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Conserved domains on  [gi|1907200559|ref|XP_036011211|]
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cell cycle progression protein 1 isoform X5 [Mus musculus]

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]; ...
 330-487 8.85e-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: 55.71  E-value: 8.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559 330 ESEKITFETQKKNLAAENQYLRISLEKEEQALSSLQEELRQLREQI-RLLEDKGTSTQLVRENQVLKQYLEVEKQKTDSF 408
Cdd:COG1196   252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELaRLEQDIARLEERRRELEERLEELEEELAELEEE 331

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907200559 409 LREREMLLEEARMLKRDLEREQLTAMALRAELEqfipgQAQSRAESPSVQTEEKEVGLLQQRLAELEQKLIFEQQRSDL 487
Cdd:COG1196   332 LEELEEELEELEEELEEAEEELEEAEAELAEAE-----EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL 405
PTZ00121 super family cl31754
MAEBL; Provisional
 305-642 1.63e-04

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.13  E-value: 1.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559  305 RKQEQESFLDFKSLKENLERCWTVTESEKITFETQKKNLAAEN-QYLRISLEKEEQALSSLQEELRQLR-EQIRLLED-K 381
Cdd:PTZ00121  1540 KKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKaEEAKKAEEARIEEVMKLYEEEKKMKaEEAKKAEEaK 1619

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559  382 GTSTQLVRENQV------LKQYLEVEKQKTDSFLREREMLLEEARMLKRDLEREQLTAMALRAELEQfipgqaQSRAESP 455
Cdd:PTZ00121  1620 IKAEELKKAEEEkkkveqLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEED------EKKAAEA 1693

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559  456 SVQTEEKEVGLLQQRLAELEQKLIFEQQRSDLWERlYVEAKDQHGKQETDGRKrgsrgSHRAKSKSKETflgtvKETFDA 535
Cdd:PTZ00121  1694 LKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEEN-KIKAEEAKKEAEEDKKK-----AEEAKKDEEEK-----KKIAHL 1762

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559  536 MKNSTKEFVRHHKEKIKQAKEAVKENLKKFSDSVKSTFRHFKDTTKNIFD--EKGSKRFRAPKEAATEKTRTAYSYSSYS 613
Cdd:PTZ00121  1763 KKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEggKEGNLVINDSKEMEDSAIKEVADSKNMQ 1842

                          330       340       350
                   ....*....|....*....|....*....|.
gi 1907200559  614 QQEAP--NQNQNCRRPSAQRDGGREKPSHSE 642
Cdd:PTZ00121  1843 LEEADafEKHKFNKNNENGEDGNKEADFNKE 1873
PLN02328 super family cl33466
lysine-specific histone demethylase 1 homolog
 110-264 8.37e-04

lysine-specific histone demethylase 1 homolog


The actual alignment was detected with superfamily member PLN02328:

Pssm-ID: 215187 [Multi-domain]  Cd Length: 808  Bit Score: 42.67  E-value: 8.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559 110 TLEPPKLEEMGNQEVTIQEAPSSDdLNMGSSSSSQYAFCQPEPErwweklwkiPGCLRGWDDQLRLRVPSQLALQVFSSQ 189
Cdd:PLN02328    5 TKEPEDPADNVNDVVSEASSPETD-LSLSPSQSEQNIENDGQNS---------PETQSPLTELQPSPLPPNTTLDAPVSD 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559 190 PSDEESSSDD-----TSHEPSPAPRRRRNRKKTVSiseseepplaepedEPSKEPS-KRHFSR-GLNKCVILALVIAVSM 262
Cdd:PLN02328   75 SQGDESSSEQqpqnpNSTEPAPPPKKRRRRKRFFT--------------EINANPAfRRHRVRgGLGKEVDVEALIAISV 140


                  ..
gi 1907200559 263 GF 264
Cdd:PLN02328  141 GF 142
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 330-487 8.85e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.71  E-value: 8.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559 330 ESEKITFETQKKNLAAENQYLRISLEKEEQALSSLQEELRQLREQI-RLLEDKGTSTQLVRENQVLKQYLEVEKQKTDSF 408
Cdd:COG1196   252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELaRLEQDIARLEERRRELEERLEELEEELAELEEE 331

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907200559 409 LREREMLLEEARMLKRDLEREQLTAMALRAELEqfipgQAQSRAESPSVQTEEKEVGLLQQRLAELEQKLIFEQQRSDL 487
Cdd:COG1196   332 LEELEEELEELEEELEEAEEELEEAEAELAEAE-----EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL 405
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
 338-490 6.64e-06

Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.


Pssm-ID: 437057 [Multi-domain]  Cd Length: 401  Bit Score: 48.91  E-value: 6.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559 338 TQKKNLAAENQYLRISLEKEEQALSSLQEELRQLREQIRLLEDKGTSTQLVRENQVlkqyleVEKQKTDSFLREREMLLE 417
Cdd:pfam19220 132 EQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQA------AELAELTRRLAELETQLD 205

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907200559 418 EARMLKRDLEREQLTAMALRAELEqfipgqAQSRAESPSVQTEEKEVGL----LQQRLAELEQKLIfeQQRSDLWER 490
Cdd:pfam19220 206 ATRARLRALEGQLAAEQAERERAE------AQLEEAVEAHRAERASLRMkleaLTARAAATEQLLA--EARNQLRDR 274
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 302-571 1.25e-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: 48.53  E-value: 1.25e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559  302 LSQRKQEQESFLDFKSLKENLErcWTVTESEKITFETQKKNLAAENQYLRISLEKEEQALSSLQ---EELRQLREQI-RL 377
Cdd:TIGR02169  203 LRREREKAERYQALLKEKREYE--GYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEkrlEEIEQLLEELnKK 280

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559  378 LEDKGTSTQL-------------------VRENQVLKQYLEVEKQKTDSflrEREMLLEEARMLKRDLEREQLTAMALRA 438
Cdd:TIGR02169  281 IKDLGEEEQLrvkekigeleaeiaslersIAEKERELEDAEERLAKLEA---EIDKLLAEIEELEREIEEERKRRDKLTE 357

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559  439 ELEQFIPGQAQSRAEspsVQTEEKEVGLLQQRLAELEQKLifeqqrSDLWERLYVEAKDQHGKQETDGRKRGSRGSHRAK 518
Cdd:TIGR02169  358 EYAELKEELEDLRAE---LEEVDKEFAETRDELKDYREKL------EKLKREINELKRELDRLQEELQRLSEELADLNAA 428

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907200559  519 SKSKET----FLGTVKETFDAMKNSTKEF--VRHHKEKIKQAKEAVKENLKKFSDSVKS 571
Cdd:TIGR02169  429 IAGIEAkineLEEEKEDKALEIKKQEWKLeqLAADLSKYEQELYDLKEEYDRVEKELSK 487
PTZ00121 PTZ00121
MAEBL; Provisional
 305-642 1.63e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.13  E-value: 1.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559  305 RKQEQESFLDFKSLKENLERCWTVTESEKITFETQKKNLAAEN-QYLRISLEKEEQALSSLQEELRQLR-EQIRLLED-K 381
Cdd:PTZ00121  1540 KKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKaEEAKKAEEARIEEVMKLYEEEKKMKaEEAKKAEEaK 1619

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559  382 GTSTQLVRENQV------LKQYLEVEKQKTDSFLREREMLLEEARMLKRDLEREQLTAMALRAELEQfipgqaQSRAESP 455
Cdd:PTZ00121  1620 IKAEELKKAEEEkkkveqLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEED------EKKAAEA 1693

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559  456 SVQTEEKEVGLLQQRLAELEQKLIFEQQRSDLWERlYVEAKDQHGKQETDGRKrgsrgSHRAKSKSKETflgtvKETFDA 535
Cdd:PTZ00121  1694 LKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEEN-KIKAEEAKKEAEEDKKK-----AEEAKKDEEEK-----KKIAHL 1762

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559  536 MKNSTKEFVRHHKEKIKQAKEAVKENLKKFSDSVKSTFRHFKDTTKNIFD--EKGSKRFRAPKEAATEKTRTAYSYSSYS 613
Cdd:PTZ00121  1763 KKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEggKEGNLVINDSKEMEDSAIKEVADSKNMQ 1842

                          330       340       350
                   ....*....|....*....|....*....|.
gi 1907200559  614 QQEAP--NQNQNCRRPSAQRDGGREKPSHSE 642
Cdd:PTZ00121  1843 LEEADafEKHKFNKNNENGEDGNKEADFNKE 1873
PLN02328 PLN02328
lysine-specific histone demethylase 1 homolog
 110-264 8.37e-04

lysine-specific histone demethylase 1 homolog


Pssm-ID: 215187 [Multi-domain]  Cd Length: 808  Bit Score: 42.67  E-value: 8.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559 110 TLEPPKLEEMGNQEVTIQEAPSSDdLNMGSSSSSQYAFCQPEPErwweklwkiPGCLRGWDDQLRLRVPSQLALQVFSSQ 189
Cdd:PLN02328    5 TKEPEDPADNVNDVVSEASSPETD-LSLSPSQSEQNIENDGQNS---------PETQSPLTELQPSPLPPNTTLDAPVSD 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559 190 PSDEESSSDD-----TSHEPSPAPRRRRNRKKTVSiseseepplaepedEPSKEPS-KRHFSR-GLNKCVILALVIAVSM 262
Cdd:PLN02328   75 SQGDESSSEQqpqnpNSTEPAPPPKKRRRRKRFFT--------------EINANPAfRRHRVRgGLGKEVDVEALIAISV 140


                  ..
gi 1907200559 263 GF 264
Cdd:PLN02328  141 GF 142
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 306-639 2.81e-03

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 40.87  E-value: 2.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559  306 KQEQESFLDfkslkeNLERCWTVTESEKITFETQKKNLAAENQYLRISLEKEEQALSSLQEELRQLREQIRLLEdkGTST 385
Cdd:pfam15921  652 KQERDQLLN------EVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSME--GSDG 723

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559  386 QLVRENQVLKQYLEVEKQKTDS------FL--------REREMLLEEARMLKRDLEREQLTAMALRAELEQFipgQAQSR 451
Cdd:pfam15921  724 HAMKVAMGMQKQITAKRGQIDAlqskiqFLeeamtnanKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVL---RSQER 800

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559  452 AESPSVQTEEKEVGLLQQRLAELEQKLIFEQQRSdlwerlyVEAKDQHGKQETDGRKRGSRGSHRAKSKSKETFLGTVKE 531
Cdd:pfam15921  801 RLKEKVANMEVALDKASLQFAECQDIIQRQEQES-------VRLKLQHTLDVKELQGPGYTSNSSMKPRLLQPASFTRTH 873

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559  532 TFDAMKNSTKEFVRHHKEKIKQAKEAVKENLKKFSDSVKSTFRHFKDTTKNIFDEKG--------SKRFRAPKEAATEKT 603
Cdd:pfam15921  874 SNVPSSQSTASFLSHHSRKTNALKEDPTRDLKQLLQELRSVINEEPTVQLSKAEDKGrapslgalDDRVRDCIIESSLRS 953

                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1907200559  604 RTAYSYSSYSQQEAPNQNQNC-RRPSAQRDGGREKPS 639
Cdd:pfam15921  954 DICHSSSNSLQTEGSKSSETCsREPVLLHAGELEDPS 990
GvpP COG4980
Gas vesicle protein YhaH [General function prediction only];
529-586 4.34e-03

Gas vesicle protein YhaH [General function prediction only];


Pssm-ID: 444004 [Multi-domain]  Cd Length: 106  Bit Score: 37.26  E-value: 4.34e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907200559 529 VKETFDAMKNSTKEFVRHHKEKIKQAKEAVKENLKKFSDSVKSTFRHFKDTTKNIFDE 586
Cdd:COG4980    36 LKDKADDLKDKAEDLKDELKEKASELSEEAKEKLDELIEEIKEKIEELKEEVEPKIEE 93
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 330-487 8.85e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.71  E-value: 8.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559 330 ESEKITFETQKKNLAAENQYLRISLEKEEQALSSLQEELRQLREQI-RLLEDKGTSTQLVRENQVLKQYLEVEKQKTDSF 408
Cdd:COG1196   252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELaRLEQDIARLEERRRELEERLEELEEELAELEEE 331

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907200559 409 LREREMLLEEARMLKRDLEREQLTAMALRAELEqfipgQAQSRAESPSVQTEEKEVGLLQQRLAELEQKLIFEQQRSDL 487
Cdd:COG1196   332 LEELEEELEELEEELEEAEEELEEAEAELAEAE-----EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL 405
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 293-498 1.41e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.86  E-value: 1.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559 293 DELDGVKGYLSQRKqeqESFLDFKSLKENLERCwtvtesEKITFEtQKKNLAaenqylriSLEKE-EQALS--SLQEELR 369
Cdd:COG1196   162 EEAAGISKYKERKE---EAERKLEATEENLERL------EDILGE-LERQLE--------PLERQaEKAERyrELKEELK 223

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559 370 QLREQIRLLEDKGTSTQLVRENQVLKQyLEVEKQKTDSFLREREMLLEEARmLKRDLEREQLTAM-----ALRAELEQFI 444
Cdd:COG1196   224 ELEAELLLLKLRELEAELEELEAELEE-LEAELEELEAELAELEAELEELR-LELEELELELEEAqaeeyELLAELARLE 301

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907200559 445 PGQAQSRAESPSVQTEEKEvglLQQRLAELEQKLIFEQQRSDLWERLYVEAKDQ 498
Cdd:COG1196   302 QDIARLEERRRELEERLEE---LEEELAELEEELEELEEELEELEEELEEAEEE 352
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
333-478 2.35e-06

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 50.79  E-value: 2.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559 333 KITFETQKKNLAAE------NQYLRISLEKE----EQALSSLQEELRQLREQIRLLEDKgtstqlvrenqvLKQYleveK 402
Cdd:COG3206   139 EISYTSPDPELAAAvanalaEAYLEQNLELRreeaRKALEFLEEQLPELRKELEEAEAA------------LEEF----R 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559 403 QKTDSFLREREMLLEEARMlkRDLEREQLTAMALRAELEQFI----------PGQAQSRAESPSVQTEEKEVGLLQQRLA 472
Cdd:COG3206   203 QKNGLVDLSEEAKLLLQQL--SELESQLAEARAELAEAEARLaalraqlgsgPDALPELLQSPVIQQLRAQLAELEAELA 280


                  ....*.
gi 1907200559 473 ELEQKL 478
Cdd:COG3206   281 ELSARY 286
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
 338-490 6.64e-06

Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.


Pssm-ID: 437057 [Multi-domain]  Cd Length: 401  Bit Score: 48.91  E-value: 6.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559 338 TQKKNLAAENQYLRISLEKEEQALSSLQEELRQLREQIRLLEDKGTSTQLVRENQVlkqyleVEKQKTDSFLREREMLLE 417
Cdd:pfam19220 132 EQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQA------AELAELTRRLAELETQLD 205

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907200559 418 EARMLKRDLEREQLTAMALRAELEqfipgqAQSRAESPSVQTEEKEVGL----LQQRLAELEQKLIfeQQRSDLWER 490
Cdd:pfam19220 206 ATRARLRALEGQLAAEQAERERAE------AQLEEAVEAHRAERASLRMkleaLTARAAATEQLLA--EARNQLRDR 274
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
267-478 9.05e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.00  E-value: 9.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559 267 FYGKNEgnKGKGTIQiqkQLVRKTHEDELDGVKGYLSqRKQEQESFLDFKSLKEnLERCWTVTESEKITFETQKKNLAAe 346
Cdd:COG4717    28 IYGPNE--AGKSTLL---AFIRAMLLERLEKEADELF-KPQGRKPELNLKELKE-LEEELKEAEEKEEEYAELQEELEE- 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559 347 nqyLRISLEKEEQALSSLQEELRQLREQIRLLEDKGTSTQLVRE-NQVLKQYLEVEKQKTD--SFLREREMLLEEARMLK 423
Cdd:COG4717   100 ---LEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAElAELPERLEELEERLEElrELEEELEELEAELAELQ 176

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907200559 424 RDLERE-QLTAMALRAELEQFIPGQAQSRAEspsVQTEEKEVGLLQQRLAELEQKL 478
Cdd:COG4717   177 EELEELlEQLSLATEEELQDLAEELEELQQR---LAELEEELEEAQEELEELEEEL 229
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 302-571 1.25e-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: 48.53  E-value: 1.25e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559  302 LSQRKQEQESFLDFKSLKENLErcWTVTESEKITFETQKKNLAAENQYLRISLEKEEQALSSLQ---EELRQLREQI-RL 377
Cdd:TIGR02169  203 LRREREKAERYQALLKEKREYE--GYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEkrlEEIEQLLEELnKK 280

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559  378 LEDKGTSTQL-------------------VRENQVLKQYLEVEKQKTDSflrEREMLLEEARMLKRDLEREQLTAMALRA 438
Cdd:TIGR02169  281 IKDLGEEEQLrvkekigeleaeiaslersIAEKERELEDAEERLAKLEA---EIDKLLAEIEELEREIEEERKRRDKLTE 357

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559  439 ELEQFIPGQAQSRAEspsVQTEEKEVGLLQQRLAELEQKLifeqqrSDLWERLYVEAKDQHGKQETDGRKRGSRGSHRAK 518
Cdd:TIGR02169  358 EYAELKEELEDLRAE---LEEVDKEFAETRDELKDYREKL------EKLKREINELKRELDRLQEELQRLSEELADLNAA 428

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907200559  519 SKSKET----FLGTVKETFDAMKNSTKEF--VRHHKEKIKQAKEAVKENLKKFSDSVKS 571
Cdd:TIGR02169  429 IAGIEAkineLEEEKEDKALEIKKQEWKLeqLAADLSKYEQELYDLKEEYDRVEKELSK 487
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 303-491 6.11e-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: 46.59  E-value: 6.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559  303 SQRKQEQESFLDFKSLKENLERCWTVTESEKITFETQKKNLAAENQYLRISLEKEEQALSSLQEELRQLREQIRLLEDKG 382
Cdd:TIGR02168  316 RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQI 395

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559  383 TSTQL-VRENQVLKQYLEVEKQKTDSFLREREMLLEEARMLKRDLEREQltamaLRAELEQFIPGQAQSRAESPSVQTEE 461
Cdd:TIGR02168  396 ASLNNeIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEE-----LEEELEELQEELERLEEALEELREEL 470

                          170       180       190
                   ....*....|....*....|....*....|
gi 1907200559  462 KEvglLQQRLAELEQKLIFEQQRSDLWERL 491
Cdd:TIGR02168  471 EE---AEQALDAAERELAQLQARLDSLERL 497
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 301-574 1.15e-04

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: 45.43  E-value: 1.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559  301 YLSQRKQEQESFLDFKSLKENLERCWTVTESEKITFETQKKNLAAENQYLRISLEKEEQALSSLQEELRQLREQIRLLED 380
Cdd:TIGR02168  745 LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559  381 KGTSTQ-----LVRENQVLKQYLEVEKQKTDSFLREREMLLEEARMLKRDLE-------REQLTAMALRAELEQFipgQA 448
Cdd:TIGR02168  825 RLESLErriaaTERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEallneraSLEEALALLRSELEEL---SE 901

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559  449 QSRAESPSVQTEEKEVGLLQQRLAELEQKLI-FEQQRSDLWERLYVEAKD--QHGKQETDGRKRGSRGSHR--AKSKSKE 523
Cdd:TIGR02168  902 ELRELESKRSELRRELEELREKLAQLELRLEgLEVRIDNLQERLSEEYSLtlEEAEALENKIEDDEEEARRrlKRLENKI 981

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907200559  524 TFLGTVkeTFDAM-----KNSTKEFVRHHKEKIKQAKEAVKENLKKFSDSVKSTFR 574
Cdd:TIGR02168  982 KELGPV--NLAAIeeyeeLKERYDFLTAQKEDLTEAKETLEEAIEEIDREARERFK 1035
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
339-478 1.28e-04

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: 1.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559  339 QKKNLAAENQYLR--ISLEKEEQALSSLQEELRQLREQIRLLEDKGTSTQlVRENQVLKQYLEVEKQKTDSFLREREMLL 416
Cdd:COG4913    266 AARERLAELEYLRaaLRLWFAQRRLELLEAELEELRAELARLEAELERLE-ARLDALREELDELEAQIRGNGGDRLEQLE 344

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907200559  417 EEARMLKRDLER---------EQLTAMALRAEL--EQFIPGQAQSRAESPSVQTEEKEvglLQQRLAELEQKL 478
Cdd:COG4913    345 REIERLERELEErerrrarleALLAALGLPLPAsaEEFAALRAEAAALLEALEEELEA---LEEALAEAEAAL 414
PTZ00121 PTZ00121
MAEBL; Provisional
 305-642 1.63e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.13  E-value: 1.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559  305 RKQEQESFLDFKSLKENLERCWTVTESEKITFETQKKNLAAEN-QYLRISLEKEEQALSSLQEELRQLR-EQIRLLED-K 381
Cdd:PTZ00121  1540 KKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKaEEAKKAEEARIEEVMKLYEEEKKMKaEEAKKAEEaK 1619

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559  382 GTSTQLVRENQV------LKQYLEVEKQKTDSFLREREMLLEEARMLKRDLEREQLTAMALRAELEQfipgqaQSRAESP 455
Cdd:PTZ00121  1620 IKAEELKKAEEEkkkveqLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEED------EKKAAEA 1693

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559  456 SVQTEEKEVGLLQQRLAELEQKLIFEQQRSDLWERlYVEAKDQHGKQETDGRKrgsrgSHRAKSKSKETflgtvKETFDA 535
Cdd:PTZ00121  1694 LKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEEN-KIKAEEAKKEAEEDKKK-----AEEAKKDEEEK-----KKIAHL 1762

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559  536 MKNSTKEFVRHHKEKIKQAKEAVKENLKKFSDSVKSTFRHFKDTTKNIFD--EKGSKRFRAPKEAATEKTRTAYSYSSYS 613
Cdd:PTZ00121  1763 KKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEggKEGNLVINDSKEMEDSAIKEVADSKNMQ 1842

                          330       340       350
                   ....*....|....*....|....*....|.
gi 1907200559  614 QQEAP--NQNQNCRRPSAQRDGGREKPSHSE 642
Cdd:PTZ00121  1843 LEEADafEKHKFNKNNENGEDGNKEADFNKE 1873
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 306-523 1.79e-04

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 44.73  E-value: 1.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559 306 KQEQESFLDFKSLK-ENLERCWTVTESEKITFETQKKNLAAENQYLRISLEKEEQALSSLQEELRQLREQIRLlEDKGTS 384
Cdd:pfam17380 295 KMEQERLRQEKEEKaREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERIRQ-EEIAME 373

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559 385 TQLVREnqvlKQYLEVEKQKTDSFLRERemlLEEARMLKRDLEREQLTAMALRAELEQFIPGQAQSRAESPSVQTEEKEV 464
Cdd:pfam17380 374 ISRMRE----LERLQMERQQKNERVRQE---LEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAR 446

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907200559 465 GLLQQRLAELEQKLIFEQQRSDLWERlyveaKDQHGKQETDGRKRGSRGSHRAKSKSKE 523
Cdd:pfam17380 447 EMERVRLEEQERQQQVERLRQQEEER-----KRKKLELEKEKRDRKRAEEQRRKILEKE 500
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 281-487 1.93e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 44.67  E-value: 1.93e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559  281 QIQKQLVRKthEDELDGVKGYLSQRKQEQESFLDfkSLKENLERCWTVTESEKITFETQKKNLAAENQYLRISLEKEEQA 360
Cdd:TIGR02169  241 AIERQLASL--EEELEKLTEEISELEKRLEEIEQ--LLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERE 316

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559  361 LSSLQEELRQLREQI-RLLEDKGTSTQLVRENQVLKQYLEVE-------------------------KQKTDSFLREREM 414
Cdd:TIGR02169  317 LEDAEERLAKLEAEIdKLLAEIEELEREIEEERKRRDKLTEEyaelkeeledlraeleevdkefaetRDELKDYREKLEK 396

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907200559  415 LLEEARMLKRDLEREQLTAMALRAELEQFIPGQAQSRAESPSVQTEEKEvglLQQRLAELEQKLifEQQRSDL 487
Cdd:TIGR02169  397 LKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKED---KALEIKKQEWKL--EQLAADL 464
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 341-503 2.37e-04

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: 44.66  E-value: 2.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559  341 KNLAAENQYLRISLEKEEQALSSLQEELRQLREQIRLLEDKG--TSTQLVRENQVLKQYL-EVEK--QKTDSFLREREML 415
Cdd:TIGR02168  680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELeeLSRQISALRKDLARLEaEVEQleERIAQLSKELTEL 759

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559  416 LEEARMLKRDLEREQLTAMALRAELEQFIPGQAQSRAESPSVQTE----EKEVGLLQQRLAELEQKLIFEQQRSDLWERL 491
Cdd:TIGR02168  760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREAldelRAELTLLNEEAANLRERLESLERRIAATERR 839

                          170
                   ....*....|..
gi 1907200559  492 YVEAKDQHGKQE 503
Cdd:TIGR02168  840 LEDLEEQIEELS 851
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
337-503 3.05e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.14  E-value: 3.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559  337 ETQKKNLAAENQYLRISLEKEEQALSSLQEELRQLREQIRLLED-KGTSTQLVRENQVLKQYLEVEKQ-----KTDSFLR 410
Cdd:COG4913    609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRlAEYSWDEIDVASAEREIAELEAElerldASSDDLA 688

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559  411 EREMLLEEARMLKRDLEREQLTAMALRAELEQFIPG------QAQSRAESPSVQTEEKEVGLLQQRLAELEQKLIFEQQR 484
Cdd:COG4913    689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQaeeeldELQDRLEAAEDLARLELRALLEERFAAALGDAVERELR 768

                          170
                   ....*....|....*....
gi 1907200559  485 SDLWERLYVEAKDQHGKQE 503
Cdd:COG4913    769 ENLEERIDALRARLNRAEE 787
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
301-478 3.15e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.85  E-value: 3.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559 301 YLSQRKQEQESFLDF-----KSLKENLERcwtvTESEKITFETQKK--NLAAENQYLRISLEKEEQALSSLQEELRQLRE 373
Cdd:COG3206   165 NLELRREEARKALEFleeqlPELRKELEE----AEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAEAEA 240

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559 374 QIRLLEDK----GTSTQLVRENQVLKQYLEvekqktdsflREREMLLEEARMLKRDLER--EQLTAMALRAELEQFIPGQ 447
Cdd:COG3206   241 RLAALRAQlgsgPDALPELLQSPVIQQLRA----------QLAELEAELAELSARYTPNhpDVIALRAQIAALRAQLQQE 310

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1907200559 448 AQSRAESPSVQTE--EKEVGLLQQRLAELEQKL 478
Cdd:COG3206   311 AQRILASLEAELEalQAREASLQAQLAQLEARL 343
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 355-475 3.91e-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: 3.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559 355 EKEEQALSSLQEELRQLREQIRLLEDKGTSTQLVRENQVLKQYLEVEKQKTDSFLREREMLLEEARMLKRDLEREQLTAM 434
Cdd:COG1196   661 SLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEE 740

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1907200559 435 ALRAELEQFIPGqAQSRAESPSVQTEEKEVGLLQQRLAELE 475
Cdd:COG1196   741 LLEEEELLEEEA-LEELPEPPDLEELERELERLEREIEALG 780
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 329-506 4.21e-04

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.21  E-value: 4.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559 329 TESEKITFETQKKNLAAENQYLRISLEKEEQALSSLQEELRQLREQIRLLEDK--------------------------- 381
Cdd:COG4942    46 LKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEleaqkeelaellralyrlgrqpplall 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559 382 ---GTSTQLVRENQVLKQYLEVEKQKTDSFLREREMLLEearmLKRDLEREQLTAMALRAELEQFIPGQAQSRAESPSVQ 458
Cdd:COG4942   126 lspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAA----LRAELEAERAELEALLAELEEERAALEALKAERQKLL 201

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1907200559 459 TE-EKEVGLLQQRLAELEQKlifEQQRSDLWERLYVEAKDQHGKQETDG 506
Cdd:COG4942   202 ARlEKELAELAAELAELQQE---AEELEALIARLEAEAAAAAERTPAAG 247
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 354-572 6.92e-04

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: 43.12  E-value: 6.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559  354 LEKEEQALSSLQEELRQLREQIRLLEdkgtstqlvRENQVLKQYLEVEKQKTD-----------SFLREREMLLEEARML 422
Cdd:TIGR02168  181 LERTRENLDRLEDILNELERQLKSLE---------RQAEKAERYKELKAELRElelallvlrleELREELEELQEELKEA 251

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559  423 KRDLEREQLTAMALRAELEQFipgQAQSRAESPSVQTEEKEVGLLQQRLAELEQKLIFEQQRSDLWERLYVEAKDQhgkQ 502
Cdd:TIGR02168  252 EEELEELTAELQELEEKLEEL---RLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQ---L 325

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559  503 ETDGRKRGSRgshRAKSKSKETFLGTVKETFDAMKNSTKEFvRHHKEKIKQAKEAVKENLKKFSDSVKST 572
Cdd:TIGR02168  326 EELESKLDEL---AEELAELEEKLEELKEELESLEAELEEL-EAELEELESRLEELEEQLETLRSKVAQL 391
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 337-509 7.10e-04

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.44  E-value: 7.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559 337 ETQKKNLAAENQYLRISLEKEEQALSSLQEELRQLREQIRLLEDK--GTSTQLVRENQVLKQYLEVEKQKTDSFLREREM 414
Cdd:COG4942    26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRirALEQELAALEAELAELEKEIAELRAELEAQKEE 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559 415 LLEEARMLKRDLEREQLTAMALRAELEQFIPGQAQSRAESPSVQTEEKEVGLLQQRLAELEQKLifEQQRSDLwERLYVE 494
Cdd:COG4942   106 LAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL--EAERAEL-EALLAE 182

                         170
                  ....*....|....*
gi 1907200559 495 AKDQHGKQETDGRKR 509
Cdd:COG4942   183 LEEERAALEALKAER 197
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 340-560 7.33e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.13  E-value: 7.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559  340 KKNLAAENQYLRISLEKEEQALSSLQEELRQLREQIRLLEDKGTstQLVRENQVLKQYLEVEKQKTDSFLREREMLLEEA 419
Cdd:TIGR02169  683 LEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIE--QLEQEEEKLKERLEELEEDLSSLEQEIENVKSEL 760

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559  420 RMLKRDLEREQLTAMALRAELEQfiPGQAQSRAESPSVQTE----EKEVGLLQQRLAELEQKLIFEQQRSDLWERLYVEA 495
Cdd:TIGR02169  761 KELEARIEELEEDLHKLEEALND--LEARLSHSRIPEIQAElsklEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQEL 838

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907200559  496 KDQhgKQETDGRKRGSRGSHRAKSKSKETFLGTVKETFDAMKNSTKEF------VRHHKEKIKQAKEAVKE 560
Cdd:TIGR02169  839 QEQ--RIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLgdlkkeRDELEAQLRELERKIEE 907
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
343-442 7.46e-04

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 42.92  E-value: 7.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559 343 LAAENQYLRISLEKEEQALSSLQEELRQLREQIRLLED-----KGTSTQLVRENQVLKQYLEVEKQKTDSFLRER---EM 414
Cdd:COG2433   390 LPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAeveelEAELEEKDERIERLERELSEARSEERREIRKDreiSR 469

                          90       100
                  ....*....|....*....|....*...
gi 1907200559 415 LLEEARMLKRDLEREQLTAMALRAELEQ 442
Cdd:COG2433   470 LDREIERLERELEEERERIEELKRKLER 497
PLN02328 PLN02328
lysine-specific histone demethylase 1 homolog
 110-264 8.37e-04

lysine-specific histone demethylase 1 homolog


Pssm-ID: 215187 [Multi-domain]  Cd Length: 808  Bit Score: 42.67  E-value: 8.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559 110 TLEPPKLEEMGNQEVTIQEAPSSDdLNMGSSSSSQYAFCQPEPErwweklwkiPGCLRGWDDQLRLRVPSQLALQVFSSQ 189
Cdd:PLN02328    5 TKEPEDPADNVNDVVSEASSPETD-LSLSPSQSEQNIENDGQNS---------PETQSPLTELQPSPLPPNTTLDAPVSD 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559 190 PSDEESSSDD-----TSHEPSPAPRRRRNRKKTVSiseseepplaepedEPSKEPS-KRHFSR-GLNKCVILALVIAVSM 262
Cdd:PLN02328   75 SQGDESSSEQqpqnpNSTEPAPPPKKRRRRKRFFT--------------EINANPAfRRHRVRgGLGKEVDVEALIAISV 140


                  ..
gi 1907200559 263 GF 264
Cdd:PLN02328  141 GF 142
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
361-491 1.01e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.59  E-value: 1.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559  361 LSSLQEELRQLREQIRLLEDKGTSTQLVRENQVLKQYLEVEKQKTDSFLREREMLLEEARMlkRDLEREQLTAMALRAEL 440
Cdd:COG4913    237 LERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAEL--EELRAELARLEAELERL 314

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907200559  441 EQFIpGQAQSRAESPSVQTEE---KEVGLLQQRLAELEQKLifeQQRSDLWERL 491
Cdd:COG4913    315 EARL-DALREELDELEAQIRGnggDRLEQLEREIERLEREL---EERERRRARL 364
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 294-487 2.20e-03

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 41.03  E-value: 2.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559 294 ELDGVKGYLSQRKQEQESFLDfkSLKENLERCwtvtesekitfETQKKNLAAENQYLRISLEKEEQALSSLQEELRQLRE 373
Cdd:pfam07888 133 ELEEDIKTLTQRVLERETELE--RMKERAKKA-----------GAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRN 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559 374 qirLLEDKGTSTQLVREN-QVLKQYLEVEKQKTdsflREREMLLEEARMLKRDLEREQLTAMALRAELEQFIPGQAQSRA 452
Cdd:pfam07888 200 ---SLAQRDTQVLQLQDTiTTLTQKLTTAHRKE----AENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQA 272

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1907200559 453 E--SPSVQTEEKEVGLLQQRLAELEQKLIFEQQRSDL 487
Cdd:pfam07888 273 ElhQARLQAAQLTLQLADASLALREGRARWAQERETL 309
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 294-496 2.59e-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: 41.20  E-value: 2.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559  294 ELDGVKGYLSQRKQEQEsflDFKSLKENLERCWTVTESEKITFETQKKNLAAENQYLRISLEKEEQALSSLQEELRQLRE 373
Cdd:TIGR02168  352 ELESLEAELEELEAELE---ELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLK 428

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559  374 QIRLLEDKGTSTQLVRENQVLKqylevEKQKTDSFLRERemlLEEARMLKRDLEREQLtamALRAELEqfipgQAQSRAE 453
Cdd:TIGR02168  429 KLEEAELKELQAELEELEEELE-----ELQEELERLEEA---LEELREELEEAEQALD---AAERELA-----QLQARLD 492

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1907200559  454 SPSVQTEEKEvGLLQQRLAELEQKLIFEQQRSDLWERLYVEAK 496
Cdd:TIGR02168  493 SLERLQENLE-GFSEGVKALLKNQSGLSGILGVLSELISVDEG 534
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 306-639 2.81e-03

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 40.87  E-value: 2.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559  306 KQEQESFLDfkslkeNLERCWTVTESEKITFETQKKNLAAENQYLRISLEKEEQALSSLQEELRQLREQIRLLEdkGTST 385
Cdd:pfam15921  652 KQERDQLLN------EVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSME--GSDG 723

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559  386 QLVRENQVLKQYLEVEKQKTDS------FL--------REREMLLEEARMLKRDLEREQLTAMALRAELEQFipgQAQSR 451
Cdd:pfam15921  724 HAMKVAMGMQKQITAKRGQIDAlqskiqFLeeamtnanKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVL---RSQER 800

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559  452 AESPSVQTEEKEVGLLQQRLAELEQKLIFEQQRSdlwerlyVEAKDQHGKQETDGRKRGSRGSHRAKSKSKETFLGTVKE 531
Cdd:pfam15921  801 RLKEKVANMEVALDKASLQFAECQDIIQRQEQES-------VRLKLQHTLDVKELQGPGYTSNSSMKPRLLQPASFTRTH 873

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559  532 TFDAMKNSTKEFVRHHKEKIKQAKEAVKENLKKFSDSVKSTFRHFKDTTKNIFDEKG--------SKRFRAPKEAATEKT 603
Cdd:pfam15921  874 SNVPSSQSTASFLSHHSRKTNALKEDPTRDLKQLLQELRSVINEEPTVQLSKAEDKGrapslgalDDRVRDCIIESSLRS 953

                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1907200559  604 RTAYSYSSYSQQEAPNQNQNC-RRPSAQRDGGREKPS 639
Cdd:pfam15921  954 DICHSSSNSLQTEGSKSSETCsREPVLLHAGELEDPS 990
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
350-494 3.67e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 3.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559 350 LRISLEKEEQALSSLQ--------EELRQLREQIRLLEDK-GTSTQLVRENQVLKQYLEvEKQKTDSFLREREMLLEEAR 420
Cdd:COG4717    47 LLERLEKEADELFKPQgrkpelnlKELKELEEELKEAEEKeEEYAELQEELEELEEELE-ELEAELEELREELEKLEKLL 125

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907200559 421 MLKRDLEREQltamALRAELEQFIPGQAQSRAESPSVQTEEKEVGLLQQRLAELEQKLIFEQQRSDLWERLYVE 494
Cdd:COG4717   126 QLLPLYQELE----ALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQ 195
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 351-478 4.04e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 4.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559 351 RISLEKEEQALSSLQEELRQLREQIRLLEDKGTSTQLVRENQVLKQYLEVEKQKTDSFLREREMLLEEARMLKRDLEREQ 430
Cdd:COG1196   662 LTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEEL 741

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1907200559 431 LTAMALRAELEQFIPGQAQSRAEspsvqteekevglLQQRLAELEQKL 478
Cdd:COG1196   742 LEEEELLEEEALEELPEPPDLEE-------------LERELERLEREI 776
GvpP COG4980
Gas vesicle protein YhaH [General function prediction only];
529-586 4.34e-03

Gas vesicle protein YhaH [General function prediction only];


Pssm-ID: 444004 [Multi-domain]  Cd Length: 106  Bit Score: 37.26  E-value: 4.34e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907200559 529 VKETFDAMKNSTKEFVRHHKEKIKQAKEAVKENLKKFSDSVKSTFRHFKDTTKNIFDE 586
Cdd:COG4980    36 LKDKADDLKDKAEDLKDELKEKASELSEEAKEKLDELIEEIKEKIEELKEEVEPKIEE 93
DUF6627 pfam20332
Family of unknown function (DUF6627); This family of proteins is functionally uncharacterized. ...
 396-474 6.16e-03

Family of unknown function (DUF6627); This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria. Proteins in this family are approximately 130 amino acids in length.


Pssm-ID: 466482  Cd Length: 125  Bit Score: 37.51  E-value: 6.16e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907200559 396 QYLEVEKQKTDsflreREMLLEearMLKRDLEREQLTAMALRaeleqfiPGQAQSRAESPSVQteekEVGLLQQRLAEL 474
Cdd:pfam20332  29 QVIASEQAQVD-----RAQLLS---TLDRDDVQQQLTAMGVD-------PAQAAERVNRMTDQ----EVAQLNERLEDL 88
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
 331-482 6.53e-03

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 39.36  E-value: 6.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200559 331 SEKITFETQKKNLAAENQYLRISLEKEEqalSSLQEELRQLREQIRLLEDKgtstqlvrenqvlkqyLEVEKQKTDSFLR 410
Cdd:pfam09787  54 QERDLLREEIQKLRGQIQQLRTELQELE---AQQQEEAESSREQLQELEEQ----------------LATERSARREAEA 114

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907200559 411 EREMLLEEARMLKRDLEREQLTAMALRAELEQFI---PGQAQSRAESPSVQTEekevglLQQRLAELEQKLIFEQ 482
Cdd:pfam09787 115 ELERLQEELRYLEEELRRSKATLQSRIKDREAEIeklRNQLTSKSQSSSSQSE------LENRLHQLTETLIQKQ 183
 
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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