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Conserved domains on  [gi|386763826|ref|NP_001245529|]
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uncharacterized protein Dmel_CG3556, isoform B [Drosophila melanogaster]

Protein Classification

prenyltransferase/squalene oxidase repeat-containing protein( domain architecture ID 693)

prenyltransferase/squalene oxidase repeat-containing protein similar to Streptomyces anulatus copalyl diphosphate synthase and Aspergillus fumigatus squalene hopane cyclase afumA

CATH:  1.50.10.20
EC:  5.-.-.-
Gene Ontology:  GO:0016853
SCOP:  3001024

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Cobalamin_bind super family cl19924
Eukaryotic cobalamin-binding protein;
249-377 7.31e-06

Eukaryotic cobalamin-binding protein;


The actual alignment was detected with superfamily member pfam01122:

Pssm-ID: 460073  Cd Length: 302  Bit Score: 48.02  E-value: 7.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763826  249 KLARYVLALGSLCKDPKHFHGHDLVATLQH--HEPAQDIEF-------------ALTTLSACSSAAHVRKRQIRRLLDIA 313
Cdd:pfam01122  73 QLALYILALRSSCEDPGTIKGDRLVSQLKRkmEEEKENIGHhhggppltnyyqySLGILALCVHNKRVSLHVVAKLFAPE 152

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386763826  314 SG---VTDQ-SVDAIAMVILALRCI-------VTDHRHR---HLQHFVRRpargLATLQDQRGSFGSLRSTALAMQAL 377
Cdd:pfam01122 153 HKnllHGGQfSVDTGAMAGLALTCVknsiegsNEGLRALisqAIKSLVEK----ILSSQKDNGLIGNIYSTGLAMQAL 226
Prenyltrans pfam00432
Prenyltransferase and squalene oxidase repeat;
389-419 4.46e-03

Prenyltransferase and squalene oxidase repeat;


:

Pssm-ID: 395346 [Multi-domain]  Cd Length: 44  Bit Score: 35.18  E-value: 4.46e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 386763826  389 NRTAASRYILSRQRADGGWSEEPlqdGQEPD 419
Cdd:pfam00432   2 DKEKLVDYLLSCQNEDGGFGGRP---GGESD 29
 
Name Accession Description Interval E-value
Cobalamin_bind pfam01122
Eukaryotic cobalamin-binding protein;
249-377 7.31e-06

Eukaryotic cobalamin-binding protein;


Pssm-ID: 460073  Cd Length: 302  Bit Score: 48.02  E-value: 7.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763826  249 KLARYVLALGSLCKDPKHFHGHDLVATLQH--HEPAQDIEF-------------ALTTLSACSSAAHVRKRQIRRLLDIA 313
Cdd:pfam01122  73 QLALYILALRSSCEDPGTIKGDRLVSQLKRkmEEEKENIGHhhggppltnyyqySLGILALCVHNKRVSLHVVAKLFAPE 152

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386763826  314 SG---VTDQ-SVDAIAMVILALRCI-------VTDHRHR---HLQHFVRRpargLATLQDQRGSFGSLRSTALAMQAL 377
Cdd:pfam01122 153 HKnllHGGQfSVDTGAMAGLALTCVknsiegsNEGLRALisqAIKSLVEK----ILSSQKDNGLIGNIYSTGLAMQAL 226
CAL1 COG5029
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, ...
 313-417 1.85e-04

Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, Lipid transport and metabolism];


Pssm-ID: 444045 [Multi-domain]  Cd Length: 259  Bit Score: 43.54  E-value: 1.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763826 313 ASGVTDQSVDAIAMVIL-ALRCIVTDHRHRHLQHF--VRRPARGLATLQdqRGSFGSLRSTALAMQALQDLEYDPAghwN 389
Cdd:COG5029  136 PGRRSDTNPTAAAIGALrALGALDDPIETKVIRFLrdVQSPEGGFAYNT--RIGEADLLSTFTAILTLYDLGAAPK---L 210

                         90       100
                 ....*....|....*....|....*...
gi 386763826 390 RTAASRYILSRQRADGGWSEEPLqDGQE 417
Cdd:COG5029  211 VDDLQAYILSLQLPDGGFEGAPW-DGVE 237
ISOPREN_C2_like cd00688
This group contains class II terpene cyclases, protein prenyltransferases beta subunit, two ...
 165-411 2.43e-04

This group contains class II terpene cyclases, protein prenyltransferases beta subunit, two broadly specific proteinase inhibitors alpha2-macroglobulin (alpha (2)-M) and pregnancy zone protein (PZP) and, the C3 C4 and C5 components of vertebrate complement. Class II terpene cyclases include squalene cyclase (SQCY) and 2,3-oxidosqualene cyclase (OSQCY), these integral membrane proteins catalyze a cationic cyclization cascade converting linear triterpenes to fused ring compounds. The protein prenyltransferases include protein farnesyltransferase (FTase) and geranylgeranyltransferase types I and II (GGTase-I and GGTase-II) which catalyze the carboxyl-terminal lipidation of Ras, Rab, and several other cellular signal transduction proteins, facilitating membrane associations and specific protein-protein interactions. Alpha (2)-M is a major carrier protein in serum and involved in the immobilization and entrapment of proteases. PZP is a pregnancy associated protein. Alpha (2)-M and PZP are known to bind to and, may modulate, the activity of placental protein-14 in T-cell growth and cytokine production thereby protecting the allogeneic fetus from attack by the maternal immune system.


Pssm-ID: 238362 [Multi-domain]  Cd Length: 300  Bit Score: 43.31  E-value: 2.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763826 165 QEAILRALDWLKEKRASDYGWGndthvvilakeLSGGRDPNDSVDghvqviqeledTLSVkemeIEILAMLDRHHTLPKP 244
Cdd:cd00688   51 DENIEKGIQRLLSYQLSDGGFS-----------GWGGNDYPSLWL-----------TAYA----LKALLLAGDYIAVDRI 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763826 245 lDLDKLARYVLalgSLCKDPKHFHGHDLVATLQHHEPaQDIE---FALTTLSACSSAAHVRKRQ-----IRRLLDIASGV 316
Cdd:cd00688  105 -DLARALNWLL---SLQNEDGGFREDGPGNHRIGGDE-SDVRltaYALIALALLGKLDPDPLIEkaldyLLSCQNYDGGF 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763826 317 TDQSVD---AIAMVILALRCIvtdhrHRHLQHFVRRPARGLATLQDQRGSFGSLR----------STALAMQALQDLEYd 383
Cdd:cd00688  180 GPGGEShgyGTACAAAALALL-----GDLDSPDAKKALRWLLSRQRPDGGWGEGRdrtnklsdscYTEWAAYALLALGK- 253

                        250       260
                 ....*....|....*....|....*...
gi 386763826 384 PAGHWNRTAASRYILSRQRADGGWSEEP 411
Cdd:cd00688  254 LGDLEDAEKLVKWLLSQQNEDGGFSSKP 281
squalene_cyclas TIGR01787
squalene/oxidosqualene cyclases; This family of enzymes catalyzes the cyclization of the ...
 320-409 5.19e-04

squalene/oxidosqualene cyclases; This family of enzymes catalyzes the cyclization of the triterpenes squalene or 2-3-oxidosqualene to a variety of products including hopene, lanosterol, cycloartenol, amyrin, lupeol, and isomultiflorenol.


Pssm-ID: 273809 [Multi-domain]  Cd Length: 621  Bit Score: 42.81  E-value: 5.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763826  320 SVDAIAMVILALRCIVtdHRHRHLQHFVRRPARGLATLQDQRGS-FGS--LRSTALAMQALQDLEYdpAGHWNRTAAS-- 394
Cdd:TIGR01787 437 YVDVTARVIQALGAFG--HRADEIRNVLERALEYLRREQRADGSwFGRwgVNYTYGTGFVLSALAA--AGRTYRNCPEvq 512

                          90
                  ....*....|....*...
gi 386763826  395 ---RYILSRQRADGGWSE 409
Cdd:TIGR01787 513 kacDWLLSRQMPDGGWGE 530
Prenyltrans pfam00432
Prenyltransferase and squalene oxidase repeat;
389-419 4.46e-03

Prenyltransferase and squalene oxidase repeat;


Pssm-ID: 395346 [Multi-domain]  Cd Length: 44  Bit Score: 35.18  E-value: 4.46e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 386763826  389 NRTAASRYILSRQRADGGWSEEPlqdGQEPD 419
Cdd:pfam00432   2 DKEKLVDYLLSCQNEDGGFGGRP---GGESD 29
 
Name Accession Description Interval E-value
Cobalamin_bind pfam01122
Eukaryotic cobalamin-binding protein;
249-377 7.31e-06

Eukaryotic cobalamin-binding protein;


Pssm-ID: 460073  Cd Length: 302  Bit Score: 48.02  E-value: 7.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763826  249 KLARYVLALGSLCKDPKHFHGHDLVATLQH--HEPAQDIEF-------------ALTTLSACSSAAHVRKRQIRRLLDIA 313
Cdd:pfam01122  73 QLALYILALRSSCEDPGTIKGDRLVSQLKRkmEEEKENIGHhhggppltnyyqySLGILALCVHNKRVSLHVVAKLFAPE 152

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386763826  314 SG---VTDQ-SVDAIAMVILALRCI-------VTDHRHR---HLQHFVRRpargLATLQDQRGSFGSLRSTALAMQAL 377
Cdd:pfam01122 153 HKnllHGGQfSVDTGAMAGLALTCVknsiegsNEGLRALisqAIKSLVEK----ILSSQKDNGLIGNIYSTGLAMQAL 226
CAL1 COG5029
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, ...
 313-417 1.85e-04

Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, Lipid transport and metabolism];


Pssm-ID: 444045 [Multi-domain]  Cd Length: 259  Bit Score: 43.54  E-value: 1.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763826 313 ASGVTDQSVDAIAMVIL-ALRCIVTDHRHRHLQHF--VRRPARGLATLQdqRGSFGSLRSTALAMQALQDLEYDPAghwN 389
Cdd:COG5029  136 PGRRSDTNPTAAAIGALrALGALDDPIETKVIRFLrdVQSPEGGFAYNT--RIGEADLLSTFTAILTLYDLGAAPK---L 210

                         90       100
                 ....*....|....*....|....*...
gi 386763826 390 RTAASRYILSRQRADGGWSEEPLqDGQE 417
Cdd:COG5029  211 VDDLQAYILSLQLPDGGFEGAPW-DGVE 237
ISOPREN_C2_like cd00688
This group contains class II terpene cyclases, protein prenyltransferases beta subunit, two ...
 165-411 2.43e-04

This group contains class II terpene cyclases, protein prenyltransferases beta subunit, two broadly specific proteinase inhibitors alpha2-macroglobulin (alpha (2)-M) and pregnancy zone protein (PZP) and, the C3 C4 and C5 components of vertebrate complement. Class II terpene cyclases include squalene cyclase (SQCY) and 2,3-oxidosqualene cyclase (OSQCY), these integral membrane proteins catalyze a cationic cyclization cascade converting linear triterpenes to fused ring compounds. The protein prenyltransferases include protein farnesyltransferase (FTase) and geranylgeranyltransferase types I and II (GGTase-I and GGTase-II) which catalyze the carboxyl-terminal lipidation of Ras, Rab, and several other cellular signal transduction proteins, facilitating membrane associations and specific protein-protein interactions. Alpha (2)-M is a major carrier protein in serum and involved in the immobilization and entrapment of proteases. PZP is a pregnancy associated protein. Alpha (2)-M and PZP are known to bind to and, may modulate, the activity of placental protein-14 in T-cell growth and cytokine production thereby protecting the allogeneic fetus from attack by the maternal immune system.


Pssm-ID: 238362 [Multi-domain]  Cd Length: 300  Bit Score: 43.31  E-value: 2.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763826 165 QEAILRALDWLKEKRASDYGWGndthvvilakeLSGGRDPNDSVDghvqviqeledTLSVkemeIEILAMLDRHHTLPKP 244
Cdd:cd00688   51 DENIEKGIQRLLSYQLSDGGFS-----------GWGGNDYPSLWL-----------TAYA----LKALLLAGDYIAVDRI 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763826 245 lDLDKLARYVLalgSLCKDPKHFHGHDLVATLQHHEPaQDIE---FALTTLSACSSAAHVRKRQ-----IRRLLDIASGV 316
Cdd:cd00688  105 -DLARALNWLL---SLQNEDGGFREDGPGNHRIGGDE-SDVRltaYALIALALLGKLDPDPLIEkaldyLLSCQNYDGGF 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763826 317 TDQSVD---AIAMVILALRCIvtdhrHRHLQHFVRRPARGLATLQDQRGSFGSLR----------STALAMQALQDLEYd 383
Cdd:cd00688  180 GPGGEShgyGTACAAAALALL-----GDLDSPDAKKALRWLLSRQRPDGGWGEGRdrtnklsdscYTEWAAYALLALGK- 253

                        250       260
                 ....*....|....*....|....*...
gi 386763826 384 PAGHWNRTAASRYILSRQRADGGWSEEP 411
Cdd:cd00688  254 LGDLEDAEKLVKWLLSQQNEDGGFSSKP 281
squalene_cyclas TIGR01787
squalene/oxidosqualene cyclases; This family of enzymes catalyzes the cyclization of the ...
 320-409 5.19e-04

squalene/oxidosqualene cyclases; This family of enzymes catalyzes the cyclization of the triterpenes squalene or 2-3-oxidosqualene to a variety of products including hopene, lanosterol, cycloartenol, amyrin, lupeol, and isomultiflorenol.


Pssm-ID: 273809 [Multi-domain]  Cd Length: 621  Bit Score: 42.81  E-value: 5.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763826  320 SVDAIAMVILALRCIVtdHRHRHLQHFVRRPARGLATLQDQRGS-FGS--LRSTALAMQALQDLEYdpAGHWNRTAAS-- 394
Cdd:TIGR01787 437 YVDVTARVIQALGAFG--HRADEIRNVLERALEYLRREQRADGSwFGRwgVNYTYGTGFVLSALAA--AGRTYRNCPEvq 512

                          90
                  ....*....|....*...
gi 386763826  395 ---RYILSRQRADGGWSE 409
Cdd:TIGR01787 513 kacDWLLSRQMPDGGWGE 530
Prenyltrans pfam00432
Prenyltransferase and squalene oxidase repeat;
389-419 4.46e-03

Prenyltransferase and squalene oxidase repeat;


Pssm-ID: 395346 [Multi-domain]  Cd Length: 44  Bit Score: 35.18  E-value: 4.46e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 386763826  389 NRTAASRYILSRQRADGGWSEEPlqdGQEPD 419
Cdd:pfam00432   2 DKEKLVDYLLSCQNEDGGFGGRP---GGESD 29
SQCY cd02889
Squalene cyclase (SQCY) domain; found in class II terpene cyclases that have an alpha 6 - ...
 327-411 5.92e-03

Squalene cyclase (SQCY) domain; found in class II terpene cyclases that have an alpha 6 - alpha 6 barrel fold. Squalene cyclase (SQCY) and 2,3-oxidosqualene cyclase (OSQCY) are integral membrane proteins that catalyze a cationic cyclization cascade converting linear triterpenes to fused ring compounds. Bacterial SQCY catalyzes the convertion of squalene to hopene or diplopterol. Eukaryotic OSQCY transforms the 2,3-epoxide of squalene to compounds such as, lanosterol (a metabolic precursor of cholesterol and steroid hormones) in mammals and fungi or, cycloartenol in plants. Deletion of a single glycine residue of Alicyclobacillus acidocaldarius SQCY alters its substrate specificity into that of eukaryotic OSQCY. Both enzymes have a second minor domain, which forms an alpha-alpha barrel that is inserted into the major domain. This group also contains SQCY-like archael sequences and some bacterial SQCY's which lack this minor domain.


Pssm-ID: 239219 [Multi-domain]  Cd Length: 348  Bit Score: 39.13  E-value: 5.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763826 327 VILALRCIVTDHRHRHlqhfVRRPARGLATLQDQRGSFG-SLRS----------------TALAMQALQdleydPAGHWN 389
Cdd:cd02889  225 ALEALAAAGEDENSPY----VRKACDWLLSKQNPDGGWGeSYESyedpsyagggrstvvqTAWALLALM-----AAGEPD 295

                         90       100
                 ....*....|....*....|....*
gi 386763826 390 RTAASR---YILSRQRADGGWSEEP 411
Cdd:cd02889  296 SEAVKRgvkYLLNTQQEDGDWPQEE 320
GGTase-I cd02895
Geranylgeranyltransferase types I (GGTase-I)-like proteins containing the protein ...
 324-411 8.38e-03

Geranylgeranyltransferase types I (GGTase-I)-like proteins containing the protein prenyltransferase (PTase) domain, beta subunit (alpha 6 - alpha 6 barrel fold). GGTase-I s are a subgroup of the protein prenyltransferase family of lipid-modifying enzymes PTases catalyze the carboxyl-terminal lipidation of Ras, Rab, and several other cellular signal transduction proteins, facilitating membrane associations and specific protein-protein interactions. Prenyltransferases employ a Zn2+ ion to alkylate a thiol group catalyzing the formation of thioether linkages between cysteine residues at or near the C-terminus of protein acceptors and the C1 atom of isoprenoid lipids (geranylgeranyl (20-carbon) in the case of GGTase-I ). GGTase-I prenylates the cysteine in the terminal sequence, "CAAX" when X is Leu or Phe. Substrates for GTTase-I include the gamma subunit of neural G-proteins and several Ras-related G-proteins. PTases are heterodimeric with both alpha and beta subunits required for catalytic activity.


Pssm-ID: 239225 [Multi-domain]  Cd Length: 307  Bit Score: 38.41  E-value: 8.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386763826 324 IAMVILALRC--IVTDHRHRhlqhfVRRPA--RGLATLQDQRGSFGS----------LRSTALAMQALQDLEYDPAGHWN 389
Cdd:cd02895   92 LAMTYFALLSllILGDDLSR-----VDRKAilNFLSKLQLPDGSFGSvldseggendMRFCYCAVAICYMLDDWSEEDID 166

                         90       100
                 ....*....|....*....|..
gi 386763826 390 RTAASRYILSRQRADGGWSEEP 411
Cdd:cd02895  167 KEKLIDYIKSSQSYDGGFGQGP 188
 
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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