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Conserved domains on  [gi|158138570|ref|NP_001103371|]
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EMILIN-3 precursor [Rattus norvegicus]

Protein Classification

kinesin family protein( domain architecture ID 13728255)

kinesin family protein is a microtubule-dependent molecular motor that plays an important role in intracellular transport and in cell division and has ATPase-containing motor domain; similar to carboxy-terminal kinesins that contains a C-terminal domain responsible for the motor activity (it hydrolyzes ATP and binds microtubules)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
EMI pfam07546
EMI domain; The Pfam alignment is truncated at the C-terminus and does not include the final ...
58-125 8.29e-19

EMI domain; The Pfam alignment is truncated at the C-terminus and does not include the final cysteine defined in Callebaut et al. This is to stop the family overlapping with other domains.


:

Pssm-ID: 462204  Cd Length: 69  Bit Score: 80.93  E-value: 8.29e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158138570   58 CAYvvhRNVTCVLQEGAESFVKAEYRN----CGWGPNCPstvRYRTVFRPRYKIGYKAVTDLAWRCCPGLTG 125
Cdd:pfam07546   4 CAY---KVVSCVVVTGTESYVQPVYKPyltwCAGHRRCS---TYRTTYRPAYRQVYKTVTRLEWRCCPGWGG 69
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
477-759 2.13e-08

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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 58.14  E-value: 2.13e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138570   477 EERLATLTGEL-KPKGAI-----PDRSVRPLVHSELAVLEQRLVSLETSCTpstttaildNLVAEVKAWQSRSEALLHQV 550
Cdd:TIGR02168  644 GYRIVTLDGDLvRPGGVItggsaKTNSSILERRREIEELEEKIEELEEKIA---------ELEKALAELRKELEELEEEL 714
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138570   551 ARHTALLQQLNGTVAEVQGQLA--EGTGSSLQGEITLLKVNLNSVSKSLTGLSDSVSQYSDAFLAAntsLDERERrVEAE 628
Cdd:TIGR02168  715 EQLRKELEELSRQISALRKDLArlEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEA---EAEIEE-LEAQ 790
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138570   629 VHAIQEQVSSQGSRLQAghrqvlnLRGELEQLKAGVANVAGGLSRCRDTAQELQhtvSHFDQRVAQVEGAYERLGLLAAH 708
Cdd:TIGR02168  791 IEQLKEELKALREALDE-------LRAELTLLNEEAANLRERLESLERRIAATE---RRLEDLEEQIEELSEDIESLAAE 860
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 158138570   709 LNSLPTEQLRSREGLWGHIDKlnhtLAQHTQDIARLRDDLLDCRAQLAEVR 759
Cdd:TIGR02168  861 IEELEELIEELESELEALLNE----RASLEEALALLRSELEELSEELRELE 907
 
Name Accession Description Interval E-value
EMI pfam07546
EMI domain; The Pfam alignment is truncated at the C-terminus and does not include the final ...
58-125 8.29e-19

EMI domain; The Pfam alignment is truncated at the C-terminus and does not include the final cysteine defined in Callebaut et al. This is to stop the family overlapping with other domains.


Pssm-ID: 462204  Cd Length: 69  Bit Score: 80.93  E-value: 8.29e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158138570   58 CAYvvhRNVTCVLQEGAESFVKAEYRN----CGWGPNCPstvRYRTVFRPRYKIGYKAVTDLAWRCCPGLTG 125
Cdd:pfam07546   4 CAY---KVVSCVVVTGTESYVQPVYKPyltwCAGHRRCS---TYRTTYRPAYRQVYKTVTRLEWRCCPGWGG 69
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
477-759 2.13e-08

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: 58.14  E-value: 2.13e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138570   477 EERLATLTGEL-KPKGAI-----PDRSVRPLVHSELAVLEQRLVSLETSCTpstttaildNLVAEVKAWQSRSEALLHQV 550
Cdd:TIGR02168  644 GYRIVTLDGDLvRPGGVItggsaKTNSSILERRREIEELEEKIEELEEKIA---------ELEKALAELRKELEELEEEL 714
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138570   551 ARHTALLQQLNGTVAEVQGQLA--EGTGSSLQGEITLLKVNLNSVSKSLTGLSDSVSQYSDAFLAAntsLDERERrVEAE 628
Cdd:TIGR02168  715 EQLRKELEELSRQISALRKDLArlEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEA---EAEIEE-LEAQ 790
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138570   629 VHAIQEQVSSQGSRLQAghrqvlnLRGELEQLKAGVANVAGGLSRCRDTAQELQhtvSHFDQRVAQVEGAYERLGLLAAH 708
Cdd:TIGR02168  791 IEQLKEELKALREALDE-------LRAELTLLNEEAANLRERLESLERRIAATE---RRLEDLEEQIEELSEDIESLAAE 860
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 158138570   709 LNSLPTEQLRSREGLWGHIDKlnhtLAQHTQDIARLRDDLLDCRAQLAEVR 759
Cdd:TIGR02168  861 IEELEELIEELESELEALLNE----RASLEEALALLRSELEELSEELRELE 907
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
529-676 2.44e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.99  E-value: 2.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138570  529 LDNLVAEVKAWQSRSEALLHQVARHTALLQQLNGTVAEVQGQLAEGTG---SSLQGEITLLKVNLNSVSKSLTGLSDSVS 605
Cdd:COG4913   290 LELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGdrlEQLEREIERLERELEERERRRARLEALLA 369
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158138570  606 QY-------SDAFLAANTSLDERERRVEAEVHAIQEQVSSQGSRLQAGHRQVLNLRGELEQLKAGVANVAGGLSRCRD 676
Cdd:COG4913   370 ALglplpasAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRD 447
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
531-702 6.82e-05

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 46.71  E-value: 6.82e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138570   531 NLVAEVKAWQSRSEALLHQVARHTALLQQLNGTVAEVQGQLAEGTG--SSLQGEITLLKVNLNSVSKSLTGLSDSV---- 604
Cdd:pfam01576  388 ELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEklSKLQSELESVSSLLNEAEGKNIKLSKDVssle 467
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138570   605 SQYSDA--FLAANT----SLDERERRVEAEVHAIQEQVSSQGSRLQAGHRQVLNLRGELEQLKAGVANVAGGLSRCRDTA 678
Cdd:pfam01576  468 SQLQDTqeLLQEETrqklNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGK 547
                          170       180
                   ....*....|....*....|....
gi 158138570   679 QELQHTVSHFDQRVAQVEGAYERL 702
Cdd:pfam01576  548 KRLQRELEALTQQLEEKAAAYDKL 571
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
294-764 1.74e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 45.03  E-value: 1.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138570 294 TSLALLEEYVDQRLQRLWGSLLDGFEQKLQGVQSECDlRVQEVRQQCEEG-QAASQRLHQSLDGRElalrrELSQLGTQL 372
Cdd:PRK02224 187 GSLDQLKAQIEEKEEKDLHERLNGLESELAELDEEIE-RYEEQREQARETrDEADEVLEEHEERRE-----ELETLEAEI 260
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138570 373 QGLTLTGGGtCCSQLALISARVDSLERNLQAVTETQGGpsTLAADELARLSAAMLQGGVDGLLEGLETINRTENGARGCC 452
Cdd:PRK02224 261 EDLRETIAE-TEREREELAEEVRDLRERLEELEEERDD--LLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAA 337
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138570 453 LRMEMGGWGVGGFGSTLEERVQSLEERLATLTGEL-KPKGAIPDRSvrplvhSELAVLEQRLVSLETSCTPSTTTaiLDN 531
Cdd:PRK02224 338 QAHNEEAESLREDADDLEERAEELREEAAELESELeEAREAVEDRR------EEIEELEEEIEELRERFGDAPVD--LGN 409
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138570 532 LVAEVKAWQSRSEALLHQVARHTALLQQLNGTVAEVQGQLAEGT---------GSSLQGEITLLKVNLNSVSKSLTGLSD 602
Cdd:PRK02224 410 AEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKcpecgqpveGSPHVETIEEDRERVEELEAELEDLEE 489
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138570 603 SVSQYSDAfLAANTSLDERERRVEA---EVHAIQEQVSSQGSRLQAGHRQVLNLRGELEQLKAGVANVAGGLSRCRDTAQ 679
Cdd:PRK02224 490 EVEEVEER-LERAEDLVEAEDRIERleeRREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAE 568
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138570 680 ELQHTVSHFDQRVAQVEGAYERLGLLAAHLNslpteqlrsreglwghidklnhTLAQHTQDIARLRDDlldcRAQLAEVR 759
Cdd:PRK02224 569 EAREEVAELNSKLAELKERIESLERIRTLLA----------------------AIADAEDEIERLREK----REALAELN 622

                 ....*
gi 158138570 760 PGRAD 764
Cdd:PRK02224 623 DERRE 627
 
Name Accession Description Interval E-value
EMI pfam07546
EMI domain; The Pfam alignment is truncated at the C-terminus and does not include the final ...
58-125 8.29e-19

EMI domain; The Pfam alignment is truncated at the C-terminus and does not include the final cysteine defined in Callebaut et al. This is to stop the family overlapping with other domains.


Pssm-ID: 462204  Cd Length: 69  Bit Score: 80.93  E-value: 8.29e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158138570   58 CAYvvhRNVTCVLQEGAESFVKAEYRN----CGWGPNCPstvRYRTVFRPRYKIGYKAVTDLAWRCCPGLTG 125
Cdd:pfam07546   4 CAY---KVVSCVVVTGTESYVQPVYKPyltwCAGHRRCS---TYRTTYRPAYRQVYKTVTRLEWRCCPGWGG 69
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
477-759 2.13e-08

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: 58.14  E-value: 2.13e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138570   477 EERLATLTGEL-KPKGAI-----PDRSVRPLVHSELAVLEQRLVSLETSCTpstttaildNLVAEVKAWQSRSEALLHQV 550
Cdd:TIGR02168  644 GYRIVTLDGDLvRPGGVItggsaKTNSSILERRREIEELEEKIEELEEKIA---------ELEKALAELRKELEELEEEL 714
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138570   551 ARHTALLQQLNGTVAEVQGQLA--EGTGSSLQGEITLLKVNLNSVSKSLTGLSDSVSQYSDAFLAAntsLDERERrVEAE 628
Cdd:TIGR02168  715 EQLRKELEELSRQISALRKDLArlEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEA---EAEIEE-LEAQ 790
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138570   629 VHAIQEQVSSQGSRLQAghrqvlnLRGELEQLKAGVANVAGGLSRCRDTAQELQhtvSHFDQRVAQVEGAYERLGLLAAH 708
Cdd:TIGR02168  791 IEQLKEELKALREALDE-------LRAELTLLNEEAANLRERLESLERRIAATE---RRLEDLEEQIEELSEDIESLAAE 860
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 158138570   709 LNSLPTEQLRSREGLWGHIDKlnhtLAQHTQDIARLRDDLLDCRAQLAEVR 759
Cdd:TIGR02168  861 IEELEELIEELESELEALLNE----RASLEEALALLRSELEELSEELRELE 907
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
469-757 2.28e-08

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: 57.76  E-value: 2.28e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138570   469 LEERVQSLEERLATLTGELKPkgaipdrsvrplVHSELAVLEQRLVSLETscTPSTTTAILDNLVAEVKAWQSRSEALLH 548
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAE------------LRKELEELEEELEQLRK--ELEELSRQISALRKDLARLEAEVEQLEE 747
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138570   549 QVARHTALLQQLNGTVAEVQGQLAEgtgssLQGEITLLKVNLNSVSKSLTGLSDSVSQYSDAFLAANtsldERERRVEAE 628
Cdd:TIGR02168  748 RIAQLSKELTELEAEIEELEERLEE-----AEEELAEAEAEIEELEAQIEQLKEELKALREALDELR----AELTLLNEE 818
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138570   629 VHAIQEQVSSQGSRLQAGHRQVLNLRGELEQLKAGVANVAGGLSRCRDTAQELQHTVSHFDQRVAQVEGAY----ERLGL 704
Cdd:TIGR02168  819 AANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALallrSELEE 898
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 158138570   705 LAAHLNSLPTEQLRSREGLwghiDKLNHTLAQHTQDIARLRDDLLDCRAQLAE 757
Cdd:TIGR02168  899 LSEELRELESKRSELRREL----EELREKLAQLELRLEGLEVRIDNLQERLSE 947
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
467-669 1.18e-06

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 52.37  E-value: 1.18e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138570   467 STLEERVQSLEERLATLTGELKPKGAIPDRSVRPLVHS--ELAVLEQRLVSLEtsctpstttAILDNLVAEVKAWQSRSE 544
Cdd:TIGR02168  298 SRLEQQKQILRERLANLERQLEELEAQLEELESKLDELaeELAELEEKLEELK---------EELESLEAELEELEAELE 368
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138570   545 ALLHQVARHTALLQQLNGTVAEVQGQLAegtgsSLQGEITLLKVNLNSVSKSLTGLSDSVSQYSDAFLAAN--------- 615
Cdd:TIGR02168  369 ELESRLEELEEQLETLRSKVAQLELQIA-----SLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAElkelqaele 443
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138570   616 ------TSLDERERRVEAEVHAIQEQVSSQGSRLQAGHRQVLNLRGELEQLKAGVANVAG 669
Cdd:TIGR02168  444 eleeelEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
417-761 1.12e-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: 49.28  E-value: 1.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138570   417 DELARLSAAMLQGGVDGLLEGLETINRTENGARGCCLRMEMGGWGVGGFGSTLEERVQSLEERLATLTGELKPKGAIPDR 496
Cdd:TIGR02168  220 AELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISR 299
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138570   497 svrplVHSELAVLEQRLVSLETSctpstttaiLDNLVAEVKAWQSRSEALLHQVARHTALLQQLNGTVAEVQGQLAEGTG 576
Cdd:TIGR02168  300 -----LEQQKQILRERLANLERQ---------LEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEA 365
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138570   577 sslqgeitlLKVNLNSVSKSLTglsdsvsqysDAFLAANTSLDERERRVEaevhAIQEQVSSQGSRLQAGHRQVLNLRGE 656
Cdd:TIGR02168  366 ---------ELEELESRLEELE----------EQLETLRSKVAQLELQIA----SLNNEIERLEARLERLEDRRERLQQE 422
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138570   657 LEQL--KAGVANVAGGLSRCRDTAQELQHTVSHFDQRVAQVEGAYERLGLLAAHLNSLPTE--QLRSR----EGLWGHID 728
Cdd:TIGR02168  423 IEELlkKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERElaQLQARldslERLQENLE 502
                          330       340       350
                   ....*....|....*....|....*....|...
gi 158138570   729 KLNHTLAQHTQDiARLRDDLLDCRAQLAEVRPG 761
Cdd:TIGR02168  503 GFSEGVKALLKN-QSGLSGILGVLSELISVDEG 534
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
529-676 2.44e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.99  E-value: 2.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138570  529 LDNLVAEVKAWQSRSEALLHQVARHTALLQQLNGTVAEVQGQLAEGTG---SSLQGEITLLKVNLNSVSKSLTGLSDSVS 605
Cdd:COG4913   290 LELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGdrlEQLEREIERLERELEERERRRARLEALLA 369
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158138570  606 QY-------SDAFLAANTSLDERERRVEAEVHAIQEQVSSQGSRLQAGHRQVLNLRGELEQLKAGVANVAGGLSRCRD 676
Cdd:COG4913   370 ALglplpasAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRD 447
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
531-702 6.82e-05

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 46.71  E-value: 6.82e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138570   531 NLVAEVKAWQSRSEALLHQVARHTALLQQLNGTVAEVQGQLAEGTG--SSLQGEITLLKVNLNSVSKSLTGLSDSV---- 604
Cdd:pfam01576  388 ELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEklSKLQSELESVSSLLNEAEGKNIKLSKDVssle 467
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138570   605 SQYSDA--FLAANT----SLDERERRVEAEVHAIQEQVSSQGSRLQAGHRQVLNLRGELEQLKAGVANVAGGLSRCRDTA 678
Cdd:pfam01576  468 SQLQDTqeLLQEETrqklNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGK 547
                          170       180
                   ....*....|....*....|....
gi 158138570   679 QELQHTVSHFDQRVAQVEGAYERL 702
Cdd:pfam01576  548 KRLQRELEALTQQLEEKAAAYDKL 571
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
294-764 1.74e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 45.03  E-value: 1.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138570 294 TSLALLEEYVDQRLQRLWGSLLDGFEQKLQGVQSECDlRVQEVRQQCEEG-QAASQRLHQSLDGRElalrrELSQLGTQL 372
Cdd:PRK02224 187 GSLDQLKAQIEEKEEKDLHERLNGLESELAELDEEIE-RYEEQREQARETrDEADEVLEEHEERRE-----ELETLEAEI 260
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138570 373 QGLTLTGGGtCCSQLALISARVDSLERNLQAVTETQGGpsTLAADELARLSAAMLQGGVDGLLEGLETINRTENGARGCC 452
Cdd:PRK02224 261 EDLRETIAE-TEREREELAEEVRDLRERLEELEEERDD--LLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAA 337
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138570 453 LRMEMGGWGVGGFGSTLEERVQSLEERLATLTGEL-KPKGAIPDRSvrplvhSELAVLEQRLVSLETSCTPSTTTaiLDN 531
Cdd:PRK02224 338 QAHNEEAESLREDADDLEERAEELREEAAELESELeEAREAVEDRR------EEIEELEEEIEELRERFGDAPVD--LGN 409
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138570 532 LVAEVKAWQSRSEALLHQVARHTALLQQLNGTVAEVQGQLAEGT---------GSSLQGEITLLKVNLNSVSKSLTGLSD 602
Cdd:PRK02224 410 AEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKcpecgqpveGSPHVETIEEDRERVEELEAELEDLEE 489
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138570 603 SVSQYSDAfLAANTSLDERERRVEA---EVHAIQEQVSSQGSRLQAGHRQVLNLRGELEQLKAGVANVAGGLSRCRDTAQ 679
Cdd:PRK02224 490 EVEEVEER-LERAEDLVEAEDRIERleeRREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAE 568
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138570 680 ELQHTVSHFDQRVAQVEGAYERLGLLAAHLNslpteqlrsreglwghidklnhTLAQHTQDIARLRDDlldcRAQLAEVR 759
Cdd:PRK02224 569 EAREEVAELNSKLAELKERIESLERIRTLLA----------------------AIADAEDEIERLREK----REALAELN 622

                 ....*
gi 158138570 760 PGRAD 764
Cdd:PRK02224 623 DERRE 627
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
319-763 3.21e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 3.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138570 319 EQKLQGVQ---SECDLRVQEVRQQCE--EGQAASQRLHQSLdgRELALRRELSQLGTQLQGLTLtgggtccsQLALISAR 393
Cdd:COG1196  178 ERKLEATEenlERLEDILGELERQLEplERQAEKAERYREL--KEELKELEAELLLLKLRELEA--------ELEELEAE 247
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138570 394 VDSLERNLQAVTETQggpSTLAAD-ELARLSAAMLQGGVDGLLEGLETINRTENGARGcclrmemggwgvggFGSTLEER 472
Cdd:COG1196  248 LEELEAELEELEAEL---AELEAElEELRLELEELELELEEAQAEEYELLAELARLEQ--------------DIARLEER 310
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138570 473 VQSLEERLATLTGELKPKGA--IPDRSVRPLVHSELAVLEQRLVSLETSctPSTTTAILDNLVAEVKAWQSRSEALLHQV 550
Cdd:COG1196  311 RRELEERLEELEEELAELEEelEELEEELEELEEELEEAEEELEEAEAE--LAEAEEALLEAEAELAEAEEELEELAEEL 388
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138570 551 ARHTALLQQLNGTVAEVQGQLAEgtgssLQGEITLLKVNLNSVSKSLTGLSDSVsqysDAFLAANTSLDERERRVEAEVH 630
Cdd:COG1196  389 LEALRAAAELAAQLEELEEAEEA-----LLERLERLEEELEELEEALAELEEEE----EEEEEALEEAAEEEAELEEEEE 459
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138570 631 AIQEQVSSQGSRLQAGHRQVLNLRGELEQLKAGvanvagglsrcRDTAQELQHTVSHFDQRVAQVEGAyERLGLLAAHLN 710
Cdd:COG1196  460 ALLELLAELLEEAALLEAALAELLEELAEAAAR-----------LLLLLEAEADYEGFLEGVKAALLL-AGLRGLAGAVA 527
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|...
gi 158138570 711 SLPTEQLRSREGLwghidkLNHTLAQHTQDIARLRDDLLDCRAQLAEVRPGRA 763
Cdd:COG1196  528 VLIGVEAAYEAAL------EAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRA 574
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
579-754 6.03e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 6.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138570  579 LQGEITLLKVNLNSVSKSLTGLSDSVSQYSDAFLAANTSLDERERRV-----EAEVHAIQEQVSsqgsRLQAGHRQVLNL 653
Cdd:COG4913   615 LEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvasaEREIAELEAELE----RLDASSDDLAAL 690
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138570  654 RGELEQLKAGVANVAGGLSRCRDTAQELQHTVSHFDQRVAQVEGAYERLGLLAAHLNSLPTEQLRSREGLWGHIDK---- 729
Cdd:COG4913   691 EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERElren 770
                         170       180
                  ....*....|....*....|....*
gi 158138570  730 LNHTLAQHTQDIARLRDDLLDCRAQ 754
Cdd:COG4913   771 LEERIDALRARLNRAEEELERAMRA 795
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
618-757 6.62e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 6.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138570  618 LDERERRVEAEVHAIQEQVSS-QGSRLQAGHRQVLNLRGELEQLKAgvanvagGLSRCRDTAQELQHTVSHFDQRVAQVE 696
Cdd:COG4913   307 LEAELERLEARLDALREELDElEAQIRGNGGDRLEQLEREIERLER-------ELEERERRRARLEALLAALGLPLPASA 379
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158138570  697 GAYERL-GLLAAHLNSLPTEQLRSREGLWGHID---KLNHTLAQHTQDIARLR-------DDLLDCRAQLAE 757
Cdd:COG4913   380 EEFAALrAEAAALLEALEEELEALEEALAEAEAalrDLRRELRELEAEIASLErrksnipARLLALRDALAE 451
 
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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