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Conserved domains on  [gi|1622846200|ref|XP_028685614|]
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transmembrane and coiled-coil domain protein 3 isoform X1 [Macaca mulatta]

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 ...
 71-470 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: 600.10  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622846200  71 VKLTADSLKQKILKVTEQIKIEQTSRDGNVAEYLKLVNSADKQQAGRIKQVFEKKNQKSAHSIAQLQKKLEQYHRKLREI 150
Cdd:pfam10267   1 SRAAIEHLQQKILKIKEQIKIEQTARDENVAEYLKLANNADKQQLARIKQVFEKKNQKSAQNIAQLQKKLEQYHRRLKEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622846200 151 E---QNGASRSSKdiSKDHLKDIHRSLKDahvksrtaphCMESSKSGMPGVSLTPPVFVFNKSREFANLIRNKFGSADNI 227
Cdd:pfam10267  81 EngeQSSVTSHRQ--PKEVLRDVGQGLRD----------VGGNIRDGISGLSGGPPPTVFSKPREFAHLIKNKFGSADNI 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622846200 228 AHLKNSLEEFRPEASARAYGGS-ATIVNKPKYGSDDECSSGT--SGSADSNGNQSFGA----GGASTLDSQGKLAVILEE 300
Cdd:pfam10267 149 NSLKSSLETSHDEGGGRKLSGStFSTVTKPKYPSDDECSSSSveSISAGSNGNPPPHGadngGQQAESDSQNGLAAILEE 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622846200 301 LREIKDTQAQLAEDIEALKVQFKREYGFISQTLQEERYRYERLEDQLHDLTDLHQHETANLKQELASIEEKVAYQAYERS 380
Cdd:pfam10267 229 LQEIKEAQVQLEEKLERLKTQFKKEYKFLTQALQEERYRYERLEEQLNDLTELHQNEIANLKQELASMEEKVAYQSYERA 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622846200 381 RDIQEALESCQTRISKLELHQQEQQALQTDTV---NAKVLLGKCINVILAFMTVILVCVSTIAKFVSPMMKSRCHILGTF 457
Cdd:pfam10267 309 RDIQEALESCQTRISKMELQQQQQQLVQLEGLenaNARALLGKLINIVLAILTVILVLVSTAAKFVAPLLKTRLRILTTI 388

                         410
                  ....*....|...
gi 1622846200 458 FAVTLLAIFCKNW 470
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 ...
 71-470 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: 600.10  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622846200  71 VKLTADSLKQKILKVTEQIKIEQTSRDGNVAEYLKLVNSADKQQAGRIKQVFEKKNQKSAHSIAQLQKKLEQYHRKLREI 150
Cdd:pfam10267   1 SRAAIEHLQQKILKIKEQIKIEQTARDENVAEYLKLANNADKQQLARIKQVFEKKNQKSAQNIAQLQKKLEQYHRRLKEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622846200 151 E---QNGASRSSKdiSKDHLKDIHRSLKDahvksrtaphCMESSKSGMPGVSLTPPVFVFNKSREFANLIRNKFGSADNI 227
Cdd:pfam10267  81 EngeQSSVTSHRQ--PKEVLRDVGQGLRD----------VGGNIRDGISGLSGGPPPTVFSKPREFAHLIKNKFGSADNI 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622846200 228 AHLKNSLEEFRPEASARAYGGS-ATIVNKPKYGSDDECSSGT--SGSADSNGNQSFGA----GGASTLDSQGKLAVILEE 300
Cdd:pfam10267 149 NSLKSSLETSHDEGGGRKLSGStFSTVTKPKYPSDDECSSSSveSISAGSNGNPPPHGadngGQQAESDSQNGLAAILEE 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622846200 301 LREIKDTQAQLAEDIEALKVQFKREYGFISQTLQEERYRYERLEDQLHDLTDLHQHETANLKQELASIEEKVAYQAYERS 380
Cdd:pfam10267 229 LQEIKEAQVQLEEKLERLKTQFKKEYKFLTQALQEERYRYERLEEQLNDLTELHQNEIANLKQELASMEEKVAYQSYERA 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622846200 381 RDIQEALESCQTRISKLELHQQEQQALQTDTV---NAKVLLGKCINVILAFMTVILVCVSTIAKFVSPMMKSRCHILGTF 457
Cdd:pfam10267 309 RDIQEALESCQTRISKMELQQQQQQLVQLEGLenaNARALLGKLINIVLAILTVILVLVSTAAKFVAPLLKTRLRILTTI 388

                         410
                  ....*....|...
gi 1622846200 458 FAVTLLAIFCKNW 470
Cdd:pfam10267 389 LLVLLLIIFWKNW 401
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
289-414 1.03e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 51.45  E-value: 1.03e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622846200  289 DSQGKLAVILEELREIKDTQAQLAEDIEALKVQfkreygfiSQTLQEERYRYERLEDQLHDLTDL--HQHETANLKQELA 366
Cdd:COG4913    607 DNRAKLAALEAELAELEEELAEAEERLEALEAE--------LDALQERREALQRLAEYSWDEIDVasAEREIAELEAELE 678

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622846200  367 SIE---------EKVAYQAYERSRDIQEALESCQTRISKLEL----HQQEQQALQTDTVNA 414
Cdd:COG4913    679 RLDassddlaalEEQLEELEAELEELEEELDELKGEIGRLEKeleqAEEELDELQDRLEAA 739
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 293-406 1.37e-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: 1.37e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622846200  293 KLAVILEELREIKDT---QAQLAEDIEALKVQFKR-EYGFISQTLQEERYRYERLEDQLHDLTDLHQHETANLKQELASI 368
Cdd:TIGR02168  190 RLEDILNELERQLKSlerQAEKAERYKELKAELRElELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKL 269

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1622846200  369 EEKVAY--QAYERSRDIQEALESCQTRISKLELHQQEQQA 406
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 ...
 71-470 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: 600.10  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622846200  71 VKLTADSLKQKILKVTEQIKIEQTSRDGNVAEYLKLVNSADKQQAGRIKQVFEKKNQKSAHSIAQLQKKLEQYHRKLREI 150
Cdd:pfam10267   1 SRAAIEHLQQKILKIKEQIKIEQTARDENVAEYLKLANNADKQQLARIKQVFEKKNQKSAQNIAQLQKKLEQYHRRLKEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622846200 151 E---QNGASRSSKdiSKDHLKDIHRSLKDahvksrtaphCMESSKSGMPGVSLTPPVFVFNKSREFANLIRNKFGSADNI 227
Cdd:pfam10267  81 EngeQSSVTSHRQ--PKEVLRDVGQGLRD----------VGGNIRDGISGLSGGPPPTVFSKPREFAHLIKNKFGSADNI 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622846200 228 AHLKNSLEEFRPEASARAYGGS-ATIVNKPKYGSDDECSSGT--SGSADSNGNQSFGA----GGASTLDSQGKLAVILEE 300
Cdd:pfam10267 149 NSLKSSLETSHDEGGGRKLSGStFSTVTKPKYPSDDECSSSSveSISAGSNGNPPPHGadngGQQAESDSQNGLAAILEE 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622846200 301 LREIKDTQAQLAEDIEALKVQFKREYGFISQTLQEERYRYERLEDQLHDLTDLHQHETANLKQELASIEEKVAYQAYERS 380
Cdd:pfam10267 229 LQEIKEAQVQLEEKLERLKTQFKKEYKFLTQALQEERYRYERLEEQLNDLTELHQNEIANLKQELASMEEKVAYQSYERA 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622846200 381 RDIQEALESCQTRISKLELHQQEQQALQTDTV---NAKVLLGKCINVILAFMTVILVCVSTIAKFVSPMMKSRCHILGTF 457
Cdd:pfam10267 309 RDIQEALESCQTRISKMELQQQQQQLVQLEGLenaNARALLGKLINIVLAILTVILVLVSTAAKFVAPLLKTRLRILTTI 388

                         410
                  ....*....|...
gi 1622846200 458 FAVTLLAIFCKNW 470
Cdd:pfam10267 389 LLVLLLIIFWKNW 401
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
289-414 1.03e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 51.45  E-value: 1.03e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622846200  289 DSQGKLAVILEELREIKDTQAQLAEDIEALKVQfkreygfiSQTLQEERYRYERLEDQLHDLTDL--HQHETANLKQELA 366
Cdd:COG4913    607 DNRAKLAALEAELAELEEELAEAEERLEALEAE--------LDALQERREALQRLAEYSWDEIDVasAEREIAELEAELE 678

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622846200  367 SIE---------EKVAYQAYERSRDIQEALESCQTRISKLEL----HQQEQQALQTDTVNA 414
Cdd:COG4913    679 RLDassddlaalEEQLEELEAELEELEEELDELKGEIGRLEKeleqAEEELDELQDRLEAA 739
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
291-406 4.93e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.00  E-value: 4.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622846200 291 QGKLAVILEELREIKDTQAQLAEDIEALKVQFK-----REYGFISQTLQEERYRYERLEDQLHDLTDLHQH------ETA 359
Cdd:COG4717    94 QEELEELEEELEELEAELEELREELEKLEKLLQllplyQELEALEAELAELPERLEELEERLEELRELEEEleeleaELA 173

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1622846200 360 NLKQELASIEEKVAYQAYERSRDIQEALESCQTRISKLELHQQEQQA 406
Cdd:COG4717   174 ELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE 220
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 293-406 1.37e-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: 1.37e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622846200  293 KLAVILEELREIKDT---QAQLAEDIEALKVQFKR-EYGFISQTLQEERYRYERLEDQLHDLTDLHQHETANLKQELASI 368
Cdd:TIGR02168  190 RLEDILNELERQLKSlerQAEKAERYKELKAELRElELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKL 269

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1622846200  369 EEKVAY--QAYERSRDIQEALESCQTRISKLELHQQEQQA 406
Cdd:TIGR02168  270 EELRLEvsELEEEIEELQKELYALANEISRLEQQKQILRE 309
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 293-406 1.30e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 1.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622846200 293 KLAVILEELREIKDTQAQLAEDIEALKVQFKR---EYGFISQTLQEERYRYERLEDQLHDLtdlhQHETANLKQELASIE 369
Cdd:COG1196   226 EAELLLLKLRELEAELEELEAELEELEAELEEleaELAELEAELEELRLELEELELELEEA----QAEEYELLAELARLE 301

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1622846200 370 EKVAYQAyERSRDIQEALESCQTRISKLELHQQEQQA 406
Cdd:COG1196   302 QDIARLE-ERRRELEERLEELEEELAELEEELEELEE 337
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 291-410 2.10e-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: 2.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622846200  291 QGKLAVILEELREIKDTQAQLAEDIEALKVQFKREYGFISQ------TLQEERYRYERLEDQLHDLTDLHQHETANLKQE 364
Cdd:TIGR02169  349 RKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDyrekleKLKREINELKRELDRLQEELQRLSEELADLNAA 428

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1622846200  365 LASIEEKVAyQAYERSRDIQEALESCQTRIS----KLELHQQEQQALQTD 410
Cdd:TIGR02169  429 IAGIEAKIN-ELEEEKEDKALEIKKQEWKLEqlaaDLSKYEQELYDLKEE 477
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 293-406 2.61e-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: 39.52  E-value: 2.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622846200 293 KLAVILEELREIKDTQAQLAEDIEALKVQF-----------------KREYGFISQTLQEERYRYERLEDQL------HD 349
Cdd:COG1579    11 DLQELDSELDRLEHRLKELPAELAELEDELaalearleaakteledlEKEIKRLELEIEEVEARIKKYEEQLgnvrnnKE 90

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622846200 350 LTDLhQHETANLKQELASIEEKVAyQAYERSRDIQEALESCQTRISKLELHQQEQQA 406
Cdd:COG1579    91 YEAL-QKEIESLKRRISDLEDEIL-ELMERIEELEEELAELEAELAELEAELEEKKA 145
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
293-411 2.84e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.14  E-value: 2.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622846200 293 KLAVILEELREIKDTQAQLAEDIEALKVQFKReygfisqtLQEERYRYERLEDQLHDLTDLHQhetanLKQELASIEEKV 372
Cdd:COG4717    82 EAEEKEEEYAELQEELEELEEELEELEAELEE--------LREELEKLEKLLQLLPLYQELEA-----LEAELAELPERL 148

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1622846200 373 AyQAYERSRDIQEALESCQTRISKLELHQQEQQALQTDT 411
Cdd:COG4717   149 E-ELEERLEELRELEEELEELEAELAELQEELEELLEQL 186
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 289-398 2.84e-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: 2.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622846200  289 DSQGKLAVILEELREIKDTQAQLAEDIEALKVQFKR---EYGFISQTLQEERYRYERLEDQLHDLtdlhQHETANLKQEL 365
Cdd:TIGR02169  858 NLNGKKEELEEELEELEAALRDLESRLGDLKKERDEleaQLRELERKIEELEAQIEKKRKRLSEL----KAKLEALEEEL 933

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1622846200  366 ASIEEKVAYQAYERS-----RDIQEALESCQTRISKLE 398
Cdd:TIGR02169  934 SEIEDPKGEDEEIPEeelslEDVQAELQRVEEEIRALE 971
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 293-409 3.88e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.92  E-value: 3.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622846200 293 KLAVILEELREIKDTQAQLAEDIEALKVQfkreygfiSQTLQEERYRYERLEDQLHDLTDLHQHETANLKQELASIEEKV 372
Cdd:COG1196   282 ELEEAQAEEYELLAELARLEQDIARLEER--------RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1622846200 373 AYQAYERSRDIQEALESCQTRISKLELHQQEQQALQT 409
Cdd:COG1196   354 EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
284-408 4.22e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 39.61  E-value: 4.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622846200 284 GASTLDSQGKLAV-ILEELR-EIKDTQAQLAED---IEALKVQFKREYGFI-----SQTLQEERYRYERLEDQLHDL--- 350
Cdd:COG3206   206 GLVDLSEEAKLLLqQLSELEsQLAEARAELAEAearLAALRAQLGSGPDALpellqSPVIQQLRAQLAELEAELAELsar 285

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622846200 351 -TDLHQhETANLKQELASIEEKVAYQAYERSRDIQEALESCQTRISKL--ELHQQEQQALQ 408
Cdd:COG3206   286 yTPNHP-DVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLqaQLAQLEARLAE 345
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
297-407 6.64e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.13  E-value: 6.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622846200  297 ILEELREIKDTQAQLAEDIEALK-VQFKREYGFISQTLQEERYRYERLEDQLHDLT---DLHQHETANLKQELASIEEKV 372
Cdd:COG4913    253 LLEPIRELAERYAAARERLAELEyLRAALRLWFAQRRLELLEAELEELRAELARLEaelERLEARLDALREELDELEAQI 332

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1622846200  373 AYQAYERSRDIQEALESCQTRISKLELHQQEQQAL 407
Cdd:COG4913    333 RGNGGDRLEQLEREIERLERELEERERRRARLEAL 367
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
331-410 7.20e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.98  E-value: 7.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622846200 331 QTLQEERYRYERLEDQLHDLtdlhQHETANLKQELASIEEKV--------AYQAYERSRDIQEALESCQTRISKLELHQQ 402
Cdd:COG4717    81 KEAEEKEEEYAELQEELEEL----EEELEELEAELEELREELeklekllqLLPLYQELEALEAELAELPERLEELEERLE 156


                  ....*...
gi 1622846200 403 EQQALQTD 410
Cdd:COG4717   157 ELRELEEE 164
 
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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