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Conserved domains on  [gi|597500993|sp|F4HRI2|]
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RecName: Full=E3 ubiquitin-protein ligase CCNB1IP1 homolog; AltName: Full=RING finger-containing protein HEI10; AltName: Full=RING-type E3 ubiquitin transferase HEI10

Protein Classification

RING finger protein; Siz/PIAS RING finger protein( domain architecture ID 10630239)

RING finger protein may function as an E3 ubiquitin protein ligase that mediates the ubiquitination of target proteins by bringing the ubiquitin-charged E2 ubiquitin-conjugating enzyme and the acceptor protein together to enable the direct transfer of ubiquitin; similar to Homo sapiens E3 ubiquitin-protein ligase RNF10| Siz/PIAS (protein inhibitor of activated signal transducer and activator of transcription) RING (SP-RING) finger protein may function as an E3-type small ubiquitin-like modifier (SUMO) ligase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
zf-RING_5 pfam14634
zinc-RING finger domain;
2-43 1.18e-04

zinc-RING finger domain;


:

Pssm-ID: 434085 [Multi-domain]  Cd Length: 43  Bit Score: 38.95  E-value: 1.18e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 597500993    2 RCNACWRDLEG--RAISTTCGHLLCTEDASKILSNDgACPICDQ 43
Cdd:pfam14634   1 HCNKCFKELSKtrPFYLTSCGHIFCEECLTRLLQER-QCPICKK 43
BORCS5-like super family cl10855
BLOC-1-related complex subunit 5, and related proteins; This model includes BLOC-1-related ...
 106-173 4.95e-04

BLOC-1-related complex subunit 5, and related proteins; This model includes BLOC-1-related complex subunit 5 (BORCS5), which is also called loss of heterozygosity 12 chromosomal region 1 (LOH12CR1), myristoylated lysosomal protein, or myrlysin. BORCS5 is a component of BLOC-1 related complex (BORC), a multisubunit complex that also contains Lyspersin/C17orf59, Diaskedin/C10orf32, KxDL1, MEF2BNB, BLOS1, BLOS2, and Snapin subunits. BLOC-1 is important for the biogenesis of lysosome-related organelles, and BORC is important for the positioning of the lysosome in the cytoplasm. The BORC complex associates with the lysosomal membrane where it recruits the small GTPase Arl8, which leads in turn to the kinesin-dependent movement of lysosomes toward the plus ends of microtubules in the peripheral cytoplasm. LOH12CR1 may function as a tumor suppressor by inhibiting tumor growth through deregulation of the G1/S checkpoint in human colorectal carcinoma. It has been shown to bind to LKB1, a well-known tumor suppressor gene in colorectal cancer; its expression level could be used as a promising biomarker in patients. This domain has also been found in many hypothetical proteins involved in loss of heterozygosity and thus tumor suppression.


The actual alignment was detected with superfamily member pfam10158:

Pssm-ID: 447990  Cd Length: 131  Bit Score: 39.41  E-value: 4.95e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 597500993  106 QKCEGMQAKFSEKMEQVHTAYQKMGKRCQMMEQEVENLTKDKQELQEKFSEKSRQKRKLDEMYDQLRS 173
Cdd:pfam10158  31 NLCTRLQEHFNVCAKAVASDQNKIVARIKEVDASIITLFAETVAHQKQYASYAEQFSKVNQISDQLCR 98
 
Name Accession Description Interval E-value
zf-RING_5 pfam14634
zinc-RING finger domain;
2-43 1.18e-04

zinc-RING finger domain;


Pssm-ID: 434085 [Multi-domain]  Cd Length: 43  Bit Score: 38.95  E-value: 1.18e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 597500993    2 RCNACWRDLEG--RAISTTCGHLLCTEDASKILSNDgACPICDQ 43
Cdd:pfam14634   1 HCNKCFKELSKtrPFYLTSCGHIFCEECLTRLLQER-QCPICKK 43
LOH1CR12 pfam10158
Tumour suppressor protein; This is a region of 130 amino acids that is the most conserved ...
 106-173 4.95e-04

Tumour suppressor protein; This is a region of 130 amino acids that is the most conserved region of hypothetical proteins involved in loss of heterozygosity and thus tumour suppression. The exact function of family members is not known. This region is also found in subunit 5 of the BLOC-1-related complex, which is also found in the BORC complex. BLOC-1 is important for the biogenesis of lysosome-related organelles, and BORC is important for the positioning of the lysosome in the cytoplasm. The BORC complex associates with the lysosomal membrane where it recruits the small GTPase Arl8, which leads in turn to the kinesin-dependent movement of lysosomes toward the plus ends of microtubules in the peripheral cytoplasm.


Pssm-ID: 287167  Cd Length: 131  Bit Score: 39.41  E-value: 4.95e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 597500993  106 QKCEGMQAKFSEKMEQVHTAYQKMGKRCQMMEQEVENLTKDKQELQEKFSEKSRQKRKLDEMYDQLRS 173
Cdd:pfam10158  31 NLCTRLQEHFNVCAKAVASDQNKIVARIKEVDASIITLFAETVAHQKQYASYAEQFSKVNQISDQLCR 98
F-BAR_Fes_Fer cd07657
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Fes (feline sarcoma) and Fer ...
 86-176 1.96e-03

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Fes (feline sarcoma) and Fer (Fes related) tyrosine kinases; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Fes (feline sarcoma), also called Fps (Fujinami poultry sarcoma), and Fer (Fes related) are cytoplasmic (or nonreceptor) tyrosine kinases that play roles in haematopoiesis, inflammation and immunity, growth factor signaling, cytoskeletal regulation, cell migration and adhesion, and the regulation of cell-cell interactions. Although Fes and Fer show redundancy in their biological functions, they show differences in their expression patterns. Fer is ubiquitously expressed while Fes is expressed predominantly in myeloid and endothelial cells. Fes and Fer contain an N-terminal F-BAR domain, an SH2 domain, and a C-terminal catalytic kinase domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules. The F-BAR domain of Fes is critical in its role in microtubule nucleation and bundling.


Pssm-ID: 153341 [Multi-domain]  Cd Length: 237  Bit Score: 38.90  E-value: 1.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597500993  86 IAQRDLEMQYKMNRVVAQCRQKCEGMQAKFSEKMEQVHTAYQKMGKRCQMMEQEVENLTKD-KQELQEKFSEksrqKRKL 164
Cdd:cd07657   63 ISKSWKEIMDSTDQLSKLIKQHAEALESGTLDKLTLLIKDKRKAKKAYQEERQQIDEQYKKlTDEVEKLKSE----YQKL 138

                         90
                 ....*....|..
gi 597500993 165 DEMYDQLRSEYE 176
Cdd:cd07657  139 LEDYKAAKSKFE 150
RING-HC_RAD18 cd16529
RING finger, HC subclass, found in postreplication repair protein RAD18 and similar proteins; ...
 1-41 4.78e-03

RING finger, HC subclass, found in postreplication repair protein RAD18 and similar proteins; RAD18, also known as HR18 or RING finger protein 73 (RNF73), is an E3 ubiquitin-protein ligase involved in post replication repair of UV-damaged DNA via its recruitment to stalled replication forks. It associates to the E2 ubiquitin conjugating enzyme UBE2B to form the UBE2B-RAD18 ubiquitin ligase complex involved in mono-ubiquitination of DNA-associated PCNA on K164. It also interacts with another E2 ubiquitin conjugating enzyme RAD6 to form a complex that monoubiquitinates proliferating cell nuclear antigen at stalled replication forks in DNA translesion synthesis. Moreover, Rad18 is a key factor in double-strand break DNA damage response (DDR) pathways via its association with K63-linked polyubiquitylated chromatin proteins. It can function as a mediator for DNA damage response signals to activate the G2/M checkpoint in order to maintain genome integrity and cell survival after ionizing radiation (IR) exposure. RAD18 contains a C3HC4-type RING-HC finger, a ubiquitin-binding zinc finger domain (UBZ), a SAP (SAF-A/B, Acinus and PIAS) domain, and a RAD6-binding domain (R6BD).


Pssm-ID: 438192 [Multi-domain]  Cd Length: 54  Bit Score: 34.59  E-value: 4.78e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 597500993   1 MRCNACWRDLEGRAISTTCGHLLCTEDASKILSNDGACPIC 41
Cdd:cd16529    5 LRCPICFEYFNTAMMITQCSHNYCSLCIRRFLSYKTQCPTC 45
 
Name Accession Description Interval E-value
zf-RING_5 pfam14634
zinc-RING finger domain;
2-43 1.18e-04

zinc-RING finger domain;


Pssm-ID: 434085 [Multi-domain]  Cd Length: 43  Bit Score: 38.95  E-value: 1.18e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 597500993    2 RCNACWRDLEG--RAISTTCGHLLCTEDASKILSNDgACPICDQ 43
Cdd:pfam14634   1 HCNKCFKELSKtrPFYLTSCGHIFCEECLTRLLQER-QCPICKK 43
LOH1CR12 pfam10158
Tumour suppressor protein; This is a region of 130 amino acids that is the most conserved ...
 106-173 4.95e-04

Tumour suppressor protein; This is a region of 130 amino acids that is the most conserved region of hypothetical proteins involved in loss of heterozygosity and thus tumour suppression. The exact function of family members is not known. This region is also found in subunit 5 of the BLOC-1-related complex, which is also found in the BORC complex. BLOC-1 is important for the biogenesis of lysosome-related organelles, and BORC is important for the positioning of the lysosome in the cytoplasm. The BORC complex associates with the lysosomal membrane where it recruits the small GTPase Arl8, which leads in turn to the kinesin-dependent movement of lysosomes toward the plus ends of microtubules in the peripheral cytoplasm.


Pssm-ID: 287167  Cd Length: 131  Bit Score: 39.41  E-value: 4.95e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 597500993  106 QKCEGMQAKFSEKMEQVHTAYQKMGKRCQMMEQEVENLTKDKQELQEKFSEKSRQKRKLDEMYDQLRS 173
Cdd:pfam10158  31 NLCTRLQEHFNVCAKAVASDQNKIVARIKEVDASIITLFAETVAHQKQYASYAEQFSKVNQISDQLCR 98
F-BAR_Fes_Fer cd07657
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Fes (feline sarcoma) and Fer ...
 86-176 1.96e-03

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Fes (feline sarcoma) and Fer (Fes related) tyrosine kinases; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Fes (feline sarcoma), also called Fps (Fujinami poultry sarcoma), and Fer (Fes related) are cytoplasmic (or nonreceptor) tyrosine kinases that play roles in haematopoiesis, inflammation and immunity, growth factor signaling, cytoskeletal regulation, cell migration and adhesion, and the regulation of cell-cell interactions. Although Fes and Fer show redundancy in their biological functions, they show differences in their expression patterns. Fer is ubiquitously expressed while Fes is expressed predominantly in myeloid and endothelial cells. Fes and Fer contain an N-terminal F-BAR domain, an SH2 domain, and a C-terminal catalytic kinase domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules. The F-BAR domain of Fes is critical in its role in microtubule nucleation and bundling.


Pssm-ID: 153341 [Multi-domain]  Cd Length: 237  Bit Score: 38.90  E-value: 1.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597500993  86 IAQRDLEMQYKMNRVVAQCRQKCEGMQAKFSEKMEQVHTAYQKMGKRCQMMEQEVENLTKD-KQELQEKFSEksrqKRKL 164
Cdd:cd07657   63 ISKSWKEIMDSTDQLSKLIKQHAEALESGTLDKLTLLIKDKRKAKKAYQEERQQIDEQYKKlTDEVEKLKSE----YQKL 138

                         90
                 ....*....|..
gi 597500993 165 DEMYDQLRSEYE 176
Cdd:cd07657  139 LEDYKAAKSKFE 150
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 88-178 4.63e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 38.62  E-value: 4.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597500993    88 QRDLEMQYKMNRV-VAQCRQKCEGMQAKFSEKMEQVHTAYQKMGKRCQMMEQEVENLTKDK------------------- 147
Cdd:pfam01576  333 KKALEEETRSHEAqLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELrtlqqakqdsehkrkkleg 412

                           90       100       110
                   ....*....|....*....|....*....|...
gi 597500993   148 --QELQEKFSEKSRQKRKLDEMYDQLRSEYESV 178
Cdd:pfam01576  413 qlQELQARLSESERQRAELAEKLSKLQSELESV 445
RING-HC_RAD18 cd16529
RING finger, HC subclass, found in postreplication repair protein RAD18 and similar proteins; ...
 1-41 4.78e-03

RING finger, HC subclass, found in postreplication repair protein RAD18 and similar proteins; RAD18, also known as HR18 or RING finger protein 73 (RNF73), is an E3 ubiquitin-protein ligase involved in post replication repair of UV-damaged DNA via its recruitment to stalled replication forks. It associates to the E2 ubiquitin conjugating enzyme UBE2B to form the UBE2B-RAD18 ubiquitin ligase complex involved in mono-ubiquitination of DNA-associated PCNA on K164. It also interacts with another E2 ubiquitin conjugating enzyme RAD6 to form a complex that monoubiquitinates proliferating cell nuclear antigen at stalled replication forks in DNA translesion synthesis. Moreover, Rad18 is a key factor in double-strand break DNA damage response (DDR) pathways via its association with K63-linked polyubiquitylated chromatin proteins. It can function as a mediator for DNA damage response signals to activate the G2/M checkpoint in order to maintain genome integrity and cell survival after ionizing radiation (IR) exposure. RAD18 contains a C3HC4-type RING-HC finger, a ubiquitin-binding zinc finger domain (UBZ), a SAP (SAF-A/B, Acinus and PIAS) domain, and a RAD6-binding domain (R6BD).


Pssm-ID: 438192 [Multi-domain]  Cd Length: 54  Bit Score: 34.59  E-value: 4.78e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 597500993   1 MRCNACWRDLEGRAISTTCGHLLCTEDASKILSNDGACPIC 41
Cdd:cd16529    5 LRCPICFEYFNTAMMITQCSHNYCSLCIRRFLSYKTQCPTC 45
RING-HC_RNF222 cd16564
RING finger, HC subclass, found in RING finger protein 222 (RNF222) and similar proteins; ...
 2-48 5.64e-03

RING finger, HC subclass, found in RING finger protein 222 (RNF222) and similar proteins; RNF222 is an uncharacterized C3HC4-type RING-HC finger-containing protein. It may function as an E3 ubiquitin-protein ligase.


Pssm-ID: 438226 [Multi-domain]  Cd Length: 50  Bit Score: 34.30  E-value: 5.64e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 597500993   2 RCNACWRDLEGRAISTTCGHLLCTEDASKIL-SNDGACPICDQVLSKS 48
Cdd:cd16564    2 ECPVCYEDFDDAPRILSCGHSFCEDCLVKQLvSMTISCPICRRVTFIS 49
RING-HC_IRC20-like cd23135
RING finger, HC subclass, found in Saccharomyces cerevisiae increased recombination centers ...
 3-41 7.38e-03

RING finger, HC subclass, found in Saccharomyces cerevisiae increased recombination centers protein 20 (IRC20) and similar proteins; IRC20 is an uncharacterized ATP-dependent helicase that is probably involved in a pathway contributing to genomic integrity. IRC20 contains a typical C3HC4-type RING-HC finger.


Pssm-ID: 438497 [Multi-domain]  Cd Length: 44  Bit Score: 34.03  E-value: 7.38e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 597500993   3 CNACWRDLEGRAIsTTCGHLLCTEDASKILSNDGACPIC 41
Cdd:cd23135    6 CSICFSEIRSGAI-LKCGHFFCLSCIASWLREKSTCPLC 43
 
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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