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Conserved domains on  [gi|666335587|ref|NP_001287965|]
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transmembrane and coiled-coil domain protein 3 isoform 2 [Homo sapiens]

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 ...
33-432 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: 593.93  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335587   33 VKLTADSLKQKILKVTEQIKIEQTSRDGNVAEYLKLVNNADKQQAGRIKQVFEKKNQKSAHSIAQLQKKLEQYHRKLREI 112
Cdd:pfam10267   1 SRAAIEHLQQKILKIKEQIKIEQTARDENVAEYLKLANNADKQQLARIKQVFEKKNQKSAQNIAQLQKKLEQYHRRLKEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335587  113 E---QNGASRSSKdiSKDHLKDIHRSLKDahvksrtaphCMESSKSGMPGVSLTPPVFVFNKSREFANLIRNKFGSADNI 189
Cdd:pfam10267  81 EngeQSSVTSHRQ--PKEVLRDVGQGLRD----------VGGNIRDGISGLSGGPPPTVFSKPREFAHLIKNKFGSADNI 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335587  190 AHLKNSLEEFRPEASARAYGGS-ATIVNKPKYGSDDECSSGT--SGSADSNGNQSFGA----GGASTLDSQGKLAVILEE 262
Cdd:pfam10267 149 NSLKSSLETSHDEGGGRKLSGStFSTVTKPKYPSDDECSSSSveSISAGSNGNPPPHGadngGQQAESDSQNGLAAILEE 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335587  263 LREIKDTQAQLAEDIEALKVQFKREYGFISQTLQEERYRYERLEDQLHDLTDLHQHETANLKQELASIEEKVAYQAYERS 342
Cdd:pfam10267 229 LQEIKEAQVQLEEKLERLKTQFKKEYKFLTQALQEERYRYERLEEQLNDLTELHQNEIANLKQELASMEEKVAYQSYERA 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335587  343 RDIQEALESCQTRISKLELHQQEQQALQTDTV---NAKVLLGRCINVILAFMTVILVCVSTIAKFVSPMMKSRCHILGTF 419
Cdd:pfam10267 309 RDIQEALESCQTRISKMELQQQQQQLVQLEGLenaNARALLGKLINIVLAILTVILVLVSTAAKFVAPLLKTRLRILTTI 388
                         410
                  ....*....|...
gi 666335587  420 FAVTLLAIFCKNW 432
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 ...
33-432 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: 593.93  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335587   33 VKLTADSLKQKILKVTEQIKIEQTSRDGNVAEYLKLVNNADKQQAGRIKQVFEKKNQKSAHSIAQLQKKLEQYHRKLREI 112
Cdd:pfam10267   1 SRAAIEHLQQKILKIKEQIKIEQTARDENVAEYLKLANNADKQQLARIKQVFEKKNQKSAQNIAQLQKKLEQYHRRLKEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335587  113 E---QNGASRSSKdiSKDHLKDIHRSLKDahvksrtaphCMESSKSGMPGVSLTPPVFVFNKSREFANLIRNKFGSADNI 189
Cdd:pfam10267  81 EngeQSSVTSHRQ--PKEVLRDVGQGLRD----------VGGNIRDGISGLSGGPPPTVFSKPREFAHLIKNKFGSADNI 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335587  190 AHLKNSLEEFRPEASARAYGGS-ATIVNKPKYGSDDECSSGT--SGSADSNGNQSFGA----GGASTLDSQGKLAVILEE 262
Cdd:pfam10267 149 NSLKSSLETSHDEGGGRKLSGStFSTVTKPKYPSDDECSSSSveSISAGSNGNPPPHGadngGQQAESDSQNGLAAILEE 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335587  263 LREIKDTQAQLAEDIEALKVQFKREYGFISQTLQEERYRYERLEDQLHDLTDLHQHETANLKQELASIEEKVAYQAYERS 342
Cdd:pfam10267 229 LQEIKEAQVQLEEKLERLKTQFKKEYKFLTQALQEERYRYERLEEQLNDLTELHQNEIANLKQELASMEEKVAYQSYERA 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335587  343 RDIQEALESCQTRISKLELHQQEQQALQTDTV---NAKVLLGRCINVILAFMTVILVCVSTIAKFVSPMMKSRCHILGTF 419
Cdd:pfam10267 309 RDIQEALESCQTRISKMELQQQQQQLVQLEGLenaNARALLGKLINIVLAILTVILVLVSTAAKFVAPLLKTRLRILTTI 388
                         410
                  ....*....|...
gi 666335587  420 FAVTLLAIFCKNW 432
Cdd:pfam10267 389 LLVLLLIIFWKNW 401
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
251-376 1.57e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 50.68  E-value: 1.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335587  251 DSQGKLAVILEELREIKDTQAQLAEDIEALKVQfkreygfiSQTLQEERYRYERLEDQLHDLTDL--HQHETANLKQELA 328
Cdd:COG4913   607 DNRAKLAALEAELAELEEELAEAEERLEALEAE--------LDALQERREALQRLAEYSWDEIDVasAEREIAELEAELE 678
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 666335587  329 SIE---------EKVAYQAYERSRDIQEALESCQTRISKLEL----HQQEQQALQTDTVNA 376
Cdd:COG4913   679 RLDassddlaalEEQLEELEAELEELEEELDELKGEIGRLEKeleqAEEELDELQDRLEAA 739
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
255-368 2.33e-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: 2.33e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335587   255 KLAVILEELREIKDT---QAQLAEDIEALKVQFKR-EYGFISQTLQEERYRYERLEDQLHDLTDLHQHETANLKQELASI 330
Cdd:TIGR02168  190 RLEDILNELERQLKSlerQAEKAERYKELKAELRElELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKL 269
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 666335587   331 EEKVAY--QAYERSRDIQEALESCQTRISKLELHQQEQQA 368
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 ...
33-432 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: 593.93  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335587   33 VKLTADSLKQKILKVTEQIKIEQTSRDGNVAEYLKLVNNADKQQAGRIKQVFEKKNQKSAHSIAQLQKKLEQYHRKLREI 112
Cdd:pfam10267   1 SRAAIEHLQQKILKIKEQIKIEQTARDENVAEYLKLANNADKQQLARIKQVFEKKNQKSAQNIAQLQKKLEQYHRRLKEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335587  113 E---QNGASRSSKdiSKDHLKDIHRSLKDahvksrtaphCMESSKSGMPGVSLTPPVFVFNKSREFANLIRNKFGSADNI 189
Cdd:pfam10267  81 EngeQSSVTSHRQ--PKEVLRDVGQGLRD----------VGGNIRDGISGLSGGPPPTVFSKPREFAHLIKNKFGSADNI 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335587  190 AHLKNSLEEFRPEASARAYGGS-ATIVNKPKYGSDDECSSGT--SGSADSNGNQSFGA----GGASTLDSQGKLAVILEE 262
Cdd:pfam10267 149 NSLKSSLETSHDEGGGRKLSGStFSTVTKPKYPSDDECSSSSveSISAGSNGNPPPHGadngGQQAESDSQNGLAAILEE 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335587  263 LREIKDTQAQLAEDIEALKVQFKREYGFISQTLQEERYRYERLEDQLHDLTDLHQHETANLKQELASIEEKVAYQAYERS 342
Cdd:pfam10267 229 LQEIKEAQVQLEEKLERLKTQFKKEYKFLTQALQEERYRYERLEEQLNDLTELHQNEIANLKQELASMEEKVAYQSYERA 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335587  343 RDIQEALESCQTRISKLELHQQEQQALQTDTV---NAKVLLGRCINVILAFMTVILVCVSTIAKFVSPMMKSRCHILGTF 419
Cdd:pfam10267 309 RDIQEALESCQTRISKMELQQQQQQLVQLEGLenaNARALLGKLINIVLAILTVILVLVSTAAKFVAPLLKTRLRILTTI 388
                         410
                  ....*....|...
gi 666335587  420 FAVTLLAIFCKNW 432
Cdd:pfam10267 389 LLVLLLIIFWKNW 401
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
251-376 1.57e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 50.68  E-value: 1.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335587  251 DSQGKLAVILEELREIKDTQAQLAEDIEALKVQfkreygfiSQTLQEERYRYERLEDQLHDLTDL--HQHETANLKQELA 328
Cdd:COG4913   607 DNRAKLAALEAELAELEEELAEAEERLEALEAE--------LDALQERREALQRLAEYSWDEIDVasAEREIAELEAELE 678
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 666335587  329 SIE---------EKVAYQAYERSRDIQEALESCQTRISKLEL----HQQEQQALQTDTVNA 376
Cdd:COG4913   679 RLDassddlaalEEQLEELEAELEELEEELDELKGEIGRLEKeleqAEEELDELQDRLEAA 739
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
253-368 9.00e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.23  E-value: 9.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335587 253 QGKLAVILEELREIKDTQAQLAEDIEALKVQFK-----REYGFISQTLQEERYRYERLEDQLHDLTDLHQH------ETA 321
Cdd:COG4717   94 QEELEELEEELEELEAELEELREELEKLEKLLQllplyQELEALEAELAELPERLEELEERLEELRELEEEleeleaELA 173
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 666335587 322 NLKQELASIEEKVAYQAYERSRDIQEALESCQTRISKLELHQQEQQA 368
Cdd:COG4717  174 ELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE 220
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
255-368 2.33e-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: 2.33e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335587   255 KLAVILEELREIKDT---QAQLAEDIEALKVQFKR-EYGFISQTLQEERYRYERLEDQLHDLTDLHQHETANLKQELASI 330
Cdd:TIGR02168  190 RLEDILNELERQLKSlerQAEKAERYKELKAELRElELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKL 269
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 666335587   331 EEKVAY--QAYERSRDIQEALESCQTRISKLELHQQEQQA 368
Cdd:TIGR02168  270 EELRLEvsELEEEIEELQKELYALANEISRLEQQKQILRE 309
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
255-368 2.30e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 2.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335587 255 KLAVILEELREIKDTQAQLAEDIEALKVQFKR---EYGFISQTLQEERYRYERLEDQLHDLtdlhQHETANLKQELASIE 331
Cdd:COG1196  226 EAELLLLKLRELEAELEELEAELEELEAELEEleaELAELEAELEELRLELEELELELEEA----QAEEYELLAELARLE 301
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 666335587 332 EKVAYQAyERSRDIQEALESCQTRISKLELHQQEQQA 368
Cdd:COG1196  302 QDIARLE-ERRRELEERLEELEEELAELEEELEELEE 337
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
253-372 3.17e-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: 40.05  E-value: 3.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335587   253 QGKLAVILEELREIKDTQAQLAEDIEALKVQFKREYGFISQ------TLQEERYRYERLEDQLHDLTDLHQHETANLKQE 326
Cdd:TIGR02169  349 RKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDyrekleKLKREINELKRELDRLQEELQRLSEELADLNAA 428
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 666335587   327 LASIEEKVAyQAYERSRDIQEALESCQTRIS----KLELHQQEQQALQTD 372
Cdd:TIGR02169  429 IAGIEAKIN-ELEEEKEDKALEIKKQEWKLEqlaaDLSKYEQELYDLKEE 477
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
255-368 3.65e-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: 38.75  E-value: 3.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335587 255 KLAVILEELREIKDTQAQLAEDIEALKVQF-----------------KREYGFISQTLQEERYRYERLEDQL------HD 311
Cdd:COG1579   11 DLQELDSELDRLEHRLKELPAELAELEDELaalearleaakteledlEKEIKRLELEIEEVEARIKKYEEQLgnvrnnKE 90
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 666335587 312 LTDLhQHETANLKQELASIEEKVAyQAYERSRDIQEALESCQTRISKLELHQQEQQA 368
Cdd:COG1579   91 YEAL-QKEIESLKRRISDLEDEIL-ELMERIEELEEELAELEAELAELEAELEEKKA 145
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
251-360 4.40e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 39.67  E-value: 4.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335587   251 DSQGKLAVILEELREIKDTQAQLAEDIEALKVQFKR---EYGFISQTLQEERYRYERLEDQLHDLtdlhQHETANLKQEL 327
Cdd:TIGR02169  858 NLNGKKEELEEELEELEAALRDLESRLGDLKKERDEleaQLRELERKIEELEAQIEKKRKRLSEL----KAKLEALEEEL 933
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 666335587   328 ASIEEKVAYQAYERS-----RDIQEALESCQTRISKLE 360
Cdd:TIGR02169  934 SEIEDPKGEDEEIPEeelslEDVQAELQRVEEEIRALE 971
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
255-384 4.69e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.37  E-value: 4.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335587 255 KLAVILEELREIKDTQAQLAEDIEALKVQFKReygfisqtLQEERYRYERLEDQLHDLTDLHQhetanLKQELASIEEKV 334
Cdd:COG4717   82 EAEEKEEEYAELQEELEELEEELEELEAELEE--------LREELEKLEKLLQLLPLYQELEA-----LEAELAELPERL 148
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 666335587 335 AyQAYERSRDIQEALESCQTRISKL-ELHQQEQQALQTDTVNAKVLLGRCI 384
Cdd:COG4717  149 E-ELEERLEELRELEEELEELEAELaELQEELEELLEQLSLATEEELQDLA 198
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
255-371 5.82e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.15  E-value: 5.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335587 255 KLAVILEELREIKDTQAQLAEDIEALKVQfkreygfiSQTLQEERYRYERLEDQLHDLTDLHQHETANLKQELASIEEKV 334
Cdd:COG1196  282 ELEEAQAEEYELLAELARLEQDIARLEER--------RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 666335587 335 AYQAYERSRDIQEALESCQTRISKLELHQQEQQALQT 371
Cdd:COG1196  354 EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
259-369 8.46e-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: 8.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335587  259 ILEELREIKDTQAQLAEDIEALK-VQFKREYGFISQTLQEERYRYERLEDQLHDLT---DLHQHETANLKQELASIEEKV 334
Cdd:COG4913   253 LLEPIRELAERYAAARERLAELEyLRAALRLWFAQRRLELLEAELEELRAELARLEaelERLEARLDALREELDELEAQI 332
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 666335587  335 AYQAYERSRDIQEALESCQTRISKLELHQQEQQAL 369
Cdd:COG4913   333 RGNGGDRLEQLEREIERLERELEERERRRARLEAL 367
 
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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