ------TLQEERYRYERLEDQLHDLTDLHQHETANLKQE 357
Cdd:TIGR02169  349 RKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDyrekleKLKREINELKRELDRLQEELQRLSEELADLNAA 428

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 296452938   358 LASIEEKVAyQAYERSRDIQEALESCQTRIS----KLELHQQEQQALQTD 403
Cdd:TIGR02169  429 IAGIEAKIN-ELEEEKEDKALEIKKQEWKLEqlaaDLSKYEQELYDLKEE 477
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
286-415 2.44e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 2.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296452938 286 KLAVILEELREIKDTQAQLAEDIEALKVQFKReygfisqtLQEERYRYERLEDQLHDLTDLHQhetanLKQELASIEEKV 365
Cdd:COG4717   82 EAEEKEEEYAELQEELEELEEELEELEAELEE--------LREELEKLEKLLQLLPLYQELEA-----LEAELAELPERL 148

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 296452938 366 AyQAYERSRDIQEALESCQTRISKL-ELHQQEQQALQTDTVNAKVLLGRCI 415
Cdd:COG4717  149 E-ELEERLEELRELEEELEELEAELaELQEELEELLEQLSLATEEELQDLA 198
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 282-391 2.87e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.44  E-value: 2.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296452938   282 DSQGKLAVILEELREIKDTQAQLAEDIEALKVQFKR---EYGFISQTLQEERYRYERLEDQLHDLtdlhQHETANLKQEL 358
Cdd:TIGR02169  858 NLNGKKEELEEELEELEAALRDLESRLGDLKKERDEleaQLRELERKIEELEAQIEKKRKRLSEL----KAKLEALEEEL 933

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 296452938   359 ASIEEKVAYQAYERS-----RDIQEALESCQTRISKLE 391
Cdd:TIGR02169  934 SEIEDPKGEDEEIPEeelslEDVQAELQRVEEEIRALE 971
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 286-402 4.75e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.53  E-value: 4.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296452938 286 KLAVILEELREIKDTQAQLAEDIEALKVQfkreygfiSQTLQEERYRYERLEDQLHDLTDLHQHETANLKQELASIEEKV 365
Cdd:COG1196  282 ELEEAQAEEYELLAELARLEQDIARLEER--------RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 296452938 366 AYQAYERSRDIQEALESCQTRISKLELHQQEQQALQT 402
Cdd:COG1196  354 EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
324-403 6.70e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.98  E-value: 6.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296452938 324 QTLQEERYRYERLEDQLHDLtdlhQHETANLKQELASIEEKV--------AYQAYERSRDIQEALESCQTRISKLELHQQ 395
Cdd:COG4717   81 KEAEEKEEEYAELQEELEEL----EEELEELEAELEELREELeklekllqLLPLYQELEALEAELAELPERLEELEERLE 156


                 ....*...
gi 296452938 396 EQQALQTD 403
Cdd:COG4717  157 ELRELEEE 164
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
290-400 8.71e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.74  E-value: 8.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296452938  290 ILEELREIKDTQAQLAEDIEALK-VQFKREYGFISQTLQEERYRYERLEDQLHDLT---DLHQHETANLKQELASIEEKV 365
Cdd:COG4913   253 LLEPIRELAERYAAARERLAELEyLRAALRLWFAQRRLELLEAELEELRAELARLEaelERLEARLDALREELDELEAQI 332

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 296452938  366 AYQAYERSRDIQEALESCQTRISKLELHQQEQQAL 400
Cdd:COG4913   333 RGNGGDRLEQLEREIERLERELEERERRRARLEAL 367
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
277-401 8.91e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 38.46  E-value: 8.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296452938 277 GASTLDSQGKLAV-ILEELR-EIKDTQAQLAED---IEALKVQFKREYGFI-----SQTLQEERYRYERLEDQLHDL--- 343
Cdd:COG3206  206 GLVDLSEEAKLLLqQLSELEsQLAEARAELAEAearLAALRAQLGSGPDALpellqSPVIQQLRAQLAELEAELAELsar 285

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 296452938 344 -TDLHQhETANLKQELASIEEKVAYQAYERSRDIQEALESCQTRISKL--ELHQQEQQALQ 401
Cdd:COG3206  286 yTPNHP-DVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLqaQLAQLEARLAE 345
 
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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