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Conserved domains on  [gi|1376261892|ref|XP_024514089|]
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chitin synthase, putative [Cryptococcus neoformans var. neoformans JEC21]

Protein Classification

Chitin_synth_1 and Glyco_tranf_GTA_type domain-containing protein( domain architecture ID 10938212)

protein containing domains Chitin_synth_1N, Chitin_synth_1, and Glyco_tranf_GTA_type

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Chitin_synth_1 pfam01644
Chitin synthase; This region is found commonly in chitin synthases classes I, II and III. ...
342-504 3.04e-116

Chitin synthase; This region is found commonly in chitin synthases classes I, II and III. Chitin a linear homopolymer of GlcNAc residues, it is an important component of the cell wall of fungi and is synthesized on the cytoplasmic surface of the cell membrane by membrane bound chitin synthases.


:

Pssm-ID: 426363  Cd Length: 163  Bit Score: 342.62  E-value: 3.04e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376261892 342 MYNENAELFCRTLYGVMKNIAHLCGRKNSRVWGKDGWQKVVVCIVADGRKAVNPRVLDCLAALGVYQEGAMTNTVKDRPV 421
Cdd:pfam01644   1 MYNEDEILLARTLHGVMKNIAHLCSRKRSKTWGPDGWKKVVVCIVSDGRNKINPRTLDLLAALGVYQEGIAKNDVNGKPV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376261892 422 TAHVFEYTTSFALDGDLHFKYPDKGIVPCQIIFCMKEKNAKKINSHRWFFNAFAPLLSPNVCILLDVGTQPAPKSIYHLW 501
Cdd:pfam01644  81 TAHLFEYTTQLSVDEDLKFKGNEKGIVPVQIIFCLKEKNAKKINSHRWFFNAFGPLLQPNVCVLLDVGTKPGPTSIYHLW 160

                  ...
gi 1376261892 502 KAF 504
Cdd:pfam01644 161 KAF 163
Chitin_synth_1N super family cl07142
Chitin synthase N-terminal; This is the N-terminal domain of Chitin synthase (pfam01644).
276-341 1.75e-17

Chitin synthase N-terminal; This is the N-terminal domain of Chitin synthase (pfam01644).


The actual alignment was detected with superfamily member pfam08407:

Pssm-ID: 462467  Cd Length: 70  Bit Score: 76.74  E-value: 1.75e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1376261892 276 NGFFAIEMNIPTRLAQFLP-IKGVEEQKTTRYTAITTDPDDVPAAGFRLRQNITSppRQTELFIVIT 341
Cdd:pfam08407   6 NGNLVLDCPVPSRLLNALPrRKGSREFTHMRYTAVTCDPDDFTKNGYTLRQALYG--RETELFIVIT 70
Glyco_tranf_GTA_type super family cl11394
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
472-584 6.14e-16

Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold; Glycosyltransferases (GTs) are enzymes that synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities.


The actual alignment was detected with superfamily member cd06423:

Pssm-ID: 472172 [Multi-domain]  Cd Length: 180  Bit Score: 76.11  E-value: 6.14e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376261892 472 NAFAPLLSPNVCILLDVGTQPAPKSIYHLWKAFDVNSNVGGACGEIATFKGKTwrsllNPLVAAQAFEYKMSNILDKPLE 551
Cdd:cd06423    71 NAGLRHAKGDIVVVLDADTILEPDALKRLVVPFFADPKVGAVQGRVRVRNGSE-----NLLTRLQAIEYLSIFRLGRRAQ 145
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1376261892 552 SLFGYCTVLPGAFSAYRWIALQNNGDGRTGPLA 584
Cdd:cd06423   146 SALGGVLVLSGAFGAFRREALREVGGWDEDTLT 178
PRK10263 super family cl35903
DNA translocase FtsK; Provisional
45-172 6.26e-05

DNA translocase FtsK; Provisional


The actual alignment was detected with superfamily member PRK10263:

Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 46.23  E-value: 6.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376261892   45 NPFS-DAREVGAYAQLQGEEPinSAPLYQPPYAPQLLVAQPTPVSARLPFFEAALARARGIQTPNLPEAPTPTYAQPLPS 123
Cdd:PRK10263   720 NPFSlDDFEFSPMKALLDDGP--HEPLFTPIVEPVQQPQQPVAPQQQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQP 797
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1376261892  124 YLPPPDPNHPDLSVG-LTQANTIRYAIDPRSHLREESRSPSPFMDDSFVY 172
Cdd:PRK10263   798 VAPQPQYQQPQQPVApQPQYQQPQQPVAPQPQYQQPQQPVAPQPQDTLLH 847
 
Name Accession Description Interval E-value
Chitin_synth_1 pfam01644
Chitin synthase; This region is found commonly in chitin synthases classes I, II and III. ...
342-504 3.04e-116

Chitin synthase; This region is found commonly in chitin synthases classes I, II and III. Chitin a linear homopolymer of GlcNAc residues, it is an important component of the cell wall of fungi and is synthesized on the cytoplasmic surface of the cell membrane by membrane bound chitin synthases.


Pssm-ID: 426363  Cd Length: 163  Bit Score: 342.62  E-value: 3.04e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376261892 342 MYNENAELFCRTLYGVMKNIAHLCGRKNSRVWGKDGWQKVVVCIVADGRKAVNPRVLDCLAALGVYQEGAMTNTVKDRPV 421
Cdd:pfam01644   1 MYNEDEILLARTLHGVMKNIAHLCSRKRSKTWGPDGWKKVVVCIVSDGRNKINPRTLDLLAALGVYQEGIAKNDVNGKPV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376261892 422 TAHVFEYTTSFALDGDLHFKYPDKGIVPCQIIFCMKEKNAKKINSHRWFFNAFAPLLSPNVCILLDVGTQPAPKSIYHLW 501
Cdd:pfam01644  81 TAHLFEYTTQLSVDEDLKFKGNEKGIVPVQIIFCLKEKNAKKINSHRWFFNAFGPLLQPNVCVLLDVGTKPGPTSIYHLW 160

                  ...
gi 1376261892 502 KAF 504
Cdd:pfam01644 161 KAF 163
Chitin_synth_C cd04190
C-terminal domain of Chitin Synthase catalyzes the incorporation of GlcNAc from substrate ...
338-604 3.12e-58

C-terminal domain of Chitin Synthase catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin; Chitin synthase, also called UDP-N-acetyl-D-glucosamine:chitin 4-beta-N-acetylglucosaminyltransferase, catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin, which is a linear homopolymer of GlcNAc residues formed by covalent beta-1,4 linkages. Chitin is an important component of the cell wall of fungi and bacteria and it is synthesized on the cytoplasmic surface of the cell membrane by membrane bound chitin synthases. Studies with fungi have revealed that most of them contain more than one chitin synthase gene. At least five subclasses of chitin synthases have been identified.


Pssm-ID: 133033 [Multi-domain]  Cd Length: 244  Bit Score: 195.22  E-value: 3.12e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376261892 338 IVITMYNENAELFCRTLYGVMKNIAHLCGRknsrvwGKDGWQKVVVCIVADGRKavnprvldclaalgvyqegamtntvk 417
Cdd:cd04190     1 VCVTMYNEDEEELARTLDSILKNDYPFCAR------GGDSWKKIVVCVIFDGAI-------------------------- 48
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376261892 418 drpvtahvfeyttsfaldgdlhfkypdkgivpcqiifcmkEKNAKKINSHRWFFNAFAPLLS---PNVCILLDVGTQPAP 494
Cdd:cd04190    49 ----------------------------------------KKNRGKRDSQLWFFNYFCRVLFpddPEFILLVDADTKFDP 88
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376261892 495 KSIYHLWKAFDVNSNVGGACGEIATFKGKtwrslLNPLVAAQAFEYKMSNILDKPLESLFGYCTVLPGAFSAYRWIALQN 574
Cdd:cd04190    89 DSIVQLYKAMDKDPEIGGVCGEIHPMGKK-----QGPLVMYQVFEYAISHWLDKAFESVFGFVTCLPGCFSMYRIEALKG 163
                         250       260       270
                  ....*....|....*....|....*....|
gi 1376261892 575 NGDGrTGPLASYfaGEQLNTGKADTFTGNM 604
Cdd:cd04190   164 DNGG-KGPLLDY--AYLTNTVDSLHKKNNL 190
Chitin_synth_1N pfam08407
Chitin synthase N-terminal; This is the N-terminal domain of Chitin synthase (pfam01644).
276-341 1.75e-17

Chitin synthase N-terminal; This is the N-terminal domain of Chitin synthase (pfam01644).


Pssm-ID: 462467  Cd Length: 70  Bit Score: 76.74  E-value: 1.75e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1376261892 276 NGFFAIEMNIPTRLAQFLP-IKGVEEQKTTRYTAITTDPDDVPAAGFRLRQNITSppRQTELFIVIT 341
Cdd:pfam08407   6 NGNLVLDCPVPSRLLNALPrRKGSREFTHMRYTAVTCDPDDFTKNGYTLRQALYG--RETELFIVIT 70
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
472-584 6.14e-16

CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins. Cellulose synthase catalyzes the polymerization reaction of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues in plants, most algae, some bacteria and fungi, and even some animals. In bacteria, algae and lower eukaryotes, there is a second unrelated type of cellulose synthase (Type II), which produces acylated cellulose, a derivative of cellulose. Chitin synthase catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin, which is a linear homopolymer of beta-(1,4)-linked GlcNAc residues and Glucan Biosynthesis protein catalyzes the elongation of beta-1,2 polyglucose chains of Glucan.


Pssm-ID: 133045 [Multi-domain]  Cd Length: 180  Bit Score: 76.11  E-value: 6.14e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376261892 472 NAFAPLLSPNVCILLDVGTQPAPKSIYHLWKAFDVNSNVGGACGEIATFKGKTwrsllNPLVAAQAFEYKMSNILDKPLE 551
Cdd:cd06423    71 NAGLRHAKGDIVVVLDADTILEPDALKRLVVPFFADPKVGAVQGRVRVRNGSE-----NLLTRLQAIEYLSIFRLGRRAQ 145
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1376261892 552 SLFGYCTVLPGAFSAYRWIALQNNGDGRTGPLA 584
Cdd:cd06423   146 SALGGVLVLSGAFGAFRREALREVGGWDEDTLT 178
Chitin_synth_2 pfam03142
Chitin synthase; Members of this family are fungal chitin synthase EC:2.4.1.16 enzymes. They ...
483-583 1.52e-10

Chitin synthase; Members of this family are fungal chitin synthase EC:2.4.1.16 enzymes. They catalyze chitin synthesis as follows: UDP-N-acetyl-D-glucosamine + {(1,4)-(N-acetyl-beta-D-glucosaminyl)}(N) <=> UDP + {(1,4)-(N-acetyl-beta-D-glucosaminyl)}(N+1).


Pssm-ID: 367353 [Multi-domain]  Cd Length: 527  Bit Score: 64.01  E-value: 1.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376261892 483 CILLDVGTQPAPKSIYHLWKAFDVNSNVGGACGE--IATfKGKTWrsllnpLVAAQAFEYKMSNILDKPLESLFGYCTVL 560
Cdd:pfam03142 205 VLMVDADTKVFPDSLTRMVACMVDDPEIMGLCGEtkIAN-KRQSW------VTAIQVFEYYISHHLSKAFESVFGGVTCL 277
                          90       100
                  ....*....|....*....|...
gi 1376261892 561 PGAFSAYRwIALQNNGDGRTGPL 583
Cdd:pfam03142 278 PGCFSMYR-IKAPKGGDGYWVPI 299
PRK10263 PRK10263
DNA translocase FtsK; Provisional
45-172 6.26e-05

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 46.23  E-value: 6.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376261892   45 NPFS-DAREVGAYAQLQGEEPinSAPLYQPPYAPQLLVAQPTPVSARLPFFEAALARARGIQTPNLPEAPTPTYAQPLPS 123
Cdd:PRK10263   720 NPFSlDDFEFSPMKALLDDGP--HEPLFTPIVEPVQQPQQPVAPQQQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQP 797
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1376261892  124 YLPPPDPNHPDLSVG-LTQANTIRYAIDPRSHLREESRSPSPFMDDSFVY 172
Cdd:PRK10263   798 VAPQPQYQQPQQPVApQPQYQQPQQPVAPQPQYQQPQQPVAPQPQDTLLH 847
 
Name Accession Description Interval E-value
Chitin_synth_1 pfam01644
Chitin synthase; This region is found commonly in chitin synthases classes I, II and III. ...
342-504 3.04e-116

Chitin synthase; This region is found commonly in chitin synthases classes I, II and III. Chitin a linear homopolymer of GlcNAc residues, it is an important component of the cell wall of fungi and is synthesized on the cytoplasmic surface of the cell membrane by membrane bound chitin synthases.


Pssm-ID: 426363  Cd Length: 163  Bit Score: 342.62  E-value: 3.04e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376261892 342 MYNENAELFCRTLYGVMKNIAHLCGRKNSRVWGKDGWQKVVVCIVADGRKAVNPRVLDCLAALGVYQEGAMTNTVKDRPV 421
Cdd:pfam01644   1 MYNEDEILLARTLHGVMKNIAHLCSRKRSKTWGPDGWKKVVVCIVSDGRNKINPRTLDLLAALGVYQEGIAKNDVNGKPV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376261892 422 TAHVFEYTTSFALDGDLHFKYPDKGIVPCQIIFCMKEKNAKKINSHRWFFNAFAPLLSPNVCILLDVGTQPAPKSIYHLW 501
Cdd:pfam01644  81 TAHLFEYTTQLSVDEDLKFKGNEKGIVPVQIIFCLKEKNAKKINSHRWFFNAFGPLLQPNVCVLLDVGTKPGPTSIYHLW 160

                  ...
gi 1376261892 502 KAF 504
Cdd:pfam01644 161 KAF 163
Chitin_synth_C cd04190
C-terminal domain of Chitin Synthase catalyzes the incorporation of GlcNAc from substrate ...
338-604 3.12e-58

C-terminal domain of Chitin Synthase catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin; Chitin synthase, also called UDP-N-acetyl-D-glucosamine:chitin 4-beta-N-acetylglucosaminyltransferase, catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin, which is a linear homopolymer of GlcNAc residues formed by covalent beta-1,4 linkages. Chitin is an important component of the cell wall of fungi and bacteria and it is synthesized on the cytoplasmic surface of the cell membrane by membrane bound chitin synthases. Studies with fungi have revealed that most of them contain more than one chitin synthase gene. At least five subclasses of chitin synthases have been identified.


Pssm-ID: 133033 [Multi-domain]  Cd Length: 244  Bit Score: 195.22  E-value: 3.12e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376261892 338 IVITMYNENAELFCRTLYGVMKNIAHLCGRknsrvwGKDGWQKVVVCIVADGRKavnprvldclaalgvyqegamtntvk 417
Cdd:cd04190     1 VCVTMYNEDEEELARTLDSILKNDYPFCAR------GGDSWKKIVVCVIFDGAI-------------------------- 48
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376261892 418 drpvtahvfeyttsfaldgdlhfkypdkgivpcqiifcmkEKNAKKINSHRWFFNAFAPLLS---PNVCILLDVGTQPAP 494
Cdd:cd04190    49 ----------------------------------------KKNRGKRDSQLWFFNYFCRVLFpddPEFILLVDADTKFDP 88
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376261892 495 KSIYHLWKAFDVNSNVGGACGEIATFKGKtwrslLNPLVAAQAFEYKMSNILDKPLESLFGYCTVLPGAFSAYRWIALQN 574
Cdd:cd04190    89 DSIVQLYKAMDKDPEIGGVCGEIHPMGKK-----QGPLVMYQVFEYAISHWLDKAFESVFGFVTCLPGCFSMYRIEALKG 163
                         250       260       270
                  ....*....|....*....|....*....|
gi 1376261892 575 NGDGrTGPLASYfaGEQLNTGKADTFTGNM 604
Cdd:cd04190   164 DNGG-KGPLLDY--AYLTNTVDSLHKKNNL 190
Chitin_synth_1N pfam08407
Chitin synthase N-terminal; This is the N-terminal domain of Chitin synthase (pfam01644).
276-341 1.75e-17

Chitin synthase N-terminal; This is the N-terminal domain of Chitin synthase (pfam01644).


Pssm-ID: 462467  Cd Length: 70  Bit Score: 76.74  E-value: 1.75e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1376261892 276 NGFFAIEMNIPTRLAQFLP-IKGVEEQKTTRYTAITTDPDDVPAAGFRLRQNITSppRQTELFIVIT 341
Cdd:pfam08407   6 NGNLVLDCPVPSRLLNALPrRKGSREFTHMRYTAVTCDPDDFTKNGYTLRQALYG--RETELFIVIT 70
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
472-584 6.14e-16

CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins. Cellulose synthase catalyzes the polymerization reaction of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues in plants, most algae, some bacteria and fungi, and even some animals. In bacteria, algae and lower eukaryotes, there is a second unrelated type of cellulose synthase (Type II), which produces acylated cellulose, a derivative of cellulose. Chitin synthase catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin, which is a linear homopolymer of beta-(1,4)-linked GlcNAc residues and Glucan Biosynthesis protein catalyzes the elongation of beta-1,2 polyglucose chains of Glucan.


Pssm-ID: 133045 [Multi-domain]  Cd Length: 180  Bit Score: 76.11  E-value: 6.14e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376261892 472 NAFAPLLSPNVCILLDVGTQPAPKSIYHLWKAFDVNSNVGGACGEIATFKGKTwrsllNPLVAAQAFEYKMSNILDKPLE 551
Cdd:cd06423    71 NAGLRHAKGDIVVVLDADTILEPDALKRLVVPFFADPKVGAVQGRVRVRNGSE-----NLLTRLQAIEYLSIFRLGRRAQ 145
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1376261892 552 SLFGYCTVLPGAFSAYRWIALQNNGDGRTGPLA 584
Cdd:cd06423   146 SALGGVLVLSGAFGAFRREALREVGGWDEDTLT 178
Chitin_synth_2 pfam03142
Chitin synthase; Members of this family are fungal chitin synthase EC:2.4.1.16 enzymes. They ...
483-583 1.52e-10

Chitin synthase; Members of this family are fungal chitin synthase EC:2.4.1.16 enzymes. They catalyze chitin synthesis as follows: UDP-N-acetyl-D-glucosamine + {(1,4)-(N-acetyl-beta-D-glucosaminyl)}(N) <=> UDP + {(1,4)-(N-acetyl-beta-D-glucosaminyl)}(N+1).


Pssm-ID: 367353 [Multi-domain]  Cd Length: 527  Bit Score: 64.01  E-value: 1.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376261892 483 CILLDVGTQPAPKSIYHLWKAFDVNSNVGGACGE--IATfKGKTWrsllnpLVAAQAFEYKMSNILDKPLESLFGYCTVL 560
Cdd:pfam03142 205 VLMVDADTKVFPDSLTRMVACMVDDPEIMGLCGEtkIAN-KRQSW------VTAIQVFEYYISHHLSKAFESVFGGVTCL 277
                          90       100
                  ....*....|....*....|...
gi 1376261892 561 PGAFSAYRwIALQNNGDGRTGPL 583
Cdd:pfam03142 278 PGCFSMYR-IKAPKGGDGYWVPI 299
PRK10263 PRK10263
DNA translocase FtsK; Provisional
45-172 6.26e-05

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 46.23  E-value: 6.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376261892   45 NPFS-DAREVGAYAQLQGEEPinSAPLYQPPYAPQLLVAQPTPVSARLPFFEAALARARGIQTPNLPEAPTPTYAQPLPS 123
Cdd:PRK10263   720 NPFSlDDFEFSPMKALLDDGP--HEPLFTPIVEPVQQPQQPVAPQQQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQP 797
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1376261892  124 YLPPPDPNHPDLSVG-LTQANTIRYAIDPRSHLREESRSPSPFMDDSFVY 172
Cdd:PRK10263   798 VAPQPQYQQPQQPVApQPQYQQPQQPVAPQPQYQQPQQPVAPQPQDTLLH 847
 
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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