NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|27883842|ref|NP_005171|]
View 

polycomb complex protein BMI-1 [Homo sapiens]

Graphical summary

show options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
RING cd00162
RING-finger (Really Interesting New Gene) domain, a specialized type of Zn-finger of 40 to 60 ...
17-56 1.12e-08

RING-finger (Really Interesting New Gene) domain, a specialized type of Zn-finger of 40 to 60 residues that binds two atoms of zinc; defined by the 'cross-brace' motif C-X2-C-X(9-39)-C-X(1-3)- H-X(2-3)-(N/C/H)-X2-C-X(4-48)C-X2-C; probably involved in mediating protein-protein interactions; identified in a proteins with a wide range of functions such as viral replication, signal transduction, and development; has two variants, the C3HC4-type and a C3H2C3-type (RING-H2 finger), which have different cysteine/histidine pattern; a subset of RINGs are associated with B-Boxes (C-X2-H-X7-C-X7-C-X2-C-H-X2-H)


:

Pssm-ID: 238093  Cd Length: 45  Bit Score: 50.52  E-value: 1.12e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 27883842  17 MCVLCGGYFIDATTIIECLHSFCKTCIVRYLETSKY-CPIC 56
Cdd:cd00162   1 ECPICLEEFREPVVLLPCGHVFCRSCIDKWLKSGKNtCPLC 41
 
Name Accession Description Interval E-value
RING cd00162
RING-finger (Really Interesting New Gene) domain, a specialized type of Zn-finger of 40 to 60 ...
17-56 1.12e-08

RING-finger (Really Interesting New Gene) domain, a specialized type of Zn-finger of 40 to 60 residues that binds two atoms of zinc; defined by the 'cross-brace' motif C-X2-C-X(9-39)-C-X(1-3)- H-X(2-3)-(N/C/H)-X2-C-X(4-48)C-X2-C; probably involved in mediating protein-protein interactions; identified in a proteins with a wide range of functions such as viral replication, signal transduction, and development; has two variants, the C3HC4-type and a C3H2C3-type (RING-H2 finger), which have different cysteine/histidine pattern; a subset of RINGs are associated with B-Boxes (C-X2-H-X7-C-X7-C-X2-C-H-X2-H)


Pssm-ID: 238093  Cd Length: 45  Bit Score: 50.52  E-value: 1.12e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 27883842  17 MCVLCGGYFIDATTIIECLHSFCKTCIVRYLETSKY-CPIC 56
Cdd:cd00162   1 ECPICLEEFREPVVLLPCGHVFCRSCIDKWLKSGKNtCPLC 41
zf-C3HC4 pfam00097
Zinc finger, C3HC4 type (RING finger); The C3HC4 type zinc-finger (RING finger) is a ...
18-56 1.25e-11

Zinc finger, C3HC4 type (RING finger); The C3HC4 type zinc-finger (RING finger) is a cysteine-rich domain of 40 to 60 residues that coordinates two zinc ions, and has the consensus sequence: C-X2-C-X(9-39)-C-X(1-3)-H-X(2-3)-C-X2-C-X(4-48)-C-X2-C where X is any amino acid. Many proteins containing a RING finger play a key role in the ubiquitination pathway.


Pssm-ID: 249586  Cd Length: 40  Bit Score: 58.53  E-value: 1.25e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 27883842    18 CVLCGGYFIDATTIIECLHSFCKTCIVRYLE-TSKYCPIC 56
Cdd:pfam00097   1 CPICLEEPKDPVTLLPCGHLFCSKCIRSWLEsGNVTCPLC 40
RING smart00184
Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and ...
18-56 1.45e-08

Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and is likely to be a general function of this domain; Various RING fingers exhibit binding activity towards E2 ubiquitin-conjugating enzymes (Ubc' s)


Pssm-ID: 214546  Cd Length: 40  Bit Score: 50.20  E-value: 1.45e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 27883842     18 CVLCGGYFIDATTIIECLHSFCKTCIVRYLETS-KYCPIC 56
Cdd:smart00184   1 CPICLEEYLKDPVILPCGHTFCRSCIRKWLESGnNTCPIC 40
RAD18 COG5432
RING-finger-containing E3 ubiquitin ligase [Signal transduction mechanisms]
4-168 6.03e-06

RING-finger-containing E3 ubiquitin ligase [Signal transduction mechanisms]


Pssm-ID: 227719 [Multi-domain]  Cd Length: 391  Bit Score: 46.23  E-value: 6.03e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883842   4 TTRI-KITELNPHLMCVLCGGYFiDATTIIECLHSFCKTCIVRYLETSKYCPICDVQVHKTRpllnIRSDKTLQDIV--- 79
Cdd:COG5432  13 QTKIpSLKGLDSMLRCRICDCRI-SIPCETTCGHTFCSLCIRRHLGTQPFCPVCREDPCESR----LRGSSGSREINesh 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883842  80 YKLVPGLFK-----NEMKRRRDFYAAHPSaDAANGSNEDRGEVADEDKRIITDDEiislsieffdqNRLDRKVNKDKEKS 154
Cdd:COG5432  88 ARNRDLLRKvleslCRLPRPIKEERPCRW-ETVIAQDSASGDEEWEDDLASNSSP-----------ASIAKKTSRDSKKR 155
                       170
                ....*....|....
gi 27883842 155 KEEvndkRYLRCPA 168
Cdd:COG5432 156 KRE----DLVHCPA 165
rad18 TIGR00599
DNA repair protein rad18; All proteins in this family for which functions are known are ...
8-180 7.37e-06

DNA repair protein rad18; All proteins in this family for which functions are known are involved in nucleotide excision repair.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University) [DNA metabolism, DNA replication, recombination, and repair].


Pssm-ID: 233043 [Multi-domain]  Cd Length: 397  Bit Score: 45.76  E-value: 7.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883842     8 KITELNP---HLMCVLCGGYFiDATTIIECLHSFCKTCIVRYLETSKYCPICDVQVHKTRpllnIRSDKTLQDIVYKlvp 84
Cdd:TIGR00599  16 PIPSLYPldtSLRCHICKDFF-DVPVLTSCSHTFCSLCIRRCLSNQPKCPLCRAEDQESK----LRSNWLVSEIVES--- 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883842    85 glFKNEMKRRRDFYAAHPSADAANGsnEDRGEVADEDKRIITDDEIISLSIEFFDQNRLDRKVNKDKEKSKEEV------ 158
Cdd:TIGR00599  88 --FKNLRPSLLEFLRIPKTTPVENP--DLAGPENSSKIELIEESESDGVDAEDEDLQRSATSSRALAARSTADIlqlssd 163
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 27883842   159 ----NDKRYLR---------CPAAMTVMHLRKFLR 180
Cdd:TIGR00599 164 pskrNDADYRSeppneglvqCPICQQRMPEKAVER 198
PRK10803 PRK10803
tol-pal system protein YbgF; Provisional
224-281 4.20e-03

tol-pal system protein YbgF; Provisional


Pssm-ID: 182745 [Multi-domain]  Cd Length: 263  Bit Score: 36.70  E-value: 4.20e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 27883842  224 KYRVRPTCKRMK-ISHQRDGLTNAGELESDSGSDKANSPAGGIPSTSSCLPSPSTPVQS 281
Cdd:PRK10803  81 QYQLNQVVERQKqIYLQIDSLSSGGAAAQSTSGDQSGAAASATPAADAGTANAGAPVQS 139
 
Name Accession Description Interval E-value
RING cd00162
RING-finger (Really Interesting New Gene) domain, a specialized type of Zn-finger of 40 to 60 ...
17-56 1.12e-08

RING-finger (Really Interesting New Gene) domain, a specialized type of Zn-finger of 40 to 60 residues that binds two atoms of zinc; defined by the 'cross-brace' motif C-X2-C-X(9-39)-C-X(1-3)- H-X(2-3)-(N/C/H)-X2-C-X(4-48)C-X2-C; probably involved in mediating protein-protein interactions; identified in a proteins with a wide range of functions such as viral replication, signal transduction, and development; has two variants, the C3HC4-type and a C3H2C3-type (RING-H2 finger), which have different cysteine/histidine pattern; a subset of RINGs are associated with B-Boxes (C-X2-H-X7-C-X7-C-X2-C-H-X2-H)


Pssm-ID: 238093  Cd Length: 45  Bit Score: 50.52  E-value: 1.12e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 27883842  17 MCVLCGGYFIDATTIIECLHSFCKTCIVRYLETSKY-CPIC 56
Cdd:cd00162   1 ECPICLEEFREPVVLLPCGHVFCRSCIDKWLKSGKNtCPLC 41
zf-C3HC4 pfam00097
Zinc finger, C3HC4 type (RING finger); The C3HC4 type zinc-finger (RING finger) is a ...
18-56 1.25e-11

Zinc finger, C3HC4 type (RING finger); The C3HC4 type zinc-finger (RING finger) is a cysteine-rich domain of 40 to 60 residues that coordinates two zinc ions, and has the consensus sequence: C-X2-C-X(9-39)-C-X(1-3)-H-X(2-3)-C-X2-C-X(4-48)-C-X2-C where X is any amino acid. Many proteins containing a RING finger play a key role in the ubiquitination pathway.


Pssm-ID: 249586  Cd Length: 40  Bit Score: 58.53  E-value: 1.25e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 27883842    18 CVLCGGYFIDATTIIECLHSFCKTCIVRYLE-TSKYCPIC 56
Cdd:pfam00097   1 CPICLEEPKDPVTLLPCGHLFCSKCIRSWLEsGNVTCPLC 40
zf-C3HC4_2 pfam13923
Zinc finger, C3HC4 type (RING finger);
18-56 1.56e-09

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 258185  Cd Length: 39  Bit Score: 52.85  E-value: 1.56e-09
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 27883842    18 CVLCGGYFIDATTIIECLHSFCKTCIVRYLETSKYCPIC 56
Cdd:pfam13923   1 CPICLDLLKDPVVLTPCGHVFCRECILRLLKKNKKCPIC 39
RING smart00184
Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and ...
18-56 1.45e-08

Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and is likely to be a general function of this domain; Various RING fingers exhibit binding activity towards E2 ubiquitin-conjugating enzymes (Ubc' s)


Pssm-ID: 214546  Cd Length: 40  Bit Score: 50.20  E-value: 1.45e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 27883842     18 CVLCGGYFIDATTIIECLHSFCKTCIVRYLETS-KYCPIC 56
Cdd:smart00184   1 CPICLEEYLKDPVILPCGHTFCRSCIRKWLESGnNTCPIC 40
zf-RING_2 pfam13639
Ring finger domain;
17-56 2.96e-06

Ring finger domain;


Pssm-ID: 257949  Cd Length: 44  Bit Score: 43.53  E-value: 2.96e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 27883842    17 MCVLCGGYFIDATTIIE--CLHSFCKTCIVRYLETSKYCPIC 56
Cdd:pfam13639   2 ECPICLDEFEEGEEVVVlpCGHVFHKECLDKWLRSSPTCPLC 43
zf-C3HC4_3 pfam13920
Zinc finger, C3HC4 type (RING finger);
17-63 5.65e-03

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 258183  Cd Length: 49  Bit Score: 34.29  E-value: 5.65e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 27883842    17 MCVLCGGYFIDaTTIIECLH-SFCKTCIVRyLETSKYCPICDVQVHKT 63
Cdd:pfam13920   4 LCVICLERPRN-VVFLPCGHlCLCEECAKR-LRSKKKCPICRQPIESV 49
zf-rbx1 pfam12678
RING-H2 zinc finger; There are 8 cysteine/ histidine residues which are proposed to be the ...
33-56 5.88e-03

RING-H2 zinc finger; There are 8 cysteine/ histidine residues which are proposed to be the conserved residues involved in zinc binding. The protein, of which this domain is the conserved region, participates in diverse functions relevant to chromosome metabolizm and cell cycle control.


Pssm-ID: 257215  Cd Length: 73  Bit Score: 34.33  E-value: 5.88e-03
                          10        20
                  ....*....|....*....|....
gi 27883842    33 ECLHSFCKTCIVRYLETSKYCPIC 56
Cdd:pfam12678  49 ECGHAFHLHCISRWLKTRNTCPLC 72
RAD18 COG5432
RING-finger-containing E3 ubiquitin ligase [Signal transduction mechanisms]
4-168 6.03e-06

RING-finger-containing E3 ubiquitin ligase [Signal transduction mechanisms]


Pssm-ID: 227719 [Multi-domain]  Cd Length: 391  Bit Score: 46.23  E-value: 6.03e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883842   4 TTRI-KITELNPHLMCVLCGGYFiDATTIIECLHSFCKTCIVRYLETSKYCPICDVQVHKTRpllnIRSDKTLQDIV--- 79
Cdd:COG5432  13 QTKIpSLKGLDSMLRCRICDCRI-SIPCETTCGHTFCSLCIRRHLGTQPFCPVCREDPCESR----LRGSSGSREINesh 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883842  80 YKLVPGLFK-----NEMKRRRDFYAAHPSaDAANGSNEDRGEVADEDKRIITDDEiislsieffdqNRLDRKVNKDKEKS 154
Cdd:COG5432  88 ARNRDLLRKvleslCRLPRPIKEERPCRW-ETVIAQDSASGDEEWEDDLASNSSP-----------ASIAKKTSRDSKKR 155
                       170
                ....*....|....
gi 27883842 155 KEEvndkRYLRCPA 168
Cdd:COG5432 156 KRE----DLVHCPA 165
rad18 TIGR00599
DNA repair protein rad18; All proteins in this family for which functions are known are ...
8-180 7.37e-06

DNA repair protein rad18; All proteins in this family for which functions are known are involved in nucleotide excision repair.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University) [DNA metabolism, DNA replication, recombination, and repair].


Pssm-ID: 233043 [Multi-domain]  Cd Length: 397  Bit Score: 45.76  E-value: 7.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883842     8 KITELNP---HLMCVLCGGYFiDATTIIECLHSFCKTCIVRYLETSKYCPICDVQVHKTRpllnIRSDKTLQDIVYKlvp 84
Cdd:TIGR00599  16 PIPSLYPldtSLRCHICKDFF-DVPVLTSCSHTFCSLCIRRCLSNQPKCPLCRAEDQESK----LRSNWLVSEIVES--- 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27883842    85 glFKNEMKRRRDFYAAHPSADAANGsnEDRGEVADEDKRIITDDEIISLSIEFFDQNRLDRKVNKDKEKSKEEV------ 158
Cdd:TIGR00599  88 --FKNLRPSLLEFLRIPKTTPVENP--DLAGPENSSKIELIEESESDGVDAEDEDLQRSATSSRALAARSTADIlqlssd 163
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 27883842   159 ----NDKRYLR---------CPAAMTVMHLRKFLR 180
Cdd:TIGR00599 164 pskrNDADYRSeppneglvqCPICQQRMPEKAVER 198
COG5222 COG5222
Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only]
8-56 3.28e-03

Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only]


Pssm-ID: 227547 [Multi-domain]  Cd Length: 427  Bit Score: 37.42  E-value: 3.28e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 27883842   8 KITELNPHLMCVLCGGYFIDATTIIECLHSFCKTCI-VRYLETSKYCPIC 56
Cdd:COG5222 267 KMQPPNISLKCPLCHCLLRNPMKTPCCGHTFCDECIgTALLDSDFKCPNC 316
PRK10803 PRK10803
tol-pal system protein YbgF; Provisional
224-281 4.20e-03

tol-pal system protein YbgF; Provisional


Pssm-ID: 182745 [Multi-domain]  Cd Length: 263  Bit Score: 36.70  E-value: 4.20e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 27883842  224 KYRVRPTCKRMK-ISHQRDGLTNAGELESDSGSDKANSPAGGIPSTSSCLPSPSTPVQS 281
Cdd:PRK10803  81 QYQLNQVVERQKqIYLQIDSLSSGGAAAQSTSGDQSGAAASATPAADAGTANAGAPVQS 139
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.11
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH