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Conserved domains on  [gi|569007485|ref|XP_006527247|]
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vesicle transport through interaction with t-SNAREs homolog 1A isoform X1 [Mus musculus]

Protein Classification

vesicle transport through interaction with t-SNAREs homolog 1A( domain architecture ID 10523358)

vesicle transport through interaction with t-SNAREs homolog 1A is a v-SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) that mediates vesicle transport pathways through interactions with t-SNAREs on the target membrane

CATH:  1.20.58.400
Gene Ontology:  GO:0005484|GO:0006906|GO:0015031
SCOP:  4000986
TCDB:  1.F.1

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SNARE_Vti1a cd15891
SNARE motif of Vti1b-like; Vti1a (vesicle transport through interaction with t-SNAREs homolog ...
 129-190 1.12e-31

SNARE motif of Vti1b-like; Vti1a (vesicle transport through interaction with t-SNAREs homolog 1A) belongs to the Qb subgroup of SNAREs (soluble N-ethylmaleimide-sensitive factor attachment protein receptor). Vti1a interacts with syntaxin 16 (Qa), syntaxin 6 (Qc), and the lysosomal R-SNARE VAMP4 to form an endosomal SNARE core complex that mediates transport from the early endosomes to the TGN (trans-Golgi network). SNARE proteins consist of coiled-coil helices (called SNARE motifs) which mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles. Examples for members of the Qb SNAREs are N-terminal domains of SNAP23 and SNAP25, Vti1, Sec20 and GS27.


:

Pssm-ID: 277244  Cd Length: 62  Bit Score: 112.01  E-value: 1.12e-31
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569007485 129 TERLERSSRRLEAGYQIAVETEQIGQEMLENLSHDREKIQRARDRLRDADANLGKSSRILTG 190
Cdd:cd15891    1 TERLERSSRRLEDGYRIAVETEQIGAQILDDLHSQRETIQRSRDRLRETDSELGKSSRVLSG 62
V-SNARE pfam05008
Vesicle transport v-SNARE protein N-terminus; V-SNARE proteins are required for protein ...
 12-90 2.03e-26

Vesicle transport v-SNARE protein N-terminus; V-SNARE proteins are required for protein traffic between eukaryotic organelles. The v-SNAREs on transport vesicles interact with t-SNAREs on target membranes in order to facilitate this. This domain is the N-terminal half of the V-Snare proteins.


:

Pssm-ID: 461516  Cd Length: 79  Bit Score: 98.83  E-value: 2.03e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569007485   12 FAVLTAEITSKIARVPRLPPDEKKQMVANVEKQLEEARELLEQMDLEVREIPPQSRGMYSNRMRSYKQEMGKLETDFKR 90
Cdd:pfam05008   1 FKELLAEITRKLARLSSLPGEERKAALREIERKLDEAEELLDQMELEVRNLPSSERSKYKAKLREYKSDLKKLKKELKR 79
 
Name Accession Description Interval E-value
SNARE_Vti1a cd15891
SNARE motif of Vti1b-like; Vti1a (vesicle transport through interaction with t-SNAREs homolog ...
 129-190 1.12e-31

SNARE motif of Vti1b-like; Vti1a (vesicle transport through interaction with t-SNAREs homolog 1A) belongs to the Qb subgroup of SNAREs (soluble N-ethylmaleimide-sensitive factor attachment protein receptor). Vti1a interacts with syntaxin 16 (Qa), syntaxin 6 (Qc), and the lysosomal R-SNARE VAMP4 to form an endosomal SNARE core complex that mediates transport from the early endosomes to the TGN (trans-Golgi network). SNARE proteins consist of coiled-coil helices (called SNARE motifs) which mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles. Examples for members of the Qb SNAREs are N-terminal domains of SNAP23 and SNAP25, Vti1, Sec20 and GS27.


Pssm-ID: 277244  Cd Length: 62  Bit Score: 112.01  E-value: 1.12e-31
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569007485 129 TERLERSSRRLEAGYQIAVETEQIGQEMLENLSHDREKIQRARDRLRDADANLGKSSRILTG 190
Cdd:cd15891    1 TERLERSSRRLEDGYRIAVETEQIGAQILDDLHSQRETIQRSRDRLRETDSELGKSSRVLSG 62
V-SNARE pfam05008
Vesicle transport v-SNARE protein N-terminus; V-SNARE proteins are required for protein ...
 12-90 2.03e-26

Vesicle transport v-SNARE protein N-terminus; V-SNARE proteins are required for protein traffic between eukaryotic organelles. The v-SNAREs on transport vesicles interact with t-SNAREs on target membranes in order to facilitate this. This domain is the N-terminal half of the V-Snare proteins.


Pssm-ID: 461516  Cd Length: 79  Bit Score: 98.83  E-value: 2.03e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569007485   12 FAVLTAEITSKIARVPRLPPDEKKQMVANVEKQLEEARELLEQMDLEVREIPPQSRGMYSNRMRSYKQEMGKLETDFKR 90
Cdd:pfam05008   1 FKELLAEITRKLARLSSLPGEERKAALREIERKLDEAEELLDQMELEVRNLPSSERSKYKAKLREYKSDLKKLKKELKR 79
V-SNARE_C pfam12352
Snare region anchored in the vesicle membrane C-terminus; Within the SNARE proteins ...
 130-194 7.53e-20

Snare region anchored in the vesicle membrane C-terminus; Within the SNARE proteins interactions in the C-terminal half of the SNARE helix are critical to the driving of membrane fusion; whereas interactions in the N-terminal half of the SNARE domain are important for promoting priming or docking of the vesicle pfam05008.


Pssm-ID: 289148  Cd Length: 66  Bit Score: 81.12  E-value: 7.53e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569007485  130 ERLERSSRRLEAGYQIAVETEQIGQEMLENLSHDREKIQRARDRLRDADANLGKSSRILTGMLRR 194
Cdd:pfam12352   1 ERLLREHDRLKNSHRIADETISIGQAILEDLHSQRETLKRARNKLHNTDNRLGKSNSTLRLINRR 65
t_SNARE smart00397
Helical region found in SNAREs; All alpha-helical motifs that form twisted and parallel ...
 127-191 1.44e-08

Helical region found in SNAREs; All alpha-helical motifs that form twisted and parallel four-helix bundles in target soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein (SNAP) receptor proteins. This motif found in "Q-SNAREs".


Pssm-ID: 197699 [Multi-domain]  Cd Length: 66  Bit Score: 50.66  E-value: 1.44e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569007485   127 DNTERLERSSRRLEAGYQIAVETEQIGQEMLENLSHDREKIQRARDRLRDADANLGKSSRILTGM 191
Cdd:smart00397   2 QALAREEERDEELEQLEKSIQELKQIFLDMGTELEEQGEQLDRIEDNVDDADVNLKKANKRLKKA 66
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
46-183 9.46e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.60  E-value: 9.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007485  46 EEARELLEQMDLEvREIPPQSRGMYSNRMRSYKQEMGKLETDFKRSRIAYSDEVRNELLGDAGNSSENQLIKLREERAHL 125
Cdd:COG4717  319 EELEELLAALGLP-PDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEY 397

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007485 126 LDNTERLERSSRRLEA--GYQIAVETEQIGQEMLENLSHDREKIQRARDRLRDADANLGK 183
Cdd:COG4717  398 QELKEELEELEEQLEEllGELEELLEALDEEELEEELEELEEELEELEEELEELREELAE 457
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 4-176 5.31e-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: 5.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007485     4 DFEGYEQDFAVLTAEiTSKIARVPRLppDEKKQMVANVEKQLEEARELLEQMDLEVREIPPQSRGMYSNRMRSYKQEMGK 83
Cdd:TIGR02169  222 EYEGYELLKEKEALE-RQKEAIERQL--ASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGE 298

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007485    84 LETDFKR----------------SRIAYSDEVRNELLGDAGNSSEN------QLIKLREERAHLLDNTERLERSSRRLEA 141
Cdd:TIGR02169  299 LEAEIASlersiaekereledaeERLAKLEAEIDKLLAEIEELEREieeerkRRDKLTEEYAELKEELEDLRAELEEVDK 378

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 569007485   142 GYQIAVETEQIGQEMLENLSHDREKIQRARDRLRD 176
Cdd:TIGR02169  379 EFAETRDELKDYREKLEKLKREINELKRELDRLQE 413
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
40-181 7.11e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 37.74  E-value: 7.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007485  40 NVEKQLEEARELLEQMDLEVREIPP--QSRGMY---SNRMRSYKQEMGKLETDFKRsriaYSDEVRN--ELLGDAgNSSE 112
Cdd:PRK03918 263 ELEERIEELKKEIEELEEKVKELKElkEKAEEYiklSEFYEEYLDELREIEKRLSR----LEEEINGieERIKEL-EEKE 337

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007485 113 NQLIKLREERAHLLDNTERLERSSRRLEAGYQIAVETEQIGQE-----------MLENLSHDREKIQRARDRLRDADANL 181
Cdd:PRK03918 338 ERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRltgltpeklekELEELEKAKEEIEEEISKITARIGEL 417
 
Name Accession Description Interval E-value
SNARE_Vti1a cd15891
SNARE motif of Vti1b-like; Vti1a (vesicle transport through interaction with t-SNAREs homolog ...
 129-190 1.12e-31

SNARE motif of Vti1b-like; Vti1a (vesicle transport through interaction with t-SNAREs homolog 1A) belongs to the Qb subgroup of SNAREs (soluble N-ethylmaleimide-sensitive factor attachment protein receptor). Vti1a interacts with syntaxin 16 (Qa), syntaxin 6 (Qc), and the lysosomal R-SNARE VAMP4 to form an endosomal SNARE core complex that mediates transport from the early endosomes to the TGN (trans-Golgi network). SNARE proteins consist of coiled-coil helices (called SNARE motifs) which mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles. Examples for members of the Qb SNAREs are N-terminal domains of SNAP23 and SNAP25, Vti1, Sec20 and GS27.


Pssm-ID: 277244  Cd Length: 62  Bit Score: 112.01  E-value: 1.12e-31
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569007485 129 TERLERSSRRLEAGYQIAVETEQIGQEMLENLSHDREKIQRARDRLRDADANLGKSSRILTG 190
Cdd:cd15891    1 TERLERSSRRLEDGYRIAVETEQIGAQILDDLHSQRETIQRSRDRLRETDSELGKSSRVLSG 62
V-SNARE pfam05008
Vesicle transport v-SNARE protein N-terminus; V-SNARE proteins are required for protein ...
 12-90 2.03e-26

Vesicle transport v-SNARE protein N-terminus; V-SNARE proteins are required for protein traffic between eukaryotic organelles. The v-SNAREs on transport vesicles interact with t-SNAREs on target membranes in order to facilitate this. This domain is the N-terminal half of the V-Snare proteins.


Pssm-ID: 461516  Cd Length: 79  Bit Score: 98.83  E-value: 2.03e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569007485   12 FAVLTAEITSKIARVPRLPPDEKKQMVANVEKQLEEARELLEQMDLEVREIPPQSRGMYSNRMRSYKQEMGKLETDFKR 90
Cdd:pfam05008   1 FKELLAEITRKLARLSSLPGEERKAALREIERKLDEAEELLDQMELEVRNLPSSERSKYKAKLREYKSDLKKLKKELKR 79
SNARE_Vti1 cd15862
SNARE motif of Vti1; Vti1 (vesicle transport through interaction with t-SNAREs homolog 1) ...
 129-190 3.54e-20

SNARE motif of Vti1; Vti1 (vesicle transport through interaction with t-SNAREs homolog 1) belongs to the Qb subgroup of SNAREs (soluble N-ethylmaleimide-sensitive factor attachment protein receptor). Vti1b interacts with syntaxin 7 (Qa), syntaxin 8 (Qc), and the lysosomal R-SNARE VAMP8 or VAMP7 to form the endosomal SNARE core complex that mediates transport from the early endosomes and the MVBs (multivesicular bodies), and from the MVBs to the lysosomes, respectively. Vti1a interacts with syntaxin 16 (Qa), syntaxin 6 (Qc), and the lysosomal R-SNARE VAMP4 to form an endosomal SNARE core complex that mediates transport from the early endosomes to the TGN (trans-Golgi network). SNARE proteins consist of coiled-coil helices (called SNARE motifs) which mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles. Examples for members of the Qb SNAREs are N-terminal domains of SNAP23 and SNAP25, Vti1, Sec20 and GS27.


Pssm-ID: 277215  Cd Length: 62  Bit Score: 81.81  E-value: 3.54e-20
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569007485 129 TERLERSSRRLEAGYQIAVETEQIGQEMLENLSHDREKIQRARDRLRDADANLGKSSRILTG 190
Cdd:cd15862    1 TDRLDRSSDRLEDSRRIAAETEEVGANILEDLGRQRETLLRARDRLRETDGNLDRSRRILKS 62
V-SNARE_C pfam12352
Snare region anchored in the vesicle membrane C-terminus; Within the SNARE proteins ...
 130-194 7.53e-20

Snare region anchored in the vesicle membrane C-terminus; Within the SNARE proteins interactions in the C-terminal half of the SNARE helix are critical to the driving of membrane fusion; whereas interactions in the N-terminal half of the SNARE domain are important for promoting priming or docking of the vesicle pfam05008.


Pssm-ID: 289148  Cd Length: 66  Bit Score: 81.12  E-value: 7.53e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569007485  130 ERLERSSRRLEAGYQIAVETEQIGQEMLENLSHDREKIQRARDRLRDADANLGKSSRILTGMLRR 194
Cdd:pfam12352   1 ERLLREHDRLKNSHRIADETISIGQAILEDLHSQRETLKRARNKLHNTDNRLGKSNSTLRLINRR 65
SNARE_Vti1b cd15890
SNARE motif of Vti1b-like; Vti1b (vesicle transport through interaction with t-SNAREs homolog ...
 129-190 7.75e-17

SNARE motif of Vti1b-like; Vti1b (vesicle transport through interaction with t-SNAREs homolog 1B) belongs to the Qb subgroup of SNAREs (soluble N-ethylmaleimide-sensitive factor attachment protein receptor). Vti1b interacts with syntaxin 7 (Qa), syntaxin 8 (Qc), and the lysosomal R-SNARE VAMP8 or VAMP7 to form the endosomal SNARE core complexes that mediate transport from the early endosomes and the MVBs (multivesicular bodies), and from the MVBs to the lysosomes, respectively. SNARE proteins consist of coiled-coil helices (called SNARE motifs) which mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles. Examples for members of the Qb SNAREs are N-terminal domains of SNAP23 and SNAP25, Vti1, Sec20 and GS27.


Pssm-ID: 277243  Cd Length: 62  Bit Score: 72.99  E-value: 7.75e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569007485 129 TERLERSSRRLEAGYQIAVETEQIGQEMLENLSHDREKIQRARDRLRDADANLGKSSRILTG 190
Cdd:cd15890    1 TESLNRTSDSLARSQRIAAETEQIGTEIIEELGEQREQLLRTRDRLEETDANLSRARRILRS 62
t_SNARE smart00397
Helical region found in SNAREs; All alpha-helical motifs that form twisted and parallel ...
 127-191 1.44e-08

Helical region found in SNAREs; All alpha-helical motifs that form twisted and parallel four-helix bundles in target soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein (SNAP) receptor proteins. This motif found in "Q-SNAREs".


Pssm-ID: 197699 [Multi-domain]  Cd Length: 66  Bit Score: 50.66  E-value: 1.44e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569007485   127 DNTERLERSSRRLEAGYQIAVETEQIGQEMLENLSHDREKIQRARDRLRDADANLGKSSRILTGM 191
Cdd:smart00397   2 QALAREEERDEELEQLEKSIQELKQIFLDMGTELEEQGEQLDRIEDNVDDADVNLKKANKRLKKA 66
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
46-183 9.46e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.60  E-value: 9.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007485  46 EEARELLEQMDLEvREIPPQSRGMYSNRMRSYKQEMGKLETDFKRSRIAYSDEVRNELLGDAGNSSENQLIKLREERAHL 125
Cdd:COG4717  319 EELEELLAALGLP-PDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEY 397

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007485 126 LDNTERLERSSRRLEA--GYQIAVETEQIGQEMLENLSHDREKIQRARDRLRDADANLGK 183
Cdd:COG4717  398 QELKEELEELEEQLEEllGELEELLEALDEEELEEELEELEEELEELEEELEELREELAE 457
SNARE_SNAP25N_23N_29N_SEC9N cd15861
N-terminal SNARE motif of SNAP25, SNAP23, SNAP29, and SEC9; N-terminal SNARE motif of members ...
 127-190 2.53e-04

N-terminal SNARE motif of SNAP25, SNAP23, SNAP29, and SEC9; N-terminal SNARE motif of members of the Qb/Qc subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins. Qb/Qc SNAREs consist of 2 coiled-coil helices (called SNARE motifs, one belonging to the Qb subgroup and one belonging to the Qc subgroup), which mediate the interactions with other SNARE proteins, and a transmembrane domain. In general, the SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles. Examples for members of the Qb/Qc SNAREs are SNAP23, SNAP25, SNAP29, SNAP47 and SEC9.


Pssm-ID: 277214  Cd Length: 65  Bit Score: 38.32  E-value: 2.53e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569007485 127 DNTERLERSSRrleagyqIAVETEQIGQEMLENLSHDREKIQRARDRLRDADANLGKSSRILTG 190
Cdd:cd15861    9 ETTESIRRALR-------LAEETKEIGADTLEELHRQGEQLERIHNDVDDIDSNLKRAEKLLKE 65
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 4-176 5.31e-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: 5.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007485     4 DFEGYEQDFAVLTAEiTSKIARVPRLppDEKKQMVANVEKQLEEARELLEQMDLEVREIPPQSRGMYSNRMRSYKQEMGK 83
Cdd:TIGR02169  222 EYEGYELLKEKEALE-RQKEAIERQL--ASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGE 298

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007485    84 LETDFKR----------------SRIAYSDEVRNELLGDAGNSSEN------QLIKLREERAHLLDNTERLERSSRRLEA 141
Cdd:TIGR02169  299 LEAEIASlersiaekereledaeERLAKLEAEIDKLLAEIEELEREieeerkRRDKLTEEYAELKEELEDLRAELEEVDK 378

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 569007485   142 GYQIAVETEQIGQEMLENLSHDREKIQRARDRLRD 176
Cdd:TIGR02169  379 EFAETRDELKDYREKLEKLKREINELKRELDRLQE 413
7TMR-HDED pfam07697
7TM-HD extracellular; This entry represents the extracellular domain of the 7TM-HD (7TM ...
 33-177 1.10e-03

7TM-HD extracellular; This entry represents the extracellular domain of the 7TM-HD (7TM Receptors with HD hydrolase).


Pssm-ID: 462232 [Multi-domain]  Cd Length: 219  Bit Score: 39.62  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007485   33 EKKQMVANVEKQLEEARELLEQMDLEVREIPPQSRGM--YSNRMRSYKQEMGKLETDFKRSRIAYSDEVRNELLgdagNS 110
Cdd:pfam07697  27 KREEAAESVPPVYDLDPEVTEEVVQRLEELFDAIDEVraATNSEEDLEEKIEQLKEALPFYLQSESDEELEALL----NL 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007485  111 SENQLIKLREERAHLLD---------NTERLERSSRRLEAGYQIAVETEQIGQEMLE-----NLSHDREKIQRARDRLRD 176
Cdd:pfam07697 103 SDEDLQELQDGILQILErilsqgireDELEEAREAVAEQLKASLSSELRELASKLLSsvlkpNLFYDEEATEERREEAAE 182


                  .
gi 569007485  177 A 177
Cdd:pfam07697 183 A 183
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
40-181 7.11e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 37.74  E-value: 7.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007485  40 NVEKQLEEARELLEQMDLEVREIPP--QSRGMY---SNRMRSYKQEMGKLETDFKRsriaYSDEVRN--ELLGDAgNSSE 112
Cdd:PRK03918 263 ELEERIEELKKEIEELEEKVKELKElkEKAEEYiklSEFYEEYLDELREIEKRLSR----LEEEINGieERIKEL-EEKE 337

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007485 113 NQLIKLREERAHLLDNTERLERSSRRLEAGYQIAVETEQIGQE-----------MLENLSHDREKIQRARDRLRDADANL 181
Cdd:PRK03918 338 ERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRltgltpeklekELEELEKAKEEIEEEISKITARIGEL 417
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
32-181 7.31e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 37.69  E-value: 7.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007485  32 DEKKQMVANVEKQLEEARELLEQMDLEVREI--------PPQSRGMYSNRMRSYKQEMGKLETDFK---------RSRIA 94
Cdd:COG3206  171 EEARKALEFLEEQLPELRKELEEAEAALEEFrqknglvdLSEEAKLLLQQLSELESQLAEARAELAeaearlaalRAQLG 250

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007485  95 YSDEVRNELLGDAGNSS-ENQLIKLREERAHLLdntERL-ERSSRRLEAGYQIAVETEQIGQEMLENLSHDREKIQRARD 172
Cdd:COG3206  251 SGPDALPELLQSPVIQQlRAQLAELEAELAELS---ARYtPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQA 327


                 ....*....
gi 569007485 173 RLRDADANL 181
Cdd:COG3206  328 REASLQAQL 336
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 32-197 7.62e-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: 7.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007485  32 DEKKQMVANVEKQLEEARELLEQMDLEVREIppqsrgmySNRMRSYKQEMGKLETDFKRSRIAYSdEVRNELlgdagNSS 111
Cdd:COG1196  235 RELEAELEELEAELEELEAELEELEAELAEL--------EAELEELRLELEELELELEEAQAEEY-ELLAEL-----ARL 300

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007485 112 ENQLIKLREERAHLLDNTERLERSSRRLEAgyQIAVETEQIgQEMLENLSHDREKIQRARDRLRDADANLGKSSRILTGM 191
Cdd:COG1196  301 EQDIARLEERRRELEERLEELEEELAELEE--ELEELEEEL-EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377


                 ....*.
gi 569007485 192 LRRWKA 197
Cdd:COG1196  378 EEELEE 383
 
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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