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Conserved domains on  [gi|2078151963|gb|KAG8597254|]
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hypothetical protein GDO81_002223 [Engystomops pustulosus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SNARE_SNAP29C cd15856
C-terminal SNARE motif of SNAP29; C-terminal SNARE motif of SNAP29, a member of the Qb/Qc ...
 731-788 3.13e-24

C-terminal SNARE motif of SNAP29; C-terminal SNARE motif of SNAP29, a member of the Qb/Qc subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins. SNAP29 interacts with STX17 (Qa) and the lysosomal R-SNARE VAMP8. The complex plays a role in autophagosome-lysosome fusion. Autophagosome transports cytoplasmic materials including cytoplasmic proteins, glycogen, lipids, organelles, and invading bacteria to the lysosome for degradation. 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. Other members of the Qb/Qc SNAREs are SNAP23, SNAP25, SNAP47 and SEC9.


:

Pssm-ID: 277209  Cd Length: 59  Bit Score: 96.09  E-value: 3.13e-24
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2078151963 731 HQKIDNNLDDMSLGLGRLKGLALGLQSEIDEQDDVLGRLTGKVDKLDLNIKTTDKRIK 788
Cdd:cd15856     1 DQQLDENLDEMSSGLSRLKGLALGLGTEIDSQNDLLDRITDKADKADIKIKKQNKQMN 58
RNase_H_like super family cl14782
Ribonuclease H-like superfamily, including RNase H, HI, HII, HIII, and RNase-like domain IV of ...
 78-135 4.31e-10

Ribonuclease H-like superfamily, including RNase H, HI, HII, HIII, and RNase-like domain IV of spliceosomal protein Prp8; Ribonuclease H (RNase H) enzymes are divided into two major families, Type 1 and Type 2, based on amino acid sequence similarities and biochemical properties. RNase H is an endonuclease that cleaves the RNA strand of an RNA/DNA hybrid in a sequence non-specific manner in the presence of divalent cations. It is widely present in various organisms, including bacteria, archaea, and eukaryotes. Most prokaryotic and eukaryotic genomes contain multiple RNase H genes. Despite the lack of amino acid sequence homology, type 1 and type 2 RNase H share a main-chain fold and steric configurations of the four acidic active-site residues and have the same catalytic mechanism and functions in cells. RNase H is involved in DNA replication, repair and transcription. An important RNase H function is to remove Okazaki fragments during DNA replication. RNase H inhibitors have been explored as anti-HIV drug targets since RNase H inactivation inhibits reverse transcription. This model also includes the Prp8 domain IV, which adopts the RNase fold but shows low sequence homology; domain IV is implicated in key spliceosomal interactions.


The actual alignment was detected with superfamily member cd09275:

Pssm-ID: 449355  Cd Length: 120  Bit Score: 58.06  E-value: 4.31e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2078151963  78 TDASQSGWGADIAGLPVQGLWPSSIRSRSSNFRELRAVLETLRASAQSLRGKHVRIYS 135
Cdd:cd09275     4 TDASLSGWGAYLLNSRAHGPWSADERNKHINLLELKAVLLALQHFAAELKNRKILIRT 61
XerD super family cl44177
Site-specific recombinase XerD [Replication, recombination and repair];
305-619 2.50e-09

Site-specific recombinase XerD [Replication, recombination and repair];


The actual alignment was detected with superfamily member COG4974:

Pssm-ID: 443999 [Multi-domain]  Cd Length: 291  Bit Score: 59.24  E-value: 2.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2078151963 305 ISTLKASRKPVTHTI--YARIWGRFVSFC---GRTPPNQMSPnvSQVLDFLQAGFDKGLKTNSLKVQISALSAFFDTpLA 379
Cdd:COG4974    11 LEELKREKGLSPNTIkaYRRDLRRFLRFLeelGKIPLAEITP--EDIRAYLNYLRERGLSPSTINRYLAALRSFFRY-AV 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2078151963 380 ENRWIQRfVKATARPRPHIKQNIPNWdLSL--VLDYLTKIPFEPLETFRLRELtlkltFLIAITTARRLGEIQSLSIKEp 457
Cdd:COG4974    88 REGLLED-NPAAKVKLPKKPRKLPRV-LTEeeIEALLEALDTETPEGLRDRAL-----LLLLYATGLRVSELLGLKWSD- 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2078151963 458 yLKICEDKIVLMLDKaftpkvassfhRNQEIILPsfcqnpkhakeqeWHKlDVRRYLLHYLEVTKswRKDNNILlqFKGK 537
Cdd:COG4974   160 -IDLDRGTIRVRRGK-----------GGKERTVP-------------LSP-EALEALREYLEERR--PRDSDYL--FPTR 209

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2078151963 538 sKGRKASKASIARWIRTVIKEAydannlDISGTIRAHSTRGVAASWAEKRGASLEDICRAATWSTHLTFAKHYRLDVQSA 617
Cdd:COG4974   210 -RGRPLSRRAIRKILKRLAKRA------GIPKRVTPHSLRHTFATHLLEAGVDLRTVQELLGHSSISTTQIYTHVSDEEL 282


                  ..
gi 2078151963 618 RD 619
Cdd:COG4974   283 RE 284
 
Name Accession Description Interval E-value
SNARE_SNAP29C cd15856
C-terminal SNARE motif of SNAP29; C-terminal SNARE motif of SNAP29, a member of the Qb/Qc ...
 731-788 3.13e-24

C-terminal SNARE motif of SNAP29; C-terminal SNARE motif of SNAP29, a member of the Qb/Qc subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins. SNAP29 interacts with STX17 (Qa) and the lysosomal R-SNARE VAMP8. The complex plays a role in autophagosome-lysosome fusion. Autophagosome transports cytoplasmic materials including cytoplasmic proteins, glycogen, lipids, organelles, and invading bacteria to the lysosome for degradation. 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. Other members of the Qb/Qc SNAREs are SNAP23, SNAP25, SNAP47 and SEC9.


Pssm-ID: 277209  Cd Length: 59  Bit Score: 96.09  E-value: 3.13e-24
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2078151963 731 HQKIDNNLDDMSLGLGRLKGLALGLQSEIDEQDDVLGRLTGKVDKLDLNIKTTDKRIK 788
Cdd:cd15856     1 DQQLDENLDEMSSGLSRLKGLALGLGTEIDSQNDLLDRITDKADKADIKIKKQNKQMN 58
RNase_HI_RT_DIRS1 cd09275
DIRS1 family of RNase HI in long-term repeat retroelements; Ribonuclease H (RNase H) enzymes ...
 78-135 4.31e-10

DIRS1 family of RNase HI in long-term repeat retroelements; Ribonuclease H (RNase H) enzymes are divided into two major families, Type 1 and Type 2, based on amino acid sequence similarities and biochemical properties. RNase H is an endonuclease that cleaves the RNA strand of an RNA/DNA hybrid in a sequence non-specific manner in the presence of divalent cations. RNase H is widely present in various organisms, including bacteria, archaea and eukaryotes. RNase HI has also been observed as adjunct domains to the reverse transcriptase gene in retroviruses, in long-term repeat (LTR)-bearing retrotransposons and non-LTR retrotransposons. RNase HI in LTR retrotransposons perform degradation of the original RNA template, generation of a polypurine tract (the primer for plus-strand DNA synthesis), and final removal of RNA primers from newly synthesized minus and plus strands. The catalytic residues for RNase H enzymatic activity, three aspartatic acids and one glutamic acid residue (DEDD), are unvaried across all RNase H domains. Phylogenetic patterns of RNase HI of LTR retroelements is classified into five major families, Ty3/Gypsy, Ty1/Copia, Bel/Pao, DIRS1 and the vertebrate retroviruses. The structural features of DIRS1-group elements are different from typical LTR elements. RNase H inhibitors have been explored as an anti-HIV drug target because RNase H inactivation inhibits reverse transcription.


Pssm-ID: 260007  Cd Length: 120  Bit Score: 58.06  E-value: 4.31e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2078151963  78 TDASQSGWGADIAGLPVQGLWPSSIRSRSSNFRELRAVLETLRASAQSLRGKHVRIYS 135
Cdd:cd09275     4 TDASLSGWGAYLLNSRAHGPWSADERNKHINLLELKAVLLALQHFAAELKNRKILIRT 61
XerD COG4974
Site-specific recombinase XerD [Replication, recombination and repair];
305-619 2.50e-09

Site-specific recombinase XerD [Replication, recombination and repair];


Pssm-ID: 443999 [Multi-domain]  Cd Length: 291  Bit Score: 59.24  E-value: 2.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2078151963 305 ISTLKASRKPVTHTI--YARIWGRFVSFC---GRTPPNQMSPnvSQVLDFLQAGFDKGLKTNSLKVQISALSAFFDTpLA 379
Cdd:COG4974    11 LEELKREKGLSPNTIkaYRRDLRRFLRFLeelGKIPLAEITP--EDIRAYLNYLRERGLSPSTINRYLAALRSFFRY-AV 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2078151963 380 ENRWIQRfVKATARPRPHIKQNIPNWdLSL--VLDYLTKIPFEPLETFRLRELtlkltFLIAITTARRLGEIQSLSIKEp 457
Cdd:COG4974    88 REGLLED-NPAAKVKLPKKPRKLPRV-LTEeeIEALLEALDTETPEGLRDRAL-----LLLLYATGLRVSELLGLKWSD- 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2078151963 458 yLKICEDKIVLMLDKaftpkvassfhRNQEIILPsfcqnpkhakeqeWHKlDVRRYLLHYLEVTKswRKDNNILlqFKGK 537
Cdd:COG4974   160 -IDLDRGTIRVRRGK-----------GGKERTVP-------------LSP-EALEALREYLEERR--PRDSDYL--FPTR 209

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2078151963 538 sKGRKASKASIARWIRTVIKEAydannlDISGTIRAHSTRGVAASWAEKRGASLEDICRAATWSTHLTFAKHYRLDVQSA 617
Cdd:COG4974   210 -RGRPLSRRAIRKILKRLAKRA------GIPKRVTPHSLRHTFATHLLEAGVDLRTVQELLGHSSISTTQIYTHVSDEEL 282


                  ..
gi 2078151963 618 RD 619
Cdd:COG4974   283 RE 284
t_SNARE smart00397
Helical region found in SNAREs; All alpha-helical motifs that form twisted and parallel ...
 730-789 1.87e-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: 51.43  E-value: 1.87e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2078151963  730 YHQKIDNNLDDMSLGLGRLKGLALGLQSEIDEQDDVLGRLTGKVDKLDLNIKTTDKRIKE 789
Cdd:smart00397   6 REEERDEELEQLEKSIQELKQIFLDMGTELEEQGEQLDRIEDNVDDADVNLKKANKRLKK 65
 
Name Accession Description Interval E-value
SNARE_SNAP29C cd15856
C-terminal SNARE motif of SNAP29; C-terminal SNARE motif of SNAP29, a member of the Qb/Qc ...
 731-788 3.13e-24

C-terminal SNARE motif of SNAP29; C-terminal SNARE motif of SNAP29, a member of the Qb/Qc subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins. SNAP29 interacts with STX17 (Qa) and the lysosomal R-SNARE VAMP8. The complex plays a role in autophagosome-lysosome fusion. Autophagosome transports cytoplasmic materials including cytoplasmic proteins, glycogen, lipids, organelles, and invading bacteria to the lysosome for degradation. 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. Other members of the Qb/Qc SNAREs are SNAP23, SNAP25, SNAP47 and SEC9.


Pssm-ID: 277209  Cd Length: 59  Bit Score: 96.09  E-value: 3.13e-24
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2078151963 731 HQKIDNNLDDMSLGLGRLKGLALGLQSEIDEQDDVLGRLTGKVDKLDLNIKTTDKRIK 788
Cdd:cd15856     1 DQQLDENLDEMSSGLSRLKGLALGLGTEIDSQNDLLDRITDKADKADIKIKKQNKQMN 58
SNARE_Qc cd15841
SNARE motif, subgroup Qc; SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein ...
 731-789 3.37e-11

SNARE motif, subgroup Qc; SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) 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). Qc-, as well as Qa- and Qb-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 Qc SNAREs are C-terminal domains of SNAP23 and SNAP25, syntaxin 8, syntaxin 6, and Bet1.


Pssm-ID: 277194 [Multi-domain]  Cd Length: 59  Bit Score: 59.11  E-value: 3.37e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2078151963 731 HQKIDNNLDDMSLGLGRLKGLALGLQSEIDEQDDVLGRLTGKVDKLDLNIKTTDKRIKE 789
Cdd:cd15841     1 MKEQDEQLDELSGSVGRLKNIALAINEELDLQNRLLDDLDEDVDKTQSRLKKVNKKLKK 59
SNARE_SEC9C cd15857
C-terminal SNARE motif of SEC9; C-terminal SNARE motif of fungal SEC9, a member of the Qb/Qc ...
 734-788 6.96e-11

C-terminal SNARE motif of SEC9; C-terminal SNARE motif of fungal SEC9, a member of the Qb/Qc subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins. SEC9 interacts with Sso1(Qa) and the lysosomal R-SNARE Snc1. The complex plays a role in post-Golgi transport. 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. Other members of the Qb/Qc SNAREs are SNAP23, SNAP25, SNAP47 and SNAP29.


Pssm-ID: 277210  Cd Length: 59  Bit Score: 57.97  E-value: 6.96e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2078151963 734 IDNNLDDMSLGLGRLKGLALGLQSEIDEQDDVLGRLTGKVDKLDLNIKTTDKRIK 788
Cdd:cd15857     4 IDDNLDEIGGVVGRLKALAMAMGEEVDSQNKRLDRIEEKTDRLDDKVHMNTERLK 58
RNase_HI_RT_DIRS1 cd09275
DIRS1 family of RNase HI in long-term repeat retroelements; Ribonuclease H (RNase H) enzymes ...
 78-135 4.31e-10

DIRS1 family of RNase HI in long-term repeat retroelements; Ribonuclease H (RNase H) enzymes are divided into two major families, Type 1 and Type 2, based on amino acid sequence similarities and biochemical properties. RNase H is an endonuclease that cleaves the RNA strand of an RNA/DNA hybrid in a sequence non-specific manner in the presence of divalent cations. RNase H is widely present in various organisms, including bacteria, archaea and eukaryotes. RNase HI has also been observed as adjunct domains to the reverse transcriptase gene in retroviruses, in long-term repeat (LTR)-bearing retrotransposons and non-LTR retrotransposons. RNase HI in LTR retrotransposons perform degradation of the original RNA template, generation of a polypurine tract (the primer for plus-strand DNA synthesis), and final removal of RNA primers from newly synthesized minus and plus strands. The catalytic residues for RNase H enzymatic activity, three aspartatic acids and one glutamic acid residue (DEDD), are unvaried across all RNase H domains. Phylogenetic patterns of RNase HI of LTR retroelements is classified into five major families, Ty3/Gypsy, Ty1/Copia, Bel/Pao, DIRS1 and the vertebrate retroviruses. The structural features of DIRS1-group elements are different from typical LTR elements. RNase H inhibitors have been explored as an anti-HIV drug target because RNase H inactivation inhibits reverse transcription.


Pssm-ID: 260007  Cd Length: 120  Bit Score: 58.06  E-value: 4.31e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2078151963  78 TDASQSGWGADIAGLPVQGLWPSSIRSRSSNFRELRAVLETLRASAQSLRGKHVRIYS 135
Cdd:cd09275     4 TDASLSGWGAYLLNSRAHGPWSADERNKHINLLELKAVLLALQHFAAELKNRKILIRT 61
XerD COG4974
Site-specific recombinase XerD [Replication, recombination and repair];
305-619 2.50e-09

Site-specific recombinase XerD [Replication, recombination and repair];


Pssm-ID: 443999 [Multi-domain]  Cd Length: 291  Bit Score: 59.24  E-value: 2.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2078151963 305 ISTLKASRKPVTHTI--YARIWGRFVSFC---GRTPPNQMSPnvSQVLDFLQAGFDKGLKTNSLKVQISALSAFFDTpLA 379
Cdd:COG4974    11 LEELKREKGLSPNTIkaYRRDLRRFLRFLeelGKIPLAEITP--EDIRAYLNYLRERGLSPSTINRYLAALRSFFRY-AV 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2078151963 380 ENRWIQRfVKATARPRPHIKQNIPNWdLSL--VLDYLTKIPFEPLETFRLRELtlkltFLIAITTARRLGEIQSLSIKEp 457
Cdd:COG4974    88 REGLLED-NPAAKVKLPKKPRKLPRV-LTEeeIEALLEALDTETPEGLRDRAL-----LLLLYATGLRVSELLGLKWSD- 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2078151963 458 yLKICEDKIVLMLDKaftpkvassfhRNQEIILPsfcqnpkhakeqeWHKlDVRRYLLHYLEVTKswRKDNNILlqFKGK 537
Cdd:COG4974   160 -IDLDRGTIRVRRGK-----------GGKERTVP-------------LSP-EALEALREYLEERR--PRDSDYL--FPTR 209

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2078151963 538 sKGRKASKASIARWIRTVIKEAydannlDISGTIRAHSTRGVAASWAEKRGASLEDICRAATWSTHLTFAKHYRLDVQSA 617
Cdd:COG4974   210 -RGRPLSRRAIRKILKRLAKRA------GIPKRVTPHSLRHTFATHLLEAGVDLRTVQELLGHSSISTTQIYTHVSDEEL 282


                  ..
gi 2078151963 618 RD 619
Cdd:COG4974   283 RE 284
t_SNARE smart00397
Helical region found in SNAREs; All alpha-helical motifs that form twisted and parallel ...
 730-789 1.87e-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: 51.43  E-value: 1.87e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2078151963  730 YHQKIDNNLDDMSLGLGRLKGLALGLQSEIDEQDDVLGRLTGKVDKLDLNIKTTDKRIKE 789
Cdd:smart00397   6 REEERDEELEQLEKSIQELKQIFLDMGTELEEQGEQLDRIEDNVDDADVNLKKANKRLKK 65
XerC COG4973
Site-specific recombinase XerC [Replication, recombination and repair];
312-452 1.30e-07

Site-specific recombinase XerC [Replication, recombination and repair];


Pssm-ID: 443998 [Multi-domain]  Cd Length: 287  Bit Score: 53.81  E-value: 1.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2078151963 312 RKPVTHTIYARIWGRFVSFCGR--TPPNQMSPnvSQVLDFLQAGFDKGLKTNSLKVQISALSAFFDTpLAENRWIQ---- 385
Cdd:COG4973    20 LSPKTLEAYRRDLRRLIPLLGDadLPLEELTP--ADVRRFLARLHRRGLSPRTLNRRLSALRSFFNW-AVREGLLEanpa 96

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2078151963 386 RFVKATARPRPHIKqnipNWDLSLVLDYLTKIPFEPLETfRLRELtlkltFLIAITTARRLGEIQSL 452
Cdd:COG4973    97 AGVKAPKAPRKLPR----ALTVDELAQLLDALADDPLAV-RDRAI-----VELLYSTGLRLGELVGL 153
SNARE_SNAP47C cd15854
C-terminal SNARE motif of SNAP47; C-terminal SNARE motif of SNAP47, a member of the Qb/Qc ...
 745-788 2.49e-07

C-terminal SNARE motif of SNAP47; C-terminal SNARE motif of SNAP47, a member of the Qb/Qc subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins. The exact funtion of SNAP47 is unknown. 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. Other members of the Qb/Qc SNAREs are SNAP23, SNAP25, SNAP29 and SEC9.


Pssm-ID: 277207  Cd Length: 59  Bit Score: 48.32  E-value: 2.49e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2078151963 745 LGRLKGLALGLQSEIDEQDDVLGRLTGKVDKLDLNIKTTDKRIK 788
Cdd:cd15854    15 LRKLKSLALEAETELERQDEALDVLSDSVDRATLNIDKHNRRMK 58
SNARE_SNAP25C cd15885
C-terminal SNARE motif of SNAP25; C-terminal SNARE motifs of SNAP25, a member of the Qb/Qc ...
 735-789 1.66e-04

C-terminal SNARE motif of SNAP25; C-terminal SNARE motifs of SNAP25, a member of the Qb/Qc subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins. SNAP25 interacts with Syntaxin-1 (Qa) and the R-SNARE VAMP2 (also called synaptobrevin-2). The complex plays a role in transport of secretory granule from trans-Golgi network to the plasma membrane. 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. Other members of the Qb/Qc SNAREs are SNAP23, SNAP29, SNAP47 and SEC9.


Pssm-ID: 277238  Cd Length: 59  Bit Score: 40.03  E-value: 1.66e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2078151963 735 DNNLDDMSLGLGRLKGLALGLQSEIDEQDDVLGRLTGKVDKLDLNIKTTDKRIKE 789
Cdd:cd15885     5 EENLGQVSGMIGNLRNMAIDMGSEIESQNRQIDRINEKAESNETRIDSANKRATK 59
SNARE_SNAP23C cd15884
C-terminal SNARE motif of SNAP23; C-terminal SNARE motifs of SNAP23, a member of the Qb/Qc ...
 734-789 1.63e-03

C-terminal SNARE motif of SNAP23; C-terminal SNARE motifs of SNAP23, a member of the Qb/Qc subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins. SNAP23 interacts with Syntaxin-4 (Qa) and the R-SNARE VAMP8. The complex plays a role in exocytosis of secretory granule. 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. Other members of the Qb/Qc SNAREs are SNAP25, SNAP29, SNAP47 and SEC9.


Pssm-ID: 277237  Cd Length: 59  Bit Score: 37.44  E-value: 1.63e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2078151963 734 IDNNLDDMSLGLGRLKGLALGLQSEIDEQDDVLGRLTGKVDkldlnikTTDKRIKE 789
Cdd:cd15884     4 MDENLTQVGSILGNLKSMALDMGNELDKQNKQIGRINEKAD-------MNSDRIDE 52
SNARE_SNAP25C_23C cd15855
C-terminal SNARE motif of SNAP25 and SNAP23; C-terminal SNARE motifs of SNAP25 and SNAP23, ...
 733-774 1.88e-03

C-terminal SNARE motif of SNAP25 and SNAP23; C-terminal SNARE motifs of SNAP25 and SNAP23, members of the Qb/Qc subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins. SNAP23 interacts with STX4 (Qa) and the lysosomal R-SNARE VAMP8. The complex plays a role in transport of secretory granule from trans-Golgi network to the plasma membrane. SNAP25 interacts with Syntaxin-1 (Qa) and the R-SNARE VAMP2 (also called synaptobrevin-2). The complex plays a role in transport of secretory granule from trans-Golgi network to the plasma membrane. 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. Other members of the Qb/Qc SNAREs are SNAP29, SNAP47 and SEC9.


Pssm-ID: 277208  Cd Length: 59  Bit Score: 37.11  E-value: 1.88e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2078151963 733 KIDNNLDDMSLGLGRLKGLALGLQSEIDEQDDVLGRLTGKVD 774
Cdd:cd15855     3 EMDENLQQVSGILGNLRHMALDMGNEIDTQNRQLDRIDEKAD 44
SNARE_Syntaxin8 cd15852
SNARE motif of syntaxin 8; Syntaxin 8 forms a complex with syntaxin 7 (Qa), Vti1b (Qb) and ...
 735-790 2.24e-03

SNARE motif of syntaxin 8; Syntaxin 8 forms a complex with syntaxin 7 (Qa), Vti1b (Qb) and either VAMP7 or VAMP8 (R-SNARE) and is involved in the transport from early endosomes to the lysosome. Syntaxin 8 is a member of the Qc subgroup of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins, which consist of coiled-coil helices (called SNARE motifs) that mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complexes mediate 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.


Pssm-ID: 277205 [Multi-domain]  Cd Length: 59  Bit Score: 36.82  E-value: 2.24e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2078151963 735 DNNLDDMSLGLGRLKGLALGLQSEIDEQDDVLGRLTGKVDKldlniktTDKRIKEE 790
Cdd:cd15852     5 DQGLDALSSIISRQKQIGQAIGDEVDDQNEIIDDLADGMDR-------TDARLRRE 53
SNARE_VAM7 cd15858
SNARE motif of VAM7; Fungal VAM7 (vacuolar morphogenesis protein 7) is a member of the Qc ...
 735-788 3.46e-03

SNARE motif of VAM7; Fungal VAM7 (vacuolar morphogenesis protein 7) is a member of the Qc subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) protein family involved in vacuolar protein transport and membrane fusion. 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). Qc-, as well as Qa- and Qb-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.


Pssm-ID: 277211 [Multi-domain]  Cd Length: 59  Bit Score: 36.33  E-value: 3.46e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2078151963 735 DNNLDDMSLGLGRLKGLALGLQSEIDEQDDVLGRLTGKVDKLDLNIKTTDKRIK 788
Cdd:cd15858     5 DQQLEQLRKIVQRQKELGLAINQELEEQNELLDELDEDVDRTGGKLRVANKRAK 58
 
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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