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Conserved domains on  [gi|1985671669|emb|CAE6264967|]
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unnamed protein product [Arabidopsis arenosa]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Foie-gras_1 pfam11817
Foie gras liver health family 1; Mutating the gene foie gras in zebrafish has been shown to ...
342-611 5.89e-80

Foie gras liver health family 1; Mutating the gene foie gras in zebrafish has been shown to affect development; the mutants develop large, lipid-filled hepatocytes in the liver, resembling those in individuals with fatty liver disease. Foie-gras protein is long and has several well-defined domains though none of them has a known function. We have annotated this one as the first. The C-terminus of this region contains TPR repeats.


:

Pssm-ID: 463359  Cd Length: 248  Bit Score: 263.86  E-value: 5.89e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985671669  342 RLVEIKIIAEQLHFKISTLLLHGGKLIEAVTWFHQHKASYEKVVGSTDF--IFLHW-DWMSRQFLVFAELLETSSATGQS 418
Cdd:pfam11817    1 RFNEARLLADVIAFKIIRLLLWNGQPSDAVRQFRKHRERVKDVVGRRGKgtAFYGWeAWESRQFSVMAELIREAIIPGLT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985671669  419 FSSSNqgtaeisltefefYPAYYYQLAAHYLKDKKSALELLLSMSEIaQEIDTSSASITPSVYVGQfaqllekgetlTLH 498
Cdd:pfam11817   81 PLQTQ-------------HPGYWYQLAARHAMARRSLAEQIPEEDRV-PPGQSPASSLASSFYVYD-----------TYL 135
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985671669  499 SITDEEYTRYTISEAKRFQDSLEIIAWLKRSYESFTNLKARRMAALCAFELAREYFDSADPSNAKFFFDISANLYRQEGW 578
Cdd:pfam11817  136 APEPHEEYPLSGSEEKGVDHSTLIIALLSRALAEFSKRKQTRMAALLSLEMAEEYLRLGDWAKALELLRPLTLSYRQEGW 215
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1985671669  579 VTLLWEVLGYLRECSRNLGALKDFVEFSLEMVA 611
Cdd:pfam11817  216 WTLLEEVLWALRECALLVGDVKDVLAVDWELLS 248
Adaptin_binding pfam10199
Alpha and gamma adaptin binding protein p34; p34 is a protein involved in membrane trafficking. ...
1470-1644 9.97e-08

Alpha and gamma adaptin binding protein p34; p34 is a protein involved in membrane trafficking. It is known to interact with both alpha and gamma adaptin. It has been speculated that p34 may play a chaperone role such as preventing the soluble adaptors from co-assembling with soluble clathrin, or helping to remove the adaptors from the coated vesicle. Another possible function is in aiding the recruitment of soluble adaptors onto the membrane.


:

Pssm-ID: 462994  Cd Length: 96  Bit Score: 51.35  E-value: 9.97e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985671669 1470 DSQGVERLFGALSAHMWPGMILKSGDTIndpvlaqgeelseeeseyeleyevlsagsgdpweniderwvsasethshada 1549
Cdd:pfam10199    1 EKQGIERIVEILETHEWSNMELKSDDGS---------------------------------------------------- 28
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985671669 1550 ggstsqenLHVENNMVKsnkvvdeelrpsgsrlepQNDTDRAIVTDEKPLDTENEKcYEFEDVEQLMSEIGNIRDNLRLM 1629
Cdd:pfam10199   29 --------LQREKLSLE------------------KADSQGQSLPNGKDLQDGDEE-LDVEDFENLLSKLKQARDMAREL 81
                          170
                   ....*....|....*
gi 1985671669 1630 PDFQRREIAANLAMK 1644
Cdd:pfam10199   82 PDEERKEFAAKVAED 96
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
1274-1409 2.05e-05

Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.


:

Pssm-ID: 206648 [Multi-domain]  Cd Length: 161  Bit Score: 46.68  E-value: 2.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985671669 1274 LVVGSSGVGKRTLLSRLLSVEFEDSSESPSQT---EVHGWTINTKYYTAdvsvcisHICD-----DYSLPNLPHSHPLVA 1345
Cdd:cd00882      1 VVVGRGGVGKSSLLNALLGGEVGEVSDVPGTTrdpDVYVKELDKGKVKL-------VLVDtpgldEFGGLGREELARLLL 73
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1985671669 1346 -----LVMVFDLSELSTLVALQDWVSHTDINNFDILLCIGNKVDRVPHHLAHDEYRRRLLKATDPSRIL 1409
Cdd:cd00882     74 rgadlILLVVDSTDRESEEDAKLLILRRLRKEGIPIILVGNKIDLLEEREVEELLRLEELAKILGVPVF 142
 
Name Accession Description Interval E-value
Foie-gras_1 pfam11817
Foie gras liver health family 1; Mutating the gene foie gras in zebrafish has been shown to ...
342-611 5.89e-80

Foie gras liver health family 1; Mutating the gene foie gras in zebrafish has been shown to affect development; the mutants develop large, lipid-filled hepatocytes in the liver, resembling those in individuals with fatty liver disease. Foie-gras protein is long and has several well-defined domains though none of them has a known function. We have annotated this one as the first. The C-terminus of this region contains TPR repeats.


Pssm-ID: 463359  Cd Length: 248  Bit Score: 263.86  E-value: 5.89e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985671669  342 RLVEIKIIAEQLHFKISTLLLHGGKLIEAVTWFHQHKASYEKVVGSTDF--IFLHW-DWMSRQFLVFAELLETSSATGQS 418
Cdd:pfam11817    1 RFNEARLLADVIAFKIIRLLLWNGQPSDAVRQFRKHRERVKDVVGRRGKgtAFYGWeAWESRQFSVMAELIREAIIPGLT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985671669  419 FSSSNqgtaeisltefefYPAYYYQLAAHYLKDKKSALELLLSMSEIaQEIDTSSASITPSVYVGQfaqllekgetlTLH 498
Cdd:pfam11817   81 PLQTQ-------------HPGYWYQLAARHAMARRSLAEQIPEEDRV-PPGQSPASSLASSFYVYD-----------TYL 135
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985671669  499 SITDEEYTRYTISEAKRFQDSLEIIAWLKRSYESFTNLKARRMAALCAFELAREYFDSADPSNAKFFFDISANLYRQEGW 578
Cdd:pfam11817  136 APEPHEEYPLSGSEEKGVDHSTLIIALLSRALAEFSKRKQTRMAALLSLEMAEEYLRLGDWAKALELLRPLTLSYRQEGW 215
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1985671669  579 VTLLWEVLGYLRECSRNLGALKDFVEFSLEMVA 611
Cdd:pfam11817  216 WTLLEEVLWALRECALLVGDVKDVLAVDWELLS 248
Adaptin_binding pfam10199
Alpha and gamma adaptin binding protein p34; p34 is a protein involved in membrane trafficking. ...
1470-1644 9.97e-08

Alpha and gamma adaptin binding protein p34; p34 is a protein involved in membrane trafficking. It is known to interact with both alpha and gamma adaptin. It has been speculated that p34 may play a chaperone role such as preventing the soluble adaptors from co-assembling with soluble clathrin, or helping to remove the adaptors from the coated vesicle. Another possible function is in aiding the recruitment of soluble adaptors onto the membrane.


Pssm-ID: 462994  Cd Length: 96  Bit Score: 51.35  E-value: 9.97e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985671669 1470 DSQGVERLFGALSAHMWPGMILKSGDTIndpvlaqgeelseeeseyeleyevlsagsgdpweniderwvsasethshada 1549
Cdd:pfam10199    1 EKQGIERIVEILETHEWSNMELKSDDGS---------------------------------------------------- 28
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985671669 1550 ggstsqenLHVENNMVKsnkvvdeelrpsgsrlepQNDTDRAIVTDEKPLDTENEKcYEFEDVEQLMSEIGNIRDNLRLM 1629
Cdd:pfam10199   29 --------LQREKLSLE------------------KADSQGQSLPNGKDLQDGDEE-LDVEDFENLLSKLKQARDMAREL 81
                          170
                   ....*....|....*
gi 1985671669 1630 PDFQRREIAANLAMK 1644
Cdd:pfam10199   82 PDEERKEFAAKVAED 96
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
1274-1409 2.05e-05

Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.


Pssm-ID: 206648 [Multi-domain]  Cd Length: 161  Bit Score: 46.68  E-value: 2.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985671669 1274 LVVGSSGVGKRTLLSRLLSVEFEDSSESPSQT---EVHGWTINTKYYTAdvsvcisHICD-----DYSLPNLPHSHPLVA 1345
Cdd:cd00882      1 VVVGRGGVGKSSLLNALLGGEVGEVSDVPGTTrdpDVYVKELDKGKVKL-------VLVDtpgldEFGGLGREELARLLL 73
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1985671669 1346 -----LVMVFDLSELSTLVALQDWVSHTDINNFDILLCIGNKVDRVPHHLAHDEYRRRLLKATDPSRIL 1409
Cdd:cd00882     74 rgadlILLVVDSTDRESEEDAKLLILRRLRKEGIPIILVGNKIDLLEEREVEELLRLEELAKILGVPVF 142
Roc pfam08477
Ras of Complex, Roc, domain of DAPkinase; Roc, or Ras of Complex, proteins are mitochondrial ...
1273-1384 4.10e-04

Ras of Complex, Roc, domain of DAPkinase; Roc, or Ras of Complex, proteins are mitochondrial Rho proteins (Miro-1, and Miro-2) and atypical Rho GTPases. Full-length proteins have a unique domain organization, with tandem GTP-binding domains and two EF hand domains (pfam00036) that may bind calcium. They are also larger than classical small GTPases. It has been proposed that they are involved in mitochondrial homeostasis and apoptosis.


Pssm-ID: 462490 [Multi-domain]  Cd Length: 114  Bit Score: 41.72  E-value: 4.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985671669 1273 VLVVGSSGVGKRTLLSRLLSVEFEDSSESPSQTEVHGWTINTkyYTADVSVCISHICDD------YSLpnlphsHPL--- 1343
Cdd:pfam08477    2 VVLLGDSGVGKTSLLKRFVDDTFDPKYKSTIGVDFKTKTVLE--NDDNGKKIKLNIWDTagqerfRSL------HPFyyr 73
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1985671669 1344 --VALVMVFDLSELSTlvaLQDWVShtDINNF---DILLCIGNKVD 1384
Cdd:pfam08477   74 gaAAALLVYDSRTFSN---LKYWLR--ELKKYagnSPVILVGNKID 114
 
Name Accession Description Interval E-value
Foie-gras_1 pfam11817
Foie gras liver health family 1; Mutating the gene foie gras in zebrafish has been shown to ...
342-611 5.89e-80

Foie gras liver health family 1; Mutating the gene foie gras in zebrafish has been shown to affect development; the mutants develop large, lipid-filled hepatocytes in the liver, resembling those in individuals with fatty liver disease. Foie-gras protein is long and has several well-defined domains though none of them has a known function. We have annotated this one as the first. The C-terminus of this region contains TPR repeats.


Pssm-ID: 463359  Cd Length: 248  Bit Score: 263.86  E-value: 5.89e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985671669  342 RLVEIKIIAEQLHFKISTLLLHGGKLIEAVTWFHQHKASYEKVVGSTDF--IFLHW-DWMSRQFLVFAELLETSSATGQS 418
Cdd:pfam11817    1 RFNEARLLADVIAFKIIRLLLWNGQPSDAVRQFRKHRERVKDVVGRRGKgtAFYGWeAWESRQFSVMAELIREAIIPGLT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985671669  419 FSSSNqgtaeisltefefYPAYYYQLAAHYLKDKKSALELLLSMSEIaQEIDTSSASITPSVYVGQfaqllekgetlTLH 498
Cdd:pfam11817   81 PLQTQ-------------HPGYWYQLAARHAMARRSLAEQIPEEDRV-PPGQSPASSLASSFYVYD-----------TYL 135
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985671669  499 SITDEEYTRYTISEAKRFQDSLEIIAWLKRSYESFTNLKARRMAALCAFELAREYFDSADPSNAKFFFDISANLYRQEGW 578
Cdd:pfam11817  136 APEPHEEYPLSGSEEKGVDHSTLIIALLSRALAEFSKRKQTRMAALLSLEMAEEYLRLGDWAKALELLRPLTLSYRQEGW 215
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1985671669  579 VTLLWEVLGYLRECSRNLGALKDFVEFSLEMVA 611
Cdd:pfam11817  216 WTLLEEVLWALRECALLVGDVKDVLAVDWELLS 248
Adaptin_binding pfam10199
Alpha and gamma adaptin binding protein p34; p34 is a protein involved in membrane trafficking. ...
1470-1644 9.97e-08

Alpha and gamma adaptin binding protein p34; p34 is a protein involved in membrane trafficking. It is known to interact with both alpha and gamma adaptin. It has been speculated that p34 may play a chaperone role such as preventing the soluble adaptors from co-assembling with soluble clathrin, or helping to remove the adaptors from the coated vesicle. Another possible function is in aiding the recruitment of soluble adaptors onto the membrane.


Pssm-ID: 462994  Cd Length: 96  Bit Score: 51.35  E-value: 9.97e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985671669 1470 DSQGVERLFGALSAHMWPGMILKSGDTIndpvlaqgeelseeeseyeleyevlsagsgdpweniderwvsasethshada 1549
Cdd:pfam10199    1 EKQGIERIVEILETHEWSNMELKSDDGS---------------------------------------------------- 28
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985671669 1550 ggstsqenLHVENNMVKsnkvvdeelrpsgsrlepQNDTDRAIVTDEKPLDTENEKcYEFEDVEQLMSEIGNIRDNLRLM 1629
Cdd:pfam10199   29 --------LQREKLSLE------------------KADSQGQSLPNGKDLQDGDEE-LDVEDFENLLSKLKQARDMAREL 81
                          170
                   ....*....|....*
gi 1985671669 1630 PDFQRREIAANLAMK 1644
Cdd:pfam10199   82 PDEERKEFAAKVAED 96
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
1274-1409 2.05e-05

Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.


Pssm-ID: 206648 [Multi-domain]  Cd Length: 161  Bit Score: 46.68  E-value: 2.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985671669 1274 LVVGSSGVGKRTLLSRLLSVEFEDSSESPSQT---EVHGWTINTKYYTAdvsvcisHICD-----DYSLPNLPHSHPLVA 1345
Cdd:cd00882      1 VVVGRGGVGKSSLLNALLGGEVGEVSDVPGTTrdpDVYVKELDKGKVKL-------VLVDtpgldEFGGLGREELARLLL 73
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1985671669 1346 -----LVMVFDLSELSTLVALQDWVSHTDINNFDILLCIGNKVDRVPHHLAHDEYRRRLLKATDPSRIL 1409
Cdd:cd00882     74 rgadlILLVVDSTDRESEEDAKLLILRRLRKEGIPIILVGNKIDLLEEREVEELLRLEELAKILGVPVF 142
Roc pfam08477
Ras of Complex, Roc, domain of DAPkinase; Roc, or Ras of Complex, proteins are mitochondrial ...
1273-1384 4.10e-04

Ras of Complex, Roc, domain of DAPkinase; Roc, or Ras of Complex, proteins are mitochondrial Rho proteins (Miro-1, and Miro-2) and atypical Rho GTPases. Full-length proteins have a unique domain organization, with tandem GTP-binding domains and two EF hand domains (pfam00036) that may bind calcium. They are also larger than classical small GTPases. It has been proposed that they are involved in mitochondrial homeostasis and apoptosis.


Pssm-ID: 462490 [Multi-domain]  Cd Length: 114  Bit Score: 41.72  E-value: 4.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985671669 1273 VLVVGSSGVGKRTLLSRLLSVEFEDSSESPSQTEVHGWTINTkyYTADVSVCISHICDD------YSLpnlphsHPL--- 1343
Cdd:pfam08477    2 VVLLGDSGVGKTSLLKRFVDDTFDPKYKSTIGVDFKTKTVLE--NDDNGKKIKLNIWDTagqerfRSL------HPFyyr 73
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1985671669 1344 --VALVMVFDLSELSTlvaLQDWVShtDINNF---DILLCIGNKVD 1384
Cdd:pfam08477   74 gaAAALLVYDSRTFSN---LKYWLR--ELKKYagnSPVILVGNKID 114
 
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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