NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|45433501|ref|NP_443078|]
View 

EMILIN-3 precursor [Homo sapiens]

Protein Classification

EMI and SMC_prok_B domain-containing protein( domain architecture ID 13728255)

EMI and SMC_prok_B domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
59-126 9.89e-21

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: 86.32  E-value: 9.89e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45433501    59 CAYvvhRNVTCILQEGAESYVKAEYRQ----CRWGPKCPgtvTYRTVLRPKYKVGYKTVTDLAWRCCPGFTG 126
Cdd:pfam07546   4 CAY---KVVSCVVVTGTESYVQPVYKPyltwCAGHRRCS---TYRTTYRPAYRQVYKTVTRLEWRCCPGWGG 69
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
478-758 6.36e-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: 56.60  E-value: 6.36e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433501    478 EERLATLAGEL--SHDSASPGRSARPLV----QTELAVLEQRLVSLETSCTpsttsaildSLVAEVKAWQSRSEALLRQV 551
Cdd:TIGR02168  644 GYRIVTLDGDLvrPGGVITGGSAKTNSSilerRREIEELEEKIEELEEKIA---------ELEKALAELRKELEELEEEL 714
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433501    552 ASHAALLQQLNGTVAEVQGQLA--EGTGSSLQGEITLLKVNLNSVSKSLTGLSDSVSQYSDAFLAAntsldererkvEAE 629
Cdd:TIGR02168  715 EQLRKELEELSRQISALRKDLArlEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEA-----------EAE 783
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433501    630 VQAIQEQVSSQGSRLQAGHRQVLNLRGELEQLKAGVAKVASGLSRCQDTAQKLQHTVGHFDQRVAQVEGacrRLGLLAAG 709
Cdd:TIGR02168  784 IEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSE---DIESLAAE 860
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 45433501    710 LDSLPTEPLRPREGLWSHVDQlnrtLAQHTQDIARLRDDLLDCQAQLAE 758
Cdd:TIGR02168  861 IEELEELIEELESELEALLNE----RASLEEALALLRSELEELSEELRE 905
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
320-574 4.31e-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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.89  E-value: 4.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433501    320 EQKLQGVQSECDLRVQEVRRQCEEGQAASRRLHQsLDGRELALRQELSQLGSQLQGLSVSgRGSCCGQLALINARMDGLE 399
Cdd:TIGR02168  697 EKALAELRKELEELEEELEQLRKELEELSRQISA-LRKDLARLEAEVEQLEERIAQLSKE-LTELEAEIEELEERLEEAE 774
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433501    400 RALQAVTETQRGPGAPAGDELTRLSAamLEGGVDGLLEGLETLNGTEGGARGCCLRLDMGGWGVGGFGTMLEERVQSLEE 479
Cdd:TIGR02168  775 EELAEAEAEIEELEAQIEQLKEELKA--LREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSE 852
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433501    480 RLATLAGELSHDSASPGRSARPL--VQTELAVLEQRLVSLETSCtpSTTSAILDSLVAEVKAWQSRSEALLRQVASHAAL 557
Cdd:TIGR02168  853 DIESLAAEIEELEELIEELESELeaLLNERASLEEALALLRSEL--EELSEELRELESKRSELRRELEELREKLAQLELR 930
                          250
                   ....*....|....*..
gi 45433501    558 LQQLNGTVAEVQGQLAE 574
Cdd:TIGR02168  931 LEGLEVRIDNLQERLSE 947
 
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 ...
59-126 9.89e-21

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: 86.32  E-value: 9.89e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45433501    59 CAYvvhRNVTCILQEGAESYVKAEYRQ----CRWGPKCPgtvTYRTVLRPKYKVGYKTVTDLAWRCCPGFTG 126
Cdd:pfam07546   4 CAY---KVVSCVVVTGTESYVQPVYKPyltwCAGHRRCS---TYRTTYRPAYRQVYKTVTRLEWRCCPGWGG 69
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
478-758 6.36e-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: 56.60  E-value: 6.36e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433501    478 EERLATLAGEL--SHDSASPGRSARPLV----QTELAVLEQRLVSLETSCTpsttsaildSLVAEVKAWQSRSEALLRQV 551
Cdd:TIGR02168  644 GYRIVTLDGDLvrPGGVITGGSAKTNSSilerRREIEELEEKIEELEEKIA---------ELEKALAELRKELEELEEEL 714
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433501    552 ASHAALLQQLNGTVAEVQGQLA--EGTGSSLQGEITLLKVNLNSVSKSLTGLSDSVSQYSDAFLAAntsldererkvEAE 629
Cdd:TIGR02168  715 EQLRKELEELSRQISALRKDLArlEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEA-----------EAE 783
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433501    630 VQAIQEQVSSQGSRLQAGHRQVLNLRGELEQLKAGVAKVASGLSRCQDTAQKLQHTVGHFDQRVAQVEGacrRLGLLAAG 709
Cdd:TIGR02168  784 IEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSE---DIESLAAE 860
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 45433501    710 LDSLPTEPLRPREGLWSHVDQlnrtLAQHTQDIARLRDDLLDCQAQLAE 758
Cdd:TIGR02168  861 IEELEELIEELESELEALLNE----RASLEEALALLRSELEELSEELRE 905
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
470-664 1.28e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.68  E-value: 1.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433501  470 LEERVQSLE------ERLATLAGELSHDSAspGRSARPL--VQTELAVLEQRLVSLETSctpsttsaiLDSLVAEVKAWQ 541
Cdd:COG4913  247 AREQIELLEpirelaERYAAARERLAELEY--LRAALRLwfAQRRLELLEAELEELRAE---------LARLEAELERLE 315
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433501  542 SRSEALLRQVAS-HAALLQQLNGTVAEVQGQLAEgtgssLQGEITLLKVNLNSVSKSLTGLSDSVSQYSDAFLAANTSLD 620
Cdd:COG4913  316 ARLDALREELDElEAQIRGNGGDRLEQLEREIER-----LERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAA 390
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 45433501  621 ERERKVEAEVQAIQEQVSSQGSRLQAGHRQVLNLRGELEQLKAG 664
Cdd:COG4913  391 ALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
320-574 4.31e-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: 43.89  E-value: 4.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433501    320 EQKLQGVQSECDLRVQEVRRQCEEGQAASRRLHQsLDGRELALRQELSQLGSQLQGLSVSgRGSCCGQLALINARMDGLE 399
Cdd:TIGR02168  697 EKALAELRKELEELEEELEQLRKELEELSRQISA-LRKDLARLEAEVEQLEERIAQLSKE-LTELEAEIEELEERLEEAE 774
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433501    400 RALQAVTETQRGPGAPAGDELTRLSAamLEGGVDGLLEGLETLNGTEGGARGCCLRLDMGGWGVGGFGTMLEERVQSLEE 479
Cdd:TIGR02168  775 EELAEAEAEIEELEAQIEQLKEELKA--LREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSE 852
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433501    480 RLATLAGELSHDSASPGRSARPL--VQTELAVLEQRLVSLETSCtpSTTSAILDSLVAEVKAWQSRSEALLRQVASHAAL 557
Cdd:TIGR02168  853 DIESLAAEIEELEELIEELESELeaLLNERASLEEALALLRSEL--EELSEELRELESKRSELRRELEELREKLAQLELR 930
                          250
                   ....*....|....*..
gi 45433501    558 LQQLNGTVAEVQGQLAE 574
Cdd:TIGR02168  931 LEGLEVRIDNLQERLSE 947
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
543-703 5.12e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 40.20  E-value: 5.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433501  543 RSEALLRQVAShaaLLQQLNGTVAEVQGQLAEGTGS--SLQGEITLLKVNLNSVSKSLtglsdsvSQYSDAFLAANTSLD 620
Cdd:PRK04778 102 KAKHEINEIES---LLDLIEEDIEQILEELQELLESeeKNREEVEQLKDLYRELRKSL-------LANRFSFGPALDELE 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433501  621 ERERKVEAEVQAIqEQVSSQGSRLQAgHRQVLNLRGELEQLKAGVAKVASGLSRCQDTaqklqhtvghFDQRVAQVEGAC 700
Cdd:PRK04778 172 KQLENLEEEFSQF-VELTESGDYVEA-REILDQLEEELAALEQIMEEIPELLKELQTE----------LPDQLQELKAGY 239

                 ...
gi 45433501  701 RRL 703
Cdd:PRK04778 240 REL 242
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
358-703 7.87e-03

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: 39.77  E-value: 7.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433501    358 RELALRQELSQLGSQLQGLSVSGRGsccgQLALINARMDGLERALQAVTETQRGPGAPAGDELTRLSAAM-----LEGGV 432
Cdd:pfam01576  198 KEEKGRQELEKAKRKLEGESTDLQE----QIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALkkireLEAQI 273
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433501    433 DGLLEGLETlngtEGGARGcclrldmggwgvggfgtMLEERVQSLEERLATLAGEL--SHDSASPGRSARPLVQTELAVL 510
Cdd:pfam01576  274 SELQEDLES----ERAARN-----------------KAEKQRRDLGEELEALKTELedTLDTTAAQQELRSKREQEVTEL 332
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433501    511 EQRLVSLETSCTPSTT------SAILDSLVAEVK-------AWQSRSEALLRQVASHAA---LLQQ-----------LNG 563
Cdd:pfam01576  333 KKALEEETRSHEAQLQemrqkhTQALEELTEQLEqakrnkaNLEKAKQALESENAELQAelrTLQQakqdsehkrkkLEG 412
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433501    564 TVAEVQGQLAEGTG---------SSLQGEITLLKVNLNSVSKSLTGLSDSV----SQYSDA--FLAANT----SLDERER 624
Cdd:pfam01576  413 QLQELQARLSESERqraelaeklSKLQSELESVSSLLNEAEGKNIKLSKDVssleSQLQDTqeLLQEETrqklNLSTRLR 492
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45433501    625 KVEAEVQAIQEQVSSQGSRLQAGHRQVLNLRGELEQLKAGVAKVASGLSRCQDTAQKLQHTVGHFDQRVAQVEGACRRL 703
Cdd:pfam01576  493 QLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKL 571
 
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 ...
59-126 9.89e-21

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: 86.32  E-value: 9.89e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45433501    59 CAYvvhRNVTCILQEGAESYVKAEYRQ----CRWGPKCPgtvTYRTVLRPKYKVGYKTVTDLAWRCCPGFTG 126
Cdd:pfam07546   4 CAY---KVVSCVVVTGTESYVQPVYKPyltwCAGHRRCS---TYRTTYRPAYRQVYKTVTRLEWRCCPGWGG 69
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
478-758 6.36e-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: 56.60  E-value: 6.36e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433501    478 EERLATLAGEL--SHDSASPGRSARPLV----QTELAVLEQRLVSLETSCTpsttsaildSLVAEVKAWQSRSEALLRQV 551
Cdd:TIGR02168  644 GYRIVTLDGDLvrPGGVITGGSAKTNSSilerRREIEELEEKIEELEEKIA---------ELEKALAELRKELEELEEEL 714
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433501    552 ASHAALLQQLNGTVAEVQGQLA--EGTGSSLQGEITLLKVNLNSVSKSLTGLSDSVSQYSDAFLAAntsldererkvEAE 629
Cdd:TIGR02168  715 EQLRKELEELSRQISALRKDLArlEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEA-----------EAE 783
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433501    630 VQAIQEQVSSQGSRLQAGHRQVLNLRGELEQLKAGVAKVASGLSRCQDTAQKLQHTVGHFDQRVAQVEGacrRLGLLAAG 709
Cdd:TIGR02168  784 IEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSE---DIESLAAE 860
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 45433501    710 LDSLPTEPLRPREGLWSHVDQlnrtLAQHTQDIARLRDDLLDCQAQLAE 758
Cdd:TIGR02168  861 IEELEELIEELESELEALLNE----RASLEEALALLRSELEELSEELRE 905
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
470-674 7.61e-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: 56.22  E-value: 7.61e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433501    470 LEERVQSLEERLATLAGELSHDSASP--GRSARPLVQTELAVLEQRLVSLEtsctpsttsAILDSLVAEVKAWQSRSEAL 547
Cdd:TIGR02168  300 LEQQKQILRERLANLERQLEELEAQLeeLESKLDELAEELAELEEKLEELK---------EELESLEAELEELEAELEEL 370
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433501    548 LRQVASHAALLQQLNGTVAEVQGQLAegtgsSLQGEITLLKVNLNSVSKSLTGLSDSVSQYSDAFLAAN-----TSLDER 622
Cdd:TIGR02168  371 ESRLEELEEQLETLRSKVAQLELQIA-----SLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAElkelqAELEEL 445
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 45433501    623 ER---KVEAEVQAIQEQVSSQGSRLQAGHRQVLNLRGELEQLKAGVAKVASGLSR 674
Cdd:TIGR02168  446 EEeleELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQEN 500
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
470-664 1.28e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.68  E-value: 1.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433501  470 LEERVQSLE------ERLATLAGELSHDSAspGRSARPL--VQTELAVLEQRLVSLETSctpsttsaiLDSLVAEVKAWQ 541
Cdd:COG4913  247 AREQIELLEpirelaERYAAARERLAELEY--LRAALRLwfAQRRLELLEAELEELRAE---------LARLEAELERLE 315
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433501  542 SRSEALLRQVAS-HAALLQQLNGTVAEVQGQLAEgtgssLQGEITLLKVNLNSVSKSLTGLSDSVSQYSDAFLAANTSLD 620
Cdd:COG4913  316 ARLDALREELDElEAQIRGNGGDRLEQLEREIER-----LERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAA 390
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 45433501  621 ERERKVEAEVQAIQEQVSSQGSRLQAGHRQVLNLRGELEQLKAG 664
Cdd:COG4913  391 ALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
320-663 1.92e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.93  E-value: 1.92e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433501 320 EQKLQGVQ---SECDLRVQEVRRQCE--EGQAASRRLHQSLDGRELALRQELSQLgsQLQGLSvsgrgsccGQLALINAR 394
Cdd:COG1196 178 ERKLEATEenlERLEDILGELERQLEplERQAEKAERYRELKEELKELEAELLLL--KLRELE--------AELEELEAE 247
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433501 395 MDGLERALQAVTETQRGpgapAGDELTRLSAAMLEggvdgLLEGLETLNGTEggargccLRLDMGGWGVGGFGTMLEERV 474
Cdd:COG1196 248 LEELEAELEELEAELAE----LEAELEELRLELEE-----LELELEEAQAEE-------YELLAELARLEQDIARLEERR 311
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433501 475 QSLEERLATLAGELSHDSASPG--RSARPLVQTELAVLEQRLVSLETSctPSTTSAILDSLVAEVKAWQSRSEALLRQVA 552
Cdd:COG1196 312 RELEERLEELEEELAELEEELEelEEELEELEEELEEAEEELEEAEAE--LAEAEEALLEAEAELAEAEEELEELAEELL 389
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433501 553 SHAALLQQLNGTVAEVQGQLAEgtgssLQGEITLLKVNLNSVSKSLTGLSDSVsqysDAFLAANTSLDERERKVEAEVQA 632
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEA-----LLERLERLEEELEELEEALAELEEEE----EEEEEALEEAAEEEAELEEEEEA 460
                       330       340       350
                ....*....|....*....|....*....|.
gi 45433501 633 IQEQVSSQGSRLQAGHRQVLNLRGELEQLKA 663
Cdd:COG1196 461 LLELLAELLEEAALLEAALAELLEELAEAAA 491
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
580-755 2.74e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.52  E-value: 2.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433501  580 LQGEITLLKVNLNSVSKSLTGLSDSVSQYSDAFLAANTSLDERE-----RKVEAEVQAIQEQVSsqgsRLQAGHRQVLNL 654
Cdd:COG4913  615 LEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWdeidvASAEREIAELEAELE----RLDASSDDLAAL 690
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433501  655 RGELEQLKAGVAKVASGLSRCQDTAQKLQHTVGHFDQRVAQVEGACRRLGLLAAGLDSLPTEPLRPREGLWSHVDQLNRT 734
Cdd:COG4913  691 EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELREN 770
                        170       180
                 ....*....|....*....|....*
gi 45433501  735 LAQHTQD----IARLRDDLLDCQAQ 755
Cdd:COG4913  771 LEERIDAlrarLNRAEEELERAMRA 795
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
320-574 4.31e-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: 43.89  E-value: 4.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433501    320 EQKLQGVQSECDLRVQEVRRQCEEGQAASRRLHQsLDGRELALRQELSQLGSQLQGLSVSgRGSCCGQLALINARMDGLE 399
Cdd:TIGR02168  697 EKALAELRKELEELEEELEQLRKELEELSRQISA-LRKDLARLEAEVEQLEERIAQLSKE-LTELEAEIEELEERLEEAE 774
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433501    400 RALQAVTETQRGPGAPAGDELTRLSAamLEGGVDGLLEGLETLNGTEGGARGCCLRLDMGGWGVGGFGTMLEERVQSLEE 479
Cdd:TIGR02168  775 EELAEAEAEIEELEAQIEQLKEELKA--LREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSE 852
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433501    480 RLATLAGELSHDSASPGRSARPL--VQTELAVLEQRLVSLETSCtpSTTSAILDSLVAEVKAWQSRSEALLRQVASHAAL 557
Cdd:TIGR02168  853 DIESLAAEIEELEELIEELESELeaLLNERASLEEALALLRSEL--EELSEELRELESKRSELRRELEELREKLAQLELR 930
                          250
                   ....*....|....*..
gi 45433501    558 LQQLNGTVAEVQGQLAE 574
Cdd:TIGR02168  931 LEGLEVRIDNLQERLSE 947
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
470-681 3.02e-03

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: 40.52  E-value: 3.02e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433501 470 LEERVQSLEERLATLAGELSHDsaspgRSARPLVQTELAVLEQRLVSLEtsctpsttsaildslvAEVKAWQSRSEALLR 549
Cdd:COG4942  25 AEAELEQLQQEIAELEKELAAL-----KKEEKALLKQLAALERRIAALA----------------RRIRALEQELAALEA 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433501 550 QVASHAALLQQLNGTVAEVQGQLAEGTGSS-LQGEITLLKVNLNsvSKSLTGLSDSVsQYSDAFLAANTSLDERERKVEA 628
Cdd:COG4942  84 ELAELEKEIAELRAELEAQKEELAELLRALyRLGRQPPLALLLS--PEDFLDAVRRL-QYLKYLAPARREQAEELRADLA 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 45433501 629 EVQAIQEQVSSQGSRLQAGHRQVLNLRGELEQLKAGVAKVASGLSRCQDTAQK 681
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAA 213
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
470-682 4.54e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.39  E-value: 4.54e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433501 470 LEERVQSLEERLATLAGELS-----HDSASPgrsarplvQTELAVLEQRLVSLETSctpsttsaildslVAEVKAWQSRS 544
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEefrqkNGLVDL--------SEEAKLLLQQLSELESQ-------------LAEARAELAEA 238
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433501 545 EALLRQvashaaLLQQLNGTVAEVQGQLAEGTGSSLQGEITLLKVNLNSVSKSLTGLSDSVsqysdafLAANTSLDERER 624
Cdd:COG3206 239 EARLAA------LRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDV-------IALRAQIAALRA 305
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45433501 625 KVEAEVQAIQEQVSSQGSRLQAghrQVLNLRGELEQLKAGVAKVA------SGLSRCQDTAQKL 682
Cdd:COG3206 306 QLQQEAQRILASLEAELEALQA---REASLQAQLAQLEARLAELPeleaelRRLEREVEVAREL 366
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
543-761 4.95e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 4.95e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433501 543 RSEALLRQVASHAALLQQLNGTVAEVQGQLAEgtgssLQGEITLLKVNLNSVSKSLTGLSDSVSQYSDAFLAANtsldER 622
Cdd:COG1196 219 KEELKELEAELLLLKLRELEAELEELEAELEE-----LEAELEELEAELAELEAELEELRLELEELELELEEAQ----AE 289
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433501 623 ERKVEAEVQAIQEQVSSQGSRLQAGHRQVLNLRGELEQLKAGVAKVASGLSRCQDTAQKLQHTVGHFDQRVAQVEGacRR 702
Cdd:COG1196 290 EYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE--AL 367
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 45433501 703 LGLLAAgldslptepLRPREGLWshvDQLNRTLAQHTQDIARLRDDLLDCQAQLAEQVR 761
Cdd:COG1196 368 LEAEAE---------LAEAEEEL---EELAEELLEALRAAAELAAQLEELEEAEEALLE 414
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
543-703 5.12e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 40.20  E-value: 5.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433501  543 RSEALLRQVAShaaLLQQLNGTVAEVQGQLAEGTGS--SLQGEITLLKVNLNSVSKSLtglsdsvSQYSDAFLAANTSLD 620
Cdd:PRK04778 102 KAKHEINEIES---LLDLIEEDIEQILEELQELLESeeKNREEVEQLKDLYRELRKSL-------LANRFSFGPALDELE 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433501  621 ERERKVEAEVQAIqEQVSSQGSRLQAgHRQVLNLRGELEQLKAGVAKVASGLSRCQDTaqklqhtvghFDQRVAQVEGAC 700
Cdd:PRK04778 172 KQLENLEEEFSQF-VELTESGDYVEA-REILDQLEEELAALEQIMEEIPELLKELQTE----------LPDQLQELKAGY 239

                 ...
gi 45433501  701 RRL 703
Cdd:PRK04778 240 REL 242
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
248-709 7.33e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 7.33e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433501 248 LDEILSKVTEVSNTLQTKVQLLDKVHGLalghEAHLQRLREAPPSPLTSLALLEEYVD-RRLHRLWGSL---LDGFEQKL 323
Cdd:COG4717  73 LKELEEELKEAEEKEEEYAELQEELEEL----EEELEELEAELEELREELEKLEKLLQlLPLYQELEALeaeLAELPERL 148
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433501 324 QGVQSEcDLRVQEVRRQCEEGQAASRRLHQSLD----GRELALRQELSQLGSQLQGLSvsgrgsccGQLALINARMDGLE 399
Cdd:COG4717 149 EELEER-LEELRELEEELEELEAELAELQEELEelleQLSLATEEELQDLAEELEELQ--------QRLAELEEELEEAQ 219
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433501 400 RALQAVTE--TQRGPGAPAGDELTRLSAAMLEGGVDGLLEGLETLNGTEGGARG-------------CCLRLDMGGWGVG 464
Cdd:COG4717 220 EELEELEEelEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILtiagvlflvlgllALLFLLLAREKAS 299
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433501 465 GFGTMLEERVQSLEERLAT-----LAGELSHDSASPGRSARPLVQT--ELAVLEQRLVSLETSCTPSTTSAILDSLVAEV 537
Cdd:COG4717 300 LGKEAEELQALPALEELEEeeleeLLAALGLPPDLSPEELLELLDRieELQELLREAEELEEELQLEELEQEIAALLAEA 379
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433501 538 KAwqsRSEALLRQVASHAALLQQLNGTVAEVQGQLAEGTGSSLQGEITLLKVNLNsvsksltglsdsvsqysdaflAANT 617
Cdd:COG4717 380 GV---EDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELE---------------------EELE 435
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433501 618 SLDERERKVEAEVQAIQEQVSSQGSRLQA--GHRQVLNLRGELEQLKAGVAKVASGLSRCQDTAQKLQHTVGHF-DQRVA 694
Cdd:COG4717 436 ELEEELEELEEELEELREELAELEAELEQleEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYrEERLP 515
                       490
                ....*....|....*.
gi 45433501 695 QV-EGACRRLGLLAAG 709
Cdd:COG4717 516 PVlERASEYFSRLTDG 531
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
358-703 7.87e-03

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: 39.77  E-value: 7.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433501    358 RELALRQELSQLGSQLQGLSVSGRGsccgQLALINARMDGLERALQAVTETQRGPGAPAGDELTRLSAAM-----LEGGV 432
Cdd:pfam01576  198 KEEKGRQELEKAKRKLEGESTDLQE----QIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALkkireLEAQI 273
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433501    433 DGLLEGLETlngtEGGARGcclrldmggwgvggfgtMLEERVQSLEERLATLAGEL--SHDSASPGRSARPLVQTELAVL 510
Cdd:pfam01576  274 SELQEDLES----ERAARN-----------------KAEKQRRDLGEELEALKTELedTLDTTAAQQELRSKREQEVTEL 332
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433501    511 EQRLVSLETSCTPSTT------SAILDSLVAEVK-------AWQSRSEALLRQVASHAA---LLQQ-----------LNG 563
Cdd:pfam01576  333 KKALEEETRSHEAQLQemrqkhTQALEELTEQLEqakrnkaNLEKAKQALESENAELQAelrTLQQakqdsehkrkkLEG 412
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433501    564 TVAEVQGQLAEGTG---------SSLQGEITLLKVNLNSVSKSLTGLSDSV----SQYSDA--FLAANT----SLDERER 624
Cdd:pfam01576  413 QLQELQARLSESERqraelaeklSKLQSELESVSSLLNEAEGKNIKLSKDVssleSQLQDTqeLLQEETrqklNLSTRLR 492
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45433501    625 KVEAEVQAIQEQVSSQGSRLQAGHRQVLNLRGELEQLKAGVAKVASGLSRCQDTAQKLQHTVGHFDQRVAQVEGACRRL 703
Cdd:pfam01576  493 QLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKL 571
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
527-663 8.63e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.12  E-value: 8.63e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433501 527 SAILDSLVAE-VKAWQSRSEALLRQVASHAALLQQLNGTVAEVQGQLAEGTG----------------SSLQGEITLLKV 589
Cdd:COG4372  22 TGILIAALSEqLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSeleqleeeleelneqlQAAQAELAQAQE 101
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45433501 590 NLNSVSKSLTGLSDSVSQYSdaflAANTSLDERERKVEAEVQAIQEQVSSQGSRLQAGHRQVLNLRGELEQLKA 663
Cdd:COG4372 102 ELESLQEEAEELQEELEELQ----KERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQ 171
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
524-681 9.04e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.04  E-value: 9.04e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433501 524 STTSAILDSLVAEVKAWQSRSEALLRQVASHAALLQQLNGTVAEVQGQLAEgtgssLQGEITLLKVNLNSV--------- 594
Cdd:COG3883  26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAE-----AEAEIEERREELGERaralyrsgg 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45433501 595 ----------SKSLTGLSDSVSqYSDAFLAANTSLDERERKVEAEVQAIQEQVSSQGSRLQAGHRQVLNLRGELEQLKAG 664
Cdd:COG3883 101 svsyldvllgSESFSDFLDRLS-ALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAE 179
                       170
                ....*....|....*..
gi 45433501 665 VAKVASGLSRCQDTAQK 681
Cdd:COG3883 180 QEALLAQLSAEEAAAEA 196
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH