NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|41281856|ref|NP_783322|]
View 

rab-3A-interacting protein isoform alpha 2 [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Rab11BD_RAB3IP cd21068
Rab11 binding domain of Rab-3A-interacting protein (RAB3IP); RAB3IP, also called Rabin-3, or ...
 282-474 1.06e-147

Rab11 binding domain of Rab-3A-interacting protein (RAB3IP); RAB3IP, also called Rabin-3, or SSX2-interacting protein, or Rabin8, acts as a guanine nucleotide exchange factor (GEF) which promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form. It mediates the release of GDP from RAB8A and RAB8B but not from RAB3A or RAB5. It modulates actin organization and promotes polarized transport of RAB8A-specific vesicles to the cell surface. The model corresponds to the Rab11a/Rab11b-binding region of RAB3IP lies within its carboxy-terminus, a region distinct from its GEF domain and Rab3a-binding region.


:

Pssm-ID: 411032  Cd Length: 193  Bit Score: 419.32  E-value: 1.06e-147
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281856 282 GHTRNKSTSSAMSGSHQDLSVIQPIVKDCKEADLSLYNEFRLWKDEPTMDRTCPFLDKIYQEDIFPCLTFSKSELASAVL 361
Cdd:cd21068   1 GHARNKSTSSAMSGSHQDLSVIQPIVKDCKEADLSLYNEFRLWKEEPTMDRTCPFLDRIYQEDIFPCLTFSKSELASAVL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281856 362 EAVENNTLSIEPVGLQPIRFVKASAVECGGPKKCALTGQSKSCKHRIKLGDSSNYYYISPFCRYRITSVCNFFTYIRYIQ 441
Cdd:cd21068  81 EAVENNTLSIEPVGLQPLRFVKASAVECGGPKKCALSGQTKSCKHRIKLGDSSNYYYISPFCRYRITSVCNFFTYIRYIQ 160

                       170       180       190
                ....*....|....*....|....*....|...
gi 41281856 442 QGLVKQQDVDQMFWEVMQLRKEMSLAKLGYFKE 474
Cdd:cd21068 161 QGLVKQQDVDQMFWEVMQLRKEMSLAKLGYYKE 193
Sec2p super family cl05764
GDP/GTP exchange factor Sec2p; In Saccharomyces cerevisiae, Sec2p is a GDP/GTP exchange factor ...
 189-257 1.43e-12

GDP/GTP exchange factor Sec2p; In Saccharomyces cerevisiae, Sec2p is a GDP/GTP exchange factor for Sec4p, which is required for vesicular transport at the post-Golgi stage of yeast secretion.


The actual alignment was detected with superfamily member pfam06428:

Pssm-ID: 428938 [Multi-domain]  Cd Length: 92  Bit Score: 63.36  E-value: 1.43e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41281856   189 KLKDEECERLS--KVRDQLGQELEELTASLFEEAHKMV----REANIKQATAEK---QLKEAQGKIDVLQAEVAALKT 257
Cdd:pfam06428   1 ELKEEKKKRLEaeKEKKKLEKELEDLTASLFEEANKMVaaarREKHAVEIKNDQlkeQLKEKETLLESLQEQLKELKQ 78
 
Name Accession Description Interval E-value
Rab11BD_RAB3IP cd21068
Rab11 binding domain of Rab-3A-interacting protein (RAB3IP); RAB3IP, also called Rabin-3, or ...
 282-474 1.06e-147

Rab11 binding domain of Rab-3A-interacting protein (RAB3IP); RAB3IP, also called Rabin-3, or SSX2-interacting protein, or Rabin8, acts as a guanine nucleotide exchange factor (GEF) which promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form. It mediates the release of GDP from RAB8A and RAB8B but not from RAB3A or RAB5. It modulates actin organization and promotes polarized transport of RAB8A-specific vesicles to the cell surface. The model corresponds to the Rab11a/Rab11b-binding region of RAB3IP lies within its carboxy-terminus, a region distinct from its GEF domain and Rab3a-binding region.


Pssm-ID: 411032  Cd Length: 193  Bit Score: 419.32  E-value: 1.06e-147
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281856 282 GHTRNKSTSSAMSGSHQDLSVIQPIVKDCKEADLSLYNEFRLWKDEPTMDRTCPFLDKIYQEDIFPCLTFSKSELASAVL 361
Cdd:cd21068   1 GHARNKSTSSAMSGSHQDLSVIQPIVKDCKEADLSLYNEFRLWKEEPTMDRTCPFLDRIYQEDIFPCLTFSKSELASAVL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281856 362 EAVENNTLSIEPVGLQPIRFVKASAVECGGPKKCALTGQSKSCKHRIKLGDSSNYYYISPFCRYRITSVCNFFTYIRYIQ 441
Cdd:cd21068  81 EAVENNTLSIEPVGLQPLRFVKASAVECGGPKKCALSGQTKSCKHRIKLGDSSNYYYISPFCRYRITSVCNFFTYIRYIQ 160

                       170       180       190
                ....*....|....*....|....*....|...
gi 41281856 442 QGLVKQQDVDQMFWEVMQLRKEMSLAKLGYFKE 474
Cdd:cd21068 161 QGLVKQQDVDQMFWEVMQLRKEMSLAKLGYYKE 193
Sec2p pfam06428
GDP/GTP exchange factor Sec2p; In Saccharomyces cerevisiae, Sec2p is a GDP/GTP exchange factor ...
 189-257 1.43e-12

GDP/GTP exchange factor Sec2p; In Saccharomyces cerevisiae, Sec2p is a GDP/GTP exchange factor for Sec4p, which is required for vesicular transport at the post-Golgi stage of yeast secretion.


Pssm-ID: 428938 [Multi-domain]  Cd Length: 92  Bit Score: 63.36  E-value: 1.43e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41281856   189 KLKDEECERLS--KVRDQLGQELEELTASLFEEAHKMV----REANIKQATAEK---QLKEAQGKIDVLQAEVAALKT 257
Cdd:pfam06428   1 ELKEEKKKRLEaeKEKKKLEKELEDLTASLFEEANKMVaaarREKHAVEIKNDQlkeQLKEKETLLESLQEQLKELKQ 78
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
156-256 1.26e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 54.54  E-value: 1.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281856  156 DSLSRLRSPSVLEVREKGYERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLfeEAHKMVREANIKQ--AT 233
Cdd:COG4913  272 AELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQI--RGNGGDRLEQLEReiER 349

                         90       100
                 ....*....|....*....|...
gi 41281856  234 AEKQLKEAQGKIDVLQAEVAALK 256
Cdd:COG4913  350 LERELEERERRRARLEALLAALG 372
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
158-256 4.10e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 4.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281856  158 LSRLRSPSVLEVREKGYERLKEELAKAQRELKLKDEECERLSKvrdqlgqELEELTASLFEEAHKMVREANIKQ----AT 233
Cdd:PRK03918 605 LELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRK-------ELEELEKKYSEEEYEELREEYLELsrelAG 677

                         90       100
                 ....*....|....*....|...
gi 41281856  234 AEKQLKEAQGKIDVLQAEVAALK 256
Cdd:PRK03918 678 LRAELEELEKRREEIKKTLEKLK 700
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 152-257 7.32e-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: 42.36  E-value: 7.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281856    152 GLSTDSLSRLRSPSVLEVREKG-YERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLfEEAHKMVREANIK 230
Cdd:TIGR02169  653 GAMTGGSRAPRGGILFSRSEPAeLQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKI-GEIEKEIEQLEQE 731

                           90       100
                   ....*....|....*....|....*..
gi 41281856    231 QATAEKQLKEAQGKIDVLQAEVAALKT 257
Cdd:TIGR02169  732 EEKLKERLEELEEDLSSLEQEIENVKS 758
 
Name Accession Description Interval E-value
Rab11BD_RAB3IP cd21068
Rab11 binding domain of Rab-3A-interacting protein (RAB3IP); RAB3IP, also called Rabin-3, or ...
 282-474 1.06e-147

Rab11 binding domain of Rab-3A-interacting protein (RAB3IP); RAB3IP, also called Rabin-3, or SSX2-interacting protein, or Rabin8, acts as a guanine nucleotide exchange factor (GEF) which promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form. It mediates the release of GDP from RAB8A and RAB8B but not from RAB3A or RAB5. It modulates actin organization and promotes polarized transport of RAB8A-specific vesicles to the cell surface. The model corresponds to the Rab11a/Rab11b-binding region of RAB3IP lies within its carboxy-terminus, a region distinct from its GEF domain and Rab3a-binding region.


Pssm-ID: 411032  Cd Length: 193  Bit Score: 419.32  E-value: 1.06e-147
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281856 282 GHTRNKSTSSAMSGSHQDLSVIQPIVKDCKEADLSLYNEFRLWKDEPTMDRTCPFLDKIYQEDIFPCLTFSKSELASAVL 361
Cdd:cd21068   1 GHARNKSTSSAMSGSHQDLSVIQPIVKDCKEADLSLYNEFRLWKEEPTMDRTCPFLDRIYQEDIFPCLTFSKSELASAVL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281856 362 EAVENNTLSIEPVGLQPIRFVKASAVECGGPKKCALTGQSKSCKHRIKLGDSSNYYYISPFCRYRITSVCNFFTYIRYIQ 441
Cdd:cd21068  81 EAVENNTLSIEPVGLQPLRFVKASAVECGGPKKCALSGQTKSCKHRIKLGDSSNYYYISPFCRYRITSVCNFFTYIRYIQ 160

                       170       180       190
                ....*....|....*....|....*....|...
gi 41281856 442 QGLVKQQDVDQMFWEVMQLRKEMSLAKLGYFKE 474
Cdd:cd21068 161 QGLVKQQDVDQMFWEVMQLRKEMSLAKLGYYKE 193
Rab11BD_RAB3IL1 cd21069
Rab11 binding domain of Rab-3A-interacting-like protein 1 (RAB3IL1); RAB3IL1, also called ...
 309-472 3.98e-94

Rab11 binding domain of Rab-3A-interacting-like protein 1 (RAB3IL1); RAB3IL1, also called guanine nucleotide exchange factor for Rab-3A (GRAB), or Rab3A-interacting-like protein 1, or Rabin3-like 1, acts as a guanine nucleotide exchange factor (GEF) which promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form. As a dual Rab-binding protein, RAB3IL1 could potentially link Rab3 and Rab11 and/or Rab8 and Rab11-mediated intracellular trafficking processes. It may activate RAB3A, a GTPase that regulates synaptic vesicle exocytosis. It may also activate RAB8A and RAB8B. In addition, RAB3IL1 interacts with InsP6K1 and plays a role for InsP7 in vesicle exocytosis. The model corresponds to the Rab11a/Rab11b-binding region of RAB3IL1 lies within its carboxy-terminus, a region distinct from its GEF domain and Rab3a-binding region.


Pssm-ID: 411033  Cd Length: 163  Bit Score: 281.75  E-value: 3.98e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281856 309 DCKEADLSLYNEFRLWKDEPTMDRTCPFLDKIYQEDIFPCLTFSKSELASAVLEAVENNTLSIEPVGLQPIRFVKASAVE 388
Cdd:cd21069   1 EGKEVDTVLFAEFQAWKESPTLDRSCPFLSRIYREDIGPCLDFTKRELSDLVQSAVENNTLTIEPVASQALPVVKASAVE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281856 389 CGGPKKCALTGQSKSCKHRIKLGDSSNYYYISPFCRYRITSVCNFFTYIRYIQQGLVKqQDVDQMFWEVMQLRKEMSLAK 468
Cdd:cd21069  81 CGGPKKCALSGLSRTCRHRIKLGDSGNYYYISPSCRARITAVCNFFTYIRYIQQGLVR-QDAEQMFWEVMRLRREMSLAK 159


                ....
gi 41281856 469 LGYF 472
Cdd:cd21069 160 LGFY 163
Rab11BD_RAB3IP_like cd21044
Rab11 binding domain of Rab-3A-interacting protein (RAB3IP), Rab-3A-interacting-like protein 1 ...
 311-470 5.57e-58

Rab11 binding domain of Rab-3A-interacting protein (RAB3IP), Rab-3A-interacting-like protein 1 (RAB3IL1) and similar proteins; The family includes RAB3IP and RAB3IL1, as well as Rab guanine nucleotide exchange factor SEC2 from yeast. RAB3IP, also called Rabin-3, or SSX2-interacting protein, or Rabin8, acts as a guanine nucleotide exchange factor (GEF) which promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form. It mediates the release of GDP from RAB8A and RAB8B but not from RAB3A or RAB5. It modulates actin organization and promotes polarized transport of RAB8A-specific vesicles to the cell surface. RAB3IL1, also called guanine nucleotide exchange factor for Rab-3A (GRAB), or Rab3A-interacting-like protein 1, or Rabin3-like 1, acts as a guanine nucleotide exchange factor (GEF) which promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form. As a dual Rab-binding protein, RAB3IL1 could potentially link Rab3 and Rab11 and/or Rab8 and Rab11-mediated intracellular trafficking processes. It may activate RAB3A, a GTPase that regulates synaptic vesicle exocytosis. It may also activate RAB8A and RAB8B. In addition, RAB3IL1 interacts with InsP6K1 and plays a role for InsP7 in vesicle exocytosis. SEC2 is a guanine nucleotide exchange factor for SEC4, catalyzing the dissociation of GDP from SEC4 and also potently promoting binding of GTP. Activation of SEC4 by SEC2 is needed for the directed transport of vesicles to sites of exocytosis. SEC2 binds the Rab GTPase YPT32 but does not have exchange activity on YPT32. The model corresponds to the Rab11a/Rab11b-binding region of family members which lies within the carboxy-terminus, a region distinct from their GEF domain and Rab3a-binding region.


Pssm-ID: 411031  Cd Length: 178  Bit Score: 189.11  E-value: 5.57e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281856 311 KEADLSLYNEFRLWKDEP-----TMDRTCPFLDKIYQEDIFPCLTFSKS----ELASAVLEAVENNTLSIEPVGLQPIRF 381
Cdd:cd21044   1 FEVDLVLFEEFQEFLKAPsslslSLLKSSPFLKRILAEDIEPCLRFDPAllnwLLKKRLLAAILENTLEIEPISGSTETS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281856 382 VK------ASAVECGGPKKCALTGQSK--SCKHRIKLGDS-SNYYYISPFCRYRITSVCNFFTYIRYIQQGLVKQQDVDQ 452
Cdd:cd21044  81 SSsnntapVSSPPPASPKKCALCGESRldACLYRLRLSDSdSEWYPICSYCRNRLRAVCDFFAYLRYIRQGLVKSRSIEK 160

                       170
                ....*....|....*...
gi 41281856 453 MFWEVMQLRKEMSLAKLG 470
Cdd:cd21044 161 LYLEILRLRLRMFLARLG 178
Sec2p pfam06428
GDP/GTP exchange factor Sec2p; In Saccharomyces cerevisiae, Sec2p is a GDP/GTP exchange factor ...
 189-257 1.43e-12

GDP/GTP exchange factor Sec2p; In Saccharomyces cerevisiae, Sec2p is a GDP/GTP exchange factor for Sec4p, which is required for vesicular transport at the post-Golgi stage of yeast secretion.


Pssm-ID: 428938 [Multi-domain]  Cd Length: 92  Bit Score: 63.36  E-value: 1.43e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41281856   189 KLKDEECERLS--KVRDQLGQELEELTASLFEEAHKMV----REANIKQATAEK---QLKEAQGKIDVLQAEVAALKT 257
Cdd:pfam06428   1 ELKEEKKKRLEaeKEKKKLEKELEDLTASLFEEANKMVaaarREKHAVEIKNDQlkeQLKEKETLLESLQEQLKELKQ 78
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
156-256 1.26e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 54.54  E-value: 1.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281856  156 DSLSRLRSPSVLEVREKGYERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLfeEAHKMVREANIKQ--AT 233
Cdd:COG4913  272 AELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQI--RGNGGDRLEQLEReiER 349

                         90       100
                 ....*....|....*....|...
gi 41281856  234 AEKQLKEAQGKIDVLQAEVAALK 256
Cdd:COG4913  350 LERELEERERRRARLEALLAALG 372
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
175-257 1.85e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 52.98  E-value: 1.85e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281856 175 ERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLfEEAHKMVREANIKQATAEKQLKEAQGKIDVLQAEVAA 254
Cdd:COG4372  41 DKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL-EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEE 119


                ...
gi 41281856 255 LKT 257
Cdd:COG4372 120 LQK 122
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 175-259 3.45e-07

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: 52.07  E-value: 3.45e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281856 175 ERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLfEEAHKMVREANIKQATAEKQLKEAQGKIDVLQAEVAA 254
Cdd:COG4942  23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRI-AALARRIRALEQELAALEAELAELEKEIAELRAELEA 101


                ....*
gi 41281856 255 LKTLV 259
Cdd:COG4942 102 QKEEL 106
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
167-270 6.40e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 48.36  E-value: 6.40e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281856 167 LEVREKGYERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLfEEAHKMVREANIKQATAEKQLKEAQGKID 246
Cdd:COG4372  82 LEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQR-KQLEAQIAELQSEIAEREEELKELEEQLE 160

                        90       100
                ....*....|....*....|....
gi 41281856 247 VLQAEVAALKTLVLSSSPTSPTQE 270
Cdd:COG4372 161 SLQEELAALEQELQALSEAEAEQA 184
DivIVA COG3599
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle ...
 168-256 7.73e-06

Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442818 [Multi-domain]  Cd Length: 125  Bit Score: 45.23  E-value: 7.73e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281856 168 EVRE------KGYERLKEELAKAQRELKLKDEECERLSKVRDQLGQEL-------EELTASLFEEAHKMVREANIKqatA 234
Cdd:COG3599  24 EVDEfldevaEDYERLIRENKELKEKLEELEEELEEYRELEETLQKTLvvaqetaEEVKENAEKEAELIIKEAELE---A 100

                        90       100
                ....*....|....*....|..
gi 41281856 235 EKQLKEAQGKIDVLQAEVAALK 256
Cdd:COG3599 101 EKIIEEAQEKARKIVREIEELK 122
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 167-257 9.60e-06

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 46.84  E-value: 9.60e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281856 167 LEVREKGYERLKEELAKAQRELKLKDEECE----RLSKVRDQLGQ------------ELEELTASLfEEAHKMVREANIK 230
Cdd:COG1579  40 LAALEARLEAAKTELEDLEKEIKRLELEIEeveaRIKKYEEQLGNvrnnkeyealqkEIESLKRRI-SDLEDEILELMER 118

                        90       100
                ....*....|....*....|....*..
gi 41281856 231 QATAEKQLKEAQGKIDVLQAEVAALKT 257
Cdd:COG1579 119 IEELEEELAELEAELAELEAELEEKKA 145
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 167-256 5.28e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.08  E-value: 5.28e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281856 167 LEVREKGYERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLFEEAHKMVREANIKQATAEkQLKEAQGKID 246
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE-RRRELEERLE 319

                        90
                ....*....|
gi 41281856 247 VLQAEVAALK 256
Cdd:COG1196 320 ELEEELAELE 329
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 174-255 6.95e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.70  E-value: 6.95e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281856 174 YERLKEELAKAQRELKL-----KDEECERLSKVRDQLGQELEELTASLfEEAHKMVREANIKQATAEKQLKEAQGKIDVL 248
Cdd:COG1196 215 YRELKEELKELEAELLLlklreLEAELEELEAELEELEAELEELEAEL-AELEAELEELRLELEELELELEEAQAEEYEL 293


                ....*..
gi 41281856 249 QAEVAAL 255
Cdd:COG1196 294 LAELARL 300
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 167-255 9.48e-05

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: 9.48e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281856 167 LEVREKGYERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLfEEAHKMVREANIKQATAEKQLKEAQGKID 246
Cdd:COG1196 283 LEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL-EELEEELEELEEELEEAEEELEEAEAELA 361


                ....*....
gi 41281856 247 VLQAEVAAL 255
Cdd:COG1196 362 EAEEALLEA 370
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 171-256 1.14e-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: 1.14e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281856 171 EKGYERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLfEEAHKMVREANIKQATAEKQLKEAQGKIDVLQA 250
Cdd:COG1196 301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL-EEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379


                ....*.
gi 41281856 251 EVAALK 256
Cdd:COG1196 380 ELEELA 385
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 159-264 1.18e-04

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 44.69  E-value: 1.18e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281856 159 SRLR-----SPSVLEVREKGYERLKEELAKAQRELKLKDEEceRLSKVRDQLGQELEELTAslFEEAHKMVREANIKQAT 233
Cdd:COG0542 400 ARVRmeidsKPEELDELERRLEQLEIEKEALKKEQDEASFE--RLAELRDELAELEEELEA--LKARWEAEKELIEEIQE 475

                        90       100       110
                ....*....|....*....|....*....|.
gi 41281856 234 AEKQLKEAQGKIDVLQAEVAALKTLVLSSSP 264
Cdd:COG0542 476 LKEELEQRYGKIPELEKELAELEEELAELAP 506
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
170-257 1.51e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.37  E-value: 1.51e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281856 170 REKGYERLKEELAKAQRELKLKDEECERLS---KVRDQLGQELEELTASLFEEAHKMVREANIKQATAEKQLKEAQGKID 246
Cdd:COG4717 123 KLLQLLPLYQELEALEAELAELPERLEELEerlEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELE 202

                        90
                ....*....|.
gi 41281856 247 VLQAEVAALKT 257
Cdd:COG4717 203 ELQQRLAELEE 213
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
175-256 1.52e-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: 1.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281856  175 ERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEElTASLFEEAHKMVRE-----------ANIKQATAEKQLKEAQG 243
Cdd:COG4913  341 EQLEREIERLERELEERERRRARLEALLAALGLPLPA-SAEEFAALRAEAAAllealeeeleaLEEALAEAEAALRDLRR 419

                         90
                 ....*....|...
gi 41281856  244 KIDVLQAEVAALK 256
Cdd:COG4913  420 ELRELEAEIASLE 432
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
155-256 3.06e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.22  E-value: 3.06e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281856 155 TDSLSRLRSPSVLEVREKGYERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELtaslfeEAHKMVREANIKQATA 234
Cdd:COG4717 408 EEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQL------EEDGELAELLQELEEL 481

                        90       100
                ....*....|....*....|..
gi 41281856 235 EKQLKEAQGKIDVLQAEVAALK 256
Cdd:COG4717 482 KAELRELAEEWAALKLALELLE 503
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 174-256 4.02e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 4.02e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281856 174 YERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLFEEAHKmVREANIKQATAEKQLKEAQGKIDVLQAEVA 253
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELE-LEEAQAEEYELLAELARLEQDIARLEERRR 312


                ...
gi 41281856 254 ALK 256
Cdd:COG1196 313 ELE 315
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
158-256 4.10e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 4.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281856  158 LSRLRSPSVLEVREKGYERLKEELAKAQRELKLKDEECERLSKvrdqlgqELEELTASLFEEAHKMVREANIKQ----AT 233
Cdd:PRK03918 605 LELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRK-------ELEELEKKYSEEEYEELREEYLELsrelAG 677

                         90       100
                 ....*....|....*....|...
gi 41281856  234 AEKQLKEAQGKIDVLQAEVAALK 256
Cdd:PRK03918 678 LRAELEELEKRREEIKKTLEKLK 700
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 157-254 4.41e-04

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: 42.85  E-value: 4.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281856    157 SLSRLRSP-----SVLEVREKGYERLKEELAKAQRELK-----LKDEECE---RLSKVRDQLGQELEELTASL--FEEah 221
Cdd:pfam01576  177 SLSKLKNKheamiSDLEERLKKEEKGRQELEKAKRKLEgestdLQEQIAElqaQIAELRAQLAKKEEELQAALarLEE-- 254

                           90       100       110
                   ....*....|....*....|....*....|...
gi 41281856    222 kmvrEANIKqATAEKQLKEAQGKIDVLQAEVAA 254
Cdd:pfam01576  255 ----ETAQK-NNALKKIRELEAQISELQEDLES 282
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
167-261 5.51e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 5.51e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281856 167 LEVREKGYERLK---EELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLFEEAHKMVREANIKQATAEKQLKEAQG 243
Cdd:COG4717 141 LAELPERLEELEerlEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE 220

                        90
                ....*....|....*...
gi 41281856 244 KIDVLQAEVAALKTLVLS 261
Cdd:COG4717 221 ELEELEEELEQLENELEA 238
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
159-257 5.81e-04

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: 5.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281856  159 SRLRSPSVL--EVREKgYERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEEL------------TASL------FE 218
Cdd:COG4913  596 RRIRSRYVLgfDNRAK-LAALEAELAELEEELAEAEERLEALEAELDALQERREALqrlaeyswdeidVASAereiaeLE 674

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 41281856  219 EAHKMVREANIKQATAEKQLKEAQGKIDVLQAEVAALKT 257
Cdd:COG4913  675 AELERLDASSDDLAALEEQLEELEAELEELEEELDELKG 713
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 182-259 6.33e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.12  E-value: 6.33e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41281856 182 AKAQRELKLKDEECERLSKVRDQLGQELEELTASLfEEAHKMVREANIKQATAEKQLKEAQGKIDVLQAEVAALKTLV 259
Cdd:COG3883  12 AFADPQIQAKQKELSELQAELEAAQAELDALQAEL-EELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL 88
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 152-257 7.32e-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: 42.36  E-value: 7.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281856    152 GLSTDSLSRLRSPSVLEVREKG-YERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLfEEAHKMVREANIK 230
Cdd:TIGR02169  653 GAMTGGSRAPRGGILFSRSEPAeLQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKI-GEIEKEIEQLEQE 731

                           90       100
                   ....*....|....*....|....*..
gi 41281856    231 QATAEKQLKEAQGKIDVLQAEVAALKT 257
Cdd:TIGR02169  732 EEKLKERLEELEEDLSSLEQEIENVKS 758
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
167-258 8.12e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.06  E-value: 8.12e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281856 167 LEVREKGYERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELtaslfeEAHKMVREANIKQATAEKQLKEAQGKID 246
Cdd:COG4717  76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL------EKLLQLLPLYQELEALEAELAELPERLE 149

                        90
                ....*....|..
gi 41281856 247 VLQAEVAALKTL 258
Cdd:COG4717 150 ELEERLEELREL 161
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 175-255 1.51e-03

FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440475 [Multi-domain]  Cd Length: 152  Bit Score: 39.00  E-value: 1.51e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281856 175 ERLKEELAKAQREL--KLKDEECER---LSKVRDQLGQELEELTASLFEEAHKMVREAnikQATAEKQLKEAqgkIDVLQ 249
Cdd:COG0711  44 ERAKEEAEAALAEYeeKLAEARAEAaeiIAEARKEAEAIAEEAKAEAEAEAERIIAQA---EAEIEQERAKA---LAELR 117


                ....*.
gi 41281856 250 AEVAAL 255
Cdd:COG0711 118 AEVADL 123
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 166-256 1.68e-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: 1.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281856    166 VLEVREKGYERLKEELAKAQRELKLKDEECE---RLSKVR-DQLGQELEELTASLfeeahkmvREANIKQATAEKQLKEA 241
Cdd:TIGR02168  194 ILNELERQLKSLERQAEKAERYKELKAELRElelALLVLRlEELREELEELQEEL--------KEAEEELEELTAELQEL 265

                           90
                   ....*....|....*
gi 41281856    242 QGKIDVLQAEVAALK 256
Cdd:TIGR02168  266 EEKLEELRLEVSELE 280
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 175-258 1.89e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 1.89e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281856 175 ERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLFEEAHKMVREANIKQATAEKQLKEAQGKIDVLQAEVAA 254
Cdd:COG1196 319 EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL 398


                ....
gi 41281856 255 LKTL 258
Cdd:COG1196 399 AAQL 402
flagell_FliJ TIGR02473
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ...
 165-258 2.04e-03

flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly every case, in the midst of other flagellar biosynthesis genes in bacgterial genomes. Typically the fliJ gene is found adjacent to the gene for the flagellum-specific ATPase FliI. Sequence scoring in the gray zone between trusted and noise cutoffs include both probable FliJ proteins and components of bacterial type III secretion systems.


Pssm-ID: 131526 [Multi-domain]  Cd Length: 141  Bit Score: 38.45  E-value: 2.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281856   165 SVLEVREKGYERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTAS------------LFEEAHKMVREANIKQA 232
Cdd:TIGR02473   6 KLLDLREKEEEQAKLELAKAQAEFERLETQLQQLIKYREEYEQQALEKVGAgtsalelsnyqrFIRQLDQRIQQQQQELA 85

                          90       100
                  ....*....|....*....|....*.
gi 41281856   233 TAEKQLKEAQGKIDVLQAEVAALKTL 258
Cdd:TIGR02473  86 LLQQEVEAKRERLLEARRELKALEKL 111
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
179-257 2.17e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 2.17e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281856 179 EELAKAQRELKLKDEECERLSKVRDQLGQELEELTASL----FEEAHKMVREANIKQATAEKQLKEAQGKIDVLQAEVAA 254
Cdd:COG4717 385 EELRAALEQAEEYQELKEELEELEEQLEELLGELEELLealdEEELEEELEELEEELEELEEELEELREELAELEAELEQ 464


                ...
gi 41281856 255 LKT 257
Cdd:COG4717 465 LEE 467
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 167-256 2.24e-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: 2.24e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281856 167 LEVREKGYERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLfEEAHKMVREANIKQATAEKQLKEAQGKID 246
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL-EEAQAEEYELLAELARLEQDIARLEERRR 312

                        90
                ....*....|
gi 41281856 247 VLQAEVAALK 256
Cdd:COG1196 313 ELEERLEELE 322
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 171-257 2.89e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.44  E-value: 2.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281856    171 EKGYERLKEELAKAQRELKLKDEECERLSKVRDQLG---------------QELEELTASLfEEAHKMVREANIKQATAE 235
Cdd:TIGR02169  243 ERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNkkikdlgeeeqlrvkEKIGELEAEI-ASLERSIAEKERELEDAE 321

                           90       100
                   ....*....|....*....|..
gi 41281856    236 KQLKEAQGKIDVLQAEVAALKT 257
Cdd:TIGR02169  322 ERLAKLEAEIDKLLAEIEELER 343
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
171-259 2.99e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.05  E-value: 2.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281856  171 EKGYERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLfeeahkmvreANIKQATAE-KQLKEAQGKIDVLQ 249
Cdd:PRK03918 658 EEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEEL----------EEREKAKKElEKLEKALERVEELR 727

                         90
                 ....*....|
gi 41281856  250 AEVAALKTLV 259
Cdd:PRK03918 728 EKVKKYKALL 737
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 167-254 3.56e-03

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 37.21  E-value: 3.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281856   167 LEVREKGYErlkEELAKAQREL--------------KLKDEECERLSKVRdqlgQELEELTASLFEEAHKMVREanikQA 232
Cdd:pfam20492  11 LEERLKQYE---EETKKAQEELeeseetaeeleeerRQAEEEAERLEQKR----QEAEEEKERLEESAEMEAEE----KE 79

                          90       100
                  ....*....|....*....|..
gi 41281856   233 TAEKQLKEAQGKIDVLQAEVAA 254
Cdd:pfam20492  80 QLEAELAEAQEEIARLEEEVER 101
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
175-258 4.37e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 39.46  E-value: 4.37e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281856 175 ERLKEELAKAQRELKLKDEECERLSKvrdqlgqELEELTASLFEEAHKMvREANIKQATA---EKQLKEAQGKIDVLQAE 251
Cdd:COG2433 423 ERLEAEVEELEAELEEKDERIERLER-------ELSEARSEERREIRKD-REISRLDREIerlERELEEERERIEELKRK 494


                ....*..
gi 41281856 252 VAALKTL 258
Cdd:COG2433 495 LERLKEL 501
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
168-256 4.52e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.51  E-value: 4.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281856  168 EVREKGYERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLfEEAHKMVREanikqatAEKQLKEAQG-KID 246
Cdd:COG4913  270 RLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARL-DALREELDE-------LEAQIRGNGGdRLE 341

                         90
                 ....*....|
gi 41281856  247 VLQAEVAALK 256
Cdd:COG4913  342 QLEREIERLE 351
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 167-246 5.66e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 39.42  E-value: 5.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281856  167 LEVREKGYERLKEELAKAQRELKlkdeecERLSKVRDQLGQELEELTASLFEEAHKMVREANIKQ-----ATAEKQLKEA 241
Cdd:PRK00409 539 AEALLKEAEKLKEELEEKKEKLQ------EEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQLQkggyaSVKAHELIEA 612


                 ....*
gi 41281856  242 QGKID 246
Cdd:PRK00409 613 RKRLN 617
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 174-271 6.21e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 38.66  E-value: 6.21e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281856 174 YERLKEELAKAQRELklkDEECERLSKVRDQLGQELEELTASLfEEAHKMVREANIKQATAEKQLKEAQGKIDVLQAEVA 253
Cdd:COG3883 138 LKADKAELEAKKAEL---EAKLAELEALKAELEAAKAELEAQQ-AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAA 213

                        90
                ....*....|....*...
gi 41281856 254 ALKTLVLSSSPTSPTQEP 271
Cdd:COG3883 214 AAAAAAAAAAAAAAAAAA 231
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 174-255 6.71e-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: 39.27  E-value: 6.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281856    174 YERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTA------SLFEEAHKMVREANIKQATAEKQLKEAQGKIDV 247
Cdd:TIGR02168  234 LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLevseleEEIEELQKELYALANEISRLEQQKQILRERLAN 313


                   ....*...
gi 41281856    248 LQAEVAAL 255
Cdd:TIGR02168  314 LERQLEEL 321
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 165-216 7.06e-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: 39.00  E-value: 7.06e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 41281856    165 SVLEVREKGYERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASL 216
Cdd:pfam01576  538 GTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDL 589
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 175-256 7.63e-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: 38.88  E-value: 7.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281856    175 ERLK---EELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLFEEAHKMVREANIKQATAEKQLKEAQGKIDVLQAE 251
Cdd:TIGR02168  189 DRLEdilNELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEK 268


                   ....*
gi 41281856    252 VAALK 256
Cdd:TIGR02168  269 LEELR 273
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 175-255 8.00e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 38.76  E-value: 8.00e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281856 175 ERLKEELAKAQRELKLKDE----ECERLSKVRDQLGQELEELTASLfEEAHKMVREANIKQATAEKQLKEAQGKIDVLQA 250
Cdd:COG1196 203 EPLERQAEKAERYRELKEElkelEAELLLLKLRELEAELEELEAEL-EELEAELEELEAELAELEAELEELRLELEELEL 281


                ....*
gi 41281856 251 EVAAL 255
Cdd:COG1196 282 ELEEA 286
 
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