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Conserved domains on  [gi|564359305|ref|XP_006241419|]
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rab-3A-interacting protein isoform X1 [Rattus norvegicus]

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 ...
 266-458 1.04e-143

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: 408.54  E-value: 1.04e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359305 266 GHTRNKSTSSAMSGSHQDFSAIQPIVKDCREADLSLYNEFRSWKDEPTMDRTCPFLDKIYQEDIFPCLTFAKSELASAVL 345
Cdd:cd21068    1 GHARNKSTSSAMSGSHQDLSVIQPIVKDCKEADLSLYNEFRLWKEEPTMDRTCPFLDRIYQEDIFPCLTFSKSELASAVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359305 346 EAVENNTLSIEPVGLQPIRFVKASAVECGGPKKCALTGQSKPCKHRIKLGDSSSYYYISPVCRYRITSVCNFFTYIRYIQ 425
Cdd:cd21068   81 EAVENNTLSIEPVGLQPLRFVKASAVECGGPKKCALSGQTKSCKHRIKLGDSSNYYYISPFCRYRITSVCNFFTYIRYIQ 160

                        170       180       190
                 ....*....|....*....|....*....|...
gi 564359305 426 QGLVKQQDVDQMFWEVMQLRKEMSLAKLGYFKE 458
Cdd:cd21068  161 QGLVKQQDVDQMFWEVMQLRKEMSLAKLGYYKE 193
Sec2p super family cl05764
GDP/GTP exchange factor Sec2p; In Saccharomyces cerevisiae, Sec2p is a GDP/GTP exchange factor ...
 173-241 1.96e-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: 62.97  E-value: 1.96e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564359305  173 KLKDEECERLS--KVRDQLGQELEELTASLFEEAHKMV----REANVKQATAEK---QLKEAQGKIDVLQAEVAALKT 241
Cdd:pfam06428   1 ELKEEKKKRLEaeKEKKKLEKELEDLTASLFEEANKMVaaarREKHAVEIKNDQlkeQLKEKETLLESLQEQLKELKQ 78
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 97-240 1.87e-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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.81  E-value: 1.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359305    97 EVAAGLTRFTSRKDScnAEREFlqgatvtEASAGNddifglstdsLSRLRSpsVLEVREKGYERLKEELAKAQRELKLKD 176
Cdd:TIGR02168  162 EEAAGISKYKERRKE--TERKL-------ERTREN----------LDRLED--ILNELERQLKSLERQAEKAERYKELKA 220

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564359305   177 EECE---RLSKVR-DQLGQELEELTASLfeeahkmvREANVKQATAEKQLKEAQGKIDVLQAEVAALK 240
Cdd:TIGR02168  221 ELRElelALLVLRlEELREELEELQEEL--------KEAEEELEELTAELQELEEKLEELRLEVSELE 280
 
Name Accession Description Interval E-value
Rab11BD_RAB3IP cd21068
Rab11 binding domain of Rab-3A-interacting protein (RAB3IP); RAB3IP, also called Rabin-3, or ...
 266-458 1.04e-143

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: 408.54  E-value: 1.04e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359305 266 GHTRNKSTSSAMSGSHQDFSAIQPIVKDCREADLSLYNEFRSWKDEPTMDRTCPFLDKIYQEDIFPCLTFAKSELASAVL 345
Cdd:cd21068    1 GHARNKSTSSAMSGSHQDLSVIQPIVKDCKEADLSLYNEFRLWKEEPTMDRTCPFLDRIYQEDIFPCLTFSKSELASAVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359305 346 EAVENNTLSIEPVGLQPIRFVKASAVECGGPKKCALTGQSKPCKHRIKLGDSSSYYYISPVCRYRITSVCNFFTYIRYIQ 425
Cdd:cd21068   81 EAVENNTLSIEPVGLQPLRFVKASAVECGGPKKCALSGQTKSCKHRIKLGDSSNYYYISPFCRYRITSVCNFFTYIRYIQ 160

                        170       180       190
                 ....*....|....*....|....*....|...
gi 564359305 426 QGLVKQQDVDQMFWEVMQLRKEMSLAKLGYFKE 458
Cdd:cd21068  161 QGLVKQQDVDQMFWEVMQLRKEMSLAKLGYYKE 193
Sec2p pfam06428
GDP/GTP exchange factor Sec2p; In Saccharomyces cerevisiae, Sec2p is a GDP/GTP exchange factor ...
 173-241 1.96e-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: 62.97  E-value: 1.96e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564359305  173 KLKDEECERLS--KVRDQLGQELEELTASLFEEAHKMV----REANVKQATAEK---QLKEAQGKIDVLQAEVAALKT 241
Cdd:pfam06428   1 ELKEEKKKRLEaeKEKKKLEKELEDLTASLFEEANKMVaaarREKHAVEIKNDQlkeQLKEKETLLESLQEQLKELKQ 78
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
159-241 1.52e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 53.37  E-value: 1.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359305 159 ERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLfEEAHKMVREANVKQATAEKQLKEAQGKIDVLQAEVAA 238
Cdd:COG4372   41 DKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL-EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEE 119


                 ...
gi 564359305 239 LKT 241
Cdd:COG4372  120 LQK 122
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
142-240 1.63e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.28  E-value: 1.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359305 142 LSRLRSPSVLEVREKGYERLKEELAKAQRELKLKDEECERLSKvrdqlgqELEELTASLFEEAHKMVREANVKQ----AT 217
Cdd:PRK03918 605 LELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRK-------ELEELEKKYSEEEYEELREEYLELsrelAG 677

                         90       100
                 ....*....|....*....|...
gi 564359305 218 AEKQLKEAQGKIDVLQAEVAALK 240
Cdd:PRK03918 678 LRAELEELEKRREEIKKTLEKLK 700
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 136-241 5.75e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 42.36  E-value: 5.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359305   136 GLSTDSLSRLRSPSVLEVREKG-YERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLfEEAHKMVREANVK 214
Cdd:TIGR02169  653 GAMTGGSRAPRGGILFSRSEPAeLQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKI-GEIEKEIEQLEQE 731

                           90       100
                   ....*....|....*....|....*..
gi 564359305   215 QATAEKQLKEAQGKIDVLQAEVAALKT 241
Cdd:TIGR02169  732 EEKLKERLEELEEDLSSLEQEIENVKS 758
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 97-240 1.87e-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: 40.81  E-value: 1.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359305    97 EVAAGLTRFTSRKDScnAEREFlqgatvtEASAGNddifglstdsLSRLRSpsVLEVREKGYERLKEELAKAQRELKLKD 176
Cdd:TIGR02168  162 EEAAGISKYKERRKE--TERKL-------ERTREN----------LDRLED--ILNELERQLKSLERQAEKAERYKELKA 220

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564359305   177 EECE---RLSKVR-DQLGQELEELTASLfeeahkmvREANVKQATAEKQLKEAQGKIDVLQAEVAALK 240
Cdd:TIGR02168  221 ELRElelALLVLRlEELREELEELQEEL--------KEAEEELEELTAELQELEEKLEELRLEVSELE 280
3a0801s03tim44 TIGR00984
mitochondrial import inner membrane, translocase subunit; The mitochondrial protein ...
 161-327 5.05e-03

mitochondrial import inner membrane, translocase subunit; The mitochondrial protein translocase (MPT) family, which brings nuclearly encoded preproteins into mitochondria, is very complex with 19 currently identified protein constituents.These proteins include several chaperone proteins, four proteins of the outer membrane translocase (Tom) import receptor, five proteins of the Tom channel complex, five proteins of the inner membrane translocase (Tim) and three "motor" proteins. This family is specific for the Tim proteins. [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 130057 [Multi-domain]  Cd Length: 378  Bit Score: 39.09  E-value: 5.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359305  161 LKEELAKAQrELK-----LKDE-----ECERLSKVRDQ--------------LGQELEELTASLFEEAHKMVREANVKQA 216
Cdd:TIGR00984   3 FRDELQKSQ-ELQesikqLQDRsgklnESDALKKARKAyekaesgtlkssevVGKTLGKLGDTMKKMAHKAWESELGKKM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359305  217 T--AEKQLKEAQGKIDVLQAEV---AALKTL--VLSSSPTSpTQEPLAAGKTPFKRGHTRNKSTSSAMSGSHQDFSAIQP 289
Cdd:TIGR00984  82 KkaGAETAKTAAEHVDKSAEPVrdtAVYKHVsqSMKDGKDS-SRYGFIADKEQRRRPRELTKRTDGRDFAKSRVVEANES 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 564359305  290 IVKDCREADLSLYNEFRSWKDEPTMDRTCPFLDKIYQE 327
Cdd:TIGR00984 161 VTDVVLHSDSSWYSKVEDFKESNVVYRKIQELKKKYDE 198
UBAN cd09803
polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) ...
 158-240 8.87e-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: 35.40  E-value: 8.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359305 158 YERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELT-----ASLFEEAHKMVREANVKQATAEKQLKEaqgKIDVL 232
Cdd:cd09803    3 IDELAARLQEAEEALALKQEDIDELKEEIAQQEADLETIPvlkaqAEIYKSDFEAERAAREKLHQEKEQLAE---QLEYL 79


                 ....*...
gi 564359305 233 QAEVAALK 240
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 ...
 266-458 1.04e-143

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: 408.54  E-value: 1.04e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359305 266 GHTRNKSTSSAMSGSHQDFSAIQPIVKDCREADLSLYNEFRSWKDEPTMDRTCPFLDKIYQEDIFPCLTFAKSELASAVL 345
Cdd:cd21068    1 GHARNKSTSSAMSGSHQDLSVIQPIVKDCKEADLSLYNEFRLWKEEPTMDRTCPFLDRIYQEDIFPCLTFSKSELASAVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359305 346 EAVENNTLSIEPVGLQPIRFVKASAVECGGPKKCALTGQSKPCKHRIKLGDSSSYYYISPVCRYRITSVCNFFTYIRYIQ 425
Cdd:cd21068   81 EAVENNTLSIEPVGLQPLRFVKASAVECGGPKKCALSGQTKSCKHRIKLGDSSNYYYISPFCRYRITSVCNFFTYIRYIQ 160

                        170       180       190
                 ....*....|....*....|....*....|...
gi 564359305 426 QGLVKQQDVDQMFWEVMQLRKEMSLAKLGYFKE 458
Cdd:cd21068  161 QGLVKQQDVDQMFWEVMQLRKEMSLAKLGYYKE 193
Rab11BD_RAB3IL1 cd21069
Rab11 binding domain of Rab-3A-interacting-like protein 1 (RAB3IL1); RAB3IL1, also called ...
 293-456 8.25e-94

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


Pssm-ID: 411033  Cd Length: 163  Bit Score: 280.60  E-value: 8.25e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359305 293 DCREADLSLYNEFRSWKDEPTMDRTCPFLDKIYQEDIFPCLTFAKSELASAVLEAVENNTLSIEPVGLQPIRFVKASAVE 372
Cdd:cd21069    1 EGKEVDTVLFAEFQAWKESPTLDRSCPFLSRIYREDIGPCLDFTKRELSDLVQSAVENNTLTIEPVASQALPVVKASAVE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359305 373 CGGPKKCALTGQSKPCKHRIKLGDSSSYYYISPVCRYRITSVCNFFTYIRYIQQGLVKqQDVDQMFWEVMQLRKEMSLAK 452
Cdd:cd21069   81 CGGPKKCALSGLSRTCRHRIKLGDSGNYYYISPSCRARITAVCNFFTYIRYIQQGLVR-QDAEQMFWEVMRLRREMSLAK 159


                 ....
gi 564359305 453 LGYF 456
Cdd:cd21069  160 LGFY 163
Rab11BD_RAB3IP_like cd21044
Rab11 binding domain of Rab-3A-interacting protein (RAB3IP), Rab-3A-interacting-like protein 1 ...
 296-454 3.16e-56

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: 184.49  E-value: 3.16e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359305 296 EADLSLYNEFRSWKDEP-----TMDRTCPFLDKIYQEDIFPCLTFAKS----ELASAVLEAVENNTLSIEPVGLQPIRFV 366
Cdd:cd21044    2 EVDLVLFEEFQEFLKAPsslslSLLKSSPFLKRILAEDIEPCLRFDPAllnwLLKKRLLAAILENTLEIEPISGSTETSS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359305 367 K------ASAVECGGPKKCALTGQSK--PCKHRIKLGDSSS-YYYISPVCRYRITSVCNFFTYIRYIQQGLVKQQDVDQM 437
Cdd:cd21044   82 SsnntapVSSPPPASPKKCALCGESRldACLYRLRLSDSDSeWYPICSYCRNRLRAVCDFFAYLRYIRQGLVKSRSIEKL 161

                        170
                 ....*....|....*..
gi 564359305 438 FWEVMQLRKEMSLAKLG 454
Cdd:cd21044  162 YLEILRLRLRMFLARLG 178
Sec2p pfam06428
GDP/GTP exchange factor Sec2p; In Saccharomyces cerevisiae, Sec2p is a GDP/GTP exchange factor ...
 173-241 1.96e-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: 62.97  E-value: 1.96e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564359305  173 KLKDEECERLS--KVRDQLGQELEELTASLFEEAHKMV----REANVKQATAEK---QLKEAQGKIDVLQAEVAALKT 241
Cdd:pfam06428   1 ELKEEKKKRLEaeKEKKKLEKELEDLTASLFEEANKMVaaarREKHAVEIKNDQlkeQLKEKETLLESLQEQLKELKQ 78
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
159-241 1.52e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 53.37  E-value: 1.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359305 159 ERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLfEEAHKMVREANVKQATAEKQLKEAQGKIDVLQAEVAA 238
Cdd:COG4372   41 DKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL-EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEE 119


                 ...
gi 564359305 239 LKT 241
Cdd:COG4372  120 LQK 122
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 159-243 3.29e-07

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 52.07  E-value: 3.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359305 159 ERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLfEEAHKMVREANVKQATAEKQLKEAQGKIDVLQAEVAA 238
Cdd:COG4942   23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRI-AALARRIRALEQELAALEAELAELEKEIAELRAELEA 101


                 ....*
gi 564359305 239 LKTLV 243
Cdd:COG4942  102 QKEEL 106
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
140-240 3.33e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.00  E-value: 3.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359305  140 DSLSRLRSPSVLEVREKGYERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLFEEAHKMVREANVKQATAE 219
Cdd:COG4913   272 AELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLE 351

                          90       100
                  ....*....|....*....|.
gi 564359305  220 KQLKEAQGKIDVLQAEVAALK 240
Cdd:COG4913   352 RELEERERRRARLEALLAALG 372
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
151-254 7.37e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.97  E-value: 7.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359305 151 LEVREKGYERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLfEEAHKMVREANVKQATAEKQLKEAQGKID 230
Cdd:COG4372   82 LEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQR-KQLEAQIAELQSEIAEREEELKELEEQLE 160

                         90       100
                 ....*....|....*....|....
gi 564359305 231 VLQAEVAALKTLVLSSSPTSPTQE 254
Cdd:COG4372  161 SLQEELAALEQELQALSEAEAEQA 184
DivIVA COG3599
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle ...
 152-240 1.09e-05

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: 1.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359305 152 EVRE------KGYERLKEELAKAQRELKLKDEECERLSKVRDQLGQEL-------EELTASLFEEAHKMVREANVKqatA 218
Cdd:COG3599   24 EVDEfldevaEDYERLIRENKELKEKLEELEEELEEYRELEETLQKTLvvaqetaEEVKENAEKEAELIIKEAELE---A 100

                         90       100
                 ....*....|....*....|..
gi 564359305 219 EKQLKEAQGKIDVLQAEVAALK 240
Cdd:COG3599  101 EKIIEEAQEKARKIVREIEELK 122
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 151-241 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: 46.46  E-value: 1.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359305 151 LEVREKGYERLKEELAKAQRELKLKDEECE----RLSKVRDQLGQ------------ELEELTASLfEEAHKMVREANVK 214
Cdd:COG1579   40 LAALEARLEAAKTELEDLEKEIKRLELEIEeveaRIKKYEEQLGNvrnnkeyealqkEIESLKRRI-SDLEDEILELMER 118

                         90       100
                 ....*....|....*....|....*..
gi 564359305 215 QATAEKQLKEAQGKIDVLQAEVAALKT 241
Cdd:COG1579  119 IEELEEELAELEAELAELEAELEEKKA 145
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
159-240 5.94e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.68  E-value: 5.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359305  159 ERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEElTASLFEEAHKMVRE-----------ANVKQATAEKQLKEAQG 227
Cdd:COG4913   341 EQLEREIERLERELEERERRRARLEALLAALGLPLPA-SAEEFAALRAEAAAllealeeeleaLEEALAEAEAALRDLRR 419

                          90
                  ....*....|...
gi 564359305  228 KIDVLQAEVAALK 240
Cdd:COG4913   420 ELRELEAEIASLE 432
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 158-239 8.67e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 8.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359305 158 YERLKEELAKAQRELKL-----KDEECERLSKVRDQLGQELEELTASLfEEAHKMVREANVKQATAEKQLKEAQGKIDVL 232
Cdd:COG1196  215 YRELKEELKELEAELLLlklreLEAELEELEAELEELEAELEELEAEL-AELEAELEELRLELEELELELEEAQAEEYEL 293


                 ....*..
gi 564359305 233 QAEVAAL 239
Cdd:COG1196  294 LAELARL 300
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 155-240 1.08e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.93  E-value: 1.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359305 155 EKGYERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLfEEAHKMVREANVKQATAEKQLKEAQGKIDVLQA 234
Cdd:COG1196  301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL-EEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379


                 ....*.
gi 564359305 235 EVAALK 240
Cdd:COG1196  380 ELEELA 385
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 151-240 1.25e-04

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: 1.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359305 151 LEVREKGYERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLFEEAHKMVREANVKQATAEkQLKEAQGKID 230
Cdd:COG1196  241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE-RRRELEERLE 319

                         90
                 ....*....|
gi 564359305 231 VLQAEVAALK 240
Cdd:COG1196  320 ELEEELAELE 329
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 143-248 1.38e-04

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 44.30  E-value: 1.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359305 143 SRLR-----SPSVLEVREKGYERLKEELAKAQRELKLKDEEceRLSKVRDQLGQELEELTAslFEEAHKMVREANVKQAT 217
Cdd:COG0542  400 ARVRmeidsKPEELDELERRLEQLEIEKEALKKEQDEASFE--RLAELRDELAELEEELEA--LKARWEAEKELIEEIQE 475

                         90       100       110
                 ....*....|....*....|....*....|.
gi 564359305 218 AEKQLKEAQGKIDVLQAEVAALKTLVLSSSP 248
Cdd:COG0542  476 LKEELEQRYGKIPELEKELAELEEELAELAP 506
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
154-241 1.60e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.99  E-value: 1.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359305 154 REKGYERLKEELAKAQRELKLKDEECERLS---KVRDQLGQELEELTASLFEEAHKMVREANVKQATAEKQLKEAQGKID 230
Cdd:COG4717  123 KLLQLLPLYQELEALEAELAELPERLEELEerlEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELE 202

                         90
                 ....*....|.
gi 564359305 231 VLQAEVAALKT 241
Cdd:COG4717  203 ELQQRLAELEE 213
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
142-240 1.63e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.28  E-value: 1.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359305 142 LSRLRSPSVLEVREKGYERLKEELAKAQRELKLKDEECERLSKvrdqlgqELEELTASLFEEAHKMVREANVKQ----AT 217
Cdd:PRK03918 605 LELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRK-------ELEELEKKYSEEEYEELREEYLELsrelAG 677

                         90       100
                 ....*....|....*....|...
gi 564359305 218 AEKQLKEAQGKIDVLQAEVAALK 240
Cdd:PRK03918 678 LRAELEELEKRREEIKKTLEKLK 700
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 151-239 1.64e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 1.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359305 151 LEVREKGYERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLfEEAHKMVREANVKQATAEKQLKEAQGKID 230
Cdd:COG1196  283 LEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL-EELEEELEELEEELEEAEEELEEAEAELA 361


                 ....*....
gi 564359305 231 VLQAEVAAL 239
Cdd:COG1196  362 EAEEALLEA 370
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
151-245 3.09e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.22  E-value: 3.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359305 151 LEVREKGYERLK---EELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLFEEAHKMVREANVKQATAEKQLKEAQG 227
Cdd:COG4717  141 LAELPERLEELEerlEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE 220

                         90
                 ....*....|....*...
gi 564359305 228 KIDVLQAEVAALKTLVLS 245
Cdd:COG4717  221 ELEELEEELEQLENELEA 238
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 141-238 4.33e-04

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 42.85  E-value: 4.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359305   141 SLSRLRSP-----SVLEVREKGYERLKEELAKAQRELK-----LKDEECE---RLSKVRDQLGQELEELTASL--FEEah 205
Cdd:pfam01576  177 SLSKLKNKheamiSDLEERLKKEEKGRQELEKAKRKLEgestdLQEQIAElqaQIAELRAQLAKKEEELQAALarLEE-- 254

                           90       100       110
                   ....*....|....*....|....*....|...
gi 564359305   206 kmvrEANVKqATAEKQLKEAQGKIDVLQAEVAA 238
Cdd:pfam01576  255 ----ETAQK-NNALKKIRELEAQISELQEDLES 282
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 158-240 4.42e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 4.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359305 158 YERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLFEEAHKmVREANVKQATAEKQLKEAQGKIDVLQAEVA 237
Cdd:COG1196  234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELE-LEEAQAEEYELLAELARLEQDIARLEERRR 312


                 ...
gi 564359305 238 ALK 240
Cdd:COG1196  313 ELE 315
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 166-243 5.05e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.12  E-value: 5.05e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564359305 166 AKAQRELKLKDEECERLSKVRDQLGQELEELTASLfEEAHKMVREANVKQATAEKQLKEAQGKIDVLQAEVAALKTLV 243
Cdd:COG3883   12 AFADPQIQAKQKELSELQAELEAAQAELDALQAEL-EELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL 88
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 136-241 5.75e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 42.36  E-value: 5.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359305   136 GLSTDSLSRLRSPSVLEVREKG-YERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLfEEAHKMVREANVK 214
Cdd:TIGR02169  653 GAMTGGSRAPRGGILFSRSEPAeLQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKI-GEIEKEIEQLEQE 731

                           90       100
                   ....*....|....*....|....*..
gi 564359305   215 QATAEKQLKEAQGKIDVLQAEVAALKT 241
Cdd:TIGR02169  732 EEKLKERLEELEEDLSSLEQEIENVKS 758
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
139-240 6.96e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.06  E-value: 6.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359305 139 TDSLSRLRSPSVLEVREKGYERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELtaslfeEAHKMVREANVKQATA 218
Cdd:COG4717  408 EEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQL------EEDGELAELLQELEEL 481

                         90       100
                 ....*....|....*....|..
gi 564359305 219 EKQLKEAQGKIDVLQAEVAALK 240
Cdd:COG4717  482 KAELRELAEEWAALKLALELLE 503
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
143-241 8.33e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.82  E-value: 8.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359305  143 SRLRSPSVL--EVREKgYERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEEL------------TASL------FE 202
Cdd:COG4913   596 RRIRSRYVLgfDNRAK-LAALEAELAELEEELAEAEERLEALEAELDALQERREALqrlaeyswdeidVASAereiaeLE 674

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 564359305  203 EAHKMVREANVKQATAEKQLKEAQGKIDVLQAEVAALKT 241
Cdd:COG4913   675 AELERLDASSDDLAALEEQLEELEAELEELEEELDELKG 713
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
151-242 1.70e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 1.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359305 151 LEVREKGYERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELtaslfeEAHKMVREANVKQATAEKQLKEAQGKID 230
Cdd:COG4717   76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL------EKLLQLLPLYQELEALEAELAELPERLE 149

                         90
                 ....*....|..
gi 564359305 231 VLQAEVAALKTL 242
Cdd:COG4717  150 ELEERLEELREL 161
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 97-240 1.87e-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: 40.81  E-value: 1.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359305    97 EVAAGLTRFTSRKDScnAEREFlqgatvtEASAGNddifglstdsLSRLRSpsVLEVREKGYERLKEELAKAQRELKLKD 176
Cdd:TIGR02168  162 EEAAGISKYKERRKE--TERKL-------ERTREN----------LDRLED--ILNELERQLKSLERQAEKAERYKELKA 220

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564359305   177 EECE---RLSKVR-DQLGQELEELTASLfeeahkmvREANVKQATAEKQLKEAQGKIDVLQAEVAALK 240
Cdd:TIGR02168  221 ELRElelALLVLRlEELREELEELQEEL--------KEAEEELEELTAELQELEEKLEELRLEVSELE 280
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 151-259 2.14e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 40.58  E-value: 2.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359305 151 LEVREKGYERLKEELAKAQRELKlkdeecERLSKVRDQLGQELEELTASLFEEAHKMVREANVKQ-----ATAEKQLKEA 225
Cdd:PRK00409 539 AEALLKEAEKLKEELEEKKEKLQ------EEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQLQkggyaSVKAHELIEA 612

                         90       100       110
                 ....*....|....*....|....*....|....
gi 564359305 226 QGKIDvlqaevAALKTLVLSSSPTSPTQEPLAAG 259
Cdd:PRK00409 613 RKRLN------KANEKKEKKKKKQKEKQEELKVG 640
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 159-242 2.60e-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: 2.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359305 159 ERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLFEEAHKMVREANVKQATAEKQLKEAQGKIDVLQAEVAA 238
Cdd:COG1196  319 EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL 398


                 ....
gi 564359305 239 LKTL 242
Cdd:COG1196  399 AAQL 402
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 155-241 2.66e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.44  E-value: 2.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359305   155 EKGYERLKEELAKAQRELKLKDEECERLSKVRDQLG---------------QELEELTASLfEEAHKMVREANVKQATAE 219
Cdd:TIGR02169  243 ERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNkkikdlgeeeqlrvkEKIGELEAEI-ASLERSIAEKERELEDAE 321

                           90       100
                   ....*....|....*....|..
gi 564359305   220 KQLKEAQGKIDVLQAEVAALKT 241
Cdd:TIGR02169  322 ERLAKLEAEIDKLLAEIEELER 343
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
155-243 3.02e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.05  E-value: 3.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359305 155 EKGYERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLfEEAHKMVREAnvkqataeKQLKEAQGKIDVLQA 234
Cdd:PRK03918 658 EEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEEL-EEREKAKKEL--------EKLEKALERVEELRE 728


                 ....*....
gi 564359305 235 EVAALKTLV 243
Cdd:PRK03918 729 KVKKYKALL 737
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
163-241 3.19e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.14  E-value: 3.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359305 163 EELAKAQRELKLKDEECERLSKVRDQLGQELEELTASL----FEEAHKMVREANVKQATAEKQLKEAQGKIDVLQAEVAA 238
Cdd:COG4717  385 EELRAALEQAEEYQELKEELEELEEQLEELLGELEELLealdEEELEEELEELEEELEELEEELEELREELAELEAELEQ 464


                 ...
gi 564359305 239 LKT 241
Cdd:COG4717  465 LEE 467
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 159-239 3.36e-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: 37.84  E-value: 3.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359305 159 ERLKEELAKAQREL--KLKDEECER---LSKVRDQLGQELEELTASLFEEAHKMVREANVKQATAEKQLKEAqgkidvLQ 233
Cdd:COG0711   44 ERAKEEAEAALAEYeeKLAEARAEAaeiIAEARKEAEAIAEEAKAEAEAEAERIIAQAEAEIEQERAKALAE------LR 117


                 ....*.
gi 564359305 234 AEVAAL 239
Cdd:COG0711  118 AEVADL 123
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 159-239 3.54e-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: 3.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359305 159 ERLKEELAKAQRELKLKDE----ECERLSKVRDQLGQELEELTASLfEEAHKMVREANVKQATAEKQLKEAQGKIDVLQA 234
Cdd:COG1196  203 EPLERQAEKAERYRELKEElkelEAELLLLKLRELEAELEELEAEL-EELEAELEELEAELAELEAELEELRLELEELEL 281


                 ....*
gi 564359305 235 EVAAL 239
Cdd:COG1196  282 ELEEA 286
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 158-262 3.93e-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: 3.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359305 158 YERLKEELAKAQRELklkDEECERLSKVRDQLGQELEELTASLfEEAHKMVREANVKQATAEKQLKEAQGKIDVLQAEVA 237
Cdd:COG3883  138 LKADKAELEAKKAEL---EAKLAELEALKAELEAAKAELEAQQ-AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAA 213

                         90       100
                 ....*....|....*....|....*
gi 564359305 238 ALKTLVLSSSPTSPTQEPLAAGKTP 262
Cdd:COG3883  214 AAAAAAAAAAAAAAAAAAAAAAAAA 238
3a0801s03tim44 TIGR00984
mitochondrial import inner membrane, translocase subunit; The mitochondrial protein ...
 161-327 5.05e-03

mitochondrial import inner membrane, translocase subunit; The mitochondrial protein translocase (MPT) family, which brings nuclearly encoded preproteins into mitochondria, is very complex with 19 currently identified protein constituents.These proteins include several chaperone proteins, four proteins of the outer membrane translocase (Tom) import receptor, five proteins of the Tom channel complex, five proteins of the inner membrane translocase (Tim) and three "motor" proteins. This family is specific for the Tim proteins. [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 130057 [Multi-domain]  Cd Length: 378  Bit Score: 39.09  E-value: 5.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359305  161 LKEELAKAQrELK-----LKDE-----ECERLSKVRDQ--------------LGQELEELTASLFEEAHKMVREANVKQA 216
Cdd:TIGR00984   3 FRDELQKSQ-ELQesikqLQDRsgklnESDALKKARKAyekaesgtlkssevVGKTLGKLGDTMKKMAHKAWESELGKKM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359305  217 T--AEKQLKEAQGKIDVLQAEV---AALKTL--VLSSSPTSpTQEPLAAGKTPFKRGHTRNKSTSSAMSGSHQDFSAIQP 289
Cdd:TIGR00984  82 KkaGAETAKTAAEHVDKSAEPVrdtAVYKHVsqSMKDGKDS-SRYGFIADKEQRRRPRELTKRTDGRDFAKSRVVEANES 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 564359305  290 IVKDCREADLSLYNEFRSWKDEPTMDRTCPFLDKIYQE 327
Cdd:TIGR00984 161 VTDVVLHSDSSWYSKVEDFKESNVVYRKIQELKKKYDE 198
flagell_FliJ TIGR02473
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ...
 149-243 5.70e-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: 37.29  E-value: 5.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359305  149 SVLEVREKGYERLKEELAKAQrelklkdEECERLSKVRDQLGQELEELTASLFEEahkmvreanVKQATAEKQLKEAQGK 228
Cdd:TIGR02473   6 KLLDLREKEEEQAKLELAKAQ-------AEFERLETQLQQLIKYREEYEQQALEK---------VGAGTSALELSNYQRF 69

                          90
                  ....*....|....*
gi 564359305  229 IDVLQAEVAALKTLV 243
Cdd:TIGR02473  70 IRQLDQRIQQQQQEL 84
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 151-240 6.30e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.15  E-value: 6.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359305 151 LEVREKGYERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLfEEAHKMVREANVKQATAEKQLKEAQGKID 230
Cdd:COG1196  234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL-EEAQAEEYELLAELARLEQDIARLEERRR 312

                         90
                 ....*....|
gi 564359305 231 VLQAEVAALK 240
Cdd:COG1196  313 ELEERLEELE 322
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
152-240 6.73e-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: 6.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359305  152 EVREKGYERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASLfEEAHKMVREanvkqatAEKQLKEAQG-KID 230
Cdd:COG4913   270 RLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARL-DALREELDE-------LEAQIRGNGGdRLE 341

                          90
                  ....*....|
gi 564359305  231 VLQAEVAALK 240
Cdd:COG4913   342 QLEREIERLE 351
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 151-238 6.73e-03

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


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 36.43  E-value: 6.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359305  151 LEVREKGYErlkEELAKAQREL--------------KLKDEECERLSKVRdqlgQELEELTASLFEEAHKMVREanvkQA 216
Cdd:pfam20492  11 LEERLKQYE---EETKKAQEELeeseetaeeleeerRQAEEEAERLEQKR----QEAEEEKERLEESAEMEAEE----KE 79

                          90       100
                  ....*....|....*....|..
gi 564359305  217 TAEKQLKEAQGKIDVLQAEVAA 238
Cdd:pfam20492  80 QLEAELAEAQEEIARLEEEVER 101
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 149-200 7.45e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 39.00  E-value: 7.45e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 564359305   149 SVLEVREKGYERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELTASL 200
Cdd:pfam01576  538 GTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDL 589
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
152-241 8.70e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 38.48  E-value: 8.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359305 152 EVREKGYERLkEELAKAQRELKLKDEECERLSKVRDQLGQELEELT---ASLFEEAHKMVREANVKQATAEKQLKEAQ-- 226
Cdd:PRK02224 492 EEVEERLERA-EDLVEAEDRIERLEERREDLEELIAERRETIEEKReraEELRERAAELEAEAEEKREAAAEAEEEAEea 570

                         90
                 ....*....|....*.
gi 564359305 227 -GKIDVLQAEVAALKT 241
Cdd:PRK02224 571 rEEVAELNSKLAELKE 586
UBAN cd09803
polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) ...
 158-240 8.87e-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: 35.40  E-value: 8.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359305 158 YERLKEELAKAQRELKLKDEECERLSKVRDQLGQELEELT-----ASLFEEAHKMVREANVKQATAEKQLKEaqgKIDVL 232
Cdd:cd09803    3 IDELAARLQEAEEALALKQEDIDELKEEIAQQEADLETIPvlkaqAEIYKSDFEAERAAREKLHQEKEQLAE---QLEYL 79


                 ....*...
gi 564359305 233 QAEVAALK 240
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.
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