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Conserved domains on  [gi|440215194|gb|AGB94015|]
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adenylyl cyclase X D, isoform B [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Nucleotidyl_cyc_III super family cl11967
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
321-503 2.06e-52

Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse group of nucleotidyl cyclases (NC's) containing prokaryotic and eukaryotic proteins. They can be divided into two major groups; the mononucleotidyl cyclases (MNC's) and the diguanylate cyclases (DGC's). The MNC's, which include the adenylate cyclases (AC's) and the guanylate cyclases (GC's), have a conserved cyclase homology domain (CHD), while the DGC's have a conserved GGDEF domain, named after a conserved motif within this subgroup. Their products, cyclic guanylyl and adenylyl nucleotides, are second messengers that play important roles in eukaryotic signal transduction and prokaryotic sensory pathways.


The actual alignment was detected with superfamily member pfam00211:

Pssm-ID: 448371  Cd Length: 183  Bit Score: 175.51  E-value: 2.06e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440215194  321 EPHEDVTVLYADVVNYTHLTTTLDVKKLVEALHDLFVRFDIASEEYNVLRIKFLGDCYYCVAGLANPNADHAKCCVDLGL 400
Cdd:pfam00211   4 QPYDNVTILFADIVGFTALSSRHSPEQVVRLLNELYTRFDRLLDKHKVYKVKTIGDAYMVVSGLPEPSPAHARKIAEMAL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440215194  401 RMIKDIRDVREKRHLNIDMRIGVHSGDVLSGVIGAAKWQFDIWSKDVDIANRLEATGATGRVHVSQKTLSLLDGEYFfed 480
Cdd:pfam00211  84 DMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVSEETYRLLKTEGF--- 160
                         170       180
                  ....*....|....*....|....*
gi 440215194  481 gtEKAREDPVL--QKHGIRTFLIKS 503
Cdd:pfam00211 161 --EFTERGEIEvkGKGKMKTYFLNG 183
AC_N super family cl24704
Adenylyl cyclase N-terminal extracellular and transmembrane region; This family covers the ...
42-284 1.60e-09

Adenylyl cyclase N-terminal extracellular and transmembrane region; This family covers the N-terminal extracellular region and the first transmembrane 5-6 pass region of adenylate cyclase.


The actual alignment was detected with superfamily member pfam16214:

Pssm-ID: 318454  Cd Length: 415  Bit Score: 60.02  E-value: 1.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440215194   42 RKCRNLELEDSYDLYMRRLRVGYLSLFIFIHVAVTVIHTLLLLTTPEIKYVYVdmVAYMCSGLVIWVVLGVNFRSELVSK 121
Cdd:pfam16214 176 KKFQSEKLERLYQRYFFRLNQSSLTMLMAVLVLVCLVMLAFHAARGPLQVPYV--VVLSLAIGLILVLAVLCNRNAFHQD 253
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440215194  122 HGWVV-YAtswLAVCVMVLMDIGLNVYHATSHNDILnpIYDAYTLYAIYMFMPVPylLQPFVLGSAVTFCYIINYSFVIT 200
Cdd:pfam16214 254 HMWLAcYA---VILVVLAVQVVGVLLVQPRSASEGI--WWTVFFIYTIYTLLPVR--MRAAVISGVLLSAIHLAVSLRTN 326
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440215194  201 AKDDNQMHSILNEAIYLSCVNLLGIFFRLMRDIALRTTFLDRRQYVEENLLLRYARDQERSLLLSILPAQIADRLQEDVK 280
Cdd:pfam16214 327 AQDQFLLKQLVSNVLIFSCTNIVGVCTHYPAEVSQRQAFQETRECIQARLHSQRENQQQERLLLSVLPRHVAMEMKADIN 406

                  ....
gi 440215194  281 NRIE 284
Cdd:pfam16214 407 AKQE 410
 
Name Accession Description Interval E-value
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
321-503 2.06e-52

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 425528  Cd Length: 183  Bit Score: 175.51  E-value: 2.06e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440215194  321 EPHEDVTVLYADVVNYTHLTTTLDVKKLVEALHDLFVRFDIASEEYNVLRIKFLGDCYYCVAGLANPNADHAKCCVDLGL 400
Cdd:pfam00211   4 QPYDNVTILFADIVGFTALSSRHSPEQVVRLLNELYTRFDRLLDKHKVYKVKTIGDAYMVVSGLPEPSPAHARKIAEMAL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440215194  401 RMIKDIRDVREKRHLNIDMRIGVHSGDVLSGVIGAAKWQFDIWSKDVDIANRLEATGATGRVHVSQKTLSLLDGEYFfed 480
Cdd:pfam00211  84 DMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVSEETYRLLKTEGF--- 160
                         170       180
                  ....*....|....*....|....*
gi 440215194  481 gtEKAREDPVL--QKHGIRTFLIKS 503
Cdd:pfam00211 161 --EFTERGEIEvkGKGKMKTYFLNG 183
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
325-490 8.16e-46

cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also called cyclase homology domains (CHDs), are part of the class III nucleotidyl cyclases. This class includes eukaryotic and prokaryotic adenylate cyclases (AC's) and guanylate cyclases (GC's). They seem to share a common catalytic mechanism in their requirement for two magnesium ions to bind the polyphosphate moiety of the nucleotide.


Pssm-ID: 143636 [Multi-domain]  Cd Length: 177  Bit Score: 158.13  E-value: 8.16e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440215194 325 DVTVLYADVVNYTHLTTTLDVKKLVEALHDLFVRFDIASEEYNVLRIKFLGDCYYCVAGLANPNADHAKCCVDLGLRMIK 404
Cdd:cd07302    1 EVTVLFADIVGFTALSERLGPEELVELLNEYFSAFDEIIERHGGTVDKTIGDAVMAVFGLPGAHEDHAERAVRAALEMQE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440215194 405 DIRDVREKRHL--NIDMRIGVHSGDVLSGVIGAAKWQFDIWSKDVDIANRLEATGATGRVHVSQKTLSLL-DGEYFFEDG 481
Cdd:cd07302   81 ALAELNAEREGgpPLRLRIGIHTGPVVAGVVGSERPEYTVIGDTVNLAARLESLAKPGQILVSEATYELLgDAGFEFEEL 160
                        170
                 ....*....|..
gi 440215194 482 TE---KAREDPV 490
Cdd:cd07302  161 GEvelKGKSGPV 172
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
254-476 1.25e-41

Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl cyclases. Eubacterial homologues are known. Two residues (Asn, Arg) are thought to be involved in catalysis. These cyclases have important roles in a diverse range of cellular processes.


Pssm-ID: 214485  Cd Length: 194  Bit Score: 147.40  E-value: 1.25e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440215194   254 YARDQERSLLLSILPAQIADRLqedvknrierskqqhqqqsqvdlrrsadsqtlKRWRQPDHgtlfIEPHEDVTVLYADV 333
Cdd:smart00044   1 EEKKKTDRLLDQLLPASVAEQL--------------------------------KRGGSPVP----AESYDNVTILFSDI 44
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440215194   334 VNYTHLTTTLDVKKLVEALHDLFVRFDIASEEYNVLRIKFLGDCYYCVAGLANPN-ADHAKCCVDLGLRMIKDIRDV-RE 411
Cdd:smart00044  45 VGFTSLCSTSTPEQVVNLLNDLYSRFDQIIDRHGGYKVKTIGDAYMVASGLPEEAlVDHAELIADEALDMVEELKTVlVQ 124
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 440215194   412 KRHLNIDMRIGVHSGDVLSGVIGAAKWQFDIWSKDVDIANRLEATGATGRVHVSQKTLSLLDGEY 476
Cdd:smart00044 125 HREEGLRVRIGIHTGPVVAGVVGIRMPRYCLFGDTVNLASRMESAGDPGQIQVSEETYSLLARRG 189
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
222-480 1.79e-31

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 125.69  E-value: 1.79e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440215194 222 LLGIFFRLMRDIALRTTFLDRRQYVEENLLLRYARDQERSLLLSILPAQIADRLQEDVKNRIERSKQQHQQQSQvdLRRS 301
Cdd:COG2114  121 LLALLLLLLLLLLLLLLLLALALLLLLALALLLLLLLVALLLLALLLLLLLLLLLALLLLLLLALRERERLRDL--LGRY 198
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440215194 302 ADSQTLKRWRQPDHGTLFIEPHEDVTVLYADVVNYTHLTTTLDVKKLVEALHDLFVRFDIASEEYNVLRIKFLGDCYYCV 381
Cdd:COG2114  199 LPPEVAERLLAGGEELRLGGERREVTVLFADIVGFTALSERLGPEELVELLNRYFSAMVEIIERHGGTVDKFIGDGVMAV 278
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440215194 382 AGLANPNADHAKCCVDLGLRMIKDIRDVREKRHLN----IDMRIGVHSGDVLSGVIGAA-KWQFDIWSKDVDIANRLEAT 456
Cdd:COG2114  279 FGAPVAREDHAERAVRAALAMQEALAELNAELPAEggppLRVRIGIHTGEVVVGNIGSEdRLDYTVIGDTVNLAARLESL 358
                        250       260
                 ....*....|....*....|....
gi 440215194 457 GATGRVHVSQKTLSLLDGEYFFED 480
Cdd:COG2114  359 AKPGEILVSEATYDLLRDRFEFRE 382
AC_N pfam16214
Adenylyl cyclase N-terminal extracellular and transmembrane region; This family covers the ...
42-284 1.60e-09

Adenylyl cyclase N-terminal extracellular and transmembrane region; This family covers the N-terminal extracellular region and the first transmembrane 5-6 pass region of adenylate cyclase.


Pssm-ID: 318454  Cd Length: 415  Bit Score: 60.02  E-value: 1.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440215194   42 RKCRNLELEDSYDLYMRRLRVGYLSLFIFIHVAVTVIHTLLLLTTPEIKYVYVdmVAYMCSGLVIWVVLGVNFRSELVSK 121
Cdd:pfam16214 176 KKFQSEKLERLYQRYFFRLNQSSLTMLMAVLVLVCLVMLAFHAARGPLQVPYV--VVLSLAIGLILVLAVLCNRNAFHQD 253
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440215194  122 HGWVV-YAtswLAVCVMVLMDIGLNVYHATSHNDILnpIYDAYTLYAIYMFMPVPylLQPFVLGSAVTFCYIINYSFVIT 200
Cdd:pfam16214 254 HMWLAcYA---VILVVLAVQVVGVLLVQPRSASEGI--WWTVFFIYTIYTLLPVR--MRAAVISGVLLSAIHLAVSLRTN 326
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440215194  201 AKDDNQMHSILNEAIYLSCVNLLGIFFRLMRDIALRTTFLDRRQYVEENLLLRYARDQERSLLLSILPAQIADRLQEDVK 280
Cdd:pfam16214 327 AQDQFLLKQLVSNVLIFSCTNIVGVCTHYPAEVSQRQAFQETRECIQARLHSQRENQQQERLLLSVLPRHVAMEMKADIN 406

                  ....
gi 440215194  281 NRIE 284
Cdd:pfam16214 407 AKQE 410
 
Name Accession Description Interval E-value
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
321-503 2.06e-52

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 425528  Cd Length: 183  Bit Score: 175.51  E-value: 2.06e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440215194  321 EPHEDVTVLYADVVNYTHLTTTLDVKKLVEALHDLFVRFDIASEEYNVLRIKFLGDCYYCVAGLANPNADHAKCCVDLGL 400
Cdd:pfam00211   4 QPYDNVTILFADIVGFTALSSRHSPEQVVRLLNELYTRFDRLLDKHKVYKVKTIGDAYMVVSGLPEPSPAHARKIAEMAL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440215194  401 RMIKDIRDVREKRHLNIDMRIGVHSGDVLSGVIGAAKWQFDIWSKDVDIANRLEATGATGRVHVSQKTLSLLDGEYFfed 480
Cdd:pfam00211  84 DMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVSEETYRLLKTEGF--- 160
                         170       180
                  ....*....|....*....|....*
gi 440215194  481 gtEKAREDPVL--QKHGIRTFLIKS 503
Cdd:pfam00211 161 --EFTERGEIEvkGKGKMKTYFLNG 183
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
325-490 8.16e-46

cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also called cyclase homology domains (CHDs), are part of the class III nucleotidyl cyclases. This class includes eukaryotic and prokaryotic adenylate cyclases (AC's) and guanylate cyclases (GC's). They seem to share a common catalytic mechanism in their requirement for two magnesium ions to bind the polyphosphate moiety of the nucleotide.


Pssm-ID: 143636 [Multi-domain]  Cd Length: 177  Bit Score: 158.13  E-value: 8.16e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440215194 325 DVTVLYADVVNYTHLTTTLDVKKLVEALHDLFVRFDIASEEYNVLRIKFLGDCYYCVAGLANPNADHAKCCVDLGLRMIK 404
Cdd:cd07302    1 EVTVLFADIVGFTALSERLGPEELVELLNEYFSAFDEIIERHGGTVDKTIGDAVMAVFGLPGAHEDHAERAVRAALEMQE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440215194 405 DIRDVREKRHL--NIDMRIGVHSGDVLSGVIGAAKWQFDIWSKDVDIANRLEATGATGRVHVSQKTLSLL-DGEYFFEDG 481
Cdd:cd07302   81 ALAELNAEREGgpPLRLRIGIHTGPVVAGVVGSERPEYTVIGDTVNLAARLESLAKPGQILVSEATYELLgDAGFEFEEL 160
                        170
                 ....*....|..
gi 440215194 482 TE---KAREDPV 490
Cdd:cd07302  161 GEvelKGKSGPV 172
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
254-476 1.25e-41

Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl cyclases. Eubacterial homologues are known. Two residues (Asn, Arg) are thought to be involved in catalysis. These cyclases have important roles in a diverse range of cellular processes.


Pssm-ID: 214485  Cd Length: 194  Bit Score: 147.40  E-value: 1.25e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440215194   254 YARDQERSLLLSILPAQIADRLqedvknrierskqqhqqqsqvdlrrsadsqtlKRWRQPDHgtlfIEPHEDVTVLYADV 333
Cdd:smart00044   1 EEKKKTDRLLDQLLPASVAEQL--------------------------------KRGGSPVP----AESYDNVTILFSDI 44
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440215194   334 VNYTHLTTTLDVKKLVEALHDLFVRFDIASEEYNVLRIKFLGDCYYCVAGLANPN-ADHAKCCVDLGLRMIKDIRDV-RE 411
Cdd:smart00044  45 VGFTSLCSTSTPEQVVNLLNDLYSRFDQIIDRHGGYKVKTIGDAYMVASGLPEEAlVDHAELIADEALDMVEELKTVlVQ 124
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 440215194   412 KRHLNIDMRIGVHSGDVLSGVIGAAKWQFDIWSKDVDIANRLEATGATGRVHVSQKTLSLLDGEY 476
Cdd:smart00044 125 HREEGLRVRIGIHTGPVVAGVVGIRMPRYCLFGDTVNLASRMESAGDPGQIQVSEETYSLLARRG 189
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
222-480 1.79e-31

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 125.69  E-value: 1.79e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440215194 222 LLGIFFRLMRDIALRTTFLDRRQYVEENLLLRYARDQERSLLLSILPAQIADRLQEDVKNRIERSKQQHQQQSQvdLRRS 301
Cdd:COG2114  121 LLALLLLLLLLLLLLLLLLALALLLLLALALLLLLLLVALLLLALLLLLLLLLLLALLLLLLLALRERERLRDL--LGRY 198
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440215194 302 ADSQTLKRWRQPDHGTLFIEPHEDVTVLYADVVNYTHLTTTLDVKKLVEALHDLFVRFDIASEEYNVLRIKFLGDCYYCV 381
Cdd:COG2114  199 LPPEVAERLLAGGEELRLGGERREVTVLFADIVGFTALSERLGPEELVELLNRYFSAMVEIIERHGGTVDKFIGDGVMAV 278
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440215194 382 AGLANPNADHAKCCVDLGLRMIKDIRDVREKRHLN----IDMRIGVHSGDVLSGVIGAA-KWQFDIWSKDVDIANRLEAT 456
Cdd:COG2114  279 FGAPVAREDHAERAVRAALAMQEALAELNAELPAEggppLRVRIGIHTGEVVVGNIGSEdRLDYTVIGDTVNLAARLESL 358
                        250       260
                 ....*....|....*....|....
gi 440215194 457 GATGRVHVSQKTLSLLDGEYFFED 480
Cdd:COG2114  359 AKPGEILVSEATYDLLRDRFEFRE 382
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
326-463 4.56e-29

Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse group of nucleotidyl cyclases (NC's) containing prokaryotic and eukaryotic proteins. They can be divided into two major groups; the mononucleotidyl cyclases (MNC's) and the diguanylate cyclases (DGC's). The MNC's, which include the adenylate cyclases (AC's) and the guanylate cyclases (GC's), have a conserved cyclase homology domain (CHD), while the DGC's have a conserved GGDEF domain, named after a conserved motif within this subgroup. Their products, cyclic guanylyl and adenylyl nucleotides, are second messengers that play important roles in eukaryotic signal transduction and prokaryotic sensory pathways.


Pssm-ID: 143637 [Multi-domain]  Cd Length: 133  Bit Score: 111.29  E-value: 4.56e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440215194 326 VTVLYADVVNYTHLTTTLDVKKLVEALHDLFVRFDIASEEYNVLRIKFLGDCYYCVAGlanpnADHAKCCVDLGLRMIKD 405
Cdd:cd07556    2 VTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSGDLKIKTIGDEFMVVSG-----LDHPAAAVAFAEDMREA 76
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 440215194 406 IRDVREKRHLNIDMRIGVHSGDVLSGVIGaAKWQFDIWSKDVDIANRLEATGATGRVH 463
Cdd:cd07556   77 VSALNQSEGNPVRVRIGIHTGPVVVGVIG-SRPQYDVWGALVNLASRMESQAKAGQVL 133
AC_N pfam16214
Adenylyl cyclase N-terminal extracellular and transmembrane region; This family covers the ...
42-284 1.60e-09

Adenylyl cyclase N-terminal extracellular and transmembrane region; This family covers the N-terminal extracellular region and the first transmembrane 5-6 pass region of adenylate cyclase.


Pssm-ID: 318454  Cd Length: 415  Bit Score: 60.02  E-value: 1.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440215194   42 RKCRNLELEDSYDLYMRRLRVGYLSLFIFIHVAVTVIHTLLLLTTPEIKYVYVdmVAYMCSGLVIWVVLGVNFRSELVSK 121
Cdd:pfam16214 176 KKFQSEKLERLYQRYFFRLNQSSLTMLMAVLVLVCLVMLAFHAARGPLQVPYV--VVLSLAIGLILVLAVLCNRNAFHQD 253
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440215194  122 HGWVV-YAtswLAVCVMVLMDIGLNVYHATSHNDILnpIYDAYTLYAIYMFMPVPylLQPFVLGSAVTFCYIINYSFVIT 200
Cdd:pfam16214 254 HMWLAcYA---VILVVLAVQVVGVLLVQPRSASEGI--WWTVFFIYTIYTLLPVR--MRAAVISGVLLSAIHLAVSLRTN 326
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440215194  201 AKDDNQMHSILNEAIYLSCVNLLGIFFRLMRDIALRTTFLDRRQYVEENLLLRYARDQERSLLLSILPAQIADRLQEDVK 280
Cdd:pfam16214 327 AQDQFLLKQLVSNVLIFSCTNIVGVCTHYPAEVSQRQAFQETRECIQARLHSQRENQQQERLLLSVLPRHVAMEMKADIN 406

                  ....
gi 440215194  281 NRIE 284
Cdd:pfam16214 407 AKQE 410
 
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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