NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|15387686|emb|CAC59840|]
View 

SSX2 interacting protein RAB3IP, isoform gamma2 [Homo sapiens]

Protein Classification

guanine nucleotide exchange factor domain-containing protein( domain architecture ID 6052)

guanine nucleotide exchange factor (GEF) domain-containing protein, such as Saccharomyces cerevisiae Sec2p protein that is essential for the transport of proteins from the endoplasmic reticulum (ER) to the Golgi apparatus

Gene Ontology:  GO:0005085
PubMed:  17292842

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_like super family cl41767
Rab11 binding domain of Rab-3A-interacting protein (RAB3IP), Rab-3A-interacting-like protein 1 ...
 282-312 1.52e-12

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.


The actual alignment was detected with superfamily member cd21068:

Pssm-ID: 425398  Cd Length: 193  Bit Score: 65.33  E-value: 1.52e-12
                        10        20        30
                ....*....|....*....|....*....|.
gi 15387686 282 GHTRNKSTSSAMSGSHQDLSVIQPIVKDCKE 312
Cdd:cd21068   1 GHARNKSTSSAMSGSHQDLSVIQPIVKDCKE 31
Sec2p super family cl05764
GDP/GTP exchange factor Sec2p; In Saccharomyces cerevisiae, Sec2p is a GDP/GTP exchange factor ...
 189-257 5.00e-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: 61.05  E-value: 5.00e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15387686   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 ...
 282-312 1.52e-12

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: 65.33  E-value: 1.52e-12
                        10        20        30
                ....*....|....*....|....*....|.
gi 15387686 282 GHTRNKSTSSAMSGSHQDLSVIQPIVKDCKE 312
Cdd:cd21068   1 GHARNKSTSSAMSGSHQDLSVIQPIVKDCKE 31
Sec2p pfam06428
GDP/GTP exchange factor Sec2p; In Saccharomyces cerevisiae, Sec2p is a GDP/GTP exchange factor ...
 189-257 5.00e-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: 61.05  E-value: 5.00e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15387686   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 7.31e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.77  E-value: 7.31e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15387686  156 DSLSRLRSPSVLEVREKGYERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLfeEAHKMVREANIKQ--AT 233
Cdd:COG4913  272 AELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQI--RGNGGDRLEQLEReiER 349

                         90       100
                 ....*....|....*....|...
gi 15387686  234 AEKQLKEAQGKIDVLQAEVAALK 256
Cdd:COG4913  350 LERELEERERRRARLEALLAALG 372
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
158-256 3.65e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 3.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15387686  158 LSRLRSPSVLEVREKGYERLKEELAKAQRELKLKDEECERLSKvrdqlgqELEELTASLFEEAHKMVREANIKQ----AT 233
Cdd:PRK03918 605 LELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRK-------ELEELEKKYSEEEYEELREEYLELsrelAG 677

                         90       100
                 ....*....|....*....|...
gi 15387686  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 6.39e-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: 41.59  E-value: 6.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15387686    152 GLSTDSLSRLRSPSVLEVREKG-YERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLfEEAHKMVREANIK 230
Cdd:TIGR02169  653 GAMTGGSRAPRGGILFSRSEPAeLQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKI-GEIEKEIEQLEQE 731

                           90       100
                   ....*....|....*....|....*..
gi 15387686    231 QATAEKQLKEAQGKIDVLQAEVAALKT 257
Cdd:TIGR02169  732 EEKLKERLEELEEDLSSLEQEIENVKS 758
UBAN cd09803
polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) ...
 174-256 9.88e-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: 34.63  E-value: 9.88e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15387686 174 YERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELT-----ASLFEEAHKMVREANIKQATAEKQLKEaqgKIDVL 248
Cdd:cd09803   3 IDELAARLQEAEEALALKQEDIDELKEEIAQQEADLETIPvlkaqAEIYKSDFEAERAAREKLHQEKEQLAE---QLEYL 79


                ....*...
gi 15387686 249 QAEVAALK 256
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 ...
 282-312 1.52e-12

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: 65.33  E-value: 1.52e-12
                        10        20        30
                ....*....|....*....|....*....|.
gi 15387686 282 GHTRNKSTSSAMSGSHQDLSVIQPIVKDCKE 312
Cdd:cd21068   1 GHARNKSTSSAMSGSHQDLSVIQPIVKDCKE 31
Sec2p pfam06428
GDP/GTP exchange factor Sec2p; In Saccharomyces cerevisiae, Sec2p is a GDP/GTP exchange factor ...
 189-257 5.00e-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: 61.05  E-value: 5.00e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15387686   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 7.31e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.77  E-value: 7.31e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15387686  156 DSLSRLRSPSVLEVREKGYERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLfeEAHKMVREANIKQ--AT 233
Cdd:COG4913  272 AELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQI--RGNGGDRLEQLEReiER 349

                         90       100
                 ....*....|....*....|...
gi 15387686  234 AEKQLKEAQGKIDVLQAEVAALK 256
Cdd:COG4913  350 LERELEERERRRARLEALLAALG 372
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 175-259 3.04e-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: 51.30  E-value: 3.04e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15387686 175 ERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLfEEAHKMVREANIKQATAEKQLKEAQGKIDVLQAEVAA 254
Cdd:COG4942  23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRI-AALARRIRALEQELAALEAELAELEKEIAELRAELEA 101


                ....*
gi 15387686 255 LKTLV 259
Cdd:COG4942 102 QKEEL 106
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
175-257 4.13e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 51.06  E-value: 4.13e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15387686 175 ERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLfEEAHKMVREANIKQATAEKQLKEAQGKIDVLQAEVAA 254
Cdd:COG4372  41 DKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL-EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEE 119


                ...
gi 15387686 255 LKT 257
Cdd:COG4372 120 LQK 122
DivIVA COG3599
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle ...
 168-256 9.22e-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: 44.46  E-value: 9.22e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15387686 168 EVRE------KGYERLKEELAKAQRELKLKDEECERLSKVRDQLGQEL-------EELTASLFEEAHKMVREANIKqatA 234
Cdd:COG3599  24 EVDEfldevaEDYERLIRENKELKEKLEELEEELEEYRELEETLQKTLvvaqetaEEVKENAEKEAELIIKEAELE---A 100

                        90       100
                ....*....|....*....|..
gi 15387686 235 EKQLKEAQGKIDVLQAEVAALK 256
Cdd:COG3599 101 EKIIEEAQEKARKIVREIEELK 122
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
167-270 1.20e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.43  E-value: 1.20e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15387686 167 LEVREKGYERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLfEEAHKMVREANIKQATAEKQLKEAQGKID 246
Cdd:COG4372  82 LEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQR-KQLEAQIAELQSEIAEREEELKELEEQLE 160

                        90       100
                ....*....|....*....|....
gi 15387686 247 VLQAEVAALKTLVLSSSPTSPTQE 270
Cdd:COG4372 161 SLQEELAALEQELQALSEAEAEQA 184
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 167-257 1.26e-05

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: 45.69  E-value: 1.26e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15387686 167 LEVREKGYERLKEELAKAQRELKLKDEECE----RLSKVRDQLGQ------------ELEELTASLfEEAHKMVREANIK 230
Cdd:COG1579  40 LAALEARLEAAKTELEDLEKEIKRLELEIEeveaRIKKYEEQLGNvrnnkeyealqkEIESLKRRI-SDLEDEILELMER 118

                        90       100
                ....*....|....*....|....*..
gi 15387686 231 QATAEKQLKEAQGKIDVLQAEVAALKT 257
Cdd:COG1579 119 IEELEEELAELEAELAELEAELEEKKA 145
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 167-256 5.03e-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: 5.03e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15387686 167 LEVREKGYERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLFEEAHKMVREANIKQATAEkQLKEAQGKID 246
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE-RRRELEERLE 319

                        90
                ....*....|
gi 15387686 247 VLQAEVAALK 256
Cdd:COG1196 320 ELEEELAELE 329
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 174-255 7.21e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 7.21e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15387686 174 YERLKEELAKAQRELKL-----KDEECERLSKVRDQLGQELEELTASLfEEAHKMVREANIKQATAEKQLKEAQGKIDVL 248
Cdd:COG1196 215 YRELKEELKELEAELLLlklreLEAELEELEAELEELEAELEELEAEL-AELEAELEELRLELEELELELEEAQAEEYEL 293


                ....*..
gi 15387686 249 QAEVAAL 255
Cdd:COG1196 294 LAELARL 300
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 167-255 9.31e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 9.31e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15387686 167 LEVREKGYERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLfEEAHKMVREANIKQATAEKQLKEAQGKID 246
Cdd:COG1196 283 LEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL-EELEEELEELEEELEEAEEELEEAEAELA 361


                ....*....
gi 15387686 247 VLQAEVAAL 255
Cdd:COG1196 362 EAEEALLEA 370
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
170-257 1.03e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.99  E-value: 1.03e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15387686 170 REKGYERLKEELAKAQRELKLKDEECERLS---KVRDQLGQELEELTASLFEEAHKMVREANIKQATAEKQLKEAQGKID 246
Cdd:COG4717 123 KLLQLLPLYQELEALEAELAELPERLEELEerlEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELE 202

                        90
                ....*....|.
gi 15387686 247 VLQAEVAALKT 257
Cdd:COG4717 203 ELQQRLAELEE 213
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
175-256 1.05e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.14  E-value: 1.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15387686  175 ERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEElTASLFEEAHKMVRE-----------ANIKQATAEKQLKEAQG 243
Cdd:COG4913  341 EQLEREIERLERELEERERRRARLEALLAALGLPLPA-SAEEFAALRAEAAAllealeeeleaLEEALAEAEAALRDLRR 419

                         90
                 ....*....|...
gi 15387686  244 KIDVLQAEVAALK 256
Cdd:COG4913  420 ELRELEAEIASLE 432
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 171-256 1.08e-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: 1.08e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15387686 171 EKGYERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLfEEAHKMVREANIKQATAEKQLKEAQGKIDVLQA 250
Cdd:COG1196 301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL-EEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379


                ....*.
gi 15387686 251 EVAALK 256
Cdd:COG1196 380 ELEELA 385
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 159-264 1.76e-04

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 43.15  E-value: 1.76e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15387686 159 SRLR-----SPSVLEVREKGYERLKEELAKAQRELKLKDEEceRLSKVRDQLGQ---ELEELTASLFEEahkmvREANIK 230
Cdd:COG0542 400 ARVRmeidsKPEELDELERRLEQLEIEKEALKKEQDEASFE--RLAELRDELAEleeELEALKARWEAE-----KELIEE 472

                        90       100       110
                ....*....|....*....|....*....|....
gi 15387686 231 QATAEKQLKEAQGKIDVLQAEVAALKTLVLSSSP 264
Cdd:COG0542 473 IQELKEELEQRYGKIPELEKELAELEEELAELAP 506
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
155-256 2.18e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 2.18e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15387686 155 TDSLSRLRSPSVLEVREKGYERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELtaslfeEAHKMVREANIKQATA 234
Cdd:COG4717 408 EEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQL------EEDGELAELLQELEEL 481

                        90       100
                ....*....|....*....|..
gi 15387686 235 EKQLKEAQGKIDVLQAEVAALK 256
Cdd:COG4717 482 KAELRELAEEWAALKLALELLE 503
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
158-256 3.65e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 3.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15387686  158 LSRLRSPSVLEVREKGYERLKEELAKAQRELKLKDEECERLSKvrdqlgqELEELTASLFEEAHKMVREANIKQ----AT 233
Cdd:PRK03918 605 LELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRK-------ELEELEKKYSEEEYEELREEYLELsrelAG 677

                         90       100
                 ....*....|....*....|...
gi 15387686  234 AEKQLKEAQGKIDVLQAEVAALK 256
Cdd:PRK03918 678 LRAELEELEKRREEIKKTLEKLK 700
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 174-256 3.83e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 3.83e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15387686 174 YERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLFEEAHKmVREANIKQATAEKQLKEAQGKIDVLQAEVA 253
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELE-LEEAQAEEYELLAELARLEQDIARLEERRR 312


                ...
gi 15387686 254 ALK 256
Cdd:COG1196 313 ELE 315
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
167-261 4.01e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.06  E-value: 4.01e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15387686 167 LEVREKGYERLK---EELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLFEEAHKMVREANIKQATAEKQLKEAQG 243
Cdd:COG4717 141 LAELPERLEELEerlEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE 220

                        90
                ....*....|....*...
gi 15387686 244 KIDVLQAEVAALKTLVLS 261
Cdd:COG4717 221 ELEELEEELEQLENELEA 238
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
159-257 4.16e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 4.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15387686  159 SRLRSPSVL--EVREKgYERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEEL------------TASL------FE 218
Cdd:COG4913  596 RRIRSRYVLgfDNRAK-LAALEAELAELEEELAEAEERLEALEAELDALQERREALqrlaeyswdeidVASAereiaeLE 674

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 15387686  219 EAHKMVREANIKQATAEKQLKEAQGKIDVLQAEVAALKT 257
Cdd:COG4913  675 AELERLDASSDDLAALEEQLEELEAELEELEEELDELKG 713
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
167-258 6.07e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 6.07e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15387686 167 LEVREKGYERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELtaslfeEAHKMVREANIKQATAEKQLKEAQGKID 246
Cdd:COG4717  76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL------EKLLQLLPLYQELEALEAELAELPERLE 149

                        90
                ....*....|..
gi 15387686 247 VLQAEVAALKTL 258
Cdd:COG4717 150 ELEERLEELREL 161
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 152-257 6.39e-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: 41.59  E-value: 6.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15387686    152 GLSTDSLSRLRSPSVLEVREKG-YERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLfEEAHKMVREANIK 230
Cdd:TIGR02169  653 GAMTGGSRAPRGGILFSRSEPAeLQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKI-GEIEKEIEQLEQE 731

                           90       100
                   ....*....|....*....|....*..
gi 15387686    231 QATAEKQLKEAQGKIDVLQAEVAALKT 257
Cdd:TIGR02169  732 EEKLKERLEELEEDLSSLEQEIENVKS 758
flagell_FliJ TIGR02473
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ...
 165-258 1.54e-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: 38.06  E-value: 1.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15387686   165 SVLEVREKGYERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTAS------------LFEEAHKMVREANIKQA 232
Cdd:TIGR02473   6 KLLDLREKEEEQAKLELAKAQAEFERLETQLQQLIKYREEYEQQALEKVGAgtsalelsnyqrFIRQLDQRIQQQQQELA 85

                          90       100
                  ....*....|....*....|....*.
gi 15387686   233 TAEKQLKEAQGKIDVLQAEVAALKTL 258
Cdd:TIGR02473  86 LLQQEVEAKRERLLEARRELKALEKL 111
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
179-257 1.60e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.14  E-value: 1.60e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15387686 179 EELAKAQRELKLKDEECERLSKVRDQLGQELEELTASL----FEEAHKMVREANIKQATAEKQLKEAQGKIDVLQAEVAA 254
Cdd:COG4717 385 EELRAALEQAEEYQELKEELEELEEQLEELLGELEELLealdEEELEEELEELEEELEELEEELEELREELAELEAELEQ 464


                ...
gi 15387686 255 LKT 257
Cdd:COG4717 465 LEE 467
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 157-254 1.61e-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: 1.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15387686    157 SLSRLRSP-----SVLEVREKGYERLKEELAKAQRELK-----LKDEECE---RLSKVRDQLGQELEELTASL--FEEah 221
Cdd:pfam01576  177 SLSKLKNKheamiSDLEERLKKEEKGRQELEKAKRKLEgestdLQEQIAElqaQIAELRAQLAKKEEELQAALarLEE-- 254

                           90       100       110
                   ....*....|....*....|....*....|...
gi 15387686    222 kmvrEANIKqATAEKQLKEAQGKIDVLQAEVAA 254
Cdd:pfam01576  255 ----ETAQK-NNALKKIRELEAQISELQEDLES 282
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 175-258 1.70e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 1.70e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15387686 175 ERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLFEEAHKMVREANIKQATAEKQLKEAQGKIDVLQAEVAA 254
Cdd:COG1196 319 EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL 398


                ....
gi 15387686 255 LKTL 258
Cdd:COG1196 399 AAQL 402
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 166-256 1.76e-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: 1.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15387686    166 VLEVREKGYERLKEELAKAQRELKLKDEECE---RLSKVR-DQLGQELEELTASLfeeahkmvREANIKQATAEKQLKEA 241
Cdd:TIGR02168  194 ILNELERQLKSLERQAEKAERYKELKAELRElelALLVLRlEELREELEELQEEL--------KEAEEELEELTAELQEL 265

                           90
                   ....*....|....*
gi 15387686    242 QGKIDVLQAEVAALK 256
Cdd:TIGR02168  266 EEKLEELRLEVSELE 280
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 175-255 1.88e-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: 38.23  E-value: 1.88e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15387686 175 ERLKEELAKAQREL--KLKDEECER---LSKVRDQLGQELEELTASLFEEAHKMVREAnikQATAEKQLKEAqgkIDVLQ 249
Cdd:COG0711  44 ERAKEEAEAALAEYeeKLAEARAEAaeiIAEARKEAEAIAEEAKAEAEAEAERIIAQA---EAEIEQERAKA---LAELR 117


                ....*.
gi 15387686 250 AEVAAL 255
Cdd:COG0711 118 AEVADL 123
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 182-259 2.00e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.43  E-value: 2.00e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15387686 182 AKAQRELKLKDEECERLSKVRDQLGQELEELTASLfEEAHKMVREANIKQATAEKQLKEAQGKIDVLQAEVAALKTLV 259
Cdd:COG3883  12 AFADPQIQAKQKELSELQAELEAAQAELDALQAEL-EELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL 88
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 167-256 2.11e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.92  E-value: 2.11e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15387686 167 LEVREKGYERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLfEEAHKMVREANIKQATAEKQLKEAQGKID 246
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL-EEAQAEEYELLAELARLEQDIARLEERRR 312

                        90
                ....*....|
gi 15387686 247 VLQAEVAALK 256
Cdd:COG1196 313 ELEERLEELE 322
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 171-256 2.39e-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: 39.67  E-value: 2.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15387686    171 EKGYERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLFEEAHKMVREANIKQATAEKQLKEAQGKIDVLQA 250
Cdd:TIGR02169  243 ERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEE 322


                   ....*.
gi 15387686    251 EVAALK 256
Cdd:TIGR02169  323 RLAKLE 328
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
171-259 2.79e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.28  E-value: 2.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15387686  171 EKGYERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLfeeahkmvreANIKQATAE-KQLKEAQGKIDVLQ 249
Cdd:PRK03918 658 EEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEEL----------EEREKAKKElEKLEKALERVEELR 727

                         90
                 ....*....|
gi 15387686  250 AEVAALKTLV 259
Cdd:PRK03918 728 EKVKKYKALL 737
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
168-256 3.25e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.13  E-value: 3.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15387686  168 EVREKGYERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLfEEAHKMVREanikqatAEKQLKEAQG-KID 246
Cdd:COG4913  270 RLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARL-DALREELDE-------LEAQIRGNGGdRLE 341

                         90
                 ....*....|
gi 15387686  247 VLQAEVAALK 256
Cdd:COG4913  342 QLEREIERLE 351
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
175-258 3.65e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 39.07  E-value: 3.65e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15387686 175 ERLKEELAKAQRELKLKDEECERLSKvrdqlgqELEELTASLFEEAHKMvREANIKQATA---EKQLKEAQGKIDVLQAE 251
Cdd:COG2433 423 ERLEAEVEELEAELEEKDERIERLER-------ELSEARSEERREIRKD-REISRLDREIerlERELEEERERIEELKRK 494


                ....*..
gi 15387686 252 VAALKTL 258
Cdd:COG2433 495 LERLKEL 501
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 167-246 3.83e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 39.04  E-value: 3.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15387686  167 LEVREKGYERLKEELAKAQRELKlkdeecERLSKVRDQLGQELEELTASLFEEAHKMVREANIKQ-----ATAEKQLKEA 241
Cdd:PRK00409 539 AEALLKEAEKLKEELEEKKEKLQ------EEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQLQkggyaSVKAHELIEA 612


                 ....*
gi 15387686  242 QGKID 246
Cdd:PRK00409 613 RKRLN 617
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 174-255 5.64e-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: 38.50  E-value: 5.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15387686    174 YERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTA------SLFEEAHKMVREANIKQATAEKQLKEAQGKIDV 247
Cdd:TIGR02168  234 LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLevseleEEIEELQKELYALANEISRLEQQKQILRERLAN 313


                   ....*...
gi 15387686    248 LQAEVAAL 255
Cdd:TIGR02168  314 LERQLEEL 321
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 175-256 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: 38.11  E-value: 6.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15387686    175 ERLK---EELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLFEEAHKMVREANIKQATAEKQLKEAQGKIDVLQAE 251
Cdd:TIGR02168  189 DRLEdilNELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEK 268


                   ....*
gi 15387686    252 VAALK 256
Cdd:TIGR02168  269 LEELR 273
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 175-255 8.33e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 37.99  E-value: 8.33e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15387686 175 ERLKEELAKAQRELKLKDE----ECERLSKVRDQLGQELEELTASLfEEAHKMVREANIKQATAEKQLKEAQGKIDVLQA 250
Cdd:COG1196 203 EPLERQAEKAERYRELKEElkelEAELLLLKLRELEAELEELEAEL-EELEAELEELEAELAELEAELEELRLELEELEL 281


                ....*
gi 15387686 251 EVAAL 255
Cdd:COG1196 282 ELEEA 286
UBAN cd09803
polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) ...
 174-256 9.88e-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: 34.63  E-value: 9.88e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15387686 174 YERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELT-----ASLFEEAHKMVREANIKQATAEKQLKEaqgKIDVL 248
Cdd:cd09803   3 IDELAARLQEAEEALALKQEDIDELKEEIAQQEADLETIPvlkaqAEIYKSDFEAERAAREKLHQEKEQLAE---QLEYL 79


                ....*...
gi 15387686 249 QAEVAALK 256
Cdd:cd09803  80 QRENQELK 87
 
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