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Conserved domains on  [gi|1034577848|ref|XP_006719289|]
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rab-3A-interacting protein isoform X1 [Homo sapiens]

Protein Classification

Graphical summary

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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 ...
 316-508 5.76e-148

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: 421.25  E-value: 5.76e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034577848 316 GHTRNKSTSSAMSGSHQDLSVIQPIVKDCKEADLSLYNEFRLWKDEPTMDRTCPFLDKIYQEDIFPCLTFSKSELASAVL 395
Cdd:cd21068     1 GHARNKSTSSAMSGSHQDLSVIQPIVKDCKEADLSLYNEFRLWKEEPTMDRTCPFLDRIYQEDIFPCLTFSKSELASAVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034577848 396 EAVENNTLSIEPVGLQPIRFVKASAVECGGPKKCALTGQSKSCKHRIKLGDSSNYYYISPFCRYRITSVCNFFTYIRYIQ 475
Cdd:cd21068    81 EAVENNTLSIEPVGLQPLRFVKASAVECGGPKKCALSGQTKSCKHRIKLGDSSNYYYISPFCRYRITSVCNFFTYIRYIQ 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1034577848 476 QGLVKQQDVDQMFWEVMQLRKEMSLAKLGYFKE 508
Cdd:cd21068   161 QGLVKQQDVDQMFWEVMQLRKEMSLAKLGYYKE 193
Sec2p super family cl05764
GDP/GTP exchange factor Sec2p; In Saccharomyces cerevisiae, Sec2p is a GDP/GTP exchange factor ...
 223-291 1.90e-13

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: 66.05  E-value: 1.90e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034577848 223 KLKDEECERLS--KVRDQLGQELEELTASLFEEAHKMV----REANIKQATAEK---QLKEAQGKIDVLQAEVAALKT 291
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 ...
 316-508 5.76e-148

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: 421.25  E-value: 5.76e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034577848 316 GHTRNKSTSSAMSGSHQDLSVIQPIVKDCKEADLSLYNEFRLWKDEPTMDRTCPFLDKIYQEDIFPCLTFSKSELASAVL 395
Cdd:cd21068     1 GHARNKSTSSAMSGSHQDLSVIQPIVKDCKEADLSLYNEFRLWKEEPTMDRTCPFLDRIYQEDIFPCLTFSKSELASAVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034577848 396 EAVENNTLSIEPVGLQPIRFVKASAVECGGPKKCALTGQSKSCKHRIKLGDSSNYYYISPFCRYRITSVCNFFTYIRYIQ 475
Cdd:cd21068    81 EAVENNTLSIEPVGLQPLRFVKASAVECGGPKKCALSGQTKSCKHRIKLGDSSNYYYISPFCRYRITSVCNFFTYIRYIQ 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1034577848 476 QGLVKQQDVDQMFWEVMQLRKEMSLAKLGYFKE 508
Cdd:cd21068   161 QGLVKQQDVDQMFWEVMQLRKEMSLAKLGYYKE 193
Sec2p pfam06428
GDP/GTP exchange factor Sec2p; In Saccharomyces cerevisiae, Sec2p is a GDP/GTP exchange factor ...
 223-291 1.90e-13

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: 66.05  E-value: 1.90e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034577848 223 KLKDEECERLS--KVRDQLGQELEELTASLFEEAHKMV----REANIKQATAEK---QLKEAQGKIDVLQAEVAALKT 291
Cdd:pfam06428   1 ELKEEKKKRLEaeKEKKKLEKELEDLTASLFEEANKMVaaarREKHAVEIKNDQlkeQLKEKETLLESLQEQLKELKQ 78
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
209-291 1.78e-08

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 56.45  E-value: 1.78e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034577848 209 ERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLfEEAHKMVREANIKQATAEKQLKEAQGKIDVLQAEVAA 288
Cdd:COG4372    41 DKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL-EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEE 119


                  ...
gi 1034577848 289 LKT 291
Cdd:COG4372   120 LQK 122
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
192-290 1.18e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.05  E-value: 1.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034577848 192 LSRLRSPSVLEVREKGYERLKEELAKAQRELKLKDEECERLSKvrdqlgqELEELTASLFEEAHKMVREANIKQ----AT 267
Cdd:PRK03918  605 LELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRK-------ELEELEKKYSEEEYEELREEYLELsrelAG 677

                          90       100
                  ....*....|....*....|...
gi 1034577848 268 AEKQLKEAQGKIDVLQAEVAALK 290
Cdd:PRK03918  678 LRAELEELEKRREEIKKTLEKLK 700
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 183-291 3.10e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.52  E-value: 3.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034577848  183 DIF---GLSTDSLSRLRSPSVLEVREKG-YERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLfEEAHKMV 258
Cdd:TIGR02169  647 ELFeksGAMTGGSRAPRGGILFSRSEPAeLQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKI-GEIEKEI 725

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1034577848  259 REANIKQATAEKQLKEAQGKIDVLQAEVAALKT 291
Cdd:TIGR02169  726 EQLEQEEEKLKERLEELEEDLSSLEQEIENVKS 758
UBAN cd09803
polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) ...
 208-290 3.06e-03

polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) is a regulatory subunit of the kinase complex IKK, which is involved in the activation of NF-kappaB via phosporylation of inhibitory IkappaBs. This mechanism requires the binding of NEMO to ubiquinated substrates. Binding is achieved via the UBAN motif (ubiquitin binding in ABIN and NEMO), which is described in this model. This region of NEMO has also been named CoZi (for coiled-coil 2 and leucine zipper). ABINs (A20-binding inhibitors of NF-kappaB) are sensors for ubiquitin that are involved in regulation of apoptosis, ABIN-1 is presumed to inhibit signalling via the NF-kappaB route. The UBAN motif is also found in optineurin, the product of a gene associated with glaucoma, which has been characterized as a negative regulator of NF-kappaB as well.


Pssm-ID: 197361 [Multi-domain]  Cd Length: 87  Bit Score: 36.94  E-value: 3.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034577848 208 YERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELT-----ASLFEEAHKMVREANIKQATAEKQLKEaqgKIDVL 282
Cdd:cd09803     3 IDELAARLQEAEEALALKQEDIDELKEEIAQQEADLETIPvlkaqAEIYKSDFEAERAAREKLHQEKEQLAE---QLEYL 79


                  ....*...
gi 1034577848 283 QAEVAALK 290
Cdd:cd09803    80 QRENQELK 87
 
Name Accession Description Interval E-value
Rab11BD_RAB3IP cd21068
Rab11 binding domain of Rab-3A-interacting protein (RAB3IP); RAB3IP, also called Rabin-3, or ...
 316-508 5.76e-148

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: 421.25  E-value: 5.76e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034577848 316 GHTRNKSTSSAMSGSHQDLSVIQPIVKDCKEADLSLYNEFRLWKDEPTMDRTCPFLDKIYQEDIFPCLTFSKSELASAVL 395
Cdd:cd21068     1 GHARNKSTSSAMSGSHQDLSVIQPIVKDCKEADLSLYNEFRLWKEEPTMDRTCPFLDRIYQEDIFPCLTFSKSELASAVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034577848 396 EAVENNTLSIEPVGLQPIRFVKASAVECGGPKKCALTGQSKSCKHRIKLGDSSNYYYISPFCRYRITSVCNFFTYIRYIQ 475
Cdd:cd21068    81 EAVENNTLSIEPVGLQPLRFVKASAVECGGPKKCALSGQTKSCKHRIKLGDSSNYYYISPFCRYRITSVCNFFTYIRYIQ 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1034577848 476 QGLVKQQDVDQMFWEVMQLRKEMSLAKLGYFKE 508
Cdd:cd21068   161 QGLVKQQDVDQMFWEVMQLRKEMSLAKLGYYKE 193
Rab11BD_RAB3IL1 cd21069
Rab11 binding domain of Rab-3A-interacting-like protein 1 (RAB3IL1); RAB3IL1, also called ...
 343-506 1.27e-93

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: 1.27e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034577848 343 DCKEADLSLYNEFRLWKDEPTMDRTCPFLDKIYQEDIFPCLTFSKSELASAVLEAVENNTLSIEPVGLQPIRFVKASAVE 422
Cdd:cd21069     1 EGKEVDTVLFAEFQAWKESPTLDRSCPFLSRIYREDIGPCLDFTKRELSDLVQSAVENNTLTIEPVASQALPVVKASAVE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034577848 423 CGGPKKCALTGQSKSCKHRIKLGDSSNYYYISPFCRYRITSVCNFFTYIRYIQQGLVKqQDVDQMFWEVMQLRKEMSLAK 502
Cdd:cd21069    81 CGGPKKCALSGLSRTCRHRIKLGDSGNYYYISPSCRARITAVCNFFTYIRYIQQGLVR-QDAEQMFWEVMRLRREMSLAK 159


                  ....
gi 1034577848 503 LGYF 506
Cdd:cd21069   160 LGFY 163
Rab11BD_RAB3IP_like cd21044
Rab11 binding domain of Rab-3A-interacting protein (RAB3IP), Rab-3A-interacting-like protein 1 ...
 345-504 2.20e-57

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: 188.73  E-value: 2.20e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034577848 345 KEADLSLYNEFRLWKDEP-----TMDRTCPFLDKIYQEDIFPCLTFSKS----ELASAVLEAVENNTLSIEPVGLQPIRF 415
Cdd:cd21044     1 FEVDLVLFEEFQEFLKAPsslslSLLKSSPFLKRILAEDIEPCLRFDPAllnwLLKKRLLAAILENTLEIEPISGSTETS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034577848 416 VK------ASAVECGGPKKCALTGQSK--SCKHRIKLGDS-SNYYYISPFCRYRITSVCNFFTYIRYIQQGLVKQQDVDQ 486
Cdd:cd21044    81 SSsnntapVSSPPPASPKKCALCGESRldACLYRLRLSDSdSEWYPICSYCRNRLRAVCDFFAYLRYIRQGLVKSRSIEK 160

                         170
                  ....*....|....*...
gi 1034577848 487 MFWEVMQLRKEMSLAKLG 504
Cdd:cd21044   161 LYLEILRLRLRMFLARLG 178
Sec2p pfam06428
GDP/GTP exchange factor Sec2p; In Saccharomyces cerevisiae, Sec2p is a GDP/GTP exchange factor ...
 223-291 1.90e-13

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: 66.05  E-value: 1.90e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034577848 223 KLKDEECERLS--KVRDQLGQELEELTASLFEEAHKMV----REANIKQATAEK---QLKEAQGKIDVLQAEVAALKT 291
Cdd:pfam06428   1 ELKEEKKKRLEaeKEKKKLEKELEDLTASLFEEANKMVaaarREKHAVEIKNDQlkeQLKEKETLLESLQEQLKELKQ 78
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
209-291 1.78e-08

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 56.45  E-value: 1.78e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034577848 209 ERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLfEEAHKMVREANIKQATAEKQLKEAQGKIDVLQAEVAA 288
Cdd:COG4372    41 DKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL-EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEE 119


                  ...
gi 1034577848 289 LKT 291
Cdd:COG4372   120 LQK 122
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
190-290 1.02e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 54.92  E-value: 1.02e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034577848  190 DSLSRLRSPSVLEVREKGYERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLfeEAHKMVREANIKQ--AT 267
Cdd:COG4913    272 AELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQI--RGNGGDRLEQLEReiER 349

                           90       100
                   ....*....|....*....|...
gi 1034577848  268 AEKQLKEAQGKIDVLQAEVAALK 290
Cdd:COG4913    350 LERELEERERRRARLEALLAALG 372
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 209-293 1.98e-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: 53.23  E-value: 1.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034577848 209 ERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLfEEAHKMVREANIKQATAEKQLKEAQGKIDVLQAEVAA 288
Cdd:COG4942    23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRI-AALARRIRALEQELAALEAELAELEKEIAELRAELEA 101


                  ....*
gi 1034577848 289 LKTLV 293
Cdd:COG4942   102 QKEEL 106
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
201-304 7.18e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 51.44  E-value: 7.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034577848 201 LEVREKGYERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLfEEAHKMVREANIKQATAEKQLKEAQGKID 280
Cdd:COG4372    82 LEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQR-KQLEAQIAELQSEIAEREEELKELEEQLE 160

                          90       100
                  ....*....|....*....|....
gi 1034577848 281 VLQAEVAALKTLVLSSSPTSPTQE 304
Cdd:COG4372   161 SLQEELAALEQELQALSEAEAEQA 184
DivIVA COG3599
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle ...
 202-290 2.32e-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: 46.77  E-value: 2.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034577848 202 EVRE------KGYERLKEELAKAQRELKLKDEECERLSKVRDQLGQEL-------EELTASLFEEAHKMVREANIKqatA 268
Cdd:COG3599    24 EVDEfldevaEDYERLIRENKELKEKLEELEEELEEYRELEETLQKTLvvaqetaEEVKENAEKEAELIIKEAELE---A 100

                          90       100
                  ....*....|....*....|..
gi 1034577848 269 EKQLKEAQGKIDVLQAEVAALK 290
Cdd:COG3599   101 EKIIEEAQEKARKIVREIEELK 122
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 201-291 2.66e-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: 48.77  E-value: 2.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034577848 201 LEVREKGYERLKEELAKAQRELKLKDEECE----RLSKVRDQLGQ------------ELEELTASLfEEAHKMVREANIK 264
Cdd:COG1579    40 LAALEARLEAAKTELEDLEKEIKRLELEIEeveaRIKKYEEQLGNvrnnkeyealqkEIESLKRRI-SDLEDEILELMER 118

                          90       100
                  ....*....|....*....|....*..
gi 1034577848 265 QATAEKQLKEAQGKIDVLQAEVAALKT 291
Cdd:COG1579   119 IEELEEELAELEAELAELEAELEEKKA 145
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 201-290 3.45e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 3.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034577848 201 LEVREKGYERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLFEEAHKMVREANIKQATAEkQLKEAQGKID 280
Cdd:COG1196   241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE-RRRELEERLE 319

                          90
                  ....*....|
gi 1034577848 281 VLQAEVAALK 290
Cdd:COG1196   320 ELEEELAELE 329
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 208-289 4.20e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 4.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034577848 208 YERLKEELAKAQRELKL-----KDEECERLSKVRDQLGQELEELTASLfEEAHKMVREANIKQATAEKQLKEAQGKIDVL 282
Cdd:COG1196   215 YRELKEELKELEAELLLlklreLEAELEELEAELEELEAELEELEAEL-AELEAELEELRLELEELELELEEAQAEEYEL 293


                  ....*..
gi 1034577848 283 QAEVAAL 289
Cdd:COG1196   294 LAELARL 300
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 201-289 6.51e-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: 6.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034577848 201 LEVREKGYERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLfEEAHKMVREANIKQATAEKQLKEAQGKID 280
Cdd:COG1196   283 LEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL-EELEEELEELEEELEEAEEELEEAEAELA 361


                  ....*....
gi 1034577848 281 VLQAEVAAL 289
Cdd:COG1196   362 EAEEALLEA 370
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 191-288 7.40e-05

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 45.55  E-value: 7.40e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034577848  191 SLSRLRSP-----SVLEVREKGYERLKEELAKAQRELK-----LKDEECE---RLSKVRDQLGQELEELTASL--FEEah 255
Cdd:pfam01576  177 SLSKLKNKheamiSDLEERLKKEEKGRQELEKAKRKLEgestdLQEQIAElqaQIAELRAQLAKKEEELQAALarLEE-- 254

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1034577848  256 kmvrEANIKqATAEKQLKEAQGKIDVLQAEVAA 288
Cdd:pfam01576  255 ----ETAQK-NNALKKIRELEAQISELQEDLES 282
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 205-290 7.67e-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: 7.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034577848 205 EKGYERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLfEEAHKMVREANIKQATAEKQLKEAQGKIDVLQA 284
Cdd:COG1196   301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL-EEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379


                  ....*.
gi 1034577848 285 EVAALK 290
Cdd:COG1196   380 ELEELA 385
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
204-291 7.88e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.14  E-value: 7.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034577848 204 REKGYERLKEELAKAQRELKLKDEECERLS---KVRDQLGQELEELTASLFEEAHKMVREANIKQATAEKQLKEAQGKID 280
Cdd:COG4717   123 KLLQLLPLYQELEALEAELAELPERLEELEerlEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELE 202

                          90
                  ....*....|.
gi 1034577848 281 VLQAEVAALKT 291
Cdd:COG4717   203 ELQQRLAELEE 213
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 193-298 1.01e-04

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 45.07  E-value: 1.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034577848 193 SRLR-----SPSVLEVREKGYERLKEELAKAQRELKLKDEEceRLSKVRDQLGQELEELTAslFEEAHKMVREANIKQAT 267
Cdd:COG0542   400 ARVRmeidsKPEELDELERRLEQLEIEKEALKKEQDEASFE--RLAELRDELAELEEELEA--LKARWEAEKELIEEIQE 475

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1034577848 268 AEKQLKEAQGKIDVLQAEVAALKTLVLSSSP 298
Cdd:COG0542   476 LKEELEQRYGKIPELEKELAELEEELAELAP 506
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
192-290 1.18e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.05  E-value: 1.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034577848 192 LSRLRSPSVLEVREKGYERLKEELAKAQRELKLKDEECERLSKvrdqlgqELEELTASLFEEAHKMVREANIKQ----AT 267
Cdd:PRK03918  605 LELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRK-------ELEELEKKYSEEEYEELREEYLELsrelAG 677

                          90       100
                  ....*....|....*....|...
gi 1034577848 268 AEKQLKEAQGKIDVLQAEVAALK 290
Cdd:PRK03918  678 LRAELEELEKRREEIKKTLEKLK 700
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
209-290 1.23e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.91  E-value: 1.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034577848  209 ERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEElTASLFEEAHKMVRE-----------ANIKQATAEKQLKEAQG 277
Cdd:COG4913    341 EQLEREIERLERELEERERRRARLEALLAALGLPLPA-SAEEFAALRAEAAAllealeeeleaLEEALAEAEAALRDLRR 419

                           90
                   ....*....|...
gi 1034577848  278 KIDVLQAEVAALK 290
Cdd:COG4913    420 ELRELEAEIASLE 432
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
189-290 1.66e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.37  E-value: 1.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034577848 189 TDSLSRLRSPSVLEVREKGYERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELtaslfeEAHKMVREANIKQATA 268
Cdd:COG4717   408 EEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQL------EEDGELAELLQELEEL 481

                          90       100
                  ....*....|....*....|..
gi 1034577848 269 EKQLKEAQGKIDVLQAEVAALK 290
Cdd:COG4717   482 KAELRELAEEWAALKLALELLE 503
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 208-290 2.62e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 2.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034577848 208 YERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLFEEAHKmVREANIKQATAEKQLKEAQGKIDVLQAEVA 287
Cdd:COG1196   234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELE-LEEAQAEEYELLAELARLEQDIARLEERRR 312


                  ...
gi 1034577848 288 ALK 290
Cdd:COG1196   313 ELE 315
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
201-295 2.88e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.60  E-value: 2.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034577848 201 LEVREKGYERLK---EELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLFEEAHKMVREANIKQATAEKQLKEAQG 277
Cdd:COG4717   141 LAELPERLEELEerlEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE 220

                          90
                  ....*....|....*...
gi 1034577848 278 KIDVLQAEVAALKTLVLS 295
Cdd:COG4717   221 ELEELEEELEQLENELEA 238
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 183-291 3.10e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.52  E-value: 3.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034577848  183 DIF---GLSTDSLSRLRSPSVLEVREKG-YERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLfEEAHKMV 258
Cdd:TIGR02169  647 ELFeksGAMTGGSRAPRGGILFSRSEPAeLQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKI-GEIEKEI 725

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1034577848  259 REANIKQATAEKQLKEAQGKIDVLQAEVAALKT 291
Cdd:TIGR02169  726 EQLEQEEEKLKERLEELEEDLSSLEQEIENVKS 758
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 216-293 3.32e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.89  E-value: 3.32e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034577848 216 AKAQRELKLKDEECERLSKVRDQLGQELEELTASLfEEAHKMVREANIKQATAEKQLKEAQGKIDVLQAEVAALKTLV 293
Cdd:COG3883    12 AFADPQIQAKQKELSELQAELEAAQAELDALQAEL-EELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL 88
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
193-291 4.41e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.98  E-value: 4.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034577848  193 SRLRSPSVL--EVREKgYERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEEL------------TASL------FE 252
Cdd:COG4913    596 RRIRSRYVLgfDNRAK-LAALEAELAELEEELAEAEERLEALEAELDALQERREALqrlaeyswdeidVASAereiaeLE 674

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1034577848  253 EAHKMVREANIKQATAEKQLKEAQGKIDVLQAEVAALKT 291
Cdd:COG4913    675 AELERLDASSDDLAALEEQLEELEAELEELEEELDELKG 713
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 201-288 4.53e-04

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: 39.90  E-value: 4.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034577848 201 LEVREKGYErlkEELAKAQREL------------KLK--DEECERLSKVRdqlgQELEELTASLFEEAHKMVREanikQA 266
Cdd:pfam20492  11 LEERLKQYE---EETKKAQEELeeseetaeeleeERRqaEEEAERLEQKR----QEAEEEKERLEESAEMEAEE----KE 79

                          90       100
                  ....*....|....*....|..
gi 1034577848 267 TAEKQLKEAQGKIDVLQAEVAA 288
Cdd:pfam20492  80 QLEAELAEAQEEIARLEEEVER 101
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
201-292 4.66e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 4.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034577848 201 LEVREKGYERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELtaslfeEAHKMVREANIKQATAEKQLKEAQGKID 280
Cdd:COG4717    76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL------EKLLQLLPLYQELEALEAELAELPERLE 149

                          90
                  ....*....|..
gi 1034577848 281 VLQAEVAALKTL 292
Cdd:COG4717   150 ELEERLEELREL 161
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 209-289 6.46e-04

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: 40.16  E-value: 6.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034577848 209 ERLKEELAKAQREL--KLKDEECER---LSKVRDQLGQELEELTASLFEEAHKMVREAnikQATAEKQLKEAqgkIDVLQ 283
Cdd:COG0711    44 ERAKEEAEAALAEYeeKLAEARAEAaeiIAEARKEAEAIAEEAKAEAEAEAERIIAQA---EAEIEQERAKA---LAELR 117


                  ....*.
gi 1034577848 284 AEVAAL 289
Cdd:COG0711   118 AEVADL 123
flagell_FliJ TIGR02473
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ...
 199-292 7.11e-04

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: 39.99  E-value: 7.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034577848 199 SVLEVREKGYERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTAS------------LFEEAHKMVREANIKQA 266
Cdd:TIGR02473   6 KLLDLREKEEEQAKLELAKAQAEFERLETQLQQLIKYREEYEQQALEKVGAgtsalelsnyqrFIRQLDQRIQQQQQELA 85

                          90       100
                  ....*....|....*....|....*.
gi 1034577848 267 TAEKQLKEAQGKIDVLQAEVAALKTL 292
Cdd:TIGR02473  86 LLQQEVEAKRERLLEARRELKALEKL 111
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 200-290 7.98e-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: 42.35  E-value: 7.98e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034577848  200 VLEVREKGYERLKEELAKAQRELKLKDEECE---RLSKVR-DQLGQELEELTASLfeeahkmvREANIKQATAEKQLKEA 275
Cdd:TIGR02168  194 ILNELERQLKSLERQAEKAERYKELKAELRElelALLVLRlEELREELEELQEEL--------KEAEEELEELTAELQEL 265

                           90
                   ....*....|....*
gi 1034577848  276 QGKIDVLQAEVAALK 290
Cdd:TIGR02168  266 EEKLEELRLEVSELE 280
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
205-293 9.10e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 9.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034577848 205 EKGYERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLfeeahkmvreANIKQATAE-KQLKEAQGKIDVLQ 283
Cdd:PRK03918  658 EEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEEL----------EEREKAKKElEKLEKALERVEELR 727

                          90
                  ....*....|
gi 1034577848 284 AEVAALKTLV 293
Cdd:PRK03918  728 EKVKKYKALL 737
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
213-291 1.21e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 1.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034577848 213 EELAKAQRELKLKDEECERLSKVRDQLGQELEELTASL----FEEAHKMVREANIKQATAEKQLKEAQGKIDVLQAEVAA 288
Cdd:COG4717   385 EELRAALEQAEEYQELKEELEELEEQLEELLGELEELLealdEEELEEELEELEEELEELEEELEELREELAELEAELEQ 464


                  ...
gi 1034577848 289 LKT 291
Cdd:COG4717   465 LEE 467
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 205-291 1.25e-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: 41.59  E-value: 1.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034577848  205 EKGYERLKEELAKAQRELKLKDEECERLSKVRDQLG---------------QELEELTASLfEEAHKMVREANIKQATAE 269
Cdd:TIGR02169  243 ERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNkkikdlgeeeqlrvkEKIGELEAEI-ASLERSIAEKERELEDAE 321

                           90       100
                   ....*....|....*....|..
gi 1034577848  270 KQLKEAQGKIDVLQAEVAALKT 291
Cdd:TIGR02169  322 ERLAKLEAEIDKLLAEIEELER 343
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 209-292 1.41e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 1.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034577848 209 ERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLFEEAHKMVREANIKQATAEKQLKEAQGKIDVLQAEVAA 288
Cdd:COG1196   319 EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL 398


                  ....
gi 1034577848 289 LKTL 292
Cdd:COG1196   399 AAQL 402
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 201-290 1.56e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 1.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034577848 201 LEVREKGYERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLfEEAHKMVREANIKQATAEKQLKEAQGKID 280
Cdd:COG1196   234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL-EEAQAEEYELLAELARLEQDIARLEERRR 312

                          90
                  ....*....|
gi 1034577848 281 VLQAEVAALK 290
Cdd:COG1196   313 ELEERLEELE 322
UBAN cd09803
polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) ...
 208-290 3.06e-03

polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) is a regulatory subunit of the kinase complex IKK, which is involved in the activation of NF-kappaB via phosporylation of inhibitory IkappaBs. This mechanism requires the binding of NEMO to ubiquinated substrates. Binding is achieved via the UBAN motif (ubiquitin binding in ABIN and NEMO), which is described in this model. This region of NEMO has also been named CoZi (for coiled-coil 2 and leucine zipper). ABINs (A20-binding inhibitors of NF-kappaB) are sensors for ubiquitin that are involved in regulation of apoptosis, ABIN-1 is presumed to inhibit signalling via the NF-kappaB route. The UBAN motif is also found in optineurin, the product of a gene associated with glaucoma, which has been characterized as a negative regulator of NF-kappaB as well.


Pssm-ID: 197361 [Multi-domain]  Cd Length: 87  Bit Score: 36.94  E-value: 3.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034577848 208 YERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELT-----ASLFEEAHKMVREANIKQATAEKQLKEaqgKIDVL 282
Cdd:cd09803     3 IDELAARLQEAEEALALKQEDIDELKEEIAQQEADLETIPvlkaqAEIYKSDFEAERAAREKLHQEKEQLAE---QLEYL 79


                  ....*...
gi 1034577848 283 QAEVAALK 290
Cdd:cd09803    80 QRENQELK 87
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 208-305 3.08e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.81  E-value: 3.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034577848 208 YERLKEELAKAQRELklkDEECERLSKVRDQLGQELEELTASLfEEAHKMVREANIKQATAEKQLKEAQGKIDVLQAEVA 287
Cdd:COG3883   138 LKADKAELEAKKAEL---EAKLAELEALKAELEAAKAELEAQQ-AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAA 213

                          90
                  ....*....|....*...
gi 1034577848 288 ALKTLVLSSSPTSPTQEP 305
Cdd:COG3883   214 AAAAAAAAAAAAAAAAAA 231
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 199-250 3.19e-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: 40.16  E-value: 3.19e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1034577848  199 SVLEVREKGYERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASL 250
Cdd:pfam01576  538 GTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDL 589
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
209-292 3.66e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 39.84  E-value: 3.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034577848 209 ERLKEELAKAQRELKLKDEECERLSKvrdqlgqELEELTASLFEEAHKMvREANIKQATA---EKQLKEAQGKIDVLQAE 285
Cdd:COG2433   423 ERLEAEVEELEAELEEKDERIERLER-------ELSEARSEERREIRKD-REISRLDREIerlERELEEERERIEELKRK 494


                  ....*..
gi 1034577848 286 VAALKTL 292
Cdd:COG2433   495 LERLKEL 501
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 208-289 3.73e-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: 40.04  E-value: 3.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034577848  208 YERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTA------SLFEEAHKMVREANIKQATAEKQLKEAQGKIDV 281
Cdd:TIGR02168  234 LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLevseleEEIEELQKELYALANEISRLEQQKQILRERLAN 313


                   ....*...
gi 1034577848  282 LQAEVAAL 289
Cdd:TIGR02168  314 LERQLEEL 321
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
202-290 3.89e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.90  E-value: 3.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034577848  202 EVREKGYERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLfEEAHKMVREanikqatAEKQLKEAQG-KID 280
Cdd:COG4913    270 RLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARL-DALREELDE-------LEAQIRGNGGdRLE 341

                           90
                   ....*....|
gi 1034577848  281 VLQAEVAALK 290
Cdd:COG4913    342 QLEREIERLE 351
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 201-280 4.17e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 39.81  E-value: 4.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034577848 201 LEVREKGYERLKEELAKAQRELKlkdeecERLSKVRDQLGQELEELTASLFEEAHKMVREANIKQ-----ATAEKQLKEA 275
Cdd:PRK00409  539 AEALLKEAEKLKEELEEKKEKLQ------EEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQLQkggyaSVKAHELIEA 612


                  ....*
gi 1034577848 276 QGKID 280
Cdd:PRK00409  613 RKRLN 617
TMF_TATA_bd pfam12325
TATA element modulatory factor 1 TATA binding; This is the C-terminal conserved coiled coil ...
 209-292 4.26e-03

TATA element modulatory factor 1 TATA binding; This is the C-terminal conserved coiled coil region of a family of TATA element modulatory factor 1 proteins conserved in eukaryotes. The proteins bind to the TATA element of some RNA polymerase II promoters and repress their activity. by competing with the binding of TATA binding protein. TMF1_TATA_bd is the most conserved part of the TMFs. TMFs are evolutionarily conserved golgins that bind Rab6, a ubiquitous ras-like GTP-binding Golgi protein, and contribute to Golgi organization in animal and plant cells. The Rab6-binding domain appears to be the same region as this C-terminal family.


Pssm-ID: 432481 [Multi-domain]  Cd Length: 115  Bit Score: 37.14  E-value: 4.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034577848 209 ERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLfEEahkmVREANIKQATAEKQLKEAQGKIDV------- 281
Cdd:pfam12325  15 ERLSSTIRRLEGELASLKEELARLEAQRDEARQEIVKLMKEN-EE----LKELKKELEELEKELKELEQRYETtlellge 89

                          90
                  ....*....|....*...
gi 1034577848 282 -------LQAEVAALKTL 292
Cdd:pfam12325  90 kseeveeLKADVEDLKEM 107
DivIVA pfam05103
DivIVA protein; The Bacillus subtilis divIVA1 mutation causes misplacement of the septum ...
 202-290 4.28e-03

DivIVA protein; The Bacillus subtilis divIVA1 mutation causes misplacement of the septum during cell division, resulting in the formation of small, circular, anucleate mini-cells. Inactivation of divIVA produces a mini-cell phenotype, whereas overproduction of DivIVA results in a filamentation phenotype. These proteins appear to contain coiled-coils.


Pssm-ID: 428304 [Multi-domain]  Cd Length: 131  Bit Score: 37.55  E-value: 4.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034577848 202 EVRE------KGYERLKEELAKAQRELKLKDEECERLSKVRDQLGQEL-------EELTASLFEEAHKMVREANIKqatA 268
Cdd:pfam05103  22 EVDEfldqvaEDYEALIRENAELKEKIEELEEKLAHYKNLEETLQNTLilaqetaEEVKANAQKEAELIIKEAEAK---A 98

                          90       100
                  ....*....|....*....|..
gi 1034577848 269 EKQLKEAQGKIDVLQAEVAALK 290
Cdd:pfam05103  99 ERIVDDANNEVKKINDEIEELK 120
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 209-290 4.62e-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: 39.65  E-value: 4.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034577848  209 ERLK---EELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLFEEAHKMVREANIKQATAEKQLKEAQGKIDVLQAE 285
Cdd:TIGR02168  189 DRLEdilNELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEK 268


                   ....*
gi 1034577848  286 VAALK 290
Cdd:TIGR02168  269 LEELR 273
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 209-289 5.50e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.53  E-value: 5.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034577848 209 ERLKEELAKAQRELKLKDE----ECERLSKVRDQLGQELEELTASLfEEAHKMVREANIKQATAEKQLKEAQGKIDVLQA 284
Cdd:COG1196   203 EPLERQAEKAERYRELKEElkelEAELLLLKLRELEAELEELEAEL-EELEAELEELEAELAELEAELEELRLELEELEL 281


                  ....*
gi 1034577848 285 EVAAL 289
Cdd:COG1196   282 ELEEA 286
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
202-291 8.70e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 38.87  E-value: 8.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034577848 202 EVREKGYERLkEELAKAQRELKLKDEECERLSKVRDQLGQELEELT---ASLFEEAHKMVREANIKQATAEKQLKEAQ-- 276
Cdd:PRK02224  492 EEVEERLERA-EDLVEAEDRIERLEERREDLEELIAERRETIEEKReraEELRERAAELEAEAEEKREAAAEAEEEAEea 570

                          90
                  ....*....|....*.
gi 1034577848 277 -GKIDVLQAEVAALKT 291
Cdd:PRK02224  571 rEEVAELNSKLAELKE 586
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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