NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1958660160|ref|XP_038942469|]
View 

breast cancer type 1 susceptibility protein homolog isoform X1 [Rattus norvegicus]

Protein Classification

breast cancer type 1 susceptibility protein( domain architecture ID 13010089)

breast cancer type 1 susceptibility protein (BRCA1) is an E3 ubiquitin-protein ligase that specifically mediates the formation of Lys-6-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
BRCT_assoc pfam12820
Serine-rich domain associated with BRCT; This domain is found on BRCA1 proteins.
343-504 6.51e-85

Serine-rich domain associated with BRCT; This domain is found on BRCA1 proteins.


:

Pssm-ID: 432806  Cd Length: 164  Bit Score: 274.71  E-value: 6.51e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660160  343 DSLCGRKQWNHPKSLCPENSGATTDVPWITLNSSIQKVNEWFSRTGEMLTSDNASDRRPASNAEAAVVLEVSNEVDGCFS 422
Cdd:pfam12820    1 DPLCGRKELPKQKPPCPETPRDTQDVSWITLNSSIQKVNEWFSRSDEILTSDDSHDRRSESNAEVAGALEVPNEVDGYSG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660160  423 SSKKIDLVAPDSDNAVMCTSGRDFSKPVENIINDKIFGKTYQRKGSRPHLNHVTE--IIGTFTTEPQIIQEQPFTNKLKR 500
Cdd:pfam12820   81 SSEKIDLVADDPHGALICESERVHSKPVENNIEDKIFGKTYRRKASLPNLSHITEnlILGAFAKEPQITQEHPLTNKLKR 160

                   ....
gi 1958660160  501 KRST 504
Cdd:pfam12820  161 KRRT 164
BRCT_BRCA1_rpt1 cd17735
first BRCT domain of breast cancer type 1 susceptibility protein (BRCA1) and similar proteins; ...
1596-1692 2.01e-55

first BRCT domain of breast cancer type 1 susceptibility protein (BRCA1) and similar proteins; BRCA1, also termed RING finger protein 53 (RNF53), is a RING finger protein encoded by BRCA1, a tumor suppressor gene that regulates all DNA double-strand break (DSB) repair pathways. BRCA1 is frequently mutated in patients with hereditary breast and ovarian cancer (HBOC). Its mutation is also associated with an increased risk of pancreatic, stomach, laryngeal, fallopian tube, and prostate cancer. It plays an important role in the DNA damage response signaling, and has been implicated in various cellular processes such as cell cycle regulation, transcriptional regulation, chromatin remodeling, DNA DSBs, and apoptosis. BRCA1 contains an N-terminal C3HC4-type RING-HC finger, and two BRCT (BRCA1 C-terminus domain) repeats at the C-terminus. The family corresponds to the first BRCT domain.


:

Pssm-ID: 349367  Cd Length: 97  Bit Score: 187.55  E-value: 2.01e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660160 1596 ISMVVSGLTPKEVMIVQKFAEKYRLALTDVITEETTHVIIKTDAEFVCERTLKYFLGIAGGKWIVSYSWVIKSIQERKLL 1675
Cdd:cd17735      1 MSMVASGLTPEELMLVQKFARKTGSTLTSQFTEETTHVIMKTDAELVCERTLKYFLGIAGRKWVVSYQWITQSIKEGKIL 80
                           90
                   ....*....|....*..
gi 1958660160 1676 SVHEFEVKGDVVTGSNH 1692
Cdd:cd17735     81 PEHDFEVRGDVVNGRNH 97
RING-HC_BRCA1 cd16498
RING finger, HC subclass, found in breast cancer type 1 susceptibility protein (BRCA1) and ...
6-98 7.47e-49

RING finger, HC subclass, found in breast cancer type 1 susceptibility protein (BRCA1) and similar proteins; BRCA1, also known as RING finger protein 53 (RNF53), is a RING finger protein encoded by the tumor suppressor gene BRCA1 that regulates all DNA double-strand break (DSB) repair pathways. BRCA1 is frequently mutated in patients with hereditary breast and ovarian cancer (HBOC). Its mutation is also associated with an increased risk of pancreatic, stomach, laryngeal, fallopian tube, and prostate cancer. It plays an important role in the DNA damage response signaling and has been implicated in various cellular processes such as cell cycle regulation, transcriptional regulation, chromatin remodeling, DNA DSBs, and apoptosis. BRCA1 contains an N-terminal C3HC4-type RING-HC finger, and two BRCT (BRCA1 C-terminus domain) repeats at the C-terminus.


:

Pssm-ID: 438161 [Multi-domain]  Cd Length: 94  Bit Score: 168.63  E-value: 7.47e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660160    6 VRIQEVQNVLHAMQKILECPICLELIKEPVSTKCDHIFCKFCMLKLLNQKKGPSQCPLCKNEITKRSLQGSARFSQLVEE 85
Cdd:cd16498      1 SRIERVQEVISAMQKNLECPICLELLKEPVSTKCDHQFCRFCILKLLQKKKKPAPCPLCKKSVTKRSLQESTRFKQLVEA 80
                           90
                   ....*....|...
gi 1958660160   86 LLKIIDAFELDTG 98
Cdd:cd16498     81 VKKLIDAFELDTG 93
BRCT_BRCA1_rpt2 cd17721
second (C-terminal) BRCT domain of breast cancer type 1 susceptibility protein (BRCA1) and ...
1703-1800 8.73e-46

second (C-terminal) BRCT domain of breast cancer type 1 susceptibility protein (BRCA1) and similar proteins; BRCA1, also termed RING finger protein 53 (RNF53), is a RING finger protein encoded by BRCA1, a tumor suppressor gene that regulates all DNA double-strand break (DSB) repair pathways. BRCA1 is frequently mutated in patients with hereditary breast and ovarian cancer (HBOC). Its mutation is also associated with an increased risk of pancreatic, stomach, laryngeal, fallopian tube, and prostate cancer. It plays an important role in the DNA damage response signaling, and has been implicated in various cellular processes such as cell cycle regulation, transcriptional regulation, chromatin remodeling, DNA DSBs, and apoptosis. BRCA1 contains an N-terminal C3HC4-type RING-HC finger, and two BRCT repeats at the C-terminus. The family corresponds to the second BRCT domain.


:

Pssm-ID: 349353  Cd Length: 98  Bit Score: 160.12  E-value: 8.73e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660160 1703 EKLFEGLQIYCCEPFTNMPKDELERMLQLCGASVVKELPLLTRDTGAHPIVLVQPSAWTEDNDCPDIGQLCKGRLVMWDW 1782
Cdd:cd17721      1 KLLFRGFEICCYGPFTNMTKDQLEWLLELCGATVVKEPSLFTAKPGKKRLIVVQPDAWTEDNDYNAIYRRYKALVVTREW 80
                           90
                   ....*....|....*...
gi 1958660160 1783 VLDSISVYRCRDLDAYLV 1800
Cdd:cd17721     81 VLDSVALYKVQPLDAYLL 98
 
Name Accession Description Interval E-value
BRCT_assoc pfam12820
Serine-rich domain associated with BRCT; This domain is found on BRCA1 proteins.
343-504 6.51e-85

Serine-rich domain associated with BRCT; This domain is found on BRCA1 proteins.


Pssm-ID: 432806  Cd Length: 164  Bit Score: 274.71  E-value: 6.51e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660160  343 DSLCGRKQWNHPKSLCPENSGATTDVPWITLNSSIQKVNEWFSRTGEMLTSDNASDRRPASNAEAAVVLEVSNEVDGCFS 422
Cdd:pfam12820    1 DPLCGRKELPKQKPPCPETPRDTQDVSWITLNSSIQKVNEWFSRSDEILTSDDSHDRRSESNAEVAGALEVPNEVDGYSG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660160  423 SSKKIDLVAPDSDNAVMCTSGRDFSKPVENIINDKIFGKTYQRKGSRPHLNHVTE--IIGTFTTEPQIIQEQPFTNKLKR 500
Cdd:pfam12820   81 SSEKIDLVADDPHGALICESERVHSKPVENNIEDKIFGKTYRRKASLPNLSHITEnlILGAFAKEPQITQEHPLTNKLKR 160

                   ....
gi 1958660160  501 KRST 504
Cdd:pfam12820  161 KRRT 164
BRCT_BRCA1_rpt1 cd17735
first BRCT domain of breast cancer type 1 susceptibility protein (BRCA1) and similar proteins; ...
1596-1692 2.01e-55

first BRCT domain of breast cancer type 1 susceptibility protein (BRCA1) and similar proteins; BRCA1, also termed RING finger protein 53 (RNF53), is a RING finger protein encoded by BRCA1, a tumor suppressor gene that regulates all DNA double-strand break (DSB) repair pathways. BRCA1 is frequently mutated in patients with hereditary breast and ovarian cancer (HBOC). Its mutation is also associated with an increased risk of pancreatic, stomach, laryngeal, fallopian tube, and prostate cancer. It plays an important role in the DNA damage response signaling, and has been implicated in various cellular processes such as cell cycle regulation, transcriptional regulation, chromatin remodeling, DNA DSBs, and apoptosis. BRCA1 contains an N-terminal C3HC4-type RING-HC finger, and two BRCT (BRCA1 C-terminus domain) repeats at the C-terminus. The family corresponds to the first BRCT domain.


Pssm-ID: 349367  Cd Length: 97  Bit Score: 187.55  E-value: 2.01e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660160 1596 ISMVVSGLTPKEVMIVQKFAEKYRLALTDVITEETTHVIIKTDAEFVCERTLKYFLGIAGGKWIVSYSWVIKSIQERKLL 1675
Cdd:cd17735      1 MSMVASGLTPEELMLVQKFARKTGSTLTSQFTEETTHVIMKTDAELVCERTLKYFLGIAGRKWVVSYQWITQSIKEGKIL 80
                           90
                   ....*....|....*..
gi 1958660160 1676 SVHEFEVKGDVVTGSNH 1692
Cdd:cd17735     81 PEHDFEVRGDVVNGRNH 97
RING-HC_BRCA1 cd16498
RING finger, HC subclass, found in breast cancer type 1 susceptibility protein (BRCA1) and ...
6-98 7.47e-49

RING finger, HC subclass, found in breast cancer type 1 susceptibility protein (BRCA1) and similar proteins; BRCA1, also known as RING finger protein 53 (RNF53), is a RING finger protein encoded by the tumor suppressor gene BRCA1 that regulates all DNA double-strand break (DSB) repair pathways. BRCA1 is frequently mutated in patients with hereditary breast and ovarian cancer (HBOC). Its mutation is also associated with an increased risk of pancreatic, stomach, laryngeal, fallopian tube, and prostate cancer. It plays an important role in the DNA damage response signaling and has been implicated in various cellular processes such as cell cycle regulation, transcriptional regulation, chromatin remodeling, DNA DSBs, and apoptosis. BRCA1 contains an N-terminal C3HC4-type RING-HC finger, and two BRCT (BRCA1 C-terminus domain) repeats at the C-terminus.


Pssm-ID: 438161 [Multi-domain]  Cd Length: 94  Bit Score: 168.63  E-value: 7.47e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660160    6 VRIQEVQNVLHAMQKILECPICLELIKEPVSTKCDHIFCKFCMLKLLNQKKGPSQCPLCKNEITKRSLQGSARFSQLVEE 85
Cdd:cd16498      1 SRIERVQEVISAMQKNLECPICLELLKEPVSTKCDHQFCRFCILKLLQKKKKPAPCPLCKKSVTKRSLQESTRFKQLVEA 80
                           90
                   ....*....|...
gi 1958660160   86 LLKIIDAFELDTG 98
Cdd:cd16498     81 VKKLIDAFELDTG 93
BRCT_BRCA1_rpt2 cd17721
second (C-terminal) BRCT domain of breast cancer type 1 susceptibility protein (BRCA1) and ...
1703-1800 8.73e-46

second (C-terminal) BRCT domain of breast cancer type 1 susceptibility protein (BRCA1) and similar proteins; BRCA1, also termed RING finger protein 53 (RNF53), is a RING finger protein encoded by BRCA1, a tumor suppressor gene that regulates all DNA double-strand break (DSB) repair pathways. BRCA1 is frequently mutated in patients with hereditary breast and ovarian cancer (HBOC). Its mutation is also associated with an increased risk of pancreatic, stomach, laryngeal, fallopian tube, and prostate cancer. It plays an important role in the DNA damage response signaling, and has been implicated in various cellular processes such as cell cycle regulation, transcriptional regulation, chromatin remodeling, DNA DSBs, and apoptosis. BRCA1 contains an N-terminal C3HC4-type RING-HC finger, and two BRCT repeats at the C-terminus. The family corresponds to the second BRCT domain.


Pssm-ID: 349353  Cd Length: 98  Bit Score: 160.12  E-value: 8.73e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660160 1703 EKLFEGLQIYCCEPFTNMPKDELERMLQLCGASVVKELPLLTRDTGAHPIVLVQPSAWTEDNDCPDIGQLCKGRLVMWDW 1782
Cdd:cd17721      1 KLLFRGFEICCYGPFTNMTKDQLEWLLELCGATVVKEPSLFTAKPGKKRLIVVQPDAWTEDNDYNAIYRRYKALVVTREW 80
                           90
                   ....*....|....*...
gi 1958660160 1783 VLDSISVYRCRDLDAYLV 1800
Cdd:cd17721     81 VLDSVALYKVQPLDAYLL 98
zf-C3HC4 pfam00097
Zinc finger, C3HC4 type (RING finger); The C3HC4 type zinc-finger (RING finger) is a ...
24-64 5.97e-10

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: 395049 [Multi-domain]  Cd Length: 40  Bit Score: 55.82  E-value: 5.97e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1958660160   24 CPICLELIKEPV-STKCDHIFCKFCMLKLLNqkKGPSQCPLC 64
Cdd:pfam00097    1 CPICLEEPKDPVtLLPCGHLFCSKCIRSWLE--SGNVTCPLC 40
BRCT smart00292
breast cancer carboxy-terminal domain;
1703-1787 2.33e-09

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 55.46  E-value: 2.33e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660160  1703 EKLFEGLQIYCCEPFTNMPKDELERMLQLCGASVVKELPLLTRDtgaHPIVLVQPSAWTEDNdcpdIGQLCKGRLVMWDW 1782
Cdd:smart00292    1 PKLFKGKTFYITGSFDKEERDELKELIEALGGKVTSSLSSKTTT---HVIVGSPEGGKLELL----KAIALGIPIVKEEW 73

                    ....*
gi 1958660160  1783 VLDSI 1787
Cdd:smart00292   74 LLDCL 78
BRCT pfam00533
BRCA1 C-terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ...
1702-1787 2.98e-09

BRCA1 C-terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in cell cycle checkpoint functions responsive to DNA damage. The BRCT domain of XRCC1 forms a homodimer in the crystal structure. This suggests that pairs of BRCT domains associate as homo- or heterodimers. BRCT domains are often found as tandem-repeat pairs. Structures of the BRCA1 BRCT domains revealed a basis for a widely utilized head-to-tail BRCT-BRCT oligomerization mode. This conserved tandem BRCT architecture facilitates formation of the canonical BRCT phospho-peptide interaction cleft at a groove between the BRCT domains. Disease associated missense and nonsense mutations in the BRCA1 BRCT domains disrupt peptide binding by directly occluding this peptide binding groove, or by disrupting key conserved BRCT core folding determinants.


Pssm-ID: 425736 [Multi-domain]  Cd Length: 75  Bit Score: 54.99  E-value: 2.98e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660160 1702 QEKLFEGLQIYCCePFTNMPKDELERMLQLCGASVVKELplltrDTGAHPIVlvqpsaWTEDNDCPDIGQLCKGRLVMWD 1781
Cdd:pfam00533    2 KEKLFSGKTFVIT-GLDGLERDELKELIEKLGGKVTDSL-----SKKTTHVI------VEARTKKYLKAKELGIPIVTEE 69

                   ....*.
gi 1958660160 1782 WVLDSI 1787
Cdd:pfam00533   70 WLLDCI 75
BRCT pfam00533
BRCA1 C-terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ...
1594-1669 3.66e-09

BRCA1 C-terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in cell cycle checkpoint functions responsive to DNA damage. The BRCT domain of XRCC1 forms a homodimer in the crystal structure. This suggests that pairs of BRCT domains associate as homo- or heterodimers. BRCT domains are often found as tandem-repeat pairs. Structures of the BRCA1 BRCT domains revealed a basis for a widely utilized head-to-tail BRCT-BRCT oligomerization mode. This conserved tandem BRCT architecture facilitates formation of the canonical BRCT phospho-peptide interaction cleft at a groove between the BRCT domains. Disease associated missense and nonsense mutations in the BRCA1 BRCT domains disrupt peptide binding by directly occluding this peptide binding groove, or by disrupting key conserved BRCT core folding determinants.


Pssm-ID: 425736 [Multi-domain]  Cd Length: 75  Bit Score: 54.99  E-value: 3.66e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958660160 1594 RDISMVVSGLTPKEVMIVQKFAEKYRLALTDVITEETTHVIiktdaefVCERTLKYFLGIAGGKWIVSYSWVIKSI 1669
Cdd:pfam00533    7 SGKTFVITGLDGLERDELKELIEKLGGKVTDSLSKKTTHVI-------VEARTKKYLKAKELGIPIVTEEWLLDCI 75
RING smart00184
Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and ...
24-64 8.38e-09

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 [Multi-domain]  Cd Length: 40  Bit Score: 52.90  E-value: 8.38e-09
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|..
gi 1958660160    24 CPICLE-LIKEPVSTKCDHIFCKFCMLKLLNQkkGPSQCPLC 64
Cdd:smart00184    1 CPICLEeYLKDPVILPCGHTFCRSCIRKWLES--GNNTCPIC 40
PEX10 COG5574
RING-finger-containing E3 ubiquitin ligase [Posttranslational modification, protein turnover, ...
23-65 3.95e-06

RING-finger-containing E3 ubiquitin ligase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227861 [Multi-domain]  Cd Length: 271  Bit Score: 50.28  E-value: 3.95e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1958660160   23 ECPICLELIKEPVSTKCDHIFCKFCMLKLLnQKKGPSQCPLCK 65
Cdd:COG5574    217 KCFLCLEEPEVPSCTPCGHLFCLSCLLISW-TKKKYEFCPLCR 258
rad18 TIGR00599
DNA repair protein rad18; All proteins in this family for which functions are known are ...
15-84 9.62e-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: 273165 [Multi-domain]  Cd Length: 397  Bit Score: 50.00  E-value: 9.62e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660160   15 LHAMQKILECPICLELIKEPVSTKCDHIFCKFCMLKLLNQKkgpSQCPLCKNEITKRSLQGSARFSQLVE 84
Cdd:TIGR00599   20 LYPLDTSLRCHICKDFFDVPVLTSCSHTFCSLCIRRCLSNQ---PKCPLCRAEDQESKLRSNWLVSEIVE 86
PLN03208 PLN03208
E3 ubiquitin-protein ligase RMA2; Provisional
22-73 1.23e-05

E3 ubiquitin-protein ligase RMA2; Provisional


Pssm-ID: 178747 [Multi-domain]  Cd Length: 193  Bit Score: 47.77  E-value: 1.23e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958660160   22 LECPICLELIKEPVSTKCDHIFCKFCMLKL-------------LNQKKGPSQCPLCKNEITKRSL 73
Cdd:PLN03208    19 FDCNICLDQVRDPVVTLCGHLFCWPCIHKWtyasnnsrqrvdqYDHKREPPKCPVCKSDVSEATL 83
BRCT smart00292
breast cancer carboxy-terminal domain;
1603-1669 1.63e-05

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 44.67  E-value: 1.63e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958660160  1603 LTPKEVMIVQKFAEKYRLALTDVITE------------ETTHVIIKTDAEfvceRTLKYFLGIAGGKWIVSYSWVIKSI 1669
Cdd:smart00292    4 FKGKTFYITGSFDKEERDELKELIEAlggkvtsslsskTTTHVIVGSPEG----GKLELLKAIALGIPIVKEEWLLDCL 78
 
Name Accession Description Interval E-value
BRCT_assoc pfam12820
Serine-rich domain associated with BRCT; This domain is found on BRCA1 proteins.
343-504 6.51e-85

Serine-rich domain associated with BRCT; This domain is found on BRCA1 proteins.


Pssm-ID: 432806  Cd Length: 164  Bit Score: 274.71  E-value: 6.51e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660160  343 DSLCGRKQWNHPKSLCPENSGATTDVPWITLNSSIQKVNEWFSRTGEMLTSDNASDRRPASNAEAAVVLEVSNEVDGCFS 422
Cdd:pfam12820    1 DPLCGRKELPKQKPPCPETPRDTQDVSWITLNSSIQKVNEWFSRSDEILTSDDSHDRRSESNAEVAGALEVPNEVDGYSG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660160  423 SSKKIDLVAPDSDNAVMCTSGRDFSKPVENIINDKIFGKTYQRKGSRPHLNHVTE--IIGTFTTEPQIIQEQPFTNKLKR 500
Cdd:pfam12820   81 SSEKIDLVADDPHGALICESERVHSKPVENNIEDKIFGKTYRRKASLPNLSHITEnlILGAFAKEPQITQEHPLTNKLKR 160

                   ....
gi 1958660160  501 KRST 504
Cdd:pfam12820  161 KRRT 164
BRCT_BRCA1_rpt1 cd17735
first BRCT domain of breast cancer type 1 susceptibility protein (BRCA1) and similar proteins; ...
1596-1692 2.01e-55

first BRCT domain of breast cancer type 1 susceptibility protein (BRCA1) and similar proteins; BRCA1, also termed RING finger protein 53 (RNF53), is a RING finger protein encoded by BRCA1, a tumor suppressor gene that regulates all DNA double-strand break (DSB) repair pathways. BRCA1 is frequently mutated in patients with hereditary breast and ovarian cancer (HBOC). Its mutation is also associated with an increased risk of pancreatic, stomach, laryngeal, fallopian tube, and prostate cancer. It plays an important role in the DNA damage response signaling, and has been implicated in various cellular processes such as cell cycle regulation, transcriptional regulation, chromatin remodeling, DNA DSBs, and apoptosis. BRCA1 contains an N-terminal C3HC4-type RING-HC finger, and two BRCT (BRCA1 C-terminus domain) repeats at the C-terminus. The family corresponds to the first BRCT domain.


Pssm-ID: 349367  Cd Length: 97  Bit Score: 187.55  E-value: 2.01e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660160 1596 ISMVVSGLTPKEVMIVQKFAEKYRLALTDVITEETTHVIIKTDAEFVCERTLKYFLGIAGGKWIVSYSWVIKSIQERKLL 1675
Cdd:cd17735      1 MSMVASGLTPEELMLVQKFARKTGSTLTSQFTEETTHVIMKTDAELVCERTLKYFLGIAGRKWVVSYQWITQSIKEGKIL 80
                           90
                   ....*....|....*..
gi 1958660160 1676 SVHEFEVKGDVVTGSNH 1692
Cdd:cd17735     81 PEHDFEVRGDVVNGRNH 97
RING-HC_BRCA1 cd16498
RING finger, HC subclass, found in breast cancer type 1 susceptibility protein (BRCA1) and ...
6-98 7.47e-49

RING finger, HC subclass, found in breast cancer type 1 susceptibility protein (BRCA1) and similar proteins; BRCA1, also known as RING finger protein 53 (RNF53), is a RING finger protein encoded by the tumor suppressor gene BRCA1 that regulates all DNA double-strand break (DSB) repair pathways. BRCA1 is frequently mutated in patients with hereditary breast and ovarian cancer (HBOC). Its mutation is also associated with an increased risk of pancreatic, stomach, laryngeal, fallopian tube, and prostate cancer. It plays an important role in the DNA damage response signaling and has been implicated in various cellular processes such as cell cycle regulation, transcriptional regulation, chromatin remodeling, DNA DSBs, and apoptosis. BRCA1 contains an N-terminal C3HC4-type RING-HC finger, and two BRCT (BRCA1 C-terminus domain) repeats at the C-terminus.


Pssm-ID: 438161 [Multi-domain]  Cd Length: 94  Bit Score: 168.63  E-value: 7.47e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660160    6 VRIQEVQNVLHAMQKILECPICLELIKEPVSTKCDHIFCKFCMLKLLNQKKGPSQCPLCKNEITKRSLQGSARFSQLVEE 85
Cdd:cd16498      1 SRIERVQEVISAMQKNLECPICLELLKEPVSTKCDHQFCRFCILKLLQKKKKPAPCPLCKKSVTKRSLQESTRFKQLVEA 80
                           90
                   ....*....|...
gi 1958660160   86 LLKIIDAFELDTG 98
Cdd:cd16498     81 VKKLIDAFELDTG 93
BRCT_BRCA1_rpt2 cd17721
second (C-terminal) BRCT domain of breast cancer type 1 susceptibility protein (BRCA1) and ...
1703-1800 8.73e-46

second (C-terminal) BRCT domain of breast cancer type 1 susceptibility protein (BRCA1) and similar proteins; BRCA1, also termed RING finger protein 53 (RNF53), is a RING finger protein encoded by BRCA1, a tumor suppressor gene that regulates all DNA double-strand break (DSB) repair pathways. BRCA1 is frequently mutated in patients with hereditary breast and ovarian cancer (HBOC). Its mutation is also associated with an increased risk of pancreatic, stomach, laryngeal, fallopian tube, and prostate cancer. It plays an important role in the DNA damage response signaling, and has been implicated in various cellular processes such as cell cycle regulation, transcriptional regulation, chromatin remodeling, DNA DSBs, and apoptosis. BRCA1 contains an N-terminal C3HC4-type RING-HC finger, and two BRCT repeats at the C-terminus. The family corresponds to the second BRCT domain.


Pssm-ID: 349353  Cd Length: 98  Bit Score: 160.12  E-value: 8.73e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660160 1703 EKLFEGLQIYCCEPFTNMPKDELERMLQLCGASVVKELPLLTRDTGAHPIVLVQPSAWTEDNDCPDIGQLCKGRLVMWDW 1782
Cdd:cd17721      1 KLLFRGFEICCYGPFTNMTKDQLEWLLELCGATVVKEPSLFTAKPGKKRLIVVQPDAWTEDNDYNAIYRRYKALVVTREW 80
                           90
                   ....*....|....*...
gi 1958660160 1783 VLDSISVYRCRDLDAYLV 1800
Cdd:cd17721     81 VLDSVALYKVQPLDAYLL 98
BRCT_Bard1_rpt1 cd17734
first BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar proteins; ...
1601-1675 1.95e-20

first BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar proteins; Bard1, also termed BARD-1, or RING-type E3 ubiquitin transferase BARD1, is a critical factor in BRCA1-mediated tumor suppression and may also serve as a target for tumorigenic lesions in some human cancers. It associates with BRCA1 (breast cancer-1) to form a heterodimeric BRCA1/BARD1 complex that is responsible for maintaining genomic stability through nuclear functions involving DNA damage signaling and repair, transcriptional regulation, and cell cycle control. The BRCA1/BARD1 complex catalyzes autoubiquitination of BRCA1 and trans ubiquitination of other protein substrates. Its E3 ligase activity is dramatically reduced in the presence of UBX domain protein 1 (UBXN1). BARD-1 contains an N-terminal C3HC4-type RING-HC finger that binds BRCA1, and a C-terminal region with three ankyrin repeats and tandem BRCT domains that bind CstF-50 (cleavage stimulation factor) to modulate mRNA processing and RNAP II stability in response to DNA damage. The family corresponds to the first BRCT domain.


Pssm-ID: 349366  Cd Length: 80  Bit Score: 86.89  E-value: 1.95e-20
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958660160 1601 SGLTPKEVMIVQKFAEKYRLALTDVITEETTHVIIKTDAEFVCERTLKYFLGIAGGKWIVSYSWVIKSIQERKLL 1675
Cdd:cd17734      6 SGLSSEQKKLLEKLAQLLKAKVVTEFSPEVTHVVVPADERGVCPRTMKYLMGILAGKWIVSFEWVEACLKAKKLV 80
BRCT_microcephalin_rpt2 cd17736
second BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA damage ...
1596-1673 3.08e-13

second BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA damage response protein involved in regulation of CHK1 and BRCA1. It has been implicated in chromosome condensation and DNA damage induced cellular responses. It may play a role in neurogenesis and regulation of the size of the cerebral cortex. Microcephalin contains three BRCT repeats. This family corresponds to the second repeat.


Pssm-ID: 349368  Cd Length: 76  Bit Score: 66.46  E-value: 3.08e-13
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958660160 1596 ISMVVSGLTPKEVMIVQKFAEKYRLA-LTDVITEETTHVIIKTDAefvceRTLKYFLGIAGGKWIVSYSWVIKSIQERK 1673
Cdd:cd17736      1 RTLVMTSVHSEEQELLESVVKKLGGFrVEDSVTEKTTHVVVGSPR-----RTLNVLLGIARGCWILSPDWVLESLEAGK 74
RING-HC_ScRAD18-like cd23148
RING finger, HC subclass, found in Saccharomyces cerevisiae radiation sensitivity protein 18 ...
19-73 4.05e-13

RING finger, HC subclass, found in Saccharomyces cerevisiae radiation sensitivity protein 18 (RAD18) and similar proteins; RAD18, also called RING-type E3 ubiquitin transferase RAD18, acts as a postreplication repair E3 ubiquitin-protein ligase that associates with the E2 ubiquitin conjugating enzyme UBC2/RAD6 to form the UBC2-RAD18 ubiquitin ligase complex involved in postreplicative repair (PRR) of damaged DNA. The UBC2-RAD18 complex cooperates with RAD5 and the UBC13-MMS2 dimer to attach mono-ubiquitin chains on 'Lys-164' of POL30, which is necessary for PRR. The UBC2-RAD18 complex is also involved in prevention of spontaneous mutations caused by 7,8-dihydro-8-oxoguanine. RAD18 is an E3 RING-finger protein belonging to the UBC2/RAD6 epistasis group. It contains a typical C3HC4-type RING-HC finger.


Pssm-ID: 438510 [Multi-domain]  Cd Length: 52  Bit Score: 65.25  E-value: 4.05e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958660160   19 QKILECPICLELIKEPVSTKCDHIFCKFCMLKLLNQKkgpSQCPLCKNEITKRSL 73
Cdd:cd23148      1 DHALRCHICKDLLKAPMRTPCNHTFCSFCIRTHLNND---ARCPLCKAEVTESGL 52
RING-HC_RNF10 cd16536
RING finger, HC subclass, found in RING finger protein 10 (RNF10) and similar proteins; RNF10 ...
23-74 1.06e-12

RING finger, HC subclass, found in RING finger protein 10 (RNF10) and similar proteins; RNF10 is an E3 ubiquitin-protein ligase that interacts with mesenchyme Homeobox 2 (MEOX2) transcription factor, a regulator of the proliferation, differentiation and migration of vascular smooth muscle cells and cardiomyocytes; it enhances Meox2 activation of the p21 promoter. It also regulates the expression of myelin-associated glycoprotein (MAG) genes and is required for myelin production in Schwann cells of the peripheral nervous system. Moreover, RNF10 regulates retinoic acid-induced neuronal differentiation and the cell cycle exit of P19 embryonic carcinoma cells. RNF10 contains a C3HC4-type RING-HC finger and three putative nuclear localization signals.


Pssm-ID: 438198 [Multi-domain]  Cd Length: 54  Bit Score: 64.18  E-value: 1.06e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958660160   23 ECPICLElikEPVS---TKCDHIFCKFCMLKLLN-QKKGPSQCPLCKNEITKRSLQ 74
Cdd:cd16536      2 QCPICLE---PPVApriTRCGHIFCWPCILRYLSlSEKKWRKCPICFESIHKKDLR 54
RING-HC cd16449
HC subclass of RING (RING-HC) finger and its variants; The RING finger is a specialized type ...
22-64 2.99e-11

HC subclass of RING (RING-HC) finger and its variants; The RING finger is a specialized type of Zn-finger of 40 to 60 residues that binds two atoms of zinc. It is defined by the "cross-brace" motif that chelates zinc atoms by eight amino acid residues, typically Cys or His, arranged in a characteristic spacing. Canonical RING motifs have been categorized into two major subclasses, RING-HC (C3HC4-type) and RING-H2 (C3H2C3-type), according to their Cys/His content. There are also many variants of RING fingers. Some have a different Cys/His pattern. Some lack a single Cys or His residue at typical Zn ligand positions, especially, the fourth or eighth zinc ligand is prevalently exchanged for an Asp, which can chelate Zn in a RING finger as well. This family corresponds to the HC subclass of RING (RING-HC) fingers that are characterized by containing C3HC4-type canonical RING-HC fingers or noncanonical RING-HC finger variants, including C4C4-, C3HC3D-, C2H2C4-, and C3HC5-type modified RING-HC fingers. The canonical RING-HC finger has been defined as C-X2-C-X(9-39)-C-X(1-3)-H-X(2-3)-C-X2-C-X(4-48)-C-X2-C. It binds two Zn ions in a unique "cross-brace" arrangement, which distinguishes it from tandem zinc fingers and other similar motifs. RING-HC fingers can be found in a group of diverse proteins with a variety of cellular functions, including oncogenesis, development, viral replication, signal transduction, the cell cycle, and apoptosis. Many of them are ubiquitin-protein ligases (E3s) that serve as scaffolds for binding to ubiquitin-conjugating enzymes (E2s, also referred to as ubiquitin carrier proteins or UBCs) in close proximity to substrate proteins, which enables efficient transfer of ubiquitin from E2 to the substrates.


Pssm-ID: 438113 [Multi-domain]  Cd Length: 41  Bit Score: 59.81  E-value: 2.99e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1958660160   22 LECPICLELIKEPVSTKCDHIFCKFCMLKLLnqKKGPSQCPLC 64
Cdd:cd16449      1 LECPICLERLKDPVLLPCGHVFCRECIRRLL--ESGSIKCPIC 41
RING-HC_HLTF cd16509
RING finger, HC subclass, found in helicase-like transcription factor (HLTF) and similar ...
23-73 7.25e-11

RING finger, HC subclass, found in helicase-like transcription factor (HLTF) and similar proteins; HLTF, also known as DNA-binding protein/plasminogen activator inhibitor 1 regulator, HIP116, RING finger protein 80, SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 3, or sucrose nonfermenting protein 2-like 3, is a yeast RAD5 homolog found in mammals. It has both E3 ubiquitin ligase and DNA helicase activities, and plays a pivotal role in the template-switching pathway of DNA damage tolerance. It is involved in Lys-63-linked poly-ubiquitination of proliferating cell nuclear antigen (PCNA) at Lys-164 and in the regulation of DNA damage tolerance. It shows double-stranded DNA translocase activity with 3'-5' polarity, thereby facilitating regression of the replication fork. HLTF contains an N-terminal HIRAN (HIP116 and RAD5 N-terminal) domain, a SWI/SNF helicase domain that is divided into N- and C-terminal parts by an insertion of a C3HC4-type RING-HC finger involved in the poly-ubiquitination of PCNA.


Pssm-ID: 438172 [Multi-domain]  Cd Length: 53  Bit Score: 58.86  E-value: 7.25e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1958660160   23 ECPICLELIKEPVSTKCDHIFCKFCMLKLLNQKKgpSQCPLCKNEITKRSL 73
Cdd:cd16509      5 ECAICLDSLTNPVITPCAHVFCRRCICEVIQREK--AKCPMCRAPLSASDL 53
RING-HC_AtRMA-like cd16745
RING finger, HC subclass, found in Arabidopsis thaliana RING membrane-anchor proteins (AtRMAs) ...
23-65 3.18e-10

RING finger, HC subclass, found in Arabidopsis thaliana RING membrane-anchor proteins (AtRMAs) and similar proteins; AtRMAs, including AtRma1, AtRma2, and AtRma3, are endoplasmic reticulum (ER)-localized Arabidopsis homologs of human outer membrane of the ER-anchor E3 ubiquitin-protein ligase, RING finger protein 5 (RNF5). AtRMAs possess E3 ubiquitin ligase activity, and may play a role in the growth and development of Arabidopsis. The AtRMA1 and AtRMA3 genes are predominantly expressed in major tissues, such as cotyledons, leaves, shoot-root junction, roots, and anthers, while AtRMA2 expression is restricted to the root tips and leaf hydathodes. AtRma1 probably functions with the Ubc4/5 subfamily of E2. AtRma2 is likely involved in the cellular regulation of ABP1 expression levels through interacting with auxin binding protein 1 (ABP1). AtRMA proteins contain an N-terminal C3HC4-type RING-HC finger and a trans-membrane-anchoring domain in their extreme C-terminal region.


Pssm-ID: 438403 [Multi-domain]  Cd Length: 45  Bit Score: 56.72  E-value: 3.18e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1958660160   23 ECPICLELIKEPVSTKCDHIFCKFCMLKLLNQKKGPSQCPLCK 65
Cdd:cd16745      2 ECNICLDLAQDPVVTLCGHLFCWPCLHKWLRRQSSQPECPVCK 44
BRCT cd00027
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ...
1596-1668 5.22e-10

C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The BRCT (BRCA1 C-terminus) domain is found within many DNA damage repair and cell cycle checkpoint proteins. BRCT domains interact with each other forming homo/hetero BRCT multimers, but are also involved in BRCT-non-BRCT interactions and interactions within DNA strand breaks. BRCT tandem repeats bind to phosphopeptides; it has been shown that the repeats in human BRCA1 bind specifically to pS-X-X-F motifs, mediating the interaction between BRCA1 and the DNA helicase BACH1, or BRCA1 and CtIP, a transcriptional corepressor. It is assumed that BRCT repeats play similar roles in many signaling pathways associated with the response to DNA damage.


Pssm-ID: 349339 [Multi-domain]  Cd Length: 68  Bit Score: 56.99  E-value: 5.22e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958660160 1596 ISMVVSGLTPKEVMIVQKFAEKYRLALTDVITEETTHVIIKTDaefvcERTLKYFLGIAGGKWIVSYSWVIKS 1668
Cdd:cd00027      1 LVICFSGLDDEEREELKKLIEALGGKVSESLSSKVTHLIAKSP-----SGEKYYLAALAWGIPIVSPEWLLDC 68
RING-HC_RNF138 cd16544
RING finger, HC subclass, found in RING finger protein 138 (RNF138) and similar proteins; ...
22-71 5.54e-10

RING finger, HC subclass, found in RING finger protein 138 (RNF138) and similar proteins; RNF138, also known as Nemo-like kinase-associated RING finger protein (NARF) or NLK-associated RING finger protein, is an E3 ubiquitin-protein ligase that plays an important role in glioma cell proliferation, apoptosis, and cell cycle. It specifically cooperates with the E2 conjugating enzyme E2-25K (Hip-2/UbcH1), regulates the ubiquitylation and degradation of T cell factor/lymphoid enhancer factor (TCF/LEF), and further suppresses Wnt-beta-catenin signaling. RNF138, together with three closely related proteins: RNF114, RNF125 and RNF166, forms a novel family of ubiquitin ligases with a C3HC4-type RING-HC finger, a C2HC-, and two C2H2-type zinc fingers, as well as a ubiquitin interacting motif (UIM).


Pssm-ID: 438206 [Multi-domain]  Cd Length: 53  Bit Score: 56.26  E-value: 5.54e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1958660160   22 LECPICLELIKEPVST-KCDHIFCKFCMLKLLnqKKGPSQCPLCKNEITKR 71
Cdd:cd16544      3 LTCPVCQEVLKDPVELpPCRHIFCKACILLAL--RSSGARCPLCRGPVGKT 51
zf-C3HC4 pfam00097
Zinc finger, C3HC4 type (RING finger); The C3HC4 type zinc-finger (RING finger) is a ...
24-64 5.97e-10

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: 395049 [Multi-domain]  Cd Length: 40  Bit Score: 55.82  E-value: 5.97e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1958660160   24 CPICLELIKEPV-STKCDHIFCKFCMLKLLNqkKGPSQCPLC 64
Cdd:pfam00097    1 CPICLEEPKDPVtLLPCGHLFCSKCIRSWLE--SGNVTCPLC 40
RING-HC_LONFs_rpt2 cd16514
second RING finger, HC subclass, found in the LON peptidase N-terminal domain and RING finger ...
22-65 6.32e-10

second RING finger, HC subclass, found in the LON peptidase N-terminal domain and RING finger protein family; The LON peptidase N-terminal domain and RING finger protein family includes LONRF1 (also known as RING finger protein 191 or RNF191), LONRF2 (also known as RING finger protein 192, RNF192, or neuroblastoma apoptosis-related protease), LONRF3 (also known as RING finger protein 127 or RNF127), which are characterized by containing two C3HC4-type RING-HC fingers, four tetratricopeptide (TPR) repeats, and an ATP-dependent protease La (LON) substrate-binding domain at the C-terminus. Their biological functions remain unclear. This model corresponds to the second RING-HC finger.


Pssm-ID: 438177 [Multi-domain]  Cd Length: 45  Bit Score: 56.12  E-value: 6.32e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1958660160   22 LECPICLELIKEPVSTKCDHIFCKFCMLKLLNQKkgpSQCPLCK 65
Cdd:cd16514      2 LECSLCLRLLYEPVTTPCGHTFCRACLERCLDHS---PKCPLCR 42
RING-HC_COP1 cd16504
RING finger, HC subclass, found in constitutive photomorphogenesis protein 1 (COP1) and ...
22-69 7.09e-10

RING finger, HC subclass, found in constitutive photomorphogenesis protein 1 (COP1) and similar proteins; COP1, also known as RING finger and WD repeat domain protein 2 (RFWD2) or RING finger protein 200 (RNF200), is a central regulator of photomorphogenic development in plants, which targets key transcription factors for proteasome-dependent degradation. It is localized predominantly in the nucleus, but may also be present in the cytosol. Mammalian COP1 functions as an E3 ubiquitin-protein ligase that interacts with Jun transcription factors and modulates their transcriptional activity. It also interacts with and negatively regulates the tumor-suppressor protein p53. Moreover, COP1 associates with COP9 signalosome subunit 6 (CSN6), and is involved in 14-3-3sigma ubiquitin-mediated degradation. The CSN6-COP1 link enhances ubiquitin-mediated degradation of p27(Kip1), a critical CDK inhibitor involved in cell cycle regulation, to promote cancer cell growth. Furthermore, COP1 functions as the negative regulator of ETV1 and influences prognosis in triple-negative breast cancer. COP1 contains an N-terminal extension, a C3HC4-type RING-HC finger, a coiled coil domain, and seven WD40 repeats. In human COP1, a classic leucine-rich NES, and a novel bipartite NLS is bridged by the RING-HC finger.


Pssm-ID: 438167 [Multi-domain]  Cd Length: 47  Bit Score: 56.10  E-value: 7.09e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1958660160   22 LECPICLELIKEPVSTKCDHIFCKFCMLKLLNQKkgpSQCPLCKNEIT 69
Cdd:cd16504      3 FLCPICFDIIKEAFVTKCGHSFCYKCIVKHLEQK---NRCPKCNFYLT 47
RING-HC_TRIM21_C-IV cd16596
RING finger, HC subclass, found in tripartite motif-containing protein TRIM21 and similar ...
15-89 8.66e-10

RING finger, HC subclass, found in tripartite motif-containing protein TRIM21 and similar proteins; TRIM21, also known as 52 kDa Ro protein, 52 kDa ribonucleoprotein autoantigen Ro/SS-A, Ro(SS-A), RING finger protein 81 (RNF81), or Sjoegren syndrome type A antigen (SS-A), is a ubiquitously expressed E3 ubiquitin-protein ligase and a high affinity antibody receptor uniquely expressed in the cytosol of mammalian cells. As a cytosolic Fc receptor, TRIM21 binds the Fc of virus-associated antibodies and targets the complex in the cytosol for proteasomal degradation in a process known as antibody-dependent intracellular neutralization (ADIN), and provides an intracellular immune response to protect host defense against pathogen infection. It shows remarkably broad isotype specificity as it does not only bind IgG, but also IgM and IgA. Moreover, TRIM21 promotes the cytosolic DNA sensor cGAS and the cytosolic RNA sensor RIG-I sensing of viral genomes during infection by antibody-opsonized virus. It stimulates inflammatory signaling and activates innate transcription factors, such as nuclear factor-kappaB (NF-kappaB). TRIM21 also plays an essential role in p62-regulated redox homeostasis, suggesting it may be a viable target for treating pathological conditions resulting from oxidative damage. Furthermore, TRIM21 may have implications for various autoimmune diseases associated with uncontrolled antiviral signaling through the regulation of Nmi-IFI35 complex-mediated inhibition of innate antiviral response. TRIM21 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438258 [Multi-domain]  Cd Length: 77  Bit Score: 56.83  E-value: 8.66e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958660160   15 LHAMQKILECPICLELIKEPVSTKCDHIFCKFCMLKLlnQKKGPSQCPLCKNEITKRSLQGSARFSQLVEELLKI 89
Cdd:cd16596      3 LTMMWEEVTCPICLDPFVEPVSIECGHSFCQECISQV--GKGGGSVCPVCRQRFLLKNLRPNRQLANMVNNLKEI 75
BRCT smart00292
breast cancer carboxy-terminal domain;
1703-1787 2.33e-09

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 55.46  E-value: 2.33e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660160  1703 EKLFEGLQIYCCEPFTNMPKDELERMLQLCGASVVKELPLLTRDtgaHPIVLVQPSAWTEDNdcpdIGQLCKGRLVMWDW 1782
Cdd:smart00292    1 PKLFKGKTFYITGSFDKEERDELKELIEALGGKVTSSLSSKTTT---HVIVGSPEGGKLELL----KAIALGIPIVKEEW 73

                    ....*
gi 1958660160  1783 VLDSI 1787
Cdd:smart00292   74 LLDCL 78
BRCT pfam00533
BRCA1 C-terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ...
1702-1787 2.98e-09

BRCA1 C-terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in cell cycle checkpoint functions responsive to DNA damage. The BRCT domain of XRCC1 forms a homodimer in the crystal structure. This suggests that pairs of BRCT domains associate as homo- or heterodimers. BRCT domains are often found as tandem-repeat pairs. Structures of the BRCA1 BRCT domains revealed a basis for a widely utilized head-to-tail BRCT-BRCT oligomerization mode. This conserved tandem BRCT architecture facilitates formation of the canonical BRCT phospho-peptide interaction cleft at a groove between the BRCT domains. Disease associated missense and nonsense mutations in the BRCA1 BRCT domains disrupt peptide binding by directly occluding this peptide binding groove, or by disrupting key conserved BRCT core folding determinants.


Pssm-ID: 425736 [Multi-domain]  Cd Length: 75  Bit Score: 54.99  E-value: 2.98e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660160 1702 QEKLFEGLQIYCCePFTNMPKDELERMLQLCGASVVKELplltrDTGAHPIVlvqpsaWTEDNDCPDIGQLCKGRLVMWD 1781
Cdd:pfam00533    2 KEKLFSGKTFVIT-GLDGLERDELKELIEKLGGKVTDSL-----SKKTTHVI------VEARTKKYLKAKELGIPIVTEE 69

                   ....*.
gi 1958660160 1782 WVLDSI 1787
Cdd:pfam00533   70 WLLDCI 75
RING-HC_AtBRCA1-like cd23147
RING finger, HC subclass, found in Arabidopsis thaliana protein BREAST CANCER SUSCEPTIBILITY 1 ...
18-74 3.16e-09

RING finger, HC subclass, found in Arabidopsis thaliana protein BREAST CANCER SUSCEPTIBILITY 1 homolog (AtBRCA1) and similar proteins; AtBRCA1 plays a role in DNA repair and in cell-cycle control. It is required for the repair of DNA double-strand breaks (DSBs), both natural and induced by genotoxic stress, by homologous recombination (HR). AtBRCA1 contains a typical C3HC4-type RING-HC finger.


Pssm-ID: 438509 [Multi-domain]  Cd Length: 54  Bit Score: 54.40  E-value: 3.16e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958660160   18 MQKILECPICLELIKEPVSTKCDHIFCKFCMLKLLnqkKGPSQCPLCKNEITKRSLQ 74
Cdd:cd23147      1 LGKELKCPICLSLFKSAANLSCNHCFCAGCIGESL---KLSAICPVCKIPATRRDTR 54
RING-HC_PRT1-like cd23132
RING finger, HC subclass, found in Arabidopsis thaliana proteolysis 1 protein (PRT1) and ...
22-70 3.60e-09

RING finger, HC subclass, found in Arabidopsis thaliana proteolysis 1 protein (PRT1) and similar proteins; PRT1, also called RING-type E3 ubiquitin transferase PRT1, is an E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. It functions in the N-end rule pathway of protein degradation, where it specifically recognizes and ubiquitinates proteins with an N-terminal bulky aromatic amino acid (Phe). It does not act on aliphatic hydrophobic and basic N-terminal residues (Arg or Leu) containing proteins. PRT1 contains a typical C3HC4-type RING-HC finger.


Pssm-ID: 438494 [Multi-domain]  Cd Length: 52  Bit Score: 53.96  E-value: 3.60e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1958660160   22 LECPICLELIKEPVSTKCDHIFCKFCMLKLLNqKKGPSQCPLCKNEITK 70
Cdd:cd23132      3 FLCCICLDLLYKPVVLECGHVFCFWCVHRCMN-GYDESHCPLCRRPYDH 50
BRCT pfam00533
BRCA1 C-terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ...
1594-1669 3.66e-09

BRCA1 C-terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in cell cycle checkpoint functions responsive to DNA damage. The BRCT domain of XRCC1 forms a homodimer in the crystal structure. This suggests that pairs of BRCT domains associate as homo- or heterodimers. BRCT domains are often found as tandem-repeat pairs. Structures of the BRCA1 BRCT domains revealed a basis for a widely utilized head-to-tail BRCT-BRCT oligomerization mode. This conserved tandem BRCT architecture facilitates formation of the canonical BRCT phospho-peptide interaction cleft at a groove between the BRCT domains. Disease associated missense and nonsense mutations in the BRCA1 BRCT domains disrupt peptide binding by directly occluding this peptide binding groove, or by disrupting key conserved BRCT core folding determinants.


Pssm-ID: 425736 [Multi-domain]  Cd Length: 75  Bit Score: 54.99  E-value: 3.66e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958660160 1594 RDISMVVSGLTPKEVMIVQKFAEKYRLALTDVITEETTHVIiktdaefVCERTLKYFLGIAGGKWIVSYSWVIKSI 1669
Cdd:pfam00533    7 SGKTFVITGLDGLERDELKELIEKLGGKVTDSLSKKTTHVI-------VEARTKKYLKAKELGIPIVTEEWLLDCI 75
RING-HC_RNF213 cd16561
RING finger, HC subclass, found in RING finger protein 213 (RNF213) and similar proteins; ...
23-70 3.82e-09

RING finger, HC subclass, found in RING finger protein 213 (RNF213) and similar proteins; RNF213, also known as ALK lymphoma oligomerization partner on chromosome 17 or Moyamoya steno-occlusive disease-associated AAA+ and RING finger protein (mysterin), is an intracellular soluble protein that functions as an E3 ubiquitin-protein ligase and AAA+ ATPase, which possibly contributes to vascular development through mechanical processes in the cell. It plays a unique role in endothelial cells for proper gene expression in response to inflammatory signals from the environment. Mutations in RNF213 may be associated with Moyamoya disease (MMD), an idiopathic cerebrovascular occlusive disorder prevalent in East Asia. It also acts as a nuclear marker for acanthomorph phylogeny. RNF213 contains two tandem enzymatically active AAA+ ATPase modules and a C3HC4-type RING-HC finger. It can form a huge ring-shaped oligomeric complex.


Pssm-ID: 438223 [Multi-domain]  Cd Length: 50  Bit Score: 53.82  E-value: 3.82e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1958660160   23 ECPICLELIKEPVSTKCDHIFCKFCMLKLLNQKKgpsQCPLCKNEITK 70
Cdd:cd16561      4 ECSICLEDLNDPVKLPCDHVFCEECIRQWLPGQM---SCPLCRTELPD 48
RING-HC_TRIM5-like_C-IV cd16591
RING finger, HC subclass, found in tripartite motif-containing proteins TRIM5, TRIM6, TRIM22, ...
24-84 7.56e-09

RING finger, HC subclass, found in tripartite motif-containing proteins TRIM5, TRIM6, TRIM22, TRIM34 and similar proteins; TRIM5, TRIM6, TRIM22, and TRIM34, four closely related tripartite motif-containing proteins, belong to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. TRIM5, also known as RING finger protein 88 (RNF88), is a capsid-specific restriction factor that prevents infection from non-host-adapted retroviruses in a species-specific manner by binding to and destabilizing the retroviral capsid lattice before reverse transcription is completed. Its retroviral restriction activity correlates with the ability to activate TAK1-dependent innate immune signaling. TRIM5 also acts as a pattern recognition receptor that activates innate immune signaling in response to the retroviral capsid lattice. Moreover, TRIM5 plays a role in regulating autophagy through activation of autophagy regulator BECN1 by causing its dissociation from its inhibitors BCL2 and TAB2. It also plays a role in autophagy by acting as a selective autophagy receptor which recognizes and targets HIV-1 capsid protein p24 for autophagic destruction. TRIM6, also known as RING finger protein 89 (RNF89), is an E3-ubiquitin ligase that cooperates with the E2-ubiquitin conjugase UbE2K to catalyze the synthesis of unanchored K48-linked polyubiquitin chains, and further stimulates the interferon-I kappa B kinase epsilon (IKKepsilon) kinase-mediated antiviral response. It also regulates the transcriptional activity of Myc during the maintenance of embryonic stem (ES) cell pluripotency, and may act as a novel regulator for Myc-mediated transcription in ES cells. TRIM22, also known as 50 kDa-stimulated trans-acting factor (Staf-50) or RING finger protein 94 (RNF94), is an E3 ubiquitin-protein ligase that plays an integral role in the host innate immune response to viruses. It has been shown to inhibit the replication of a number of viruses, including HIV-1, hepatitis B, and influenza A. TRIM22 acts as a suppressor of basal HIV-1 long terminal repeat (LTR)-driven transcription by preventing the transcription factor specificity protein 1 (Sp1) binding to the HIV-1 promoter. It also controls FoxO4 activity and cell survival by directing Toll-like receptor 3 (TLR3)-stimulated cells toward type I interferon (IFN) type I gene induction or apoptosis. Moreover, TRIM22 can activate the noncanonical nuclear factor-kappaB (NF-kappaB) pathway by activating I kappa B kinase alpha (IKKalpha). It also regulates nucleotide binding oligomerization domain containing 2 (NOD2)-dependent activation of interferon-beta signaling and nuclear factor-kappaB. TRIM34, also known as interferon-responsive finger protein 1 or RING finger protein 21 (RNF21), may function as antiviral protein that contribute to the defense against retroviral infections.


Pssm-ID: 438253 [Multi-domain]  Cd Length: 72  Bit Score: 53.99  E-value: 7.56e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958660160   24 CPICLELIKEPVSTKCDHIFCKFCMLKLLNQ---KKGPSQCPLCKNEITKRSLQGSARFSQLVE 84
Cdd:cd16591      9 CPICLELLTEPLSLDCGHSFCQACITANHKEsvnQEGESSCPVCRTSYQPENLRPNRHLANIVE 72
RING-HC_TRIM47-like_C-IV cd16604
RING finger, HC subclass, found in tripartite motif-containing protein 47 (TRIM47) and similar ...
22-65 8.38e-09

RING finger, HC subclass, found in tripartite motif-containing protein 47 (TRIM47) and similar proteins; TRIM47, also known as gene overexpressed in astrocytoma protein (GOA) or RING finger protein 100 (RNF100), belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, a B-box, and two coiled coil domains, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. It plays an important role in the process of dedifferentiation that is associated with astrocytoma tumorigenesis. This subfamily also includes RING finger protein 135 (RNF135). RNF135, also known as RIG-I E3 ubiquitin ligase (REUL) or Riplet, is a widely expressed E3 ubiquitin-protein ligase that consists of an N-terminal C3HC4-type RING-HC finger and C-terminal B30.2/SPRY and PRY motifs, but lacks the B-box and coiled-coil domains that are also typically present in TRIM proteins. RNF135 serves as a specific retinoic acid-inducible gene-I (RIG-I)-interacting protein that ubiquitinates RIG-I and specifically stimulates RIG-I-mediated innate antiviral activity to produce antiviral type-I interferon (IFN) during the early phase of viral infection. It also has been identified as a bio-marker and therapy target of glioblastoma. It associates with the ERK signal transduction pathway and plays a role in glioblastoma cell proliferation, migration and cell cycle.


Pssm-ID: 438266 [Multi-domain]  Cd Length: 49  Bit Score: 52.81  E-value: 8.38e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1958660160   22 LECPICLELIKEPVSTKCDHIFCKFCMLKLLNQKKGPS-QCPLCK 65
Cdd:cd16604      1 LSCPICLDLLKDPVTLPCGHSFCMGCLGALWGAGRGGRaSCPLCR 45
RING smart00184
Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and ...
24-64 8.38e-09

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 [Multi-domain]  Cd Length: 40  Bit Score: 52.90  E-value: 8.38e-09
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|..
gi 1958660160    24 CPICLE-LIKEPVSTKCDHIFCKFCMLKLLNQkkGPSQCPLC 64
Cdd:smart00184    1 CPICLEeYLKDPVILPCGHTFCRSCIRKWLES--GNNTCPIC 40
RING-HC_TRIM40-C-V cd16583
RING finger, HC subclass, found in tripartite motif-containing protein 40 (TRIM40) and similar ...
24-65 9.79e-09

RING finger, HC subclass, found in tripartite motif-containing protein 40 (TRIM40) and similar proteins; TRIM40, also known as probable E3 NEDD8-protein ligase or RING finger protein 35 (RNF35), is highly expressed in the gastrointestinal tract including the stomach, small intestine, and large intestine. It enhances neddylation of inhibitor of nuclear factor kappaB kinase subunit gamma (IKKgamma), inhibits the activity of nuclear factor-kappaB (NF-kappaB)-mediated transcription, and thus prevents inflammation-associated carcinogenesis in the gastrointestinal tract. TRIM40 belongs to the C-V subclass of the TRIM (tripartite motif) family of proteins that are defined by an N-terminal RBCC (RING, Bbox, and coiled coil) domain, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as an uncharacterized region positioned C-terminal to the RBCC domain.


Pssm-ID: 438245 [Multi-domain]  Cd Length: 63  Bit Score: 53.30  E-value: 9.79e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1958660160   24 CPICLELIKEPVSTKCDHIFCKFCMLKLLNQ--KKGPSQCPLCK 65
Cdd:cd16583      8 CPICQEPLKEAVSTDCGHLFCRMCLTQHAKKasASGVFSCPVCR 51
RING-HC_TRIM72_C-IV cd16612
RING finger, HC subclass, found in tripartite motif-containing protein 72 (TRIM72) and similar ...
18-65 1.05e-08

RING finger, HC subclass, found in tripartite motif-containing protein 72 (TRIM72) and similar proteins; TRIM72, also known as Mitsugumin-53 (MG53), is a muscle-specific protein that plays a central role in cell membrane repair by nucleating the assembly of the repair machinery at muscle injury sites. It is required in repair of alveolar epithelial cells under plasma membrane stress failure. It interacts with dysferlin to regulate sarcolemmal repair. Upregulation of TRIM72 develops obesity, systemic insulin resistance, dyslipidemia, and hyperglycemia, as well as induces diabetic cardiomyopathy through transcriptional activation of the peroxisome proliferation-activated receptor alpha (PPAR-alpha) signaling pathway. Compensation for the absence of AKT signaling by ERK signaling during TRIM72 overexpression leads to pathological hypertrophy. Moreover, TRIM72 functions as a novel negative feedback regulator of myogenesis by targeting insulin receptor substrate-1 (IRS-1). It is transcriptionally activated by the synergism of myogenin (MyoD) and myocyte enhancer factor 2 (MEF2). TRIM72 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438274 [Multi-domain]  Cd Length: 60  Bit Score: 53.20  E-value: 1.05e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1958660160   18 MQKILECPICLELIKEPVSTKCDHIFCKFCMLKL-LNQKKGPSQCPLCK 65
Cdd:cd16612      1 MHQDLSCPLCLKLFQSPVTTECGHTFCQDCLSRVpKEEDGGSTSCPTCQ 49
RING-HC_TRIM7-like_C-IV cd16594
RING finger, HC subclass, found in tripartite motif-containing proteins, TRIM7, TRIM11 and ...
19-74 1.16e-08

RING finger, HC subclass, found in tripartite motif-containing proteins, TRIM7, TRIM11 and TRIM27, and similar proteins; TRIM7, TRIM11 and TRIM27, closely related tripartite motif-containing proteins, belong to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox2, and a coiled coil region, as well as a SPRY/B30.2 domain positioned C-terminal to the RBCC domain. TRIM7, also known as glycogenin-interacting protein (GNIP) or RING finger protein 90 (RNF90), is an E3 ubiquitin-protein ligase that mediates c-Jun/AP-1 activation by Ras signalling. Its phosphorylation and activation by MSK1 in response to direct activation by the Ras-Raf-MEK-ERK pathway can stimulate TRIM7 E3 ubiquitin ligase activity in mediating Lys63-linked ubiquitination of the AP-1 coactivator RACO-1, leading to RACO-1 protein stabilization. Moreover, TRIM7 binds and activates glycogenin, the self-glucosylating initiator of glycogen biosynthesis. TRIM11, also known as protein BIA1, or RING finger protein 92 (RNF92), is an E3 ubiquitin-protein ligase involved in the development of the central nervous system. It is overexpressed in high-grade gliomas and promotes proliferation, invasion, migration and glial tumor growth. TRIM11 acts as a potential therapeutic target for congenital central hypoventilation syndrome (CCHS) by mediating the degradation of CCHS-associated polyalanine-expanded Phox2b. TRIM11 modulates the function of neurogenic transcription factor Pax6 through the ubiquitin-proteosome system, and thus plays an essential role for Pax6-dependent neurogenesis. It also binds to and destabilizes a key component of the activator-mediated cofactor complex (ARC105), humanin, a neuroprotective peptide against Alzheimer's disease-relevant insults, and further regulates ARC105 function in transforming growth factor beta (TGFbeta) signaling. Moreover, TRIM11 negatively regulates retinoic acid-inducible gene-I (RIG-I)-mediated interferon-beta (IFNbeta) production and antiviral activity by targeting TANK-binding kinase-1 (TBK1). It may contribute to the endogenous restriction of retroviruses in cells. It enhances N-tropic murine leukemia virus (N-MLV) entry by interfering with Ref1 restriction. It also suppresses the early steps of human immunodeficiency virus HIV-1 transduction, resulting in decreased reverse transcripts. TRIM27, also known as RING finger protein 76 (RNF76), RET finger protein (RFP), or zinc finger protein RFP, is a nuclear E3 ubiquitin-protein ligase that is highly expressed in testis and in various tumor cell lines. Expression of TRIM27 is associated with prognosis of colon and endometrial cancers. TRIM27 was first identified as a fusion partner of the RET receptor tyrosine kinase. It functions as a transcriptional repressor and associates with several proteins involved in transcriptional activity, such as enhancer of polycomb 1 (Epc1), a member of the Polycomb group proteins, and Mi-2beta, a main component of the nucleosome remodeling and deacetylase (NuRD) complex, and the cell cycle regulator retinoblastoma protein (RB1). It also interacts with HDAC1, leading to downregulation of thioredoxin binding protein 2 (TBP-2), which inhibits the function of thioredoxin. Moreover, TRIM27 mediates Pax7-induced ubiquitination of MyoD in skeletal muscle atrophy. In addition, it inhibits muscle differentiation by modulating serum response factor (SRF) and Epc1. TRIM27 promotes a non-canonical polyubiquitination of PTEN, a lipid phosphatase that catalyzes PtdIns(3,4,5)P3 (PIP3) to PtdIns(4,5)P2 (PIP2). It is an IKKepsilon-interacting protein that regulates IkappaB kinase (IKK) function and negatively regulates signaling involved in the antiviral response and inflammation. TRIM27 also forms a protein complex with MBD4 or MBD2 or MBD3, and thus plays an important role in the enhancement of transcriptional repression through MBD proteins in tumorigenesis, spermatogenesis, and embryogenesis. It is a component of an estrogen receptor 1 (ESR1) regulatory complex that is involved in estrogen receptor-mediated transcription in MCF-7 cells.


Pssm-ID: 438256 [Multi-domain]  Cd Length: 61  Bit Score: 53.07  E-value: 1.16e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958660160   19 QKILECPICLELIKEPVSTKCDHIFCKFCMLKLLNQKKGPSQCPLCKNEITKRSLQ 74
Cdd:cd16594      3 QEELTCPICLDYFTDPVTLDCGHSFCRACIARCWEEPETSASCPQCRETCPQRNLR 58
RING-HC_RNF5-like cd16534
RING finger, HC subclass, found in RING finger protein RNF5, RNF185 and similar proteins; RNF5 ...
23-65 1.25e-08

RING finger, HC subclass, found in RING finger protein RNF5, RNF185 and similar proteins; RNF5 and RNF185 are E3 ubiquitin-protein ligases that are anchored to the outer membrane of the endoplasmic reticulum (ER). RNF5 acts at early stages of cystic fibrosis (CF) transmembrane conductance regulator (CFTR) biosynthesis, and functions as a target for therapeutic modalities to antagonize mutant CFTR proteins in CF patients carrying the F508del allele. RNF185 controls the degradation of CFTR and CFTR F508del allele in a RING- and proteasome-dependent manner, but does not control that of other classical endoplasmic reticulum-associated degradation (ERAD) model substrates. Moreover, both RNF5 and RNF185 play important roles in cell adhesion and migration through the modulation of cell migration by ubiquitinating paxillin. Arabidopsis thaliana RING membrane-anchor proteins (AtRMAs) are also included in this family. They possess E3 ubiquitin-protein ligase activity and may play a role in the growth and development of Arabidopsis. All members of this family contain a C3HC4-type RING-HC finger.


Pssm-ID: 438196 [Multi-domain]  Cd Length: 44  Bit Score: 52.30  E-value: 1.25e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1958660160   23 ECPICLELIKEPVSTKCDHIFCKFCMLKLLNQKKGPSQCPLCK 65
Cdd:cd16534      2 ECNICLDTASDPVVTMCGHLFCWPCLYQWLETRPDRQTCPVCK 44
RING-HC_TRIM77_C-IV cd16543
RING finger, HC subclass, found in tripartite motif-containing protein 77 (TRIM77) and similar ...
22-72 2.02e-08

RING finger, HC subclass, found in tripartite motif-containing protein 77 (TRIM77) and similar proteins; TRIM77 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including two consecutive zinc-binding domains, a C3HC4-type RING-HC finger and Bbox2, as well as a SPRY/B30.2 domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438205 [Multi-domain]  Cd Length: 54  Bit Score: 52.01  E-value: 2.02e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1958660160   22 LECPICLELIKEPVSTKCDHIFCKFCMLKLLNQKKGPSQCPLCKNEITKRS 72
Cdd:cd16543      4 LTCSICLDLLKDPVTIPCGHSFCMNCITLLWDRKQGVPSCPQCRESFPPRP 54
RING-HC_MmTRIM43-like cd23133
RING finger, HC subclass, found in Mus musculus tripartite motif-containing protein 43 (TRIM43) ...
22-71 2.51e-08

RING finger, HC subclass, found in Mus musculus tripartite motif-containing protein 43 (TRIM43) and similar propteins; This subfamily includes TRIM43A, TRIM43B and TRIM43C, which are expressed specifically in mouse preimplantation embryos. They contain a typical C3HC4-type RING-HC finger.


Pssm-ID: 438495 [Multi-domain]  Cd Length: 57  Bit Score: 51.84  E-value: 2.51e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958660160   22 LECPICLELIKEPVSTKCDHIFCKFCMLKLLNQKKGPSQCPLCKNEITKR 71
Cdd:cd23133      4 LTCSICQGIFMNPVYLRCGHKFCEACLLLFQEDIKFPAYCPMCRQPFNQE 53
zf-C3HC4_2 pfam13923
Zinc finger, C3HC4 type (RING finger);
23-64 4.30e-08

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 404756 [Multi-domain]  Cd Length: 40  Bit Score: 50.51  E-value: 4.30e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1958660160   23 ECPICLELIKEP-VSTKCDHIFCKFCMLKLLNQKKgpsQCPLC 64
Cdd:pfam13923    1 MCPICMDMLKDPsTTTPCGHVFCQDCILRALRAGN---ECPLC 40
RING-HC_TRIM69_C-IV cd16611
RING finger, HC subclass, found in tripartite motif-containing protein 69 (TRIM69) and similar ...
22-73 4.89e-08

RING finger, HC subclass, found in tripartite motif-containing protein 69 (TRIM69) and similar proteins; TRIM69, also known as RFP-like domain-containing protein trimless or RING finger protein 36 (RNF36), is a testis E3 ubiquitin-protein ligase that plays a specific role in apoptosis and may also play an important role in germ cell homeostasis during spermatogenesis. TRIM69 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438273 [Multi-domain]  Cd Length: 59  Bit Score: 51.30  E-value: 4.89e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1958660160   22 LECPICLELIKEPVSTKCDHIFCKFCMLKLLNQKKGPSQCPLCKNEITKRSL 73
Cdd:cd16611      5 LHCPLCLDFFRDPVMLSCGHNFCQSCITGFWELQAEDTTCPECRELCQYRNL 56
SPL-RING_NSE2 cd16651
SPL-RING finger found in E3 SUMO-protein ligase NSE2 and similar proteins; NSE2, also known as ...
24-74 5.00e-08

SPL-RING finger found in E3 SUMO-protein ligase NSE2 and similar proteins; NSE2, also known as MMS21 homolog (MMS21) or non-structural maintenance of chromosomes element 2 homolog (Non-SMC element 2 homolog, NSMCE2), is an autosumoylating small ubiquitin-like modifier (SUMO) ligase required for the response to DNA damage. It regulates sumoylation and nuclear-to-cytoplasmic translocation of skeletal and heart muscle-specific variant of the alpha subunit of nascent polypeptide associated complex (skNAC)-Smyd1 in myogenesis. It is also required for resisting extrinsically induced genotoxic stress. Moreover, NSE2 together with its partner proteins SMC6 and SMC5 form a tight subcomplex of the structural maintenance of chromosomes SMC5-6 complex, which includes another two subcomplexes, NSE1-NSE3-NSE4 and NSE5-NSE6. SMC6 and NSE3 are sumoylated in an NSE2-dependent manner, but SMC5 and NSE1 are not. NSE2-dependent E3 SUMO ligase activity is required for efficient DNA repair, but not for SMC5-6 complex stability. NSE2 contains a RING variant known as a Siz/PIAS (protein inhibitor of activated signal transducer and activator of transcription)-like RING (SPL-RING) finger that is likely shared by the SP-RING type SUMO E3 ligases, such as PIAS family proteins. The SPL-RING finger is a variant of the RING finger, which lacks the second, fifth, and sixth zinc-binding residues of the consensus C3H2C3-/C3HC4-type RING fingers. It harbors only one Zn binding site and is required for the sumoylating activity.


Pssm-ID: 438313 [Multi-domain]  Cd Length: 67  Bit Score: 51.49  E-value: 5.00e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958660160   24 CPICLELIKEPV-STKCDHIFCKFCMLKLLNQKKGPSQCPL--CKNEITKRSLQ 74
Cdd:cd16651      3 CPITQQLMVDPVrNKKCGHTYEKAAILQYLQSRKKKAKCPVagCRNTVSKSDLV 56
RING-HC_PEX10 cd16527
RING finger, HC subclass, found in peroxin-10 (PEX10) and similar proteins; PEX10, also known ...
24-73 5.41e-08

RING finger, HC subclass, found in peroxin-10 (PEX10) and similar proteins; PEX10, also known as peroxisome biogenesis factor 10, peroxisomal biogenesis factor 10, peroxisome assembly protein 10, or RING finger protein 69 (RNF69), is an integral peroxisomal membrane protein with two transmembrane regions and a C3HC4-type RING-HC finger within its cytoplasmically exposed C-terminus. It plays an essential role in peroxisome assembly, import of target substrates, and recycling or degradation of protein complexes and amino acids. It is an essential component of the spinal locomotor circuit, and thus its mutations may be involved in peroxisomal biogenesis disorders (PBD). Mutations in human PEX10 also result in autosomal recessive ataxia. Moreover, PEX10 functions as an E3-ubiquitin ligase with an E2, UBCH5C. It mono- or poly-ubiquitinates PEX5, a key player in peroxisomal matrix protein import, in a UBC4-dependent manner, to control PEX5 receptor recycling or degradation. It also links the E2 ubiquitin conjugating enzyme PEX4 to the protein import machinery of the peroxisome.


Pssm-ID: 438190 [Multi-domain]  Cd Length: 52  Bit Score: 50.69  E-value: 5.41e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958660160   24 CPICLELIKEPVSTKCDHIFCKFCMLKLLNQKkgpSQCPLCKNEITKRSL 73
Cdd:cd16527      3 CSLCLEERRHPTATPCGHLFCWSCITEWCNEK---PECPLCREPFQPQRL 49
RING-HC_RNF8 cd16535
RING finger, HC subclass, found in RING finger protein 8 (RNF8) and similar proteins; RNF8 is ...
22-71 6.04e-08

RING finger, HC subclass, found in RING finger protein 8 (RNF8) and similar proteins; RNF8 is a telomere-associated E3 ubiquitin-protein ligase that plays an important role in DNA double-strand break (DSB) repair via histone ubiquitination. It is localized in the nucleus and interacts with class III E2s (UBE2E2, UbcH6, and UBE2E3), but not with other E2s (UbcH5, UbcH7, UbcH10, hCdc34, and hBendless). It recruits UBC13 for lysine 63-based self polyubiquitylation. Its deficiency causes neuronal pathology and cognitive decline, and its loss results in neuron degeneration. RNF8, together with RNF168, catalyzes a series of ubiquitylation events on substrates such as H2A and H2AX, with the H2AK13/15 ubiquitylation being particularly important for recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of DSBs. RNF8 mediates the ubiquitination of gammaH2AX, and recruits 53BP1 and BRCA1 to DNA damage sites which promotes DNA damage response (DDR) and inhibits chromosomal instability. Moreover, RNF8 interacts with retinoid X receptor alpha (RXR alpha) and enhances its transcription-stimulating activity. It also regulates the rate of exit from mitosis and cytokinesis. RNF8 contains an N-terminal forkhead-associated (FHA) domain and a C-terminal C3HC4-type RING-HC finger.


Pssm-ID: 438197 [Multi-domain]  Cd Length: 64  Bit Score: 50.86  E-value: 6.04e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958660160   22 LECPICLELIKEPVSTKCDHIFCKFCMLKLLNQKKgpsQCPLCKNEITKR 71
Cdd:cd16535      2 LQCSICSELFIEAVTLNCSHSFCSYCITEWMKRKK---ECPICRKPITSK 48
RING-HC_RNF146 cd16546
RING finger, HC subclass, found in RING finger protein 146 (RNF146) and similar proteins; ...
22-68 6.69e-08

RING finger, HC subclass, found in RING finger protein 146 (RNF146) and similar proteins; RNF146, also known as dactylidin, or iduna, is a cytoplasmic E3 ubiquitin-protein ligase that is responsible for PARylation-dependent ubiquitination (PARdU). It displays neuroprotective property due to its inhibition of Parthanatos, a PAR dependent cell death, via binding with Poly(ADP-ribose) (PAR). It also modulates PAR polymerase-1 (PARP-1)-mediated oxidative cell injury in cardiac myocytes. Moreover, RNF146 mediates tankyrase-dependent degradation of axin, thereby positively regulating Wnt signaling. It also facilitates DNA repair and protects against cell death induced by DNA damaging agents or gamma-irradiation by translocating to the nucleus after cellular injury and promoting the ubiquitination and degradation of various nuclear proteins involved in DNA damage repair. Furthermore, RNF146 is implicated in neurodegenerative disease and cancer development. It regulates the development and progression of non-small cell lung cancer (NSCLC) by enhancing cell growth, invasion, and survival. RNF146 contains an N-terminal C3HC4-type RING-HC finger followed by a WWE domain with a poly(ADP-ribose) (PAR) binding motif at the tail.


Pssm-ID: 438208 [Multi-domain]  Cd Length: 50  Bit Score: 50.46  E-value: 6.69e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1958660160   22 LECPICLELIKEPVSTKCDHIFCKFCMLKLLNQKKgpsQCPLCKNEI 68
Cdd:cd16546      1 PECPICLQTCIHPVKLPCGHIFCYLCVKGVAWQSK---RCALCRQEI 44
zf-RING_UBOX pfam13445
RING-type zinc-finger; This zinc-finger is a typical RING-type of plant ubiquitin ligases.
24-62 7.39e-08

RING-type zinc-finger; This zinc-finger is a typical RING-type of plant ubiquitin ligases.


Pssm-ID: 433213 [Multi-domain]  Cd Length: 38  Bit Score: 50.09  E-value: 7.39e-08
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1958660160   24 CPICLELIKEPVsTKCDHIFCKFCMLKLLNQKKGPSQCP 62
Cdd:pfam13445    1 CPICLELFTDPV-LPCGHTFCRECLEEMSLLKGGRFKCP 38
RING-HC_TRIM39_C-IV cd16601
RING finger, HC subclass, found in tripartite motif-containing protein 39 (TRIM39) and similar ...
24-64 7.60e-08

RING finger, HC subclass, found in tripartite motif-containing protein 39 (TRIM39) and similar proteins; TRIM39, also known as RING finger protein 23 (RNF23) or testis-abundant finger protein, is an E3 ubiquitin-protein ligase that plays a role in controlling DNA damage-induced apoptosis through inhibition of the anaphase promoting complex (APC/C), a multiprotein ubiquitin ligase that controls multiple cell cycle regulators, including cyclins, geminin, and others. TRIM39 also functions as a regulator of several key processes in the proliferative cycle. It directly regulates p53 stability. It modulates cell cycle progression and DNA damage responses via stabilizing p21. Moreover, TRIM39 negatively regulates the nuclear factor kappaB (NFkappaB)-mediated signaling pathway through stabilization of Cactin, an inhibitor of NFkappaB- and Toll-like receptor (TLR)-mediated transcription, which is induced by inflammatory stimulants such as tumor necrosis factor alpha. Furthermore, TRIM39 is a MOAP-1-binding protein that can promote apoptosis signaling through stabilization of MOAP-1 via the inhibition of its poly-ubiquitination process. TRIM39 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438263 [Multi-domain]  Cd Length: 44  Bit Score: 50.18  E-value: 7.60e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1958660160   24 CPICLELIKEPVSTKCDHIFCKFCMLKLLNQKKGPSQCPLC 64
Cdd:cd16601      4 CSLCKEYLKDPVIIECGHNFCRACITRFWEELDGDFPCPQC 44
RING-HC_AtBARD1-like cd23146
RING finger, HC subclass, found in Arabidopsis thaliana BRCA1-associated RING domain protein 1 ...
22-65 8.32e-08

RING finger, HC subclass, found in Arabidopsis thaliana BRCA1-associated RING domain protein 1 (AtBARD1) and similar proteins; AtBARD1, also called protein REPRESSOR OF WUSCHEL 1, binds specifically to H3K4me3 regions of target gene (e.g. WUS and WOX5) promoters to repress their transcription via chromatin remodeling. It is required for the shoot apical meristem (SAM) organization and maintenance, by confining WUS expression to the organizing center, and for the quiescent center (QC) development in the root apical meristem (RAM), by repressing WOX5 expression in the root proximal meristem. AtBARD1 plays a role in DNA repair and in cell-cycle control. It is required for the repair of DNA double-strand breaks (DSBs), both natural and induced by genotoxic stress, by homologous recombination (HR). AtBARD1 contains a typical C3HC4-type RING-HC finger.


Pssm-ID: 438508 [Multi-domain]  Cd Length: 54  Bit Score: 50.16  E-value: 8.32e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1958660160   22 LECPICLELIKEPVSTKCDHIFCKFCmlkLLNQKKGPSQCPLCK 65
Cdd:cd23146      5 LKCPICLKLLNRPVLLPCDHIFCSSC---ITDSTKVGSDCPVCK 45
RING-HC_ScPSH1-like cd16568
RING finger, HC subclass, found in Saccharomyces cerevisiae POB3/SPT16 histone-associated ...
22-70 1.02e-07

RING finger, HC subclass, found in Saccharomyces cerevisiae POB3/SPT16 histone-associated protein 1 (ScPSH1) and similar proteins; ScPSH1 is a Cse4-specific E3 ubiquitin ligase that interacts with the kinetochore protein Pat1 and targets the degradation of budding yeast centromeric histone H3 variant, CENP-ACse4, which is essential for faithful chromosome segregation. ScPSH1 contains a C3HC4-type RING-HC finger and a DNA directed RNA polymerase domain.


Pssm-ID: 438230 [Multi-domain]  Cd Length: 54  Bit Score: 50.06  E-value: 1.02e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1958660160   22 LECPICLELIKEPVSTKCDHIFCKFCMLKLLNQKKGPSqCPLCKNEITK 70
Cdd:cd16568      5 QECIICHEYLYEPMVTTCGHTYCYTCLNTWFKSNRSLS-CPDCRTKITT 52
RING-HC_RING1 cd16739
RING finger, HC subclass, found in really interesting new gene 1 protein (RING1) and similar ...
22-86 1.03e-07

RING finger, HC subclass, found in really interesting new gene 1 protein (RING1) and similar proteins; RING1, also known as polycomb complex protein RING1, RING finger protein 1 (RNF1), or RING finger protein 1A (RING1A), was identified as a transcriptional repressor that is associated with the Polycomb group (PcG) protein complex involved in stable repression of gene activity. It is a core component of polycomb repressive complex 1 (PRC1) that functions as an E3-ubuiquitin ligase that transferring the mono-ubuiquitin mark to the C-terminal tail of Histone H2A at K118/K119. PRC1 is also capable of chromatin compaction, a function not requiring histone tails, and this activity appears important in gene silencing. RING1 interacts with multiple PcG proteins and displays tumorigenic activity. It also shows zinc-dependent DNA binding activity. Moreover, RING1 inhibits transactivation of the DNA-binding protein recombination signal binding protein-Jkappa (RBP-J) by Notch through interaction with the LIM domains of KyoT2. RING1 contains a C3HC4-type RING-HC finger.


Pssm-ID: 438397 [Multi-domain]  Cd Length: 70  Bit Score: 50.46  E-value: 1.03e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958660160   22 LECPICLELIKEPVSTK-CDHIFCKFCMLKLLnqKKGPSQCPLCKNE-ITKRSLQGSARFSQLVEEL 86
Cdd:cd16739      4 LMCPICLDMLKNTMTTKeCLHRFCSDCIVTAL--RSGNKECPTCRKKlVSKRSLRPDPNFDALISKI 68
RING-HC_TRIM4_C-IV cd16590
RING finger, HC subclass, found in tripartite motif-containing protein TRIM4 and similar ...
18-66 1.06e-07

RING finger, HC subclass, found in tripartite motif-containing protein TRIM4 and similar proteins; TRIM4 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox2, and a coiled coil region, as well as a SPRY/B30.2 domain positioned C-terminal to the RBCC domain. TRIM4, also known as RING finger protein 87 (RNF87), is a cytoplasmic E3 ubiquitin-protein ligase that has recently evolved and is present only in higher mammals. It transiently interacts with mitochondria, induces mitochondrial aggregation and sensitizes the cells to hydrogen peroxide (H2O2) induced death. Its interaction with peroxiredoxin 1 (PRX1) is critical for the regulation of H2O2 induced cell death. Moreover, TRIM4 functions as a positive regulator of RIG-I-mediated type I interferon induction. It regulates the K63-linked ubiquitination of RIG-1 and assembly of antiviral signaling complex at the mitochondria.


Pssm-ID: 438252 [Multi-domain]  Cd Length: 61  Bit Score: 50.42  E-value: 1.06e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1958660160   18 MQKILECPICLELIKEPVSTKCDHIFCKFCMLKLLNQKKGPSQCPLCKN 66
Cdd:cd16590      3 IQEELTCPICLDYFQDPVSIECGHNFCRGCLHRNWAPGGGPFPCPECRH 51
RING-HC_RNF170 cd16553
RING finger, HC subclass, found in RING finger protein 170 (RNF170) and similar proteins; ...
23-69 1.07e-07

RING finger, HC subclass, found in RING finger protein 170 (RNF170) and similar proteins; RNF170, also known as putative LAG1-interacting protein, is an endoplasmic reticulum (ER) membrane-bound E3 ubiquitin-protein ligase that mediates ubiquitination-dependent degradation of type-I inositol 1,4,5-trisphosphate (IP3) receptors (ITPR1) via the endoplasmic-reticulum-associated protein degradation (ERAD) pathway. A point mutation (arginine to cysteine at position 199) in the RNF170 gene is linked with autosomal-dominant sensory ataxia (ADSA), a disease characterized by neurodegeneration in the posterior columns of the spinal cord. RNF170 contains a C3HC4-type RING-HC finger.


Pssm-ID: 438215 [Multi-domain]  Cd Length: 57  Bit Score: 49.98  E-value: 1.07e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1958660160   23 ECPICLELIKEPVSTKCDHIFCKFCMLKLLNQKK--GPSQCPLCKNEIT 69
Cdd:cd16553      3 ECPICLQDARFPVETNCGHLFCGPCIITYWRHGSwlGAVSCPVCRQTVT 51
RING-HC_TRIM50_like_C-IV cd16605
RING finger, HC subclass, found in tripartite motif-containing protein TRIM50, TRIM73, TRIM74 ...
22-65 1.11e-07

RING finger, HC subclass, found in tripartite motif-containing protein TRIM50, TRIM73, TRIM74 and similar proteins; TRIM50 is a stomach-specific E3 ubiquitin-protein ligase, encoded by the Williams-Beuren syndrome (WBS) TRIM50 gene, which regulates vesicular trafficking for acid secretion in gastric parietal cells. It colocalizes, interacts with, and increases the level of p62/SQSTM1, a multifunctional adaptor protein implicated in various cellular processes including the autophagy clearance of polyubiquitinated protein aggregates. It also promotes the formation and clearance of aggresome-associated polyubiquitinated proteins through the interaction with histone deacetylase 6 (HDAC6), a tubulin specific deacetylase that regulates microtubule-dependent aggresome formation. TRIM50 can be acetylated by PCAF and p300. TRIM50 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. This subfamily also includes two paralogs of TRIM50, tripartite motif-containing protein 73 (TRIM73), also known as tripartite motif-containing protein 50B (TRIM50B), and tripartite motif-containing protein 74 (TRIM74), also known as tripartite motif-containing protein 50C (TRIM50C), both of which are WBS-related genes encoding proteins that may also act as E3 ligases. In contrast with TRIM50, TRIM73 and TRIM74 belong to the C-V subclass of TRIM family of proteins that are defined by N-terminal RBCC domains only.


Pssm-ID: 438267 [Multi-domain]  Cd Length: 45  Bit Score: 49.75  E-value: 1.11e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1958660160   22 LECPICLELIKEPVSTKCDHIFCKFCMLKLLNQKKGPSQCPLCK 65
Cdd:cd16605      1 LLCPICLEVFKEPLMLQCGHSYCKSCLVSLSGELDGQLLCPVCR 44
mRING-HC-C3HC3D_TRAF6 cd16643
Modified RING finger, HC subclass (C3HC3D-type), found in tumor necrosis factor (TNF) ...
22-62 1.26e-07

Modified RING finger, HC subclass (C3HC3D-type), found in tumor necrosis factor (TNF) receptor-associated factor 6 (TRAF6) and similar proteins; TRAF6, also known as interleukin-1 signal transducer or RING finger protein 85 (RNF85), is a cytoplasmic adapter protein that mediates signals induced by the tumor necrosis factor receptor (TNFR) superfamily and Toll-like receptor (TLR)/interleukin-1 receptor (IL-1R) family. It functions as a mediator involved in the activation of mitogen-activated protein kinase (MAPK), phosphoinositide 3-kinase (PI3K), and interferon regulatory factor pathways, as well as in IL-1R-mediated activation of NF-kappaB. TRAF6 is also an oncogene that plays a vital role in K-RAS-mediated oncogenesis. TRAF6 contains an N-terminal domain with a modified C3HC3D-type RING-HC finger and several zinc fingers, and a C-terminal TRAF domain that comprises a coiled coil domain and a conserved TRAF-C domain.


Pssm-ID: 438305 [Multi-domain]  Cd Length: 58  Bit Score: 50.07  E-value: 1.26e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1958660160   22 LECPICLELIKEPVSTKCDHIFCKFCMLKLLNQKKgpSQCP 62
Cdd:cd16643      2 YECPICLMALREPVQTPCGHRFCKACILKSIREAG--HKCP 40
RING-HC_TRY3-like cd23137
RING finger, HC subclass, found in Candida albicans transcriptional regulator of yeast form ...
23-67 1.33e-07

RING finger, HC subclass, found in Candida albicans transcriptional regulator of yeast form adherence 3 (TRY3) and similar proteins; TRY3 acts as a transcription factor required for yeast cell adherence to silicone substrate. It contains a typical C3HC4-type RING-HC finger.


Pssm-ID: 438499 [Multi-domain]  Cd Length: 53  Bit Score: 49.77  E-value: 1.33e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1958660160   23 ECPICLELIKEPVSTKCDHIFCKFCMLKLlnQKKGPSQCPLCKNE 67
Cdd:cd23137      4 ACPICMNVAWKPVRLECSHVFCLRCLVKA--QKQKKDNCPLCRAK 46
RING-HC_TRIM25_C-IV cd16597
RING finger, HC subclass, found in tripartite motif-containing protein TRIM25 and similar ...
22-85 1.42e-07

RING finger, HC subclass, found in tripartite motif-containing protein TRIM25 and similar proteins; TRIM25, also known as estrogen-responsive finger protein (EFP), RING finger protein 147 (RNF147), or RING-type E3 ubiquitin transferase, is an E3 ubiquitin/ISG15 ligase that is induced by estrogen and is therefore particularly abundant in placenta and uterus. TRIM25 regulates various cellular processes through E3 ubiquitin ligase activity, transferring ubiquitin and ISG15 to target proteins. It mediates K63-linked polyubiquitination of retinoic acid inducible gene I (RIG-I) that is crucial for downstream antiviral interferon signaling. It is also required for melanoma differentiation-associated gene 5 (MDA5) and mitochondrial antiviral signaling (MAVS, also known as IPS-1, VISA, Cardiff) mediated activation of nuclear factor-kappaB (NF-kappaB) and interferon production. Upon UV irradiation, TRIM25 interacts with mono-ubiquitinated PCNA and promotes its ISG15 modification (ISGylation), suggesting a crucial role in termination of error-prone translesion DNA synthesis. TRIM25 also functions as a novel regulator of p53 and Mdm2. It enhances p53 and Mdm2 abundance by inhibiting their ubiquitination and degradation in 26S proteasomes. Meanwhile, it inhibits p53's transcriptional activity and dampens the response to DNA damage, and is essential for medaka development and this dependence is rescued by silencing of p53. Moreover, TRIM25 is involved in the host cellular innate immune response against retroviral infection. It interferes with the late stage of feline leukemia virus (FeLV) replication. Furthermore, TRIM25 acts as an oncogene in gastric cancer. Its blockade by RNA interference inhibits migration and invasion of gastric cancer cells through transforming growth factor-beta (TGF-beta) signaling, suggesting it presents a novel target for the detection and treatment of gastric cancer. In addition, TRIM25 acts as an RNA-specific activator for Lin28a/TuT4-mediated uridylation. TRIM25 belongs to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438259 [Multi-domain]  Cd Length: 71  Bit Score: 50.00  E-value: 1.42e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958660160   22 LECPICLELIKEPVSTKCDHIFCKFCMLK-LLNQKKGPSQCPLCKNEITKR-SLQGSARFSQLVEE 85
Cdd:cd16597      6 LTCSICLELFKDPVTLPCGHNFCGVCIEKtWDSQHGSEYSCPQCRATFPRRpELHKNTVLRNIVEQ 71
RING-HC_RING1-like cd16531
RING finger, HC subclass, found in really interesting new gene proteins RING1, RING2 and ...
21-83 1.54e-07

RING finger, HC subclass, found in really interesting new gene proteins RING1, RING2 and similar proteins; RING1, also known as polycomb complex protein RING1, RING finger protein 1 (RNF1), or RING finger protein 1A (RING1A), is a transcriptional repressor that is associated with the Polycomb group (PcG) protein complex involved in stable repression of gene activity. RING2, also known as huntingtin-interacting protein 2-interacting protein 3, HIP2-interacting protein 3, protein DinG, RING finger protein 1B (RING1B), RING finger protein 2 (RNF2), or RING finger protein BAP-1, is an E3 ubiquitin-protein ligase that interacts with both nucleosomal DNA and an acidic patch on histone H4 to achieve the specific monoubiquitination of K119 on histone H2A (H2AK119ub), thereby playing a central role in histone code and gene regulation. Both RING1 and RING2 are core components of polycomb repressive complex 1 (PRC1) that functions as an E3-ubuiquitin ligase transferring the mono-ubuiquitin mark to the C-terminal tail of Histone H2A at K118/K119. PRC1 is also capable of chromatin compaction, a function not requiring histone tails, and this activity appears important in gene silencing. RING2 acts as the main E3 ubiquitin ligase on histone H2A of the PRC1 complex, while RING1 may rather act as a modulator of RNF2/RING2 activity. Members of this family contain a C3HC4-type RING-HC finger.


Pssm-ID: 438193 [Multi-domain]  Cd Length: 66  Bit Score: 49.96  E-value: 1.54e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958660160   21 ILECPICLELIKEPVSTK-CDHIFCKFCMLKLLnqKKGPSQCPLCKNEI-TKRSLQGSARFSQLV 83
Cdd:cd16531      1 ELMCPICLGIIKNTMTVKeCLHRFCAECIEKAL--RLGNKECPTCRKHLpSRRSLRPDPNFDALI 63
RING-HC_RNF180 cd16554
RING finger, HC subclass, found in RING finger protein 180 (RNF180) and similar proteins; ...
22-70 2.18e-07

RING finger, HC subclass, found in RING finger protein 180 (RNF180) and similar proteins; RNF180, also known as Rines, is a membrane-bound E3 ubiquitin-protein ligase well conserved among vertebrates. It is a critical regulator of the monoaminergic system, as well as emotional and social behavior. It interacts with brain monoamine oxidase A (MAO-A) and targets it for ubiquitination and degradation. It also functions as a novel tumor suppressor in gastric carcinogenesis. The hypermethylated CpG site count of the RNF180 DNA promoter can be used to predict survival of gastric cancer. RNF180 contains a novel conserved dual specificity protein phosphatase Rines conserved (DSPRC) domain, a basic coiled-coil domain, a C3HC4-type RING-HC finger, and a C-terminal hydrophobic region that is predicted to be a transmembrane domain.


Pssm-ID: 438216 [Multi-domain]  Cd Length: 59  Bit Score: 49.23  E-value: 2.18e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958660160   22 LECPICLELIKEP-VSTKCDHIFCKFCMLKLLNQKKGPSQCPLCKNEITK 70
Cdd:cd16554      3 LTCPVCLDLYYDPyMCYPCGHIFCEPCLRQLAKSSPKNTPCPLCRTTIRR 52
RING-HC_RNF114 cd16540
RING finger, HC subclass, found in RING finger protein 114 (RNF114) and similar proteins; ...
24-65 2.80e-07

RING finger, HC subclass, found in RING finger protein 114 (RNF114) and similar proteins; RNF114, also known as zinc finger protein 228 (ZNF228) or zinc finger protein 313 (ZNF313), is a p21(WAF1)-targeting ubiquitin E3 ligase that interacts with X-linked inhibitor of apoptosis (XIAP)-associated factor 1 (XAF1) and may play a role in p53-mediated cell-fate decisions. It is involved in the immune response to double-stranded RNA in disease pathogenesis. Moreover, RNF114 interacts with A20 and modulates its ubiquitylation. It negatively regulates nuclear factor-kappaB (NF-kappaB)-dependent transcription and positively regulates T-cell activation. RNF114 may play a putative role in the regulation of immune responses, since it corresponds to a novel psoriasis susceptibility gene, ZNF313. RNF114, together with three closely related proteins: RNF125, RNF138 and RNF166, forms a novel family of ubiquitin ligases with a C3HC4-type RING-HC finger, a C2HC-, and two C2H2-type zinc fingers, as well as a ubiquitin interacting motif (UIM).


Pssm-ID: 438202 [Multi-domain]  Cd Length: 46  Bit Score: 48.60  E-value: 2.80e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1958660160   24 CPICLELIKEPVSTKCDHIFCKFCMLKLLNQKKgpSQCPLCK 65
Cdd:cd16540      4 CPVCLEIFETPVRVPCGHVFCNACLQECLKPKK--PVCAVCR 43
RING-HC_RNF5 cd16743
RING finger, HC subclass, found in RING finger protein 5 (RNF5) and similar proteins; RNF5, ...
23-70 3.60e-07

RING finger, HC subclass, found in RING finger protein 5 (RNF5) and similar proteins; RNF5, also known as protein G16 or Ram1, is an E3 ubiquitin-protein ligase anchored to the outer membrane of the endoplasmic reticulum (ER). It acts at early stages of cystic fibrosis (CF) transmembrane conductance regulator (CFTR) biosynthesis and functions as a target for therapeutic modalities to antagonize mutant CFTR proteins in CF patients carrying the F508del allele. It also regulates the turnover of specific G protein-coupled receptors by ubiquitinating JNK-associated membrane protein (JAMP) and preventing proteasome recruitment. RNF5 limits basal levels of autophagy and influences susceptibility to bacterial infection through the regulation of ATG4B stability. It is also involved in the degradation of Pendrin, a transmembrane chloride/anion exchanger highly expressed in thyroid, kidney, and inner ear. RNF5 plays an important role in cell adhesion and migration. It can modulate cell migration by ubiquitinating paxillin. Furthermore, RNF5 interacts with virus-induced signaling adaptor (VISA) at mitochondria in a viral infection-dependent manner, and further targets VISA at K362 and K461 for K48-linked ubiquitination and degradation after viral infection. It also negatively regulates virus-triggered signaling by targeting MITA, also known as STING, for ubiquitination and degradation at the mitochondria. In addition, RNF5 determines breast cancer response to ER stress-inducing chemotherapies through the regulation of the L-glutamine carrier proteins SLC1A5 and SLC38A2 (SLC1A5/38A2). It also has been implicated in muscle organization and in recognition and processing of misfolded proteins. RNF5 contains a C3HC4-type RING-HC finger.


Pssm-ID: 438401 [Multi-domain]  Cd Length: 54  Bit Score: 48.34  E-value: 3.60e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1958660160   23 ECPICLELIKEPVSTKCDHIFCKFCMLKLLNQKKGPSQCPLCKNEITK 70
Cdd:cd16743      2 ECNICLETARDAVVSLCGHLFCWPCLHQWLETRPERQECPVCKAGISR 49
vRING-HC-C4C4_RBBP6 cd16620
Variant RING finger, HC subclass (C4C4-type), found in retinoblastoma-binding protein 6 (RBBP6) ...
22-68 4.00e-07

Variant RING finger, HC subclass (C4C4-type), found in retinoblastoma-binding protein 6 (RBBP6) and similar proteins; RBBP6, also known as proliferation potential-related protein, protein P2P-R, retinoblastoma-binding Q protein 1 (RBQ-1), or p53-associated cellular protein of testis (PACT), is a nuclear E3 ubiquitin-protein ligase involved in multiple processes, such as the control of gene expression, mitosis, cell differentiation, and cell apoptosis. It plays a role in both promoting and inhibiting apoptosis in many human cancers, including esophageal, lung, hepatocellular, and colon cancers, familial myeloproliferative neoplasms, as well as in human immunodeficiency virus-associated nephropathy (HIVAN). It functions as an Rb- and p53-binding protein that plays an important role in chaperone-mediated ubiquitination and possibly in protein quality control. It acts as a scaffold protein to promote the assembly of the p53/TP53-MDM2 complex, resulting in an increase of MDM2-mediated ubiquitination and degradation of p53/TP53, and leading to both apoptosis and cell growth. It is also a double-stranded RNA-binding protein that plays a role in mRNA processing by regulating the human polyadenylation machinery and modulating expression of mRNAs with AU-rich 3' untranslated regions (UTRs). Moreover, RBBP6 ubiquitinates and destabilizes the transcriptional repressor ZBTB38 that negatively regulates transcription and levels of the MCM10 replication factor on chromatin. Furthermore, RBBP6 is involved in tunicamycin-induced apoptosis by mediating protein kinase (PKR) activation. RBBP6 contains an N-terminal ubiquitin-like domain and a C4C4-type RING finger, whose overall folding is similar to that of the typical C3HC4-type RING-HC finger. RBBP6 interacts with chaperones Hsp70 and Hsp40 through its N-terminal ubiquitin-like domain. It promotes the ubiquitination of p53 by Hdm2 in an E4-like manner through its RING finger. It also interacts directly with the pro-proliferative transcription factor Y-box-binding protein-1 (YB-1) via its RING finger.


Pssm-ID: 438282 [Multi-domain]  Cd Length: 55  Bit Score: 48.56  E-value: 4.00e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1958660160   22 LECPICLELIKEPVSTK-CDHIFCKFCMLKLLNQKKgpSQCPLCKNEI 68
Cdd:cd16620      4 LKCPICKDLMKDAVLTPcCGNSFCDECIRTALLEED--FTCPTCKEPD 49
RING-HC_RAD18 cd16529
RING finger, HC subclass, found in postreplication repair protein RAD18 and similar proteins; ...
22-73 6.14e-07

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: 47.68  E-value: 6.14e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958660160   22 LECPICLELIK-EPVSTKCDHIFCKFCMLKLLNQKkgpSQCPLCKNEITKRSL 73
Cdd:cd16529      5 LRCPICFEYFNtAMMITQCSHNYCSLCIRRFLSYK---TQCPTCRAAVTESDL 54
RING-HC_TRIM35_C-IV cd16599
RING finger, HC subclass, found in tripartite motif-containing protein 35 (TRIM35) and similar ...
22-84 6.26e-07

RING finger, HC subclass, found in tripartite motif-containing protein 35 (TRIM35) and similar proteins; TRIM35, also known as hemopoietic lineage switch protein 5 (HLS5), is a putative hepatocellular carcinoma (HCC) suppressor that inhibits phosphorylation of pyruvate kinase isoform M2 (PKM2), which is involved in aerobic glycolysis of cancer cells and further suppresses the Warburg effect and tumorigenicity in HCC. It also negatively regulates Toll-like receptor 7 (TLR7)- and TLR9-mediated type I interferon production by suppressing the stability of interferon regulatory factor 7 (IRF7). Moreover, TRIM35 regulates erythroid differentiation by modulating globin transcription factor 1 (GATA-1) activity. TRIM35 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438261 [Multi-domain]  Cd Length: 66  Bit Score: 48.23  E-value: 6.26e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958660160   22 LECPICLELIKEPVSTKCDHIFCKFCmLKLLNQKKGPSQCPLCKNEITKRSLQGSARFSQLVE 84
Cdd:cd16599      5 LLCPICYEPFREAVTLRCGHNFCKGC-VSRSWERQPRAPCPVCKEASSSDDLRTNHTLNNLVE 66
RING-HC_TRIM41-like_C-IV cd16602
RING finger, HC subclass, found in tripartite motif-containing proteins TRIM41, TRIM52 and ...
24-74 7.26e-07

RING finger, HC subclass, found in tripartite motif-containing proteins TRIM41, TRIM52 and similar proteins; TRIM41 and TRIM52, two closely related tripartite motif-containing proteins, have dramatically expanded RING domains compared with the rest of the TRIM family proteins. TRIM41 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. In contrast, TRIM52 lacks the putative viral recognition SPRY/B30.2 domain, and thus has been classified to the C-V subclass of the TRIM family that contains only RBCC domains. TRIM41, also known as RING finger-interacting protein with C kinase (RINCK), is an E3 ubiquitin-protein ligase that promotes the ubiquitination of protein kinase C (PKC) isozymes in cells. It specifically recognizes the C1 domain of PKC isozymes. It controls the amplitude of PKC signaling by controlling the amount of PKC in the cell. TRIM52, also known as RING finger protein 102 (RNF102), is encoded by a novel, noncanonical antiviral TRIM52 gene in primate genomes with unique specificity determined by the rapidly evolving RING domain.


Pssm-ID: 438264 [Multi-domain]  Cd Length: 53  Bit Score: 47.61  E-value: 7.26e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1958660160   24 CPICLELIKEPVSTKCDHIFCKFCMLKLLNqkkgpSQCPLCKNEITKRSLQ 74
Cdd:cd16602      6 CAICLDYFKDPVSIGCGHNFCRVCVTQLWG-----FTCPQCRKSFPRRSFR 51
RING-HC_TRIM65_C-IV cd16609
RING finger, HC subclass, found in tripartite motif-containing protein TRIM65 and similar ...
22-65 7.60e-07

RING finger, HC subclass, found in tripartite motif-containing protein TRIM65 and similar proteins; TRIM65 is an E3 ubiquitin-protein ligase that interacts with the innate immune receptor MDA5, enhancing its ability to stimulate interferon-beta signaling. It functions as a potential oncogenic protein that negatively regulates p53 through ubiquitination, providing insight into the development of novel approaches targeting TRIM65 for non-small cell lung carcinoma (NSCLC) treatment, and also overcoming chemotherapy resistance. Moreover, TRIM65 negatively regulates microRNA-driven suppression of mRNA translation by targeting TNRC6 proteins for ubiquitination and degradation. TRIM65 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438271 [Multi-domain]  Cd Length: 58  Bit Score: 47.75  E-value: 7.60e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1958660160   22 LECPICLELIKEPVSTKCDHIFCKFCMLKLLNQK-KGPSQCPLCK 65
Cdd:cd16609      4 LTCSICLGLYQDPVTLPCQHSFCRACIEDHWRQKdEGSFSCPECR 48
RING-HC_TRIM26_C-IV cd16598
RING finger, HC subclass, found in tripartite motif-containing protein 26 (TRIM26) and similar ...
18-74 8.07e-07

RING finger, HC subclass, found in tripartite motif-containing protein 26 (TRIM26) and similar proteins; TRIM26, also known as acid finger protein (AFP), RING finger protein 95 (RNF95), or zinc finger protein 173 (ZNF173), is an E3 ubiquitin-protein ligase that negatively regulates interferon-beta production and antiviral response through polyubiquitination and degradation of nuclear transcription factor IRF3. It functions as an important regulator for RNA virus-triggered innate immune response by bridging TBK1 to NEMO (NF-kappaB essential modulator, also known as IKKgamma) and mediating TBK1 activation. It also acts as a novel tumor suppressor of hepatocellular carcinoma by regulating cancer cell proliferation, colony forming ability, migration, and invasion. TRIM26 belongs the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, a B-box, and two coiled coil domains, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438260 [Multi-domain]  Cd Length: 64  Bit Score: 47.85  E-value: 8.07e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958660160   18 MQKILECPICLELIKEPVSTKCDHIFCKFCMLKLLNQKKGPSQ--CPLCKNEITKRSLQ 74
Cdd:cd16598      1 LEEEVTCSICLDYLRDPVTIDCGHNFCRSCITDYCPISGGHERpvCPLCRKPFKKENIR 59
RING-HC_LONFs_rpt1 cd16513
first RING finger, HC subclass, found in the LON peptidase N-terminal domain and RING finger ...
22-71 8.21e-07

first RING finger, HC subclass, found in the LON peptidase N-terminal domain and RING finger protein family; The LON peptidase N-terminal domain and RING finger protein family includes LONRF1 (also known as RING finger protein 191 or RNF191), LONRF2 (also known as RING finger protein 192, RNF192, or neuroblastoma apoptosis-related protease), LONRF3 (also known as RING finger protein 127 or RNF127), which are characterized by containing two C3HC4-type RING-HC fingers, four tetratricopeptide (TPR) repeats, and an ATP-dependent protease La (LON) substrate-binding domain at the C-terminus. Their biological functions remain unclear. This model corresponds to the first RING-HC finger.


Pssm-ID: 438176 [Multi-domain]  Cd Length: 47  Bit Score: 47.30  E-value: 8.21e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958660160   22 LECPICLELIKEPVSTKCDHIFCKFCMlkllnQKKGPSQCPLCKNEITKR 71
Cdd:cd16513      3 LSCPLCRGLLFEPVTLPCGHTFCKRCL-----ERDPSSRCRLCRLKLSPG 47
RING-HC_TRIM31_C-V cd16582
RING finger, HC subclass, found in tripartite motif-containing protein 31 (TRIM31) and similar ...
24-64 8.85e-07

RING finger, HC subclass, found in tripartite motif-containing protein 31 (TRIM31) and similar proteins; TRIM31 is an E3 ubiquitin-protein ligase that primarily localizes to the cytoplasm, but is also associated with the mitochondria. It can negatively regulate cell proliferation and may be a potential biomarker of gastric cancer as it is overexpressed from the early stage of gastric carcinogenesis. TRIM31 is downregulated in non-small cell lung cancer and serves as a potential tumor suppressor. It interacts with p52 (Shc) and inhibits Src-induced anchorage-independent growth. TRIM31 belongs to the C-V subclass of the TRIM (tripartite motif) family of proteins that are defined by an N-terminal RBCC (RING, Bbox, and coiled coil) domain, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as an uncharacterized region positioned C-terminal to the RBCC domain.


Pssm-ID: 438244 [Multi-domain]  Cd Length: 44  Bit Score: 47.13  E-value: 8.85e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1958660160   24 CPICLELIKEPVSTKCDHIFCKFCMLKLLNQKKGPSQCPLC 64
Cdd:cd16582      4 CPICLDILQKPVTIDCGHNFCLQCITQIGETSCGFFKCPLC 44
RING-HC_EHV1-like cd23130
RING finger, HC subclass, found in Equid alphaherpesvirus 1 (Equine herpesvirus 1/EHV-1) ...
23-69 1.20e-06

RING finger, HC subclass, found in Equid alphaherpesvirus 1 (Equine herpesvirus 1/EHV-1) regulatory protein and similar proteins; EHV-1 regulatory protein belongs to the Vmw110 (IPC0) protein family. It contains a typical C3HC4-type RING-HC finger and binds zinc stably.


Pssm-ID: 438492 [Multi-domain]  Cd Length: 51  Bit Score: 46.96  E-value: 1.20e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1958660160   23 ECPICLELIK-EPVSTKCDHIFCKFCMLKLLNQKkgpSQCPLCKNEIT 69
Cdd:cd23130      2 VCPICLDDPEdEAITLPCLHQFCYTCILRWLQTS---PTCPLCKTPVT 46
RING-HC_LNX4 cd16719
RING finger, HC subclass, found in ligand of numb protein X 4 (LNX4); LNX4, also known as PDZ ...
22-68 1.26e-06

RING finger, HC subclass, found in ligand of numb protein X 4 (LNX4); LNX4, also known as PDZ domain-containing RING finger protein 4 (PDZRN4), or SEMACAP3-like protein (SEMCAP3L), is an E3 ubiquitin-protein ligase responsible for the ubiquitination and degradation of Numb, a component of the Notch signaling pathway that functions in the specification of cell fates during development and is known to control cell numbers during neurogenesis in vertebrates. LNX4 contains an N-terminal C3HC4-type RING-HC finger, two PDZ domains, and a C-terminal LNX3 homology (LNX3H) domain.


Pssm-ID: 438379 [Multi-domain]  Cd Length: 53  Bit Score: 46.84  E-value: 1.26e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1958660160   22 LECPICLELIKEPVSTKCDHIFCKFCMLK-LLNQKKGPSQC-PLCKNEI 68
Cdd:cd16719      5 LKCKLCGKVLEEPLSTPCGHVFCAGCLLPwAVQRRLCPLQCqPIAAKEL 53
RING-HC_RFPL4B cd16623
RING finger, HC subclass, found in Ret finger protein-like 4B (RFPL4B) and similar proteins; ...
18-70 1.26e-06

RING finger, HC subclass, found in Ret finger protein-like 4B (RFPL4B) and similar proteins; RFPL4B, also called RING finger protein 211 (RNF211), is an uncharacterized RING finger protein containing a typical C3HC4-type RING-HC finger.


Pssm-ID: 438285 [Multi-domain]  Cd Length: 63  Bit Score: 47.12  E-value: 1.26e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958660160   18 MQKILE----CPICLELIKEPVSTKCDHIFCKFCMLKLLNQKKGP-SQCPLCKNEITK 70
Cdd:cd16623      1 MANRLEmeatCPICLDFFSHPISLSCAHIFCFDCIQKWMTKREDSiLTCPLCRKEQKK 58
RING-HC_TRIM43-like_C-IV cd16603
RING finger, HC subclass, found in tripartite motif-containing proteins TRIM43, TRIM48, TRIM49, ...
19-74 1.28e-06

RING finger, HC subclass, found in tripartite motif-containing proteins TRIM43, TRIM48, TRIM49, TRIM51, TRIM64 and similar proteins; The family includes a group of closely related uncharacterized tripartite motif-containing proteins, TRIM43, TRIM43B, TRIM48/RNF101, TRIM49/RNF18, TRIM49B, TRIM49C/TRIM49L2, TRIM49D/TRIM49L, TRIM51/SPRYD5, TRIM64, TRIM64B, and TRIM64C, whose biological function remain unclear. TRIM49, also known as testis-specific RING-finger protein, has moderate similarity with SS-A/Ro52 antigen, suggesting it may be one of the target proteins of autoantibodies in the sera of patients with these autoimmune disorders. All family members belong to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains as well as a SPRY/B30.2 domain positioned C-terminal to the RBCC domain. In RBCC region, they all have a C3HC4-type RING-HC finger.


Pssm-ID: 438265 [Multi-domain]  Cd Length: 59  Bit Score: 47.09  E-value: 1.28e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958660160   19 QKILECPICLELIKEPVSTKCDHIFCKFCMlkLLNQKKGPS--QCPLCKNEITKRSLQ 74
Cdd:cd16603      2 QRELTCPICMNYFIDPVTIDCGHSFCRPCL--YLNWQDIPFlaQCPECRKTTEQRNLK 57
RING-HC_RNF168 cd16550
RING finger, HC subclass, found in RING finger protein 168 (RNF168) and similar proteins; ...
24-69 1.60e-06

RING finger, HC subclass, found in RING finger protein 168 (RNF168) and similar proteins; RNF168 is an E3 ubiquitin-protein ligase that promotes noncanonical K27 ubiquitination to signal DNA damage. It, together with RNF8, functions as a DNA damage response (DDR) factor that promotes a series of ubiquitylation events on substrates, such as H2A and H2AX with H2AK13/15 ubiquitylation, facilitates recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of double-strand breaks (DSBs), and inhibits homologous recombination (HR) in cells deficient in the tumor suppressor BRCA1. RNF168 also promotes H2A neddylation, which antagonizes ubiquitylation of H2A and regulates DNA damage repair. Moreover, RNF168 forms a functional complex with RAD6A or RAD6B during the DNA damage response. RNF168 contains an N-terminal C3HC4-type RING-HC finger that catalyzes H2A-K15ub and interacts with H2A, and two MIU (motif interacting with ubiquitin) domains responsible for the interaction with K63 linked poly-ubiquitin.


Pssm-ID: 438212 [Multi-domain]  Cd Length: 48  Bit Score: 46.60  E-value: 1.60e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1958660160   24 CPICLELIKEPVSTKCDHIFCKFCMLKllNQKKGPSQCPLCKNEIT 69
Cdd:cd16550      3 CPICLEILVEPVTLPCNHTLCMPCFQS--TVEKASLCCPLCRLRIS 46
zf-RING_2 pfam13639
Ring finger domain;
23-65 1.76e-06

Ring finger domain;


Pssm-ID: 433370 [Multi-domain]  Cd Length: 44  Bit Score: 46.25  E-value: 1.76e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1958660160   23 ECPICLELIKEP---VSTKCDHIFCKFCMLKLLNQKkgpSQCPLCK 65
Cdd:pfam13639    2 ECPICLEEFEEGdkvVVLPCGHHFHRECLDKWLRSS---NTCPLCR 44
RING-HC_RNF39 cd16592
RING finger, HC subclass, found in RING finger protein 39 (RNF39) and similar proteins; RNF39, ...
24-65 1.83e-06

RING finger, HC subclass, found in RING finger protein 39 (RNF39) and similar proteins; RNF39, also called protein HZFw, may play a role in prolonged long term-potentiation (LTP) maintenance. It is involved in the etiology of Behcet's disease (BD). It may also be involved in HIV-1 replication. RNF39 acts as an E3 ubiquitin ligase that inhibits retinoic acid-inducible gene-I (RIG-I)-like receptor (RLR) pathways by mediating K48-linked ubiquitination and proteasomal degradation of DDX3X (DEAD-box RNA helicase 3, X-linked). RNF39 contains a typical C3HC4-type RING-HC finger.


Pssm-ID: 438254 [Multi-domain]  Cd Length: 58  Bit Score: 46.67  E-value: 1.83e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1958660160   24 CPICLELIKEPVSTKCDHIFCKFCMLKLLNQKKGPSQ------CPLCK 65
Cdd:cd16592      7 CPICLGYFKDPVILDCEHSFCRACIARHWGQEAMEGNgaegvfCPQCG 54
RING-HC_RING2 cd16740
RING finger, HC subclass, found in really interesting new gene 2 protein (RING2) and similar ...
17-86 1.90e-06

RING finger, HC subclass, found in really interesting new gene 2 protein (RING2) and similar proteins; RING2, also known as huntingtin-interacting protein 2-interacting protein 3, HIP2-interacting protein 3, protein DinG, RING finger protein 1B (RING1B), RING finger protein 2 (RNF2), or RING finger protein BAP-1, is an E3 ubiquitin-protein ligase that interacts with both nucleosomal DNA and an acidic patch on histone H4 to achieve the specific monoubiquitination of K119 on histone H2A (H2AK119ub), thereby playing a central role in histone code and gene regulation. RING2 is a core component of polycomb repressive complex 1 (PRC1) that functions as an E3-ubuiquitin ligase transferring the mono-ubuiquitin mark to the C-terminal tail of Histone H2A at K118/K119. PRC1 is also capable of chromatin compaction, a function not requiring histone tails, and this activity appears important in gene silencing. The enzymatic activity of RING2 is enhanced by the interaction with BMI1/PCGF4, and it is dispensable for early embryonic development and much of the gene repression activity of PRC1. Moreover, RING2 plays a key role in terminating neural precursor cell (NPC)-mediated production of subcerebral projection neurons (SCPNs) during neocortical development. It also plays a critical role in nonhomologous end-joining (NHEJ)-mediated end-to-end chromosome fusions. Furthermore, RING2 is essential for expansion of hepatic stem/progenitor cells. It promotes hepatic stem/progenitor cell expansion through simultaneous suppression of cyclin-dependent kinase inhibitors (CDKIs) Cdkn1a and Cdkn2a, known negative regulators of cell proliferation. RING2 also negatively regulates p53 expression through directly binding with both p53 and MDM2 and promoting MDM2-mediated p53 ubiquitination in selective cancer cell types to stimulate tumor development. RING2 contains a C3HC4-type RING-HC finger.


Pssm-ID: 438398 [Multi-domain]  Cd Length: 77  Bit Score: 47.39  E-value: 1.90e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958660160   17 AMQKILECPICLELIKEPVSTK-CDHIFCKFCMLKLLnqKKGPSQCPLCKNE-ITKRSLQGSARFSQLVEEL 86
Cdd:cd16740      8 SLHSELMCPICLDMLKNTMTTKeCLHRFCADCIITAL--RSGNKECPTCRKKlVSKRSLRPDPNFDALISKI 77
RING-HC_RNF125 cd16542
RING finger, HC subclass, found in RING finger protein 125 (RNF125); RNF125, also known as ...
22-65 2.19e-06

RING finger, HC subclass, found in RING finger protein 125 (RNF125); RNF125, also known as T-cell RING activation protein 1 (TRAC-1), is an E3 ubiquitin-protein ligase that is predominantly expressed in lymphoid cells, and functions as a positive regulator of T cell activation. It also down-modulates HIV replication and inhibits pathogen-induced cytokine production. It negatively regulates type I interferon signaling, which conjugates Lys(48)-linked ubiquitination to retinoic acid-inducible gene-I (RIG-I) and subsequently leads to the proteasome-dependent degradation of RIG-I. Further, RNF125 conjugates ubiquitin to melanoma differentiation-associated gene 5 (MDA5), a family protein of RIG-I. It thus acts as a negative regulator of RIG-I signaling, and is a direct target of miR-15b in the context of Japanese encephalitis virus (JEV) infection. Moreover, RNF125 binds to and ubiquitinates JAK1, prompting its degradation and inhibition of receptor tyrosine kinase (RTK) expression. It also negatively regulates p53 function through physical interaction and ubiquitin-mediated proteasome degradation. Mutations in RNF125 may lead to overgrowth syndromes (OGS). RNF125, together with three closely related proteins: RNF114, RNF138 and RNF166, forms a novel family of ubiquitin ligases with a C3HC4-type RING-HC finger, a C2HC-, and two C2H2-type zinc fingers, as well as a ubiquitin interacting motif (UIM). The UIM of RNF125 binds K48-linked poly-ubiquitin chains and is, together with the RING domain, required for auto-ubiquitination.


Pssm-ID: 438204 [Multi-domain]  Cd Length: 50  Bit Score: 46.03  E-value: 2.19e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1958660160   22 LECPICLELIKEPVSTKCDHIFCKFCMLKLLNQKKgpSQCPLCK 65
Cdd:cd16542      2 FDCAVCLEVLHQPVRTRCGHVFCRPCIATSLRNNT--WTCPYCR 43
zf-C3HC4_4 pfam15227
zinc finger of C3HC4-type, RING; This is a family of primate-specific Ret finger protein-like ...
24-64 2.24e-06

zinc finger of C3HC4-type, RING; This is a family of primate-specific Ret finger protein-like (RFPL) zinc-fingers of the C3HC4 type. Ret finger protein-like proteins are primate-specific target genes of Pax6, a key transcription factor for pancreas, eye and neocortex development. This domain is likely to be DNA-binding. This zinc-finger domain together with the RDM domain, pfam11002, forms a large zinc-finger structure of the RING/U-Box superfamily. RING-containing proteins are known to exert an E3 ubiquitin protein ligase activity with the zinc-finger structure being mandatory for binding to the E2 ubiquitin-conjugating enzyme.


Pssm-ID: 434549 [Multi-domain]  Cd Length: 42  Bit Score: 45.87  E-value: 2.24e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1958660160   24 CPICLELIKEPVSTKCDHIFCKFCMLKLLNQKKGPS-QCPLC 64
Cdd:pfam15227    1 CPICLDYLEKPVSLECGHTFCLSCINSLQKEPDGEQlSCPQC 42
RING-HC_IRC20-like cd23135
RING finger, HC subclass, found in Saccharomyces cerevisiae increased recombination centers ...
20-65 2.32e-06

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: 45.97  E-value: 2.32e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1958660160   20 KILECPICLELIKEPVSTKCDHIFCKFCMLKLLNQKkgpSQCPLCK 65
Cdd:cd23135      2 QKLSCSICFSEIRSGAILKCGHFFCLSCIASWLREK---STCPLCK 44
RING-HC_RNF185 cd16744
RING finger, HC subclass, found in RING finger protein 185 (RNF185) and similar proteins; ...
23-70 2.64e-06

RING finger, HC subclass, found in RING finger protein 185 (RNF185) and similar proteins; RNF185 is an E3 ubiquitin-protein ligase of endoplasmic reticulum-associated degradation (ERAD) that targets cystic fibrosis transmembrane conductance regulator (CFTR). It controls the degradation of CFTR and CFTR F508del allele in a RING- and proteasome-dependent manner, but does not control that of other classical ERAD model substrates. It also negatively regulates osteogenic differentiation by targeting dishevelled2 (Dvl2), a key mediator of the Wnt signaling pathway, for degradation. Moreover, RNF185 regulates selective mitochondrial autophagy through interaction with the Bcl-2 family protein BNIP1. It also plays an important role in cell adhesion and migration through the modulation of cell migration by ubiquitinating paxillin. RNF185 contains a C3HC4-type RING-HC finger.


Pssm-ID: 438402 [Multi-domain]  Cd Length: 57  Bit Score: 46.07  E-value: 2.64e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1958660160   23 ECPICLELIKEPVSTKCDHIFCKFCMLKLLNQKKGPSQCPLCKNEITK 70
Cdd:cd16744      2 ECNICLDTAKDAVVSLCGHLFCWPCLHQWLETRPNRQVCPVCKAGISR 49
RING-HC_TRIM68_C-IV cd16610
RING finger, HC subclass, found in tripartite motif-containing protein 68 (TRIM68) and similar ...
22-65 3.55e-06

RING finger, HC subclass, found in tripartite motif-containing protein 68 (TRIM68) and similar proteins; TRIM68, also known as RING finger protein 137 (RNF137) or SSA protein SS-56 (SS-56), is an E3 ubiquitin-protein ligase that negatively regulates Toll-like receptor (TLR)- and RIG-I-like receptor (RLR)-driven type I interferon production by degrading TRK fused gene (TFG), a novel driver of IFN-beta downstream of anti-viral detection systems. It also functions as a cofactor for androgen receptor-mediated transcription by regulating ligand-dependent transcription of androgen receptor in prostate cancer cells. Moreover, TRIM68 is a cellular target of autoantibody responses in Sjogre's syndrome (SS), as well as systemic lupus erythematosus (SLE). It is also an auto-antigen for T cells in SS and SLE. TRIM68 belongs the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, a B-box, and two coiled coil domains, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438272 [Multi-domain]  Cd Length: 49  Bit Score: 45.66  E-value: 3.55e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1958660160   22 LECPICLELIKEPVSTKCDHIFCKFCMLKLLnQKKGPSQ-----CPLCK 65
Cdd:cd16610      2 VACPICMTFLREPVSIDCGHSFCHSCLSGLW-EVPGESQnwgytCPLCR 49
RING-HC_RNFT1-like cd16532
RING finger, HC subclass, found in RING finger and transmembrane domain-containing protein ...
24-65 3.83e-06

RING finger, HC subclass, found in RING finger and transmembrane domain-containing protein RNFT1, RNFT2, and similar proteins; Both RNFT1 and RNFT2 are multi-pass membrane proteins containing a C3HC4-type RING-HC finger. Their biological roles remain unclear.


Pssm-ID: 438194 [Multi-domain]  Cd Length: 41  Bit Score: 45.37  E-value: 3.83e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1958660160   24 CPICLELIKEPVSTKCDHIFCKFCMLKLLNQKKgpsQCPLCK 65
Cdd:cd16532      3 CPICQDEFKDPVVLRCKHIFCEDCVSEWFERER---TCPLCR 41
PEX10 COG5574
RING-finger-containing E3 ubiquitin ligase [Posttranslational modification, protein turnover, ...
23-65 3.95e-06

RING-finger-containing E3 ubiquitin ligase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227861 [Multi-domain]  Cd Length: 271  Bit Score: 50.28  E-value: 3.95e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1958660160   23 ECPICLELIKEPVSTKCDHIFCKFCMLKLLnQKKGPSQCPLCK 65
Cdd:COG5574    217 KCFLCLEEPEVPSCTPCGHLFCLSCLLISW-TKKKYEFCPLCR 258
RING-HC_TRIM38_C-IV cd16600
RING finger, HC subclass, found in tripartite motif-containing protein 38 (TRIM38) and similar ...
18-65 5.38e-06

RING finger, HC subclass, found in tripartite motif-containing protein 38 (TRIM38) and similar proteins; TRIM38, also known as RING finger protein 15 (RNF15) or zinc finger protein RoRet, is an E3 ubiquitin-protein ligase that promotes K63- and K48-linked ubiquitination of cellular proteins and also catalyzes self-ubiquitination. It negatively regulates Tumor necrosis factor alpha (TNF-alpha)- and interleukin-1beta-triggered Nuclear factor-kappaB (NF-kappaB) activation by mediating lysosomal-dependent degradation of transforming growth factor beta (TGFbeta)-activated kinase 1 (TAK1)-binding protein (TAB)2/3, two critical components of the TAK1 kinase complex. It also inhibits TLR3/4-mediated activation of NF-kappaB and interferon regulatory factor 3 (IRF3) by mediating ubiquitin-proteasomal degradation of TNF receptor-associated factor 6 (Traf6) and NAK-associated protein 1 (Nap1), respectively. Moreover, TRIM38 negatively regulates TLR3-mediated interferon beta (IFN-beta) signaling by targeting ubiquitin-proteasomal degradation of TIR domain-containing adaptor inducing IFN-beta (TRIF). It functions as a valid target for autoantibodies in primary Sjogren's Syndrome. TRIM38 belongs the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, a B-box, and two coiled coil domains, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438262 [Multi-domain]  Cd Length: 58  Bit Score: 45.15  E-value: 5.38e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958660160   18 MQKILECPICLELIKEPVSTKCDHIFCKFCMLKLL-NQK-KGPSQ----CPLCK 65
Cdd:cd16600      2 MREEATCSICLQLMTEPVSINCGHSYCKRCIVSFLeNQSqLEPGLetfsCPQCR 55
RING-HC_Topors cd16574
RING finger, HC subclass, found in topoisomerase I-binding arginine/serine-rich protein ...
23-65 5.83e-06

RING finger, HC subclass, found in topoisomerase I-binding arginine/serine-rich protein (Topors) and similar proteins; Topors, also known as topoisomerase I-binding RING finger protein, tumor suppressor p53- binding protein 3, or p53-binding protein 3 (p53BP3), is a ubiquitously expressed nuclear E3 ubiquitin-protein ligase that can ligate both ubiquitin and small ubiquitin-like modifier (SUMO) to substrate proteins in the nucleus. It contains an N-terminal C3HC4-type RING-HC finger which ligates ubiquitin to its target proteins including DNA topoisomerase I, p53, NKX3.1, H2AX, and the AAV-2 Rep78/68 proteins. As a RING-dependent E3 ubiquitin ligase, Topors works with the E2 enzymes UbcH5a, UbcH5c, and UbcH6, but not with UbcH7, CDC34, or UbcH2b. Topors acts as a tumor suppressor in various malignancies. It regulates p53 modification, suggesting it may be responsible for astrocyte elevated gene-1 (AEG-1, also known as metadherin, or LYRIC) ubiquitin modification. Plk1-mediated phosphorylation of Topors inhibits Topors-mediated sumoylation of p53, whereas p53 ubiquitination is enhanced, leading to p53 degradation. It also functions as a negative regulator of the prostate tumor suppressor NKX3.1. Moreover, Topors is associated with promyelocytic leukemia nuclear bodies, and may be involved in the cellular response to camptothecin. It also plays a key role in the turnover of H2AX protein, discriminating the type of DNA damaging stress. Furthermore, Topors is a cilia-centrosomal protein associated with autosomal dominant retinal degeneration. Mutations in TOPORS cause autosomal dominant retinitis pigmentosa (adRP).


Pssm-ID: 438236 [Multi-domain]  Cd Length: 47  Bit Score: 44.97  E-value: 5.83e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1958660160   23 ECPICLELIKEPVST--KCDHIFCKFCMLKLLNQKkgpSQCPLCK 65
Cdd:cd16574      3 SCPICLDRFENEKAFldGCFHAFCFTCILEWSKVK---NECPLCK 44
RING-HC_BAH1-like cd23127
RING finger, HC subclass, found in Arabidopsis thaliana protein BENZOIC ACID HYPERSENSITIVE 1 ...
22-65 6.65e-06

RING finger, HC subclass, found in Arabidopsis thaliana protein BENZOIC ACID HYPERSENSITIVE 1 (BAH1) and similar proteins; This subfamily includes Arabidopsis thaliana BAH1 and BAH1-like. BAH1, also known as protein NITROGEN LIMITATION ADAPTATION (NLA), or RING-type E3 ubiquitin transferase BAH1, acts as an E3 ubiquitin-protein ligase that mediates E2-dependent protein ubiquitination. It plays a role in salicylic acid-mediated negative feedback regulation of salicylic acid (SA) accumulation. It may be involved in the overall regulation of SA, benzoic acid and phenylpropanoid biosynthesis. It controls the adaptability to nitrogen limitation by channeling the phenylpropanoid metabolic flux to the induced anthocyanin synthesis. BAH1-like, also known as RING finger protein 178, or RING-type E3 ubiquitin transferase BAH1-like, is a probable E3 ubiquitin-protein ligase. Members of this subfamily contain a typical C3HC4-type RING-HC finger.


Pssm-ID: 438489 [Multi-domain]  Cd Length: 74  Bit Score: 45.47  E-value: 6.65e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1958660160   22 LECPICLELIKEPVSTKCDHIFCKFC------MLKLLNQKKGP--SQCPLCK 65
Cdd:cd23127      9 LTCSICLDTVFDPVALGCGHLFCNSCacsaasVLIFQGLKAAPpeAKCPLCR 60
RING-HC_RNF220 cd16563
RING finger, HC subclass, found in RING finger protein 220 (RNF220) and similar proteins; ...
24-69 7.21e-06

RING finger, HC subclass, found in RING finger protein 220 (RNF220) and similar proteins; RNF220 is an E3 ubiquitin-protein ligase that promotes the ubiquitination and proteasomal degradation of Sin3B, a scaffold protein of the Sin3/HDAC (histone deacetylase) corepressor complex. It can also bind E2 and mediate auto-ubiquitination of itself. Moreover, RNF220 specifically interacts with beta-catenin, and enhances canonical Wnt signaling through ubiquitin-specific protease 7 (USP7)-mediated deubiquitination and stabilization of beta-catenin, which is independent of its E3 ligase activity. RNF220 contains a characteristic C3HC4-type RING-HC finger at its C-terminus.


Pssm-ID: 438225 [Multi-domain]  Cd Length: 52  Bit Score: 44.75  E-value: 7.21e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1958660160   24 CPICLELIKEP-VSTKCDHIFCKFCMLKLLNQKKgpsQCPLCkNEIT 69
Cdd:cd16563      3 CLICMDSYTMPlVSIQCWHVHCEECWLRTLGAKK---LCPQC-NTIT 45
RING-HC_RNF151 cd16547
RING finger, HC subclass, found in RING finger protein 151 (RNF151) and similar proteins; ...
22-68 8.43e-06

RING finger, HC subclass, found in RING finger protein 151 (RNF151) and similar proteins; RNF151 is a testis-specific RING finger protein that interacts with dysbindin, a synaptic and microtubular protein that binds brain snapin, a SNARE-binding protein that mediates intracellular membrane fusion in both neuronal and non-neuronal cells. Thus, it may be involved in acrosome formation of spermatids by interacting with multiple proteins participating in membrane biogenesis and microtubule organization. RNF151 contains a C3HC4-type RING finger domain, a putative nuclear localization signal (NLS), and a TNF receptor associated factor (TRAF)-type zinc finger domain.


Pssm-ID: 438209 [Multi-domain]  Cd Length: 49  Bit Score: 44.37  E-value: 8.43e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1958660160   22 LECPICLELIKEPVSTKCDHIFCKFCMLKLLNQKKgpsQCPLCKNEI 68
Cdd:cd16547      4 LICSICHGVLRCPVRLSCSHIFCKKCILQWLKRQE---TCPCCRKEV 47
RING-HC_ORTHRUS_rpt1 cd23138
first RING finger, HC subclass, found in Arabidopsis thaliana ORTHRUS and similar proteins; ...
22-68 8.65e-06

first RING finger, HC subclass, found in Arabidopsis thaliana ORTHRUS and similar proteins; This subfamily includes Arabidopsis thaliana ORTHRUS 1-5. They are E3 ubiquitin-protein ligases that may participate in CpG methylation-dependent transcriptional regulation and/or epigenetic transcriptional silencing. ORTHRUS 1 mediates ubiquitination with the E2 ubiquitin-conjugating enzymes UBC11, UBC8 and UBC8 homologs (e.g. UBC10, UBC11, UBC28 and UBC29) but not with UBC27, UBC30, UBC32, UBC34 and UBC36. ORTHRUS 2 and 5 mediate ubiquitination with the E2 ubiquitin-conjugating enzyme UBC11. ORTHRUS 1 and 2 promote methylation-mediated gene silencing leading, for example, to early flowering. They can bind to CpG, CpNpG, and CpNpN DNA motifs, with a strong preference for methylated forms, and with highest affinity for CpG substrates. Members of this subfamily contain two typical C3HC4-type RING-HC fingers. This model corresponds to the first one.


Pssm-ID: 438500 [Multi-domain]  Cd Length: 48  Bit Score: 44.36  E-value: 8.65e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1958660160   22 LECPICLELIKEPVSTKCDHIFCKFCMLKLLNQkkGPSQCPLCKNEI 68
Cdd:cd23138      3 LNCSFCMQLPERPVTTPCGHNFCLKCFQKWMGQ--GKKTCGTCRSPI 47
rad18 TIGR00599
DNA repair protein rad18; All proteins in this family for which functions are known are ...
15-84 9.62e-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: 273165 [Multi-domain]  Cd Length: 397  Bit Score: 50.00  E-value: 9.62e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660160   15 LHAMQKILECPICLELIKEPVSTKCDHIFCKFCMLKLLNQKkgpSQCPLCKNEITKRSLQGSARFSQLVE 84
Cdd:TIGR00599   20 LYPLDTSLRCHICKDFFDVPVLTSCSHTFCSLCIRRCLSNQ---PKCPLCRAEDQESKLRSNWLVSEIVE 86
RING-HC_SpRad8-like cd16572
RING finger, HC subclass, found in Schizosaccharomyces pombe DNA repair protein Rad8 (SpRad8) ...
23-64 1.04e-05

RING finger, HC subclass, found in Schizosaccharomyces pombe DNA repair protein Rad8 (SpRad8) and similar proteins; SpRad8 is a conserved protein homologous to Saccharomyces cerevisiae DNA repair protein Rad5 and human helicase-like transcription factor (HLTF) that is required for error-free postreplication repair by contributing to polyubiquitylation of PCNA. SpRad8 contains a C3HC4-type RING-HC finger responsible for the E3 ubiquitin ligase activity, a SNF2-family helicase domain including an ATP binding site, and a family-specific HIRAN domain (HIP116, Rad5p N-terminal domain) that contributes to nuclear localization.


Pssm-ID: 438234 [Multi-domain]  Cd Length: 61  Bit Score: 44.42  E-value: 1.04e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1958660160   23 ECPICL-ELIKEPVSTKCDHIFCKFCMLKLLNQKKGPSQCPLC 64
Cdd:cd16572      6 ECPICAeEPISELALTRCWHSACKDCLLDHIEFQKSKNEVPLC 48
RING-HC_TRIM8_C-V cd16580
RING finger, HC subclass, found in tripartite motif-containing protein 8 (TRIM8) and similar ...
22-66 1.06e-05

RING finger, HC subclass, found in tripartite motif-containing protein 8 (TRIM8) and similar proteins; TRIM8, also known as glioblastoma-expressed RING finger protein (GERP) or RING finger protein 27 (RNF27), is a probable E3 ubiquitin-protein ligase that may promote proteasomal degradation of suppressor of cytokine signaling 1 (SOCS1) and further regulate interferon-gamma signaling. It functions as a new p53 modulator that stabilizes p53 impairing its association with MDM2 and inducing the reduction of cell proliferation. TRIM8 deficit dramatically impairs p53 stabilization and activation in response to chemotherapeutic drugs. TRIM8 also modulates tumor necrosis factor-alpha (TNFalpha) and interleukin-1beta (IL-1beta)-triggered nuclear factor-kappaB (NF- kappa B) activation by targeting transforming growth factor beta (TGFbeta) activated kinase 1 (TAK1) for K63-linked polyubiquitination. Moreover, TRIM8 modulates translocation of phosphorylated STAT3 into the nucleus through interaction with Hsp90beta and consequently regulates transcription of Nanog in embryonic stem cells. It also interacts with protein inhibitor of activated STAT3 (PIAS3), which inhibits IL-6-dependent activation of STAT3. TRIM8 belongs to the C-V subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil domain, as well as an uncharacterized region positioned C-terminal to the RBCC domain. The coiled coil domain is required for homodimerization and the region immediately C-terminal to the RING motif is sufficient to mediate the interaction with SOCS1.


Pssm-ID: 438242 [Multi-domain]  Cd Length: 67  Bit Score: 44.88  E-value: 1.06e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1958660160   22 LECPICLELIKEPVSTKCDHIFCKFCMLKLLNQKKGPSQCPLCKN 66
Cdd:cd16580     12 LICPICLHVFVEPVQLPCKHNFCRGCIGEAWAKDAGLVRCPECNQ 56
RING-HC_RNF219 cd16562
RING finger, HC subclass, found in RING finger protein 219 (RNF219) and similar proteins; ...
22-68 1.17e-05

RING finger, HC subclass, found in RING finger protein 219 (RNF219) and similar proteins; RNF219 may function as a modulator of late-onset Alzheimer's disease (LOAD) associated amyloid beta A4 precursor protein (APP) endocytosis and metabolism. It genetically interacts with apolipoprotein E epsilon4 allele (APOE4). Thus, a genetic variant of RNF219 was found to affect amyloid deposition in human brain and LOAD age-of-onset. Moreover, common genetic variants at the RNF219 locus had been associated with alternations in lipid metabolism, cognitive performance and central nervous system ventricle volume. RNF219 contains a C3HC4-type RING-HC finger.


Pssm-ID: 438224 [Multi-domain]  Cd Length: 45  Bit Score: 43.96  E-value: 1.17e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1958660160   22 LECPICLELIKEPVSTKCDHIFCKFCMLKLLNQKkgpSQCPLCKNEI 68
Cdd:cd16562      2 ISCHICLGKVRQPVICSNNHVFCSSCMDVWLKNN---NQCPACRVPI 45
PLN03208 PLN03208
E3 ubiquitin-protein ligase RMA2; Provisional
22-73 1.23e-05

E3 ubiquitin-protein ligase RMA2; Provisional


Pssm-ID: 178747 [Multi-domain]  Cd Length: 193  Bit Score: 47.77  E-value: 1.23e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958660160   22 LECPICLELIKEPVSTKCDHIFCKFCMLKL-------------LNQKKGPSQCPLCKNEITKRSL 73
Cdd:PLN03208    19 FDCNICLDQVRDPVVTLCGHLFCWPCIHKWtyasnnsrqrvdqYDHKREPPKCPVCKSDVSEATL 83
RING-HC_TRIM10_C-IV cd16593
RING finger, HC subclass, found in tripartite motif-containing protein 10 (TRIM10) and similar ...
24-65 1.32e-05

RING finger, HC subclass, found in tripartite motif-containing protein 10 (TRIM10) and similar proteins; TRIM10, also known as B30-RING finger protein (RFB30), RING finger protein 9 (RNF9), or hematopoietic RING finger 1 (HERF1), is a novel hematopoiesis-specific RING finger protein required for terminal differentiation of erythroid cells. TRIM10 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438255 [Multi-domain]  Cd Length: 61  Bit Score: 44.51  E-value: 1.32e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1958660160   24 CPICLELIKEPVSTKCDHIFCKFCMLKLLNQK----KGPSQCPLCK 65
Cdd:cd16593      8 CPICQGTLREPVTIDCGHNFCRACLTRYCEIPgpdlEEPPTCPLCK 53
RING-HC_BARD1 cd16496
RING finger, HC subclass, found in BRCA1-associated RING domain protein 1 (BARD-1) and similar ...
15-65 1.43e-05

RING finger, HC subclass, found in BRCA1-associated RING domain protein 1 (BARD-1) and similar proteins; BARD-1 is a critical factor in BRCA1-mediated tumor suppression and may also serve as a target for tumorigenic lesions in some human cancers. It associates with BRCA1 (breast cancer-1) to form a heterodimeric BRCA1/BARD1 complex that is responsible for maintaining genomic stability through nuclear functions involving DNA damage signaling and repair, transcriptional regulation, and cell cycle control. The BRCA1/BARD1 complex catalyzes autoubiquitination of BRCA1 and trans ubiquitination of other protein substrates. Its E3 ligase activity is dramatically reduced in the presence of UBX domain protein 1 (UBXN1). BARD-1 contains an C3HC4-type RING-HC finger that binds BRCA1 at its N-terminus and three tandem ankyrin repeats and tandem BRCT repeat domains at its C-terminus. The BRCT repeats bind CstF-50 (cleavage stimulation factor) to modulate mRNA processing and RNAP II stability in response to DNA damage.


Pssm-ID: 438159 [Multi-domain]  Cd Length: 86  Bit Score: 45.02  E-value: 1.43e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1958660160   15 LHAMQKILECPICLELIKEPVST-KCDHIFCKFCMlkllnQKKGPSQCPLCK 65
Cdd:cd16496      9 LDELENLLRCSRCASILKEPVTLgGCEHVFCRSCV-----GDRLGNGCPVCD 55
BRCT smart00292
breast cancer carboxy-terminal domain;
1603-1669 1.63e-05

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 44.67  E-value: 1.63e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958660160  1603 LTPKEVMIVQKFAEKYRLALTDVITE------------ETTHVIIKTDAEfvceRTLKYFLGIAGGKWIVSYSWVIKSI 1669
Cdd:smart00292    4 FKGKTFYITGSFDKEERDELKELIEAlggkvtsslsskTTTHVIVGSPEG----GKLELLKAIALGIPIVKEEWLLDCL 78
RING-H2 cd16448
H2 subclass of RING (RING-H2) fingers and its variants; The RING finger is a specialized type ...
24-65 1.82e-05

H2 subclass of RING (RING-H2) fingers and its variants; The RING finger is a specialized type of Zn-finger of 40 to 60 residues that binds two atoms of zinc. It is defined by the "cross-brace" motif that chelates zinc atoms by eight amino acid residues, typically Cys or His, arranged in a characteristic spacing. Canonical RING motifs have been categorized into two major subclasses, RING-HC (C3HC4-type) and RING-H2 (C3H2C3-type), according to their Cys/His content. There are also many variants of RING fingers: some have different Cys/His patterns while some lack a single Cys or His residue at typical Zn ligand positions (the fourth or eighth zinc ligand is prevalently exchanged for an Asp, which can indeed chelate Zn in a RING finger as well). This family corresponds to the H2 subclass of RING (RING-H2) finger proteins that are characterized by containing C3H2C3-type canonical RING-H2 fingers or noncanonical RING-H2 finger variants, including C4HC3- (RING-CH alias RINGv), C3H3C2-, C3H2C2D-, C3DHC3-, and C4HC2H-type modified RING-H2 fingers. The canonical RING-H2 finger has been defined as C-X2-C-X(9-39)-C-X(1-3)-H-X(2-3)-H-X2-C-X(4-48)-C-X2-C, X is any amino acid and the number of X residues varies in different fingers. It binds two Zn ions in a unique "cross-brace" arrangement, which distinguishes it from tandem zinc fingers and other similar motifs. RING-H2 finger can be found in a group of diverse proteins with a variety of cellular functions, including oncogenesis, development, viral replication, signal transduction, the cell cycle and apoptosis. Many of them are ubiquitin-protein ligases (E3s) that serves as a scaffold for binding to ubiquitin-conjugating enzymes (E2s, also referred to as ubiquitin carrier proteins or UBCs) in close proximity to substrate proteins, which enables efficient transfer of ubiquitin from E2 to the substrates.


Pssm-ID: 438112 [Multi-domain]  Cd Length: 43  Bit Score: 43.16  E-value: 1.82e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1958660160   24 CPICLELIKEPVS---TKCDHIFCKFCMLKLLNQKKgpSQCPLCK 65
Cdd:cd16448      1 CVICLEEFEEGDVvrlLPCGHVFHLACILRWLESGN--NTCPLCR 43
RING-HC_CHR27-like cd23142
RING finger, HC subclass, found in Arabidopsis thaliana protein CHROMATIN REMODELING 27 (CHR27) ...
24-73 1.88e-05

RING finger, HC subclass, found in Arabidopsis thaliana protein CHROMATIN REMODELING 27 (CHR27) and similar proteins; CHR27, also called protein SNF2-RING-HELICASE-LIKE 1, is a probable helicase-like transcription factor involved in transcriptional gene silencing. It associates with SUVR2 and contributes to transcriptional gene silencing at RNA-directed DNA methylation (RdDM) target loci but also at RdDM-independent target loci. It may be involved in nucleosome positioning to form ordered nucleosome arrays on chromatin. It associates with SUVR2 and functions redundantly with FRG2. It is required for the efficient methylation of a broad range of RdDM target loci. CHR27 contains a typical C3HC4-type RING-HC finger.


Pssm-ID: 438504 [Multi-domain]  Cd Length: 55  Bit Score: 43.71  E-value: 1.88e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958660160   24 CPICLELIKEPVSTKCDHIFCKFCMLKLLNQKKGPSQ---CPLCKNEITKRSL 73
Cdd:cd23142      3 CPICNDPPEDAVVTLCGHVFCCECVFQYLSSDRTCRQfnhCPLCRQKLYLDDV 55
RING-HC_TRIM60-like_C-IV cd16607
RING finger, HC subclass, found in tripartite motif-containing proteins TRIM60, TRIM61, TRIM75 ...
24-65 2.02e-05

RING finger, HC subclass, found in tripartite motif-containing proteins TRIM60, TRIM61, TRIM75 and similar proteins; TRIM60, also known as RING finger protein 129 (RNF129) or RING finger protein 33 (RNF33), is a cytoplasmic protein expressed in the testis. It may play an important role in the spermatogenesis process, the development of the preimplantation embryo, and in testicular functions. RNF33 interacts with the cytoplasmic kinesin motor proteins KIF3A and KIF3B suggesting possible contribution to cargo movement along the microtubule in the expressed sites. It is also involved in spermatogenesis in Sertoli cells under the regulation of nuclear factor-kappaB (NF-kappaB). TRIM75 mainly localizes within spindles, suggesting it may function in spindle organization and thereby affect meiosis. Both TRIM60 and TRIM75 belong the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, a B2-box, and two coiled coil domains, as well as a PRY domain and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. In contrast, TRIM61 belongs to the C-V subclass of the TRIM family that contains RBCC domains only. Its biological function remains unclear.


Pssm-ID: 438269 [Multi-domain]  Cd Length: 48  Bit Score: 43.18  E-value: 2.02e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1958660160   24 CPICLELIKEPVSTKCDHIFCKFCMLKLLNQKKGPSQCPLCK 65
Cdd:cd16607      4 CPICLDYLKDPVTINCGHNFCRSCISMSWKDLQDTFPCPVCR 45
RING-HC_RAD5 cd23131
RING finger, HC subclass, found in radiation sensitivity protein 5 (RAD5) and similar proteins; ...
22-73 2.21e-05

RING finger, HC subclass, found in radiation sensitivity protein 5 (RAD5) and similar proteins; RAD5, also known as revertibility protein 2 (REV2), or DNA repair protein RAD5, is a probable helicase, and a member of the UBC2/RAD6 epistasis group. It functions with the DNA repair protein RAD18 in error-free postreplication DNA repair. It is involved in the maintenance of wild-type rates of instability of simple repetitive sequences such as poly(GT) repeats. It may also be involved in maintaining a balance which acts in favor of error-prone non-homologous joining during DNA double-strand breaks repairs. It recruits the UBC13-MMS2 dimer to chromatin for DNA repair. RAD5 contains a typical C3HC4-type RING-HC finger.


Pssm-ID: 438493 [Multi-domain]  Cd Length: 65  Bit Score: 43.97  E-value: 2.21e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958660160   22 LECPIClelIKEPVS------TKCDHIFCKFCMLKLLN--QKKGPSQ-CPLCKNEITKRSL 73
Cdd:cd23131      4 VECSIC---TQEPIEvgevvfTECGHSFCEDCLLEYIEfqNKKKLDLkCPNCREPISKYRL 61
zf-C3HC4_3 pfam13920
Zinc finger, C3HC4 type (RING finger);
20-71 2.62e-05

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 433580 [Multi-domain]  Cd Length: 50  Bit Score: 43.13  E-value: 2.62e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958660160   20 KILECPICLELIKEPVSTKCDH-IFCKFCMLKLLNQKKgpsQCPLCKNEITKR 71
Cdd:pfam13920    1 EELLCVICLDRPRNVVLLPCGHlCLCEECAERLLRKKK---KCPICRQPIESV 50
RING-HC_MID1 cd16753
RING finger, HC subclass, found in midline-1 (MID1) and similar proteins; MID1, also known as ...
22-75 2.84e-05

RING finger, HC subclass, found in midline-1 (MID1) and similar proteins; MID1, also known as midin, midline 1 RING finger protein, putative transcription factor XPRF, RING finger protein 59 (RNF59), or tripartite motif-containing protein 18 (TRIM18), is a microtubule-associated E3 ubiquitin-protein ligase implicated in epithelial-mesenchymal differentiation, cell migration and adhesion, and programmed cell death along specific regions of the ventral midline during embryogenesis. It monoubiquinates the alpha4 subunit of protein phosphatase 2A (PP2A), promoting proteosomal degradation of the catalytic subunit of PP2A (PP2Ac) and preventing the A and B subunits from forming an active complex. It promotes allergen and rhinovirus-induced asthma through the inhibition of PP2A activity. It is strongly upregulated in cytotoxic lymphocytes (CTLs) and directs lytic granule exocytosis and cytotoxicity of killer T cells. Loss-of-function mutations in MID1 lead to the human X-linked Opitz G/BBB (XLOS) syndrome characterized by defective midline development during embryogenesis. MID1 belongs to the C-I subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. MID1 hetero-dimerizes in vitro with its paralog MID2.


Pssm-ID: 438411 [Multi-domain]  Cd Length: 72  Bit Score: 43.87  E-value: 2.84e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958660160   22 LECPICLELIKEPVSTKCDHIFCKFCMLKLL-----NQKKGPS----QCPLCKNEIT--KRSLQG 75
Cdd:cd16753      6 LTCPICLELFEDPLLLPCAHSLCFNCAHRILvshcaSNESVESitafQCPTCRYVITlnQRGLEG 70
RING-HC_RNF113A_B cd16539
RING finger, HC subclass, found in RING finger proteins RNF113A, RNF113B, and similar proteins; ...
24-68 2.87e-05

RING finger, HC subclass, found in RING finger proteins RNF113A, RNF113B, and similar proteins; RNF113A, also known as zinc finger protein 183 (ZNF183), is an E3 ubiquitin-protein ligase that physically interacts with the E2 protein, UBE2U. A nonsense mutation in RNF113A is associated with an X-linked trichothiodystrophy (TTD). Its yeast ortholog Cwc24p is predicted to have a spliceosome function and acts in a complex with Cef1p to participate in pre-U3 snoRNA splicing, indirectly affecting pre-rRNA processing. It is also important for the U2 snRNP binding to primary transcripts and co-migrates with spliceosomes. Moreover, the ortholog of RNF113A in fruit flies may also act as a spliceosome and is hypothesized to be involved in splicing, namely within the central nervous system. The ortholog in Caenorhabditis elegans is involved in DNA repair of inter-strand crosslinks. RNF113B, also known as zinc finger protein 183-like 1, shows high sequence similarity with RNF113A. Both RNF113A and RNF113B contain a CCCH-type zinc finger, which is commonly found in RNA-binding proteins involved in splicing, and a C3HC4-type RING-HC finger, which is frequently found in E3 ubiquitin ligases.


Pssm-ID: 438201 [Multi-domain]  Cd Length: 54  Bit Score: 42.96  E-value: 2.87e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1958660160   24 CPICLELIKEPVSTKCDHIFCKFCMLKllnQKKGPSQCPLCKNEI 68
Cdd:cd16539      8 CFICRKPFKNPVVTKCGHYFCEKCALK---HYRKSKKCFVCGKQT 49
zf-RING_5 pfam14634
zinc-RING finger domain;
23-65 3.80e-05

zinc-RING finger domain;


Pssm-ID: 434085 [Multi-domain]  Cd Length: 43  Bit Score: 42.41  E-value: 3.80e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1958660160   23 ECPICLELIKE---PVSTKCDHIFCKFCmlklLNQKKGPSQCPLCK 65
Cdd:pfam14634    1 HCNKCFKELSKtrpFYLTSCGHIFCEEC----LTRLLQERQCPICK 42
mRING-HC-C4C4_TRIM37_C-VIII cd16619
Modified RING finger, HC subclass (C4C4-type), found in tripartite motif-containing protein 37 ...
22-64 3.84e-05

Modified RING finger, HC subclass (C4C4-type), found in tripartite motif-containing protein 37 (TRIM37) and similar proteins; TRIM37, also known as mulibrey nanism protein, or MUL, is a peroxisomal E3 ubiquitin-protein ligase that is involved in the tumorigenesis of several cancer types, including pancreatic ductal adenocarcinoma (PDAC), hepatocellular carcinoma (HCC), breast cancer, and sporadic fibrothecoma. It mono-ubiquitinates histone H2A, a chromatin modification associated with transcriptional repression. Moreover, TRIM37 possesses anti-HIV-1 activity, and interferes with viral DNA synthesis. Mutations in the human TRIM37 gene (also known as MUL) cause Mulibrey (muscle-liver-brain-eye) nanism, a rare growth disorder of prenatal onset characterized by dysmorphic features, pericardial constriction, and hepatomegaly. TRIM37 belongs to the C-VIII subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C4C4-type RING finger, whose overall folding is similar to that of the typical C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a MATH (meprin and TRAF-C homology) domain positioned C-terminal to the RBCC domain. Its MATH domain has been shown to interact with the TRAF (TNF-Receptor-Associated Factor) domain of six known TRAFs in vitro.


Pssm-ID: 438281 [Multi-domain]  Cd Length: 43  Bit Score: 42.34  E-value: 3.84e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1958660160   22 LECPICLELIKEPVS-TKCDHIFCKFCMLKLLNQKKgpSQCPLC 64
Cdd:cd16619      1 FRCFICMEKLRDPRLcPHCSKLFCKGCIRRWLSEQR--SSCPHC 42
mRING-HC-C3HC3D_LNX1-like cd16637
Modified RING finger, HC subclass (C3HC3D-type), found in ligand of Numb protein LNX1, LNX2, ...
22-63 4.27e-05

Modified RING finger, HC subclass (C3HC3D-type), found in ligand of Numb protein LNX1, LNX2, and similar proteins; The ligand of Numb protein X (LNX) family, also known as PDZ and RING (PDZRN) family, includes LNX1-5, which can interact with Numb, a key regulator of neurogenesis and neuronal differentiation. LNX5 (also known as PDZK4 or PDZRN4L) shows high sequence homology to LNX3 and LNX4, but it lacks the RING domain. LNX1-4 proteins function as E3 ubiquitin ligases and have a unique domain architecture consisting of an N-terminal RING-HC finger for E3 ubiquitin ligase activity and either two or four PDZ domains necessary for substrate-binding. LNX1/LNX2-like proteins contain a modified C3HC3D-type RING-HC finger and four PDZ domains. This model corresponds to the RING finger.


Pssm-ID: 438299 [Multi-domain]  Cd Length: 42  Bit Score: 42.38  E-value: 4.27e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1958660160   22 LECPICLELIKEPVSTKCDHIFCKFCMLKLLNQKKgpsQCPL 63
Cdd:cd16637      2 LTCHICLQPLVEPLDTPCGHTFCYKCLTNYLKIQQ---CCPL 40
RING-HC_DTX3-like cd16506
RING finger, HC subclass, found in E3 ubiquitin-protein ligase Deltex3 (DTX3), Deltex-3-like ...
23-65 4.29e-05

RING finger, HC subclass, found in E3 ubiquitin-protein ligase Deltex3 (DTX3), Deltex-3-like (DTX3L) and similar proteins; This subfamily contains Deltex3 (DTX3) and Deltex-3-like (DTX3L), both of which are E3 ubiquitin-protein ligases belonging to the Deltex (DTX) family. DTX3, also known as RING finger protein 154 (RNF154), has a biological function that remains unclear. DTX3L, also known as B-lymphoma- and BAL-associated protein (BBAP) or Rhysin-2 (Rhysin2), regulates endosomal sorting of the G protein-coupled receptor CXCR4 from endosomes to lysosomes. It also regulates subcellular localization of its partner protein, B aggressive lymphoma (BAL), by a dynamic nucleocytoplasmic trafficking mechanism. In contrast to other DTXs, both DTX3 and DTX3L contain a C3HC4-type RING-HC finger, and a previously unidentified C-terminal domain. DTX3L can associate with DTX1 through its unique N termini and further enhance self-ubiquitination.


Pssm-ID: 438169 [Multi-domain]  Cd Length: 45  Bit Score: 42.35  E-value: 4.29e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1958660160   23 ECPICLELIKEP-VSTKCDHIFCKFCMLKLLNQKKgpsQCPLCK 65
Cdd:cd16506      2 TCPICLDEIQNKkTLEKCKHSFCEDCIDRALQVKP---VCPVCG 42
RING-HC_RNF222 cd16564
RING finger, HC subclass, found in RING finger protein 222 (RNF222) and similar proteins; ...
23-70 4.55e-05

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: 42.39  E-value: 4.55e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1958660160   23 ECPICLE-LIKEPVSTKCDHIFCKFCMLKLLNQKKGpsQCPLCKNEITK 70
Cdd:cd16564      2 ECPVCYEdFDDAPRILSCGHSFCEDCLVKQLVSMTI--SCPICRRVTFI 48
RAD18 COG5432
RING-finger-containing E3 ubiquitin ligase [Signal transduction mechanisms];
15-89 5.24e-05

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


Pssm-ID: 227719 [Multi-domain]  Cd Length: 391  Bit Score: 47.77  E-value: 5.24e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660160   15 LHAMQKILECPICLELIKEPVSTKCDHIFCKFCMLKLLNQKkgpSQCPLC----------KNEITKRSLQGSARFSQLVE 84
Cdd:COG5432     19 LKGLDSMLRCRICDCRISIPCETTCGHTFCSLCIRRHLGTQ---PFCPVCredpcesrlrGSSGSREINESHARNRDLLR 95

                   ....*
gi 1958660160   85 ELLKI 89
Cdd:COG5432     96 KVLES 100
SP-RING-like cd16452
SP-RING finger and SPL-RING finger, variants of RING fingers; This family corresponds to a ...
22-64 5.53e-05

SP-RING finger and SPL-RING finger, variants of RING fingers; This family corresponds to a group of proteins with variants of RING fingers that are characterized by lacking the second, fifth, and sixth Zn2+ ion-coordinating residues compared with the classic C3H2C3-/C3HC4-type RING fingers. They include SP-RING finger found in the Siz/PIAS RING (SP-RING) family of SUMO E3 ligases and SPL-RING finger found in E3 SUMO-protein ligase NSE2. The SP-RING family includes PIAS (protein inhibitor of activated STAT) proteins, Zmiz proteins, and Siz proteins from plants and fungi. The PIAS (protein inhibitor of activated STAT) protein family modulates the activity of several transcription factors and acts as an E3 ubiquitin ligase in the sumoylation pathway. NSE2, also known as MMS21 homolog (MMS21) or non-structural maintenance of chromosomes element 2 homolog (Non-SMC element 2 homolog, NSMCE2), is an autosumoylating small ubiquitin-like modifier (SUMO) ligase required for the response to DNA damage. It regulates sumoylation and nuclear-to-cytoplasmic translocation of skeletal and heart muscle-specific variant of the alpha subunit of nascent polypeptide associated complex (skNAC)-Smyd1 in myogenesis. It is also required for resisting extrinsically induced genotoxic stress.


Pssm-ID: 438116 [Multi-domain]  Cd Length: 45  Bit Score: 41.86  E-value: 5.53e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1958660160   22 LECPICLELIKEPV-STKCDHIFCKFCMLKLLNQKKGPSQCPLC 64
Cdd:cd16452      1 LKCPITQKRMKDPVrGKHCGHCFDLEAILQYLKRRKKKWKCPVC 44
RING-HC_RNF166 cd16549
RING finger, HC subclass, found in RING finger protein 166 (RNF166) and similar proteins; ...
24-65 5.89e-05

RING finger, HC subclass, found in RING finger protein 166 (RNF166) and similar proteins; RNF166 is encoded by the gene RNF166 targeted by thyroid hormone receptor alpha1 (TRalpha1), which is important in brain development. It plays an important role in RNA virus-induced interferon-beta production by enhancing the ubiquitination of TRAF3 and TRAF6. RNF166, together with three closely related proteins: RNF114, RNF125 and RNF138, forms a novel family of ubiquitin ligases with a C3HC4-type RING-HC finger, a C2HC-, and two C2H2-type zinc fingers, as well as a ubiquitin interacting motif (UIM).


Pssm-ID: 438211 [Multi-domain]  Cd Length: 47  Bit Score: 42.11  E-value: 5.89e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1958660160   24 CPICLELIKEPVST-KCDHIFCKFCMLKLLnQKKGPsQCPLCK 65
Cdd:cd16549      4 CPICLEVYHKPVVItSCGHTFCGECLQPCL-QVASP-LCPLCR 44
RING-HC_RNFT1 cd16741
RING finger, HC subclass, found in RING finger and transmembrane domain-containing protein 1 ...
24-68 6.38e-05

RING finger, HC subclass, found in RING finger and transmembrane domain-containing protein 1 (RNFT1); RNFT1, also known as protein PTD016, is a multi-pass membrane protein containing a C3HC4-type RING-HC finger. Its biological role remains unclear.


Pssm-ID: 438399 [Multi-domain]  Cd Length: 58  Bit Score: 42.18  E-value: 6.38e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1958660160   24 CPICLELIKEPVSTKCDHIFCKFCMLKLLNQKKgpsQCPLCKNEI 68
Cdd:cd16741     17 CAICQAEFRKPILLICQHVFCEECISLWFNREK---TCPLCRTVI 58
RING-HC_TRIM13_C-V cd16762
RING finger, HC subclass, found in tripartite motif-containing protein 13 (TRIM13) and similar ...
22-67 8.62e-05

RING finger, HC subclass, found in tripartite motif-containing protein 13 (TRIM13) and similar proteins; TRIM13, also known as B-cell chronic lymphocytic leukemia tumor suppressor Leu5, leukemia-associated protein 5, putative tumor suppressor RFP2, RING finger protein 77 (RNF77), or Ret finger protein 2, is an endoplasmic reticulum (ER) membrane anchored E3 ubiquitin-protein ligase that interacts with proteins localized to the ER, including valosin-containing protein (VCP), a protein indispensable for ER-associated degradation (ERAD). It also targets the known ER proteolytic substrate CD3-delta, but not the N-end rule substrate Ub-R-YFP (yellow fluorescent protein) for degradation. Moreover, TRIM13 regulates ubiquitination and degradation of NEMO to suppress tumor necrosis factor (TNF) induced nuclear factor-kappaB (NF- kappa B) activation. It is also involved in NF-kappaB p65 activation and nuclear factor of activated T-cells (NFAT)-dependent activation of c-Rel upon T-cell receptor engagement. Furthermore, TRIM13 negatively regulates melanoma differentiation-associated gene 5 (MDA5)-mediated type I interferon production. It also regulates caspase-8 ubiquitination, translocation to autophagosomes, and activation during ER stress induced cell death. Meanwhile, TRIM13 enhances ionizing radiation-induced apoptosis by increasing p53 stability and decreasing AKT kinase activity through MDM2 and AKT degradation. TRIM13 belongs to the C-V subclass of the TRIM (tripartite motif) family of proteins that are defined by an N-terminal RBCC (RING, Bbox, and coiled coil) domain, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region. In addition, TRIM13 contains a C-terminal transmembrane domain.


Pssm-ID: 438418 [Multi-domain]  Cd Length: 56  Bit Score: 41.83  E-value: 8.62e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1958660160   22 LECPICLELIKEPVSTKCDHIFCKFCMLKLLN------QKKGPSQCPLCKNE 67
Cdd:cd16762      4 LTCPICCCLFDDPRVLPCSHNFCKKCLEGILEgnvrtmLWRPPFKCPTCRKE 55
RING-HC_TRIM58_C-IV cd16606
RING finger, HC subclass, found in tripartite motif-containing protein TRIM58 and similar ...
24-65 8.89e-05

RING finger, HC subclass, found in tripartite motif-containing protein TRIM58 and similar proteins; TRIM58, also known as protein BIA2, is an erythroid E3 ubiquitin-protein ligase induced during late erythropoiesis. It binds and ubiquitinates the intermediate chain of the microtubule motor dynein (DYNC1LI1/DYNC1LI2), stimulating the degradation of the dynein holoprotein complex. It may participate in the erythroblast enucleation process through regulation of nuclear polarization. TRIM58 belongs to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438268 [Multi-domain]  Cd Length: 53  Bit Score: 41.77  E-value: 8.89e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1958660160   24 CPICLELIKEPVSTKCDHIFCKFCMLKLLnQKKGPSQ-----CPLCK 65
Cdd:cd16606      5 CPVCLDFLQEPVSVDCGHSFCLRCISEFC-EKSDSAQggvyaCPQCR 50
mRING-HC-C3HC3D_TRAF7 cd16644
Modified RING finger, HC subclass (C3HC3D-type), found in tumor necrosis factor (TNF) ...
22-66 1.04e-04

Modified RING finger, HC subclass (C3HC3D-type), found in tumor necrosis factor (TNF) receptor-associated factor 7 (TRAF7) and similar proteins; TRAF7, also known as RING finger and WD repeat-containing protein 1 or RING finger protein 119 (RNF119), is an E3 ubiquitin-protein ligase involved in signal transduction pathways that lead either to activation or repression of NF-kappaB transcription factor by promoting K29-linked ubiquitination of several cellular targets, including the NF-kappaB essential modulator (NEMO) and the p65 subunit of NF-kappaB transcription factor. It is also involved in K29-linked polyubiquitination that has been implicated in lysosomal degradation of proteins. Moreover, TRAF7 is required for K48-linked ubiquitination of p53, a key tumor suppressor and a master regulator of various signaling pathways, such as those related to apoptosis, cell cycle and DNA repair. It is also required for tumor necrosis factor alpha (TNFalpha)-induced Jun N-terminal kinase activation and promotes cell death by regulating polyubiquitination and lysosomal degradation of c-FLIP protein. Furthermore, TRAF7 functions as small ubiquitin-like modifier (SUMO) E3 ligase involved in other post-translational modification, such as sumoylation. It binds to and stimulates sumoylation of the proto-oncogene product c-Myb, a transcription factor regulating proliferation and differentiation of hematopoietic cells. It potentiates MEKK3-induced AP1 and CHOP activation and induces apoptosis. Meanwhile, TRAF7 mediates MyoD1 regulation of the pathway and cell-cycle progression in myoblasts. It also plays a role in Toll-like receptors (TLR) signaling. TRAF7 contains an N-terminal domain with a modified C3HC3D-type RING-HC finger and an adjacent zinc finger, and a unique C-terminal domain that comprises a coiled coil domain and seven WD40 repeats.


Pssm-ID: 438306 [Multi-domain]  Cd Length: 47  Bit Score: 41.19  E-value: 1.04e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1958660160   22 LECPICLELIKEPVSTKCDHIFCKFCMLKLLNQKkgpsqCPLCKN 66
Cdd:cd16644      6 LYCPLCQRVFKDPVITSCGHTFCRRCALTAPGEK-----CPVDNM 45
RING-HC_RAG1 cd16530
RING finger, HC subclass, found in recombination activating gene-1 (RAG-1) and similar ...
20-65 1.06e-04

RING finger, HC subclass, found in recombination activating gene-1 (RAG-1) and similar proteins; RAG-1, also known as V(D)J recombination-activating protein 1, RING finger protein 74 (RNF74), or endonuclease RAG1, is the catalytic component of the RAG complex, a multiprotein complex that mediates the DNA cleavage phase during V(D)J recombination. RAG1 is a lymphoid-specific factor that mediates DNA-binding to conserved recombination signal sequences (RSS) and catalyzes DNA cleavage activities by introducing a double-strand break between the RSS and the adjacent coding segment. It also functions as an E3 ubiquitin-protein ligase that mediates monoubiquitination of histone H3, which is required for the joining step of V(D)J recombination. RAG-1 contains an N-terminal C3HC4-type RING-HC finger that mediates monoubiquitylation of histone H3, an adjacent C2H2-type zinc finger, and a nonamer binding (NBD) DNA-binding domain.


Pssm-ID: 319444 [Multi-domain]  Cd Length: 46  Bit Score: 41.27  E-value: 1.06e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1958660160   20 KILECPICLELIKEPVSTKCDHIFCKFCMLKLLnqKKGPSQCPLCK 65
Cdd:cd16530      1 KSVSCQVCEHILADPVQTPCKHLFCRTCILKCL--KVMGSYCPSCR 44
BRCT_TopBP1_rpt7 cd17738
seventh BRCT domain of DNA topoisomerase 2-binding protein 1; TopBP1, also termed DNA ...
1600-1671 1.16e-04

seventh BRCT domain of DNA topoisomerase 2-binding protein 1; TopBP1, also termed DNA topoisomerase II-beta-binding protein 1, or DNA topoisomerase II-binding protein 1, functions in DNA replication and damage response. It binds double-stranded DNA breaks and nicks as well as single-stranded DNA. TopBP1 contains six copies of BRCT domain. The family corresponds to the seventh BRCT domain. The Trp-X-X-X-Cys/Ser signature motif of the BRCT family is missing in this group.


Pssm-ID: 349370 [Multi-domain]  Cd Length: 75  Bit Score: 42.17  E-value: 1.16e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958660160 1600 VSGLTPKEVMIVQKFAEKY--RLALTDVITEETTHVIIKTDAefvceRTLKYFLGIAGGKWIVSYSWVIKSIQE 1671
Cdd:cd17738      6 LSGFSEDEKKELISIIEKLggKVLDSDEFDPKCTHLICGKPS-----RSEKFLAACAAGKWILHPSYIEASAKA 74
RING-HC_UHRF cd16613
RING finger, HC subclass, found in ubiquitin-like PHD and RING finger domain-containing ...
23-69 1.28e-04

RING finger, HC subclass, found in ubiquitin-like PHD and RING finger domain-containing proteins, UHRF1 and UHRF2, and similar proteins; UHRF1 is a unique chromatin effector protein that integrates the recognition of both histone PTMs and DNA methylation. It is essential for cell proliferation and plays a critical role in the development and progression of many human carcinomas, such as laryngeal squamous cell carcinoma (LSCC), gastric cancer (GC), esophageal squamous cell carcinoma (ESCC), colorectal cancer, prostate cancer, and breast cancer. UHRF1 acts as a transcriptional repressor through its binding to histone H3 when it is unmodified at Arg2. Its overexpression in human lung fibroblasts results in downregulation of expression of the tumor suppressor pRB. It also plays a role in transcriptional repression of the cell cycle regulator p21. Moreover, UHRF1-dependent repression of transcription factors can facilitate the G1-S transition. It interacts with Tat-interacting protein of 60 kDa (TIP60) and induces degradation-independent ubiquitination of TIP60. It is also an N-methylpurine DNA glycosylase (MPG)-interacting protein that binds MPG in a p53 status-independent manner in the DNA base excision repair (BER) pathway. In addition, UHRF1 functions as an epigenetic regulator that is important for multiple aspects of epigenetic regulation, including maintenance of DNA methylation patterns and recognition of various histone modifications. UHRF2 was originally identified as a ubiquitin ligase acting as a small ubiquitin-like modifier (SUMO) E3 ligase that enhances zinc finger protein 131 (ZNF131) SUMOylation, but does not enhance ZNF131 ubiquitination. It also ubiquitinates PCNP, a PEST-containing nuclear protein. Moreover, UHRF2 functions as a nuclear protein involved in cell-cycle regulation and has been implicated in tumorigenesis. It interacts with cyclins, CDKs, p53, pRB, PCNA, HDAC1, DNMTs, G9a, methylated histone H3 lysine 9, and methylated DNA. It interacts with the cyclin E-CDK2 complex, ubiquitinates cyclins D1 and E1, induces G1 arrest, and is involved in the G1/S transition regulation. Furthermore, UHRF2 is a direct transcriptional target of the transcription factor E2F-1 in the induction of apoptosis. It recruits HDAC1 and binds to methyl-CpG. UHRF2 also participates in the maturation of Hepatitis B virus (HBV) by interacting with the HBV core protein and promoting its degradation. Both UHRF1 and UHRF2 contain an N-terminal ubiquitin-like domain (UBL), a tandem Tudor domain (TTD), a plant homeodomain (PHD) finger, a SET- and RING-associated (SRA) domain, and a C-terminal C3HC4-type RING-HC finger.


Pssm-ID: 438275 [Multi-domain]  Cd Length: 46  Bit Score: 41.18  E-value: 1.28e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1958660160   23 ECPICLELIKEPVSTKCDHIFCKFCMLKLLnqKKGPSQCPLCKNEIT 69
Cdd:cd16613      2 TCICCQELVYKPITTPCKHNICKSCLQRSF--KAEVYTCPACRHDLG 46
RING-HC_MID2 cd16754
RING finger, HC subclass, found in midline-2 (MID2) and similar proteins; MID2, also known as ...
15-69 1.40e-04

RING finger, HC subclass, found in midline-2 (MID2) and similar proteins; MID2, also known as midin-2, midline defect 2, RING finger protein 60 (RNF60), or tripartite motif-containing protein 1 (TRIM1), is a probable E3 ubiquitin-protein ligase and is highly related to MID1 that associates with cytoplasmic microtubules along their length and throughout the cell cycle. Like MID1, MID2 associates with the microtubule network and may at least partially compensate for the loss of MID1. Both MID1 and MID2 interacts with Alpha 4, which is a regulatory subunit of PP2-type phosphatases, such as PP2A, and an integral component of the rapamycin-sensitive signaling pathway. MID2 can also substitute for MID1 to control exocytosis of lytic granules in cytotoxic T cells. Loss-of-function mutations in MID2 lead to the human X-linked intellectual disability (XLID). MID2 belongs to the C-I subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxy-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. MID2 hetero-dimerizes in vitro with its paralog MID1.


Pssm-ID: 438412 [Multi-domain]  Cd Length: 70  Bit Score: 41.89  E-value: 1.40e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958660160   15 LHAMQKILECPICLELIKEPVSTKCDHIFCKFCMLKLL-------NQKKGPS--QCPLCKNEIT 69
Cdd:cd16754      1 METLESELTCPICLELFEDPLLLPCAHSLCFSCAHRILtsgcasgESIEPPSafQCPTCRYVIS 64
RING-HC_Bre1-like cd16499
RING finger, HC subclass, found in yeast Bre1 and its homologs from eukaryotes; Bre1 is an E3 ...
17-65 1.80e-04

RING finger, HC subclass, found in yeast Bre1 and its homologs from eukaryotes; Bre1 is an E3 ubiquitin-protein ligase that catalyzes monoubiquitination of histone H2B in concert with the E2 ubiquitin-conjugating enzyme, Rad6. The Rad6-Bre1-mediated histone H2B ubiquitylation modulates the formation of double-strand breaks (DSBs) during meiosis in yeast. it is also required, indirectly, for the methylation of histone 3 on lysine 4 (H3K4) and 79. RNF20, also known as BRE1A and RNF40, also known as BRE1B, are the mammalian homologs of Bre1. They work together to form a heterodimeric Bre1 complex that facilitate the K120 monoubiquitination of histone H2B (H2Bub1), a DNA damage-induced histone modification that is crucial for recruitment of the chromatin remodeler SNF2h to DNA double-strand break (DSB) damage sites. Moreover, the Bre1 complex acts as a tumor suppressor, augmenting expression of select tumor suppressor genes and suppressing select oncogenes. Deficiency in the mammalian histone H2B ubiquitin ligase Bre1 leads to replication stress and chromosomal instability. All subfamily members contain a C3HC4-type RING-HC finger at its C-terminus.


Pssm-ID: 438162 [Multi-domain]  Cd Length: 59  Bit Score: 41.00  E-value: 1.80e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1958660160   17 AMQKILECPICLELIKEPVSTKCDHIFCKFCMLKLLN--QKKgpsqCPLCK 65
Cdd:cd16499      2 DLRELLKCSVCNDRFKDVIITKCGHVFCNECVQKRLEtrQRK----CPGCG 48
RING-HC_SH3RF1 cd16748
RING finger, HC subclass, found in SH3 domain-containing RING finger protein 1 (SH3RF1) and ...
21-65 2.02e-04

RING finger, HC subclass, found in SH3 domain-containing RING finger protein 1 (SH3RF1) and similar proteins; SH3RF1, also known as plenty of SH3s (POSH), RING finger protein 142 (RNF142), or SH3 multiple domains protein 2 (SH3MD2), is a trans-Golgi network-associated pro-apoptotic scaffold protein with E3 ubiquitin-protein ligase activity. It also plays a role in calcium homeostasis through the control of the ubiquitin domain protein Herp. It may also have a role in regulating death receptor mediated and c-Jun N-terminal kinase (JNK) mediated apoptosis, linking Rac1 to downstream components. SH3RF1 also enhances the ubiquitination of ROMK1 potassium channel resulting in its increased endocytosis. Moreover, SH3RF1 assembles an inhibitory complex with the actomyosin regulatory protein Shroom3, which links to the actin-myosin network to regulate neuronal process outgrowth. It also forms a complex with apoptosis-linked gene-2 (ALG-2) and ALG-2-interacting protein (ALIX/AIP1) in a calcium-dependent manner to play a role in the regulation of the JNK pathway. Furthermore, direct interaction of SH3RF1 and another molecular scaffold JNK-interacting protein (JIP) is required for apoptotic activation of JNKs. Interaction of SH3RF1 and E3 ubiquitin-protein isopeptide ligases, Siah proteins, further promotes JNK activation and apoptosis. In addition, SH3RF1 binds to and degrades TAK1, a crucial activator of both the JNK and the Relish signaling pathways. SH3RF1 contains an N-terminal C3HC4-type RING-HC finger responsible for the E3 ligase activity and four Src Homology 3 (SH3) domains, which are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs.


Pssm-ID: 438406 [Multi-domain]  Cd Length: 48  Bit Score: 40.76  E-value: 2.02e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1958660160   21 ILECPICLELIKEPVST-KCDHIFCKFCMLKLLNQkKGPSQCPLCK 65
Cdd:cd16748      2 LLECPVCLERLDATAKVlPCQHTFCRRCLLGIVGS-RSELRCPECR 46
RING-HC_TRIM13_like_C-V cd16581
RING finger, HC subclass, found in tripartite motif-containing proteins TRIM13, TRIM59 and ...
22-65 2.05e-04

RING finger, HC subclass, found in tripartite motif-containing proteins TRIM13, TRIM59 and similar proteins; TRIM13 and TRIM59, two closely related tripartite motif-containing proteins, belong to the C-V subclass of the TRIM (tripartite motif) family of proteins that are defined by an N-terminal RBCC (RING, Bbox, and coiled coil) domain, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, followed by a C-terminal transmembrane domain. TRIM13, also known as B-cell chronic lymphocytic leukemia tumor suppressor Leu5, leukemia-associated protein 5, putative tumor suppressor RFP2, RING finger protein 77 (RNF77), or Ret finger protein 2, is an endoplasmic reticulum (ER) membrane anchored E3 ubiquitin-protein ligase that interacts with proteins localized to the ER, including valosin-containing protein (VCP), a protein indispensable for ER-associated degradation (ERAD). TRIM59, also known as RING finger protein 104 (RNF104) or tumor suppressor TSBF-1, is a putative E3 ubiquitin-protein ligase that functions as a novel multiple cancer biomarker for immunohistochemical detection of early tumorigenesis.


Pssm-ID: 438243 [Multi-domain]  Cd Length: 50  Bit Score: 40.57  E-value: 2.05e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1958660160   22 LECPICLELIKEPVSTKCDHIFCKFCMLKLL----NQKKGPSQCPLCK 65
Cdd:cd16581      3 LTCSICYNIFDDPKILPCSHTFCKNCLEKLLaasgYYLLASLKCPTCR 50
RING-HC_TRIM17_C-IV cd16595
RING finger, HC subclass, found in tripartite motif-containing protein TRIM17 and similar ...
18-74 2.13e-04

RING finger, HC subclass, found in tripartite motif-containing protein TRIM17 and similar proteins; TRIM17, also known as RING finger protein 16 (RNF16) or testis RING finger protein (Terf), is a crucial E3 ubiquitin ligase that is necessary and sufficient for neuronal apoptosis and contributes to Mcl-1 ubiquitination in cerebellar granule neurons (CGNs). It interacts in a SUMO-dependent manner with nuclear factor of activated T cell NFATc3 transcription factor, and thus inhibits the activity of NFATc3 by preventing its nuclear localization. In contrast, it binds to and inhibits NFATc4 transcription factor in a SUMO-independent manner. Moreover, TRIM17 stimulates degradation of kinetochore protein ZW10 interacting protein (ZWINT), a known component of the kinetochore complex required for the mitotic spindle checkpoint, and negatively regulates cell proliferation. TRIM17 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438257 [Multi-domain]  Cd Length: 70  Bit Score: 41.13  E-value: 2.13e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958660160   18 MQKILECPICLELIKEPVSTKCDHIFCKFCM---------LKLLNQKKGPSQCPLCKNEITKRSLQ 74
Cdd:cd16595      2 LQEEATCSICLDYFTDPVMTTCGHNFCRACIqlswekargKKGRRKQKGSFPCPECREMSPQRNLR 67
RING-HC_RNFT2 cd16742
RING finger, HC subclass, found in RING finger and transmembrane domain-containing protein 2 ...
24-70 2.21e-04

RING finger, HC subclass, found in RING finger and transmembrane domain-containing protein 2(RNFT2); RNFT2, also known as transmembrane protein 118 (TMEM118), is a multi-pass membrane protein containing a C3HC4-type RING-HC finger. Its biological role remains unclear.


Pssm-ID: 438400 [Multi-domain]  Cd Length: 67  Bit Score: 41.02  E-value: 2.21e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1958660160   24 CPICLELIKEPVSTKCDHIFCKFCMLKLLNQKKgpsQCPLCKNEITK 70
Cdd:cd16742     16 CAICQAEFREPLILICQHVFCEECLCLWFDRER---TCPLCRSVVVE 59
RING-HC_RNF4 cd16533
RING finger, HC subclass, found in RING finger protein 4 (RNF4) and similar proteins; RNF4, ...
22-71 2.30e-04

RING finger, HC subclass, found in RING finger protein 4 (RNF4) and similar proteins; RNF4, also known as small nuclear ring finger protein (SNURF), is a SUMO-targeted E3 ubiquitin-protein ligase with a pivotal function in the DNA damage response (DDR) by interacting with the deubiquitinating enzyme ubiquitin-specific protease 11 (USP11), a known DDR-component, and further facilitating DNA repair. It plays a novel role in preventing the loss of intact chromosomes and ensures the maintenance of chromosome integrity. Moreover, RNF4 is responsible for the UbcH5A-catalyzed formation of K48 chains that target SUMO-modified promyelocytic leukemia (PML) protein for proteasomal degradation in response to arsenic treatment. It also interacts with telomeric repeat binding factor 2 (TRF2) in a small ubiquitin-like modifier (SUMO)-dependent manner and preferentially targets SUMO-conjugated TRF2 for ubiquitination through SUMO-interacting motifs (SIMs). Furthermore, RNF4 can form a complex with a Ubc13-ubiquitin conjugate and Ube2V2. It catalyzes K63-linked polyubiquitination by the Ube2V2-Ubc13 (ubiquitin-loaded) complex. Meanwhile, RNF4 negatively regulates nuclear factor kappa B (NF-kappaB) signaling by down-regulating transforming growth factor beta (TGF-beta)-activated kinase 1 (TAK1)-TAK1-binding protein2 (TAB2). RNF4 contains four SIMs followed by a C3HC4-type RING-HC finger at the C-terminus.


Pssm-ID: 438195 [Multi-domain]  Cd Length: 57  Bit Score: 40.65  E-value: 2.30e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958660160   22 LECPICLELIKE-------PVSTKCDHIFCKFCMLKLLnqkKGPSQCPLCKNEITKR 71
Cdd:cd16533      4 VSCPICMDGYSEivqsgrlIVSTECGHVFCSQCLRDSL---KNANTCPTCRKKLNHK 57
mRING-HC-C3HC3D_TRAF5 cd16642
Modified RING finger, HC subclass (C3HC3D-type), found in tumor necrosis factor (TNF) ...
24-68 2.75e-04

Modified RING finger, HC subclass (C3HC3D-type), found in tumor necrosis factor (TNF) receptor-associated factor 5 (TRAF5) and similar proteins; TRAF5, also known as RING finger protein 84 (RNF84), is an important signal transducer for a wide range of TNF receptor superfamily members, including tumor necrosis factor receptor 1 (TNFR1), TNFR2, CD40, and other lymphocyte costimulatory receptors, RANK/TRANCE-R, ectodysplasin-A Receptor (EDAR), lymphotoxin-beta receptor (LT-betaR), latent membrane protein 1 (LMP1), and IRE1. It functions as an activator of NF-kappaB, MAPK, and JNK, and is involved in both RANKL- and TNFalpha-induced osteoclastogenesis. It mediates CD40 signaling by associating with the cytoplasmic tail of CD40. It also negatively regulates Toll-like receptor (TLR) signaling and functions as a negative regulator of the interleukin 6 (IL-6) receptor signaling pathway that limits the differentiation of inflammatory CD4(+) T cells. TRAF5 contains an N-terminal domain with a modified C3HC3D-type RING-HC finger and several zinc fingers, and a C-terminal TRAF domain that comprises a coiled coil domain and a conserved TRAF-C domain.


Pssm-ID: 438304 [Multi-domain]  Cd Length: 56  Bit Score: 40.50  E-value: 2.75e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1958660160   24 CPICLELIKEPVSTKCDHIFCKFCMLKLLNQKKGPsQCPLCKNEI 68
Cdd:cd16642      7 CATCHFVLHNPHQTGCGHRFCQHCILSLLELNTTP-ICPIDKETI 50
RING-H2_RNF139-like cd16476
RING finger, H2 subclass, found in RING finger proteins RNF139, RNF145, and similar proteins; ...
24-64 3.06e-04

RING finger, H2 subclass, found in RING finger proteins RNF139, RNF145, and similar proteins; RNF139, also known as translocation in renal carcinoma on chromosome 8 protein (TRC8), is an endoplasmic reticulum (ER)-resident multi-transmembrane protein that functions as a potent growth suppressor in mammalian cells, inducing G2/M arrest, decreased DNA synthesis and increased apoptosis. It is a tumor suppressor that has been implicated in a novel regulatory relationship linking the cholesterol/lipid biosynthetic pathway with cellular growth control. A mutation in RNF139 has been identified in families with hereditary renal (RCC) and thyroid cancers. RNF145 is an uncharacterized RING finger protein encoded by the RNF145 gene, which is expressed in T lymphocytes, and its expression is altered in acute myelomonocytic and acute promyelocytic leukemias. Although its biological function remains unclear, RNF145 shows high sequence similarity with RNF139. Both RNF139 and RNF145 contain a C3H2C3-type RING-H2 finger with possible E3-ubiquitin ligase activity.


Pssm-ID: 438139 [Multi-domain]  Cd Length: 41  Bit Score: 39.75  E-value: 3.06e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1958660160   24 CPICLELIKEPVSTKCDHIFCKFCMLKLLNQKKgpsQCPLC 64
Cdd:cd16476      3 CAICYQEMKEARITPCNHFFHGLCLRKWLYVQD---TCPLC 40
RING-HC_ORTHRUS_rpt2 cd23139
second RING finger, HC subclass, found in Arabidopsis thaliana ORTHRUS and similar proteins; ...
24-69 3.09e-04

second RING finger, HC subclass, found in Arabidopsis thaliana ORTHRUS and similar proteins; This subfamily includes Arabidopsis thaliana ORTHRUS 1-5. They are E3 ubiquitin-protein ligases that may participate in CpG methylation-dependent transcriptional regulation and/or epigenetic transcriptional silencing. ORTHRUS 1 mediates ubiquitination with the E2 ubiquitin-conjugating enzymes UBC11, UBC8 and UBC8 homologs (e.g. UBC10, UBC11, UBC28 and UBC29) but not with UBC27, UBC30, UBC32, UBC34 and UBC36. ORTHRUS 2 and 5 mediate ubiquitination with the E2 ubiquitin-conjugating enzyme UBC11. ORTHRUS 1 and 2 promote methylation-mediated gene silencing leading, for example, to early flowering. They can bind to CpG, CpNpG, and CpNpN DNA motifs, with a strong preference for methylated forms, and with highest affinity for CpG substrates. Members of this subfamily contain two typical C3HC4-type RING-HC fingers. This model corresponds to the second one.


Pssm-ID: 438501 [Multi-domain]  Cd Length: 72  Bit Score: 40.91  E-value: 3.09e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958660160   24 CPICLELIKEPVSTKCDHIFCKFCML----------------KLLNQKKGPSQCPLCKNEIT 69
Cdd:cd23139      8 CQICKKVLSLPVSTPCGHNFCKACLEakfagiadvrdrgnggRSLRARKNVKPCPCCKTDIS 69
RING-HC_SIAHs cd16571
RING finger, HC subclass, found in Drosophila melanogaster protein Seven-in-Absentia (sina) ...
22-65 3.46e-04

RING finger, HC subclass, found in Drosophila melanogaster protein Seven-in-Absentia (sina) and its homologs; This subfamily includes the Drosophila melanogaster protein Seven-in-Absentia (sina), its mammalian orthologs, SIAH1 and SIAH2, plant SINA-related proteins, and similar proteins. Sina plays an important role in the phyllopod-dependent degradation of the transcriptional repressor tramtrack to allow the formation of the R7 photoreceptor in the developing eye of Drosophila melanogaster. Both SIAH1 and SIAH2 are E3 ubiquitin-protein ligases, mediating the ubiquitinylation and subsequent proteasomal degradation of biologically important target proteins that regulate general functions, such as cell cycle control, apoptosis, and DNA repair. They are inducible by the tumor suppressor and transcription factor p53. SIAH2 can also be regulated by sex hormones and cytokine signaling. Moreover, they share high sequence similarity, but possess contrary roles in cancer, with SIAH1 more often acting as a tumor suppressor while SIAH2 functions as a proto-oncogene. Plant SINAT1-5 are putative E3 ubiquitin ligases involved in the regulation of stress responses. All subfamily members possess two characteristic domains, an N-terminal C3HC4-type RING-HC finger and a C-terminal tumor necrosis factor (TNF) receptor associated factor (TRAF)-like substrate-binding domain (SBD).


Pssm-ID: 438233 [Multi-domain]  Cd Length: 39  Bit Score: 39.55  E-value: 3.46e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1958660160   22 LECPICLELIKEPVsTKCD--HIFCKFCMLKLLNqkkgpsQCPLCK 65
Cdd:cd16571      1 LECPVCFEPLLPPI-YQCSngHLLCSSCRSKLTN------KCPTCR 39
RING-HC_ZNF598 cd16615
RING finger, HC subclass, found in zinc finger protein 598 (ZNF598) and similar proteins; ...
23-70 3.65e-04

RING finger, HC subclass, found in zinc finger protein 598 (ZNF598) and similar proteins; ZNF598 associates with eukaryotic initiation factor 4E (eIF4E) homologous protein from mammals (m4EHP) by binding to Grb10-interacting GYF protein 2 (GIGYF2). The m4EHP-GIGYF2 complex functions as a translational repressor and is essential for normal embryonic development of mammalian. ZNF598 harbors a C3HC4-type RING-HC finger at its N-terminus.


Pssm-ID: 438277 [Multi-domain]  Cd Length: 51  Bit Score: 39.90  E-value: 3.65e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1958660160   23 ECPICLELIKEPVSTKCDHIFCKFCMLK---LLNQKKgpsqCPLCKNEITK 70
Cdd:cd16615      2 TCVICCEEIEYFAVGPCNHPVCYKCSLRmrvLYKDKY----CPICRTELDK 48
mRING-C3HGC3_RFWD3 cd16450
Modified RING finger, C3HGC3-type, found in RING finger and WD repeat domain-containing ...
23-72 3.88e-04

Modified RING finger, C3HGC3-type, found in RING finger and WD repeat domain-containing protein 3 (RFWD3) and similar proteins; RFWD3, also known as RING finger protein 201 (RNF201) or FLJ10520, is an E3 ubiquitin-protein ligase that forms a complex with Mdm2 and p53 to synergistically ubiquitinate p53 and acts as a positive regulator of p53 stability in response to DNA damage. It is phosphorylated by checkpoint kinase ATM/ATR and the phosphorylation mutant fails to stimulate p53 ubiquitination. RFWD3 also functions as a novel replication protein A (RPA)-associated protein involved in DNA replication checkpoint control. RFWD3 contains an N-terminal SQ-rich region followed by a RING finger domain that exhibits robust E3 ubiquitin ligase activity toward p53, a coiled-coil domain and three WD40 repeats in the C-terminus, the latter two of which may be responsible for protein-protein interaction. The RING finger in this family is a modified C3HGC3-type RING finger, but not a canonical C3H2C3-type RING-H2 finger or C3HC4-type RING-HC finger.


Pssm-ID: 438114 [Multi-domain]  Cd Length: 61  Bit Score: 40.29  E-value: 3.88e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958660160   23 ECPICLELIKEP-----VSTKCDHIFCKFCMLKLLNQKKGpsQCPLCkNEITKRS 72
Cdd:cd16450      4 TCPICFEPWTSSgehrlVSLKCGHLFGYSCIEKWLKGKGK--KCPQC-NKKAKRS 55
RING-HC_RAD16-like cd16567
RING finger, HC subclass, found in Saccharomyces cerevisiae DNA repair protein RAD16, ...
22-64 4.60e-04

RING finger, HC subclass, found in Saccharomyces cerevisiae DNA repair protein RAD16, Schizosaccharomyces pombe rhp16, and similar proteins; Budding yeast RAD16, also known as ATP-dependent helicase RAD16, is encoded by a yeast excision repair gene homologous to the recombinational repair gene RAD54 and to the SNF2 gene involved in transcriptional activation. It is a component of the global genome repair (GGR) complex that promotes global genome nucleotide excision repair (GG-NER) by removing DNA damage from non-transcribing DNA. RAD16 is involved in differential repair of DNA after UV damage, and repairs preferentially the MAT-alpha locus compared with the HML-alpha locus. Fission yeast rhp16, also known as ATP-dependent helicase rhp16, is a RAD16 homolog. It is involved in GGR via nucleotide excision repair (NER), in conjunction with rhp7, after UV irradiation. Both RAD16 and rhp16 contain a C3HC4-type RING-HC finger, as well as a DEAD-like helicase domain and a helicase superfamily C-terminal domain.


Pssm-ID: 438229 [Multi-domain]  Cd Length: 48  Bit Score: 39.63  E-value: 4.60e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1958660160   22 LECPICLELIKEPVSTKCDHIFCKFCMLKLLNQ-KKGPSQCPLC 64
Cdd:cd16567      1 LVCGICHEEAEDPVVARCHHVFCRACVKEYIESaPGGKVTCPTC 44
RING-HC_TRIM62_C-IV cd16608
RING finger, HC subclass, found in tripartite motif-containing protein 62 (TRIM62) and similar ...
22-65 5.23e-04

RING finger, HC subclass, found in tripartite motif-containing protein 62 (TRIM62) and similar proteins; TRIM62, also known as Ductal Epithelium Associated Ring Chromosome 1 (DEAR1), is a cytoplasmic E3 ubiquitin-protein ligase that was identified as a dominant regulator of acinar morphogenesis in the mammary gland. It is implicated in the inflammatory response of immune cells by regulating the Toll-like receptor 4 (TLR4) signaling pathway, leading to increased activity of the activator protein 1 (AP-1) transcription factor in primary macrophages. It is also involved in muscular protein homeostasis, especially during inflammation-induced atrophy, and may play a role in the pathogenesis of ICU-acquired weakness (ICUAW) by activating and maintaining inflammation in myocytes. Moreover, TRIM62 facilitates K27-linked poly-ubiquitination of CARD9 and also regulates CARD9-mediated anti-fungal immunity and intestinal inflammation. It also functions as a chromosome 1p35 tumor suppressor and negatively regulates transforming growth factor beta (TGFbeta)-driven epithelial-mesenchymal transition (EMT) by binding to and promoting the ubiquitination of SMAD3, a major effector of TGFbeta-mediated EMT. TRIM62 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438270 [Multi-domain]  Cd Length: 52  Bit Score: 39.41  E-value: 5.23e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1958660160   22 LECPICLELIKEPVSTKCDHIFCKFCMLKLLNQKKGpSQCPLCK 65
Cdd:cd16608      7 LLCSICLSIYQDPVSLGCEHYFCRQCITEHWSRSEH-RDCPECR 49
RING-HC_PML_C-V cd16579
RING finger, HC subclass, found in promyelocytic leukemia protein (PML) and similar proteins; ...
20-65 6.89e-04

RING finger, HC subclass, found in promyelocytic leukemia protein (PML) and similar proteins; Protein PML, also known as RING finger protein 71 (RNF71) or tripartite motif-containing protein 19 (TRIM19), is predominantly a nuclear protein with a broad intrinsic antiviral activity. It is the eponymous component of PML nuclear bodies (PML NBs) and has been implicated in a wide variety of cell processes, including DNA damage signaling, apoptosis, and transcription. PML interferes with the replication of many unrelated viruses, including human immunodeficiency virus 1 (HIV-1), human foamy virus (HFV), poliovirus, influenza virus, rabies virus, EMCV, adeno-associated virus (AAV), and vesicular stomatitis virus (VSV). It also selectively interacts with misfolded proteins through distinct substrate recognition sites and conjugates these proteins with the small ubiquitin-like modifiers (SUMOs) through its SUMO ligase activity. PML belongs to the C-V subclass of the TRIM (tripartite motif) family of proteins that are defined by an N-terminal RBCC (RING, Bbox, and coiled coil) domain, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as an uncharacterized region positioned C-terminal to the RBCC domain.


Pssm-ID: 438241 [Multi-domain]  Cd Length: 52  Bit Score: 39.08  E-value: 6.89e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1958660160   20 KILECPICLELIKEPVSTKCDHIFCKFCMLKLLNQKKGPS--QCPLCK 65
Cdd:cd16579      3 KFLRCPGCKAEYKCPKLLPCLHTVCSGCLEALAEQASETTefQCPICK 50
RING-HC_TRIM56_C-V cd16584
RING finger, HC subclass, found in tripartite motif-containing protein 56 (TRIM56) and similar ...
22-68 6.94e-04

RING finger, HC subclass, found in tripartite motif-containing protein 56 (TRIM56) and similar proteins; TRIM56, also known as RING finger protein 109 (RNF109), is a virus-inducible E3 ubiquitin ligase that restricts pestivirus infection. It positively regulates the Toll-like receptor 3 (TLR3) antiviral signaling pathway, and possesses antiviral activity against bovine viral diarrhea virus (BVDV), a ruminant pestivirus classified within the family Flaviviridae shared by tick-borne encephalitis virus (TBEV). It also possesses antiviral activity against two classical flaviviruses, yellow fever virus (YFV) and dengue virus (DENV), as well as a human coronavirus, HCoV-OC43, which is responsible for a significant share of common cold cases. It may not act on positive-strand RNA viruses indiscriminately. Moreover, TRIM56 is an interferon-inducible E3 ubiquitin ligase that modulates STING to confer double-stranded DNA-mediated innate immune responses. TRIM56 belongs to the C-V subclass of the TRIM (tripartite motif) family of proteins that are defined by an N-terminal RBCC (RING, Bbox, and coiled coil) domain, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as an uncharacterized region positioned C-terminal to the RBCC domain.


Pssm-ID: 438246 [Multi-domain]  Cd Length: 56  Bit Score: 39.20  E-value: 6.94e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1958660160   22 LECPICLELIKEPVSTKCDHIFCKFCMLKLLNQKKgpSQCPLCKNEI 68
Cdd:cd16584      2 LACKICLEQLRAPKTLPCLHTYCQDCLAQLADGGR--VRCPECRETV 46
RING-HC_NHL-1-like cd16524
RING finger, HC subclass, found in Caenorhabditis elegans RING finger protein NHL-1 and ...
18-67 7.08e-04

RING finger, HC subclass, found in Caenorhabditis elegans RING finger protein NHL-1 and similar proteins; NHL-1 functions as an E3 ubiquitin-protein ligase in the presence of both UBC-13 and UBC-1 within the ubiquitin pathway of Caenorhabditis elegans. It acts in chemosensory neurons to promote stress resistance in distal tissues by the transcription factor DAF-16 activation but is dispensable for the activation of heat shock factor 1 (HSF-1). NHL-1 belongs to the TRIM (tripartite motif)-NHL family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil domain, as well as an NHL (named after proteins NCL-1, HT2A and Lin-41 that contain repeats folded into a six-bladed beta propeller) repeat domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438187 [Multi-domain]  Cd Length: 53  Bit Score: 39.33  E-value: 7.08e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1958660160   18 MQKILECPICLELIKEPVSTKCDHIFC-KFCMLKLLNQKKGPSQCPLCKNE 67
Cdd:cd16524      2 IEQLLTCPICLDRYRRPKLLPCQHTFClSPCLEGLVDYVTRKLKCPECRAE 52
BRCT_MDC1_rpt1 cd17744
first BRCT domain of mediator of DNA damage checkpoint protein 1 (MDC1) and similar proteins; ...
1596-1675 7.47e-04

first BRCT domain of mediator of DNA damage checkpoint protein 1 (MDC1) and similar proteins; MDC1, also termed nuclear factor with BRCT domains 1 (NFBD1), is a nuclear chromatin-associated protein that is required for checkpoint mediated cell cycle arrest in response to DNA damage within both the S phase and G2/M phases of the cell cycle. It directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks. MDC1 contains a forkhead-associated (FHA) domain and two BRCT domains, as well as an internal 41-amino acid repeat sequence. The family corresponds to the first BRCT domain.


Pssm-ID: 349375  Cd Length: 72  Bit Score: 39.52  E-value: 7.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660160 1596 ISMVVSGLTPKEvmIVQKFAEKYRLALTDVItEETTHVIIKTDaefvcERTLKYFLGIAGGKWIVSYSWVIKSIQERKLL 1675
Cdd:cd17744      1 PRVLFTGVSDKE--EGEKIIKKLGGSVVDSV-EDCTHLVTDKV-----RRTVKFLCALARGIPIVSPDWLEASIKANKFL 72
RING-HC_CHFR cd16503
RING finger, HC subclass, found in checkpoint with forkhead and RING finger domains protein ...
22-70 8.15e-04

RING finger, HC subclass, found in checkpoint with forkhead and RING finger domains protein (CHFR); CHFR, also known as RING finger protein 196 (RNF196), is a checkpoint protein that delays entry into mitosis in response to stress. It functions as an E3 ubiquitin ligase that ubiquitinates and degrades its target proteins, such as Aurora-A, Plk1, Kif22, and PARP-1, which are critical for proper mitotic transitions. It also plays an important role in cell cycle progression and tumor suppression, and is negatively regulated by SUMOylation-mediated proteasomal ubiquitylation. Moreover, CHFR is involved in the early stage of the DNA damage response, which mediates the crosstalk between ubiquitination and poly-ADP-ribosylation. CHFR contains a fork head associated (FHA) domain and a C3HC4-type RING-HC finger.


Pssm-ID: 438166 [Multi-domain]  Cd Length: 55  Bit Score: 38.89  E-value: 8.15e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958660160   22 LECPICLELIKEPVSTK-CDHIFCKFCMLKLLNQKKgpSQCPLCKNEITK 70
Cdd:cd16503      3 LTCSICQDLLHDCVSLQpCMHNFCAACYSDWMERSN--TECPTCRATVQR 50
RING-H2_PA-TM-RING cd16454
RING finger, H2 subclass, found in the PA-TM-RING ubiquitin ligase family; The PA-TM-RING ...
23-65 9.56e-04

RING finger, H2 subclass, found in the PA-TM-RING ubiquitin ligase family; The PA-TM-RING family represents a group of transmembrane-type E3 ubiquitin ligases, which has been characterized by an N-terminal transient signal peptide, a PA (protease-associated) domain, a TM (transmembrane) domain, as well as a C-terminal C3H2C3-type RING-H2 finger domain. It includes RNF13, RNF167, ZNRF4 (zinc and RING finger 4), GRAIL (gene related to anergy in lymphocytes)/RNF128, RNF130, RNF133, RNF148, RNF149 and RNF150 (which are more closely related), as well as RNF43 and ZNRF3, which have substantially longer C-terminal tail extensions compared with the others. PA-TM-RING proteins are expressed at low levels in all mammalian tissues and species, but they are not present in yeast. They play a common regulatory role in intracellular trafficking/sorting, suggesting that abrogation of their function may result in dysregulation of cellular signaling events in cancer.


Pssm-ID: 438118 [Multi-domain]  Cd Length: 43  Bit Score: 38.41  E-value: 9.56e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1958660160   23 ECPICLELIKEPVSTK---CDHIFCKFCMLKLLNQKkgpSQCPLCK 65
Cdd:cd16454      1 TCAICLEEFKEGEKVRvlpCNHLFHKDCIDPWLEQH---NTCPLCR 43
RING-HC_LNX3-like cd16512
RING finger, HC subclass, found in ligand of Numb protein LNX3, LNX4, and similar proteins; ...
22-63 9.68e-04

RING finger, HC subclass, found in ligand of Numb protein LNX3, LNX4, and similar proteins; The ligand of Numb protein X (LNX) family, also known as PDZ and RING (PDZRN) family, includes LNX1-5, which can interact with Numb, a key regulator of neurogenesis and neuronal differentiation. LNX5 (also known as PDZK4, or PDZRN4L) shows high sequence homology to LNX3 and LNX4, but it lacks the RING domain. LNX1-4 proteins function as E3 ubiquitin ligases and have a unique domain architecture consisting of an N-terminal RING-HC finger for E3 ubiquitin ligase activity and either two or four PDZ domains necessary for the substrate-binding. This family corresponds to LNX3/LNX4-like proteins, which contains a C3HC4-type RING-HC finger and two PDZ domains.


Pssm-ID: 438175 [Multi-domain]  Cd Length: 43  Bit Score: 38.55  E-value: 9.68e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1958660160   22 LECPICLELIKEPVSTKCDHIFCKFCMLKLLNQKkgpSQCPL 63
Cdd:cd16512      1 LKCKLCLGVLEEPLATPCGHVFCAGCVLPWVVRN---GSCPL 39
RING-HC_DTX3L cd16712
RING finger, HC subclass, found in protein Deltex-3-like (DTX3L) and similar proteins; DTX3L, ...
19-64 9.94e-04

RING finger, HC subclass, found in protein Deltex-3-like (DTX3L) and similar proteins; DTX3L, also known as B-lymphoma- and BAL-associated protein (BBAP) or Rhysin-2 (Rhysin2), is a RING-domain E3 ubiquitin-protein ligase that regulates endosomal sorting of the G protein-coupled receptor CXCR4 from endosomes to lysosomes. It also regulates subcellular localization of its partner protein, B aggressive lymphoma (BAL), by a dynamic nucleocytoplasmic trafficking mechanism. DTX3L has a unique N-terminus, but lacks the highly basic N-terminal motif and the central proline-rich motif present in other Deltex (DTX) family members, such as DTX1, DTX2, and DTX4. Moreover, its C-terminal region is highly homologous to DTX3. It includes a C3HC4-type RING-HC finger, and a previously unidentified C-terminal domain. DTX3L can associate with DTX1 through its unique N-terminus and further enhance self-ubiquitination.


Pssm-ID: 438372 [Multi-domain]  Cd Length: 56  Bit Score: 38.95  E-value: 9.94e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1958660160   19 QKILECPICLELIKEP-VSTKCDHIFCKFCMLKLLNQKkgpSQCPLC 64
Cdd:cd16712      1 QEEDECPICMDRISNKkVLPKCKHVFCAACIDKAMKYK---PVCPVC 44
RING-H2_RHA1-like cd23121
RING finger, H2 subclass, found in Arabidopsis thaliana RING-H2 finger A1a (RHA1A), A1b (RHA1B) ...
23-67 1.00e-03

RING finger, H2 subclass, found in Arabidopsis thaliana RING-H2 finger A1a (RHA1A), A1b (RHA1B) and similar proteins; This subfamily includes Arabidopsis thaliana RHA1A, RHA1B and XERICO. RHA1A is a probable E3 ubiquitin-protein ligase that may possess E3 ubiquitin ligase activity in vitro. RHA1B possesses E3 ubiquitin-protein ligase activity when associated with the E2 enzyme UBC8 in vitro. XERICO functions on abscisic acid homeostasis at post-translational level, probably through ubiquitin/proteasome-dependent substrate-specific degradation. Members of this subfamily contain a C3H2C3-type RING-H2 finger.


Pssm-ID: 438483 [Multi-domain]  Cd Length: 50  Bit Score: 38.62  E-value: 1.00e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1958660160   23 ECPICLELI----KEPVSTKCDHIFCKFCMLKLLNQKKgpSQCPLCKNE 67
Cdd:cd23121      3 CCAICLSDFnsdeKLRQLPKCGHIFHHHCLDRWIRYNK--ITCPLCRAD 49
RING-HC_LNX3 cd16718
RING finger, HC subclass, found in ligand of numb protein X 3 (LNX3); LNX3, also known as PDZ ...
22-61 1.14e-03

RING finger, HC subclass, found in ligand of numb protein X 3 (LNX3); LNX3, also known as PDZ domain-containing RING finger protein 3 (PDZRN3), or Semaphorin cytoplasmic domain-associated protein 3 (SEMACAP3), is an E3 ubiquitin-protein ligase that was first identified as a Semaphorin-binding partner. It is also responsible for the ubiquitination and degradation of Numb, a component of the Notch signaling pathway that functions in the specification of cell fates during development and is known to control cell numbers during neurogenesis in vertebrates. LNX3 acts as a negative regulator of osteoblast differentiation by inhibiting Wnt-beta-catenin signaling. LNX3 also plays an important role in neuromuscular junction formation. It interacts with and ubiquitinates the muscle specific tyrosine kinase (MuSK), thus promoting its endocytosis and negatively regulating the cell surface expression of this key regulator of postsynaptic assembly. LNX3 contains an N-terminal C3HC4-type RING-HC finger, two PDZ domains, and a C-terminal LNX3 homology (LNX3H) domain.


Pssm-ID: 438378 [Multi-domain]  Cd Length: 47  Bit Score: 38.43  E-value: 1.14e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1958660160   22 LECPICLELIKEPVSTKCDHIFCKFCMLK-LLNQKKGPSQC 61
Cdd:cd16718      5 FKCNLCNKVLEDPLTTPCGHVFCAGCVLPwVVQQGSCPVKC 45
RING-HC_RNF112 cd16538
RING finger, HC subclass, found in RING finger protein 112 (RNF112) and similar proteins; ...
24-71 1.21e-03

RING finger, HC subclass, found in RING finger protein 112 (RNF112) and similar proteins; RNF112, also known as brain finger protein (BFP), zinc finger protein 179 (ZNF179), or neurolastin, is a peripheral membrane protein that is predominantly expressed in the central nervous system and localizes to endosomes. It contains functional GTPase and C3HC4-type RING-HC finger domains and has been identified as a brain-specific dynamin family GTPase that affects endosome size and spine density. Moreover, RNF112 acts as a downstream target of sigma-1 receptor (Sig-1R) regulation and may play a novel role in neuroprotection by mediating the neuroprotective effects of dehydroepiandrosterone (DHEA) and its sulfated analog (DHEAS).


Pssm-ID: 438200 [Multi-domain]  Cd Length: 52  Bit Score: 38.44  E-value: 1.21e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1958660160   24 CPICLELIKEPVSTKCDHIFCKFCMLKLLNQKKGPSQCPLCKNEITKR 71
Cdd:cd16538      5 CSICLERLREPISLDCGHDFCIRCFSTHRIPGCEPPCCPECRKICKQR 52
mRING-HC-C3HC3D_Roquin cd16638
Modified RING finger, HC subclass (C3HC3D-type), found in Roquin-1, Roquin-2, and similar ...
22-62 2.26e-03

Modified RING finger, HC subclass (C3HC3D-type), found in Roquin-1, Roquin-2, and similar proteins; The ROQUIN family includes Roquin-1, Roquin-2, and similar proteins, which localize to the cytoplasm and upon stress, are concentrated in stress granules. They may play essential roles in preventing T-cell-mediated autoimmune disease and in microRNA-mediated repression of inducible costimulator (Icos) mRNA. They function as E3 ubiquitin ligases consisting of an N-terminal modified C3HC3D-type RING-HC finger with a potential E3 activity, a highly conserved ROQ domain required for RNA binding and localization to stress granules, and a CCCH-type zinc finger involved in RNA recognition.


Pssm-ID: 438300 [Multi-domain]  Cd Length: 44  Bit Score: 37.33  E-value: 2.26e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1958660160   22 LECPICL----ELIKEPVSTKCDHIFCKFCMLKLLNQkkgpsQCP 62
Cdd:cd16638      2 LSCPVCTnefdGTQRKPISLGCGHTVCKTCLSKLHRK-----QCP 41
RING-HC_PCGF5 cd16737
RING finger found in polycomb group RING finger protein 5 (PCGF5) and similar proteins; PCGF5, ...
22-87 2.36e-03

RING finger found in polycomb group RING finger protein 5 (PCGF5) and similar proteins; PCGF5, also known as RING finger protein 159 (RNF159), is one of six PcG RING finger (PCGF) homologs (PCGF1/NSPc1, PCGF2/Mel-18, PCGF3, PCGF4/BMI1, PCGF5, and PCGF6/MBLR) and serves as the core component of a Polycomb repressive complex 1 (PRC1). Like other PCGF homologs, PCGF5 associates with ring finger protein 2 (RNF2) to form a RNF2-PCGF heterodimer, which is catalytically competent as an E3 ubiquitin transferase and is the scaffold for the assembly of additional components. PCGF5 contains a C3HC4-type RING-HC finger.


Pssm-ID: 438395 [Multi-domain]  Cd Length: 95  Bit Score: 38.97  E-value: 2.36e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958660160   22 LECPICL-ELIKEPVSTKCDHIFCKFCMLKLLNQKKgpsQCPLCKNEITKRSLQGSARFSQLVEELL 87
Cdd:cd16737     11 ITCRICKgYLIKPTTVTECLHTFCKSCIVQHFEDSN---DCPECGIQVHETNPLEMLRLDNTLEEII 74
RING-HC_SH3RFs cd16570
RING finger, HC subclass, found in SH3 domain-containing RING finger proteins SH3RF1, SH3RF2, ...
22-65 2.49e-03

RING finger, HC subclass, found in SH3 domain-containing RING finger proteins SH3RF1, SH3RF2, SH3RF3, and similar proteins; SH3RF1, also known as plenty of SH3s (POSH), RING finger protein 142 (RNF142), or SH3 multiple domains protein 2 (SH3MD2), is a trans-Golgi network-associated pro-apoptotic scaffold protein with E3 ubiquitin-protein ligase activity. SH3RF2, also known as heart protein phosphatase 1-binding protein (HEPP1), plenty of SH3s (POSH)-eliminating RING protein (POSHER), protein phosphatase 1 regulatory subunit 39, or RING finger protein 158 (RNF158), is a putative E3 ubiquitin-protein ligase that acts as an anti-apoptotic regulator for the c-Jun N-terminal kinase (JNK) pathway by binding to and promoting the proteasomal degradation of SH3RF1 (or POSH) that is required for pro-apoptotic JNK activation. SH3RF3, also known as plenty of SH3s 2 (POSH2) or SH3 multiple domains protein 4 (SH3MD4), is a scaffold protein with E3 ubiquitin-protein ligase activity. It was identified in the screen for interacting partners of p21-activated kinase 2 (PAK2) and may play a role in regulating c-Jun N-terminal kinase (JNK) mediated apoptosis in certain conditions. Members of this subfamily contain an N-terminal C3HC4-type RING-HC finger responsible for the E3 ligase activity and four Src Homology 3 (SH3) domains, which are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs.


Pssm-ID: 438232 [Multi-domain]  Cd Length: 44  Bit Score: 37.41  E-value: 2.49e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1958660160   22 LECPICLEliKEPVSTK---CDHIFCKFCMLKLLnQKKGPSQCPLCK 65
Cdd:cd16570      1 LECPVCLE--RLDVSAKvlpCQHTFCKRCLQIIV-ASRGELRCPECR 44
RING-HC_MID_C-I cd16575
RING finger, HC subclass, found in midline-1 (MID1), midline-2 (MID2) and similar proteins; ...
22-65 2.52e-03

RING finger, HC subclass, found in midline-1 (MID1), midline-2 (MID2) and similar proteins; MID1, also known as midin, midline 1 RING finger protein, putative transcription factor XPRF, RING finger protein 59 (RNF59), or tripartite motif-containing protein 18 (TRIM18), is a microtubule-associated E3 ubiquitin-protein ligase implicated in epithelial-mesenchymal differentiation, cell migration and adhesion, and programmed cell death along specific regions of the ventral midline during embryogenesis. MID2, also known as midin-2, midline defect 2, RING finger protein 60 (RNF60), or tripartite motif-containing protein 1 (TRIM1), associates with the microtubule network and may at least partially compensate for the loss of MID1. Both MID1 and MID2 interacts with Alpha 4, which is a regulatory subunit of PP2-type phosphatases, such as PP2A, and an integral component of the rapamycin-sensitive signaling pathway. They also play a central role in the regulation of granule exocytosis. Functional redundancy exists between MID1 and MID2 in cytotoxic lymphocytes (CTL). Both MID1 and MID2 belong to the C-I subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438237 [Multi-domain]  Cd Length: 54  Bit Score: 37.60  E-value: 2.52e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958660160   22 LECPICLELIKEPVSTKCDHIFCKFCMLKLL------NQKKGPS---QCPLCK 65
Cdd:cd16575      1 LTCPICLELFEDPLLLPCAHSLCFNCAHRILvshcasNESVESItafQCPTCR 53
RING-HC_RNF186 cd16557
RING finger, HC subclass, found in RING finger protein 186 (RNF186) and similar proteins; ...
22-65 3.16e-03

RING finger, HC subclass, found in RING finger protein 186 (RNF186) and similar proteins; RNF186 is an E3 ubiquitin-protein ligase with an N-terminal C3HC4-type RING-HC finger and two putative C-terminal transmembrane domains which enable it to localize in a certain organelle. It regulates RING-dependent self-ubiquitination, as well as endoplasmic reticulum (ER) stress-mediated apoptosis through interaction with the Bcl-2 family protein BNip1.


Pssm-ID: 438219 [Multi-domain]  Cd Length: 52  Bit Score: 37.14  E-value: 3.16e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958660160   22 LECPICLE----LIKEPVSTKCDHIFCKFCMLKLLNQKKGP--SQCPLCK 65
Cdd:cd16557      2 LECLVCRNpyscFVRKPKLLACQHAFCAICLKLILCEQDGTwsVTCPLCR 51
RING-HC_TRIM59_C-V cd16763
RING finger, HC subclass, found in tripartite motif-containing protein 59 (TRIM59) and similar ...
22-65 3.17e-03

RING finger, HC subclass, found in tripartite motif-containing protein 59 (TRIM59) and similar proteins; TRIM59, also known as RING finger protein 104 (RNF104) or tumor suppressor TSBF-1, is a putative E3 ubiquitin-protein ligase that functions as a novel multiple cancer biomarker for immunohistochemical detection of early tumorigenesis. It is upregulated in gastric cancer and promotes gastric carcinogenesis by interacting with and targeting the P53 tumor suppressor for its ubiquitination and degradation. It also acts as a novel accessory molecule involved in cytotoxicity of BCG-activated macrophages (BAM). Moreover, TRIM59 may serve as a multifunctional regulator for innate immune signaling pathways. It interacts with ECSIT and negatively regulates nuclear factor-kappaB (NF- kappa B) and interferon regulatory factor (IRF)-3/7-mediated signal pathways. TRIM59 belongs to the C-V subclass of the TRIM (tripartite motif) family of proteins that are defined by an N-terminal RBCC (RING, Bbox, and coiled coil) domain, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region. In addition, TRIM59 contains a C-terminal transmembrane domain.


Pssm-ID: 438419 [Multi-domain]  Cd Length: 56  Bit Score: 37.58  E-value: 3.17e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958660160   22 LECPICLELIKEPVSTKCDHIFCKFCMLKLLNQK---------KGPSQCPLCK 65
Cdd:cd16763      4 LTCSVCYSLFEDPRVLPCSHTFCRNCLENILQVSgnfsiwrplRPPLKCPNCR 56
RING-H2_APC11 cd16456
RING finger, H2 subclass, found in anaphase-promoting complex subunit 11 (APC11) and similar ...
24-67 3.60e-03

RING finger, H2 subclass, found in anaphase-promoting complex subunit 11 (APC11) and similar proteins; APC11, also known as cyclosome subunit 11, or hepatocellular carcinoma-associated RING finger protein, is a C3H2C3-type RING-H2 protein that facilitates ubiquitin chain formation by recruiting ubiquitin-charged ubiquitin conjugating enzymes (E2) through its RING-H2 domain. APC11 and its partner, the cullin-like subunit APC2, form the dynamic catalytic core of the gigantic, multisubunit 1.2-MDa anaphase-promoting complex/cyclosome (APC), also known as the cyclosome, which is a ubiquitin-protein ligase (E3) composed of at least 12 subunits and controls cell division by ubiquitinating cell cycle regulators, such as cyclin B and securin, to drive their timely degradation. APC11 can be inhibited by hydrogen peroxide, which may contribute to the delay in cell cycle progression through mitosis that is characteristic of cells subjected to oxidative stress. APC11 contains a canonical RING-H2-finger that coordinate two Zn2+ ions. In addition, it contains a third Zn2+-binding site that is not essential for its ligase activity.


Pssm-ID: 438120 [Multi-domain]  Cd Length: 63  Bit Score: 37.65  E-value: 3.60e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958660160   24 CPICleliKEP------VSTKCDHIFCKFCMLKLLNQKKGPSQCPLCKNE 67
Cdd:cd16456     15 CPDC----KFPgddcplVWGKCSHCFHMHCILKWLNSQQVQQHCPMCRQE 60
RING-HC_DTX3 cd16711
RING finger, HC subclass, found in E3 ubiquitin-protein ligase Deltex3 (DTX3) and similar ...
24-65 3.82e-03

RING finger, HC subclass, found in E3 ubiquitin-protein ligase Deltex3 (DTX3) and similar proteins; DTX3, also known as RING finger protein 154 (RNF154), is an E3 ubiquitin-protein ligase that belongs to the Deltex (DTX) family. In contrast to other DTXs, DTX3 does not contain two N-terminal Notch-binding WWE domains, but a short unique N-terminal domain, suggesting it does not interact with the intracellular domain of Notch. Its C-terminal region includes a C3HC4-type RING-HC finger, and a previously unidentified C-terminal domain.


Pssm-ID: 438371 [Multi-domain]  Cd Length: 54  Bit Score: 37.01  E-value: 3.82e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1958660160   24 CPICLELIKEPVS-TKCDHIFCKFCMLKLLNQKKgpsQCPLCK 65
Cdd:cd16711      4 CPICLGEIQNKKTlDKCKHSFCEDCITRALQVKK---ACPMCG 43
RING-HC_TRIM32_C-VII cd16587
RING finger, HC subclass, found in tripartite motif-containing protein 32 (TRIM32) and similar ...
22-64 3.83e-03

RING finger, HC subclass, found in tripartite motif-containing protein 32 (TRIM32) and similar proteins; TRIM32, also known as 72 kDa Tat-interacting protein, zinc finger protein HT2A, or BBS11, is an E3 ubiquitin-protein ligase that promotes degradation of several targets, including actin, PIASgamma, Abl interactor 2, dysbindin, X-linked inhibitor of apoptosis (XIAP), p73 transcription factor, thin filaments and Z-bands during fasting. It plays important roles in neuronal differentiation of neural progenitor cells, as well as in controlling cell fate in skeletal muscle progenitor cells. It reduces PI3K-Akt-FoxO signaling in muscle atrophy by promoting plakoglobin-PI3K dissociation. It also functions as a pluripotency-reprogramming roadblock that facilitates cellular transition towards differentiation by modulating the levels of Oct4 and cMyc. Moreover, TRIM32 is an intrinsic influenza A virus (IAV) restriction factor which senses and targets the polymerase basic protein 1 (PB1) for ubiquitination and protein degradation. It also plays a significant role in mediating the biological activity of the HIV-1 Tat protein in vivo, binds specifically to the activation domain of HIV-1 Tat, and can also interact with the HIV-2 and EIAV Tat proteins in vivo. Furthermore, TRIM32 regulates myoblast proliferation by controlling turnover of NDRG2 (N-myc downstream-regulated gene). It negatively regulates tumor suppressor p53 to promote tumorigenesis. It also facilitates degradation of MYCN on spindle poles and induces asymmetric cell division in human neuroblastoma cells. In addition, TRIM32 plays important roles in regulation of hyperactivities and positively regulates the development of anxiety and depression disorders induced by chronic stress. It also plays a role in regeneration by affecting satellite cell cycle progression via modulation of the SUMO ligase PIASy (PIAS4). Defects in TRIM32 leads to limb-girdle muscular dystrophy type 2H (LGMD2H), sarcotubular myopathies (STM) and Bardet-Biedl syndrome. TRIM32 belongs to the C-VII subclass of the TRIM (tripartite motif)-NHL family that is defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil domain, as well as a NHL (named after proteins NCL-1, HT2A and Lin-41 that contain repeats folded into a six-bladed beta propeller) repeat domain positioned C-terminal to the RBCC domain. The NHL domain mediates the interaction with Argonaute proteins and consequently allows TRIM32 to modulate the activity of certain miRNAs.


Pssm-ID: 438249 [Multi-domain]  Cd Length: 51  Bit Score: 37.00  E-value: 3.83e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1958660160   22 LECPICLELIKE----PVSTKCDHIFCKFCMLKLLNQKKGPS-QCPLC 64
Cdd:cd16587      1 LECPICLESFDEgqlrPKLLHCGHTICEQCLEKLLASLSINGvRCPFC 48
RING-H2_DTX1-like cd16459
RING finger, H2 subclass, found in E3 ubiquitin-protein ligase Deltex1 (DTX1), Deltex2 (DTX2), ...
23-65 3.85e-03

RING finger, H2 subclass, found in E3 ubiquitin-protein ligase Deltex1 (DTX1), Deltex2 (DTX2), Deltex4 (DTX4), and similar proteins; This subfamily contains the vertebrate homologs of Drosophila melanogaster Deltex, specifically DTX1, DTX2, and DTX4, and other similar proteins mainly from eumetazoa. The vertebrate homologs of Deltex are involved in Notch signaling and neurogenesis. Mammalian DTX1 is most closely related to the Drosophila Deltex. Both of them bind to SH3-domain containing protein Grb2 and further inhibit E2A. DTX1 functions as a Notch downstream transcription regulator. It interacts with the transcription coactivator p300 and inhibits transcription activation mediated by the neural specific transcription factor MASH1. It is also a transcription target of nuclear factor of activated T cells (NFAT) and participates in T cell anergy and Foxp3 protein level maintenance in vivo. Moreover, DTX1 promotes protein kinase C theta degradation and sustains Casitas B-lineage lymphoma expression. DTX4, also known as RING finger protein 155, shares the highest degree of sequence similarity with DTX1. So it likely interacts with the intracellular domain of Notch as well. Like DTX1 and DTX4, DTX2 is expressed in thymocytes. It interacts with the intracellular domain of Notch receptors and acts as a negative regulator of Notch signals in T cells. However, the endogenous levels of DTX1 and DTX2 is not important for regulating Notch signals during thymocyte development. In contrast to other DTXs, DTX3 does not contain two Notch-binding WWE domains at the N-terminus, but rather a short unique N-terminal domain. It does not interact with the intracellular domain of Notch. In addition, it has a different class of RING finger (C3HC4 type or RING-HC subclass), compared with the other DTXs which harbor a C3H2C3-type RING-H2 finger. Thus DTX3 is not included in this subfamily. Drosophila melanogaster Deltex also does not belong to this subfamily.


Pssm-ID: 438122 [Multi-domain]  Cd Length: 64  Bit Score: 37.50  E-value: 3.85e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660160   23 ECPICLELIKEPVS---------------TKCDHIFCKFCMLKLLN--QKKGPSQCPLCK 65
Cdd:cd16459      1 DCPICCEPLCVASGyeesklegskvvvrlKKCSHMYHKACLVAMYSngAKDGSLQCPTCK 60
RING-HC_PCGF cd16525
RING finger, HC subclass, found in Polycomb Group RING finger homologs (PCGF1, 2, 3, 4, 5 and ...
22-64 3.87e-03

RING finger, HC subclass, found in Polycomb Group RING finger homologs (PCGF1, 2, 3, 4, 5 and 6), and similar proteins; This subfamily includes six Polycomb Group (PcG) RING finger homologs (PCGF1/NSPc1, PCGF2/Mel-18, PCGF3, PCGF4/BMI1, PCGF5, and PCGF6/MBLR) that use epigenetic mechanisms to maintain or repress expression of their target genes. They were first discovered in fruit flies and are well known for silencing Hox genes through modulation of chromatin structure during embryonic development. PCGF homologs play important roles in cell proliferation, differentiation, and tumorigenesis. They all have been found to associate with ring finger protein 2 (RNF2). The RNF2-PCGF heterodimer is catalytically competent as an E3 ubiquitin transferase and is the scaffold for the assembly of additional components. Moreover, PCGF homologs are critical components in the assembly of distinct Polycomb Repression Complex 1 (PRC1) related complexes which is involved in the maintenance of gene repression and which target different genes through distinct mechanisms. The Drosophila PRC1 core complex is formed by the Polycomb (Pc), Polyhomeotic (Ph), Posterior sex combs (Psc), and Sex combs extra (Sce, also known as Ring) subunits. In mammals, the composition of PRC1 is much more diverse and varies depending on the cellular context. All PRC1 complexes contain homologs of the Drosophila Ring protein. Ring1A/RNF1 and Ring1B/RNF2 are E3 ubiquitin ligases that mark lysine 119 of histone H2A with a single ubiquitin group (H2AK119ub). Mammalian homologs of the Drosophila Psc protein, such as PCGF2/Mel-18 or PCGF4/BMI1, regulate PRC1 enzymatic activity. PRC1 complexes can be divided into at least two classes according to the presence or absence of CBX proteins, which are homologs of Drosophila Pc. Canonical PRC1 complexes contain CBX proteins that recognize and bind H3K27me3, the mark deposited by PRC2. Therefore, canonical PRC1 complexes and PRC2 can act together to repress gene transcription and maintain this repression through cell division. Non-canonical PRC1 complexes, containing RYBP (together with additional proteins, such as L3mbtl2 or Kdm2b) rather than the CBX proteins have recently been described in mammals. PCGF homologs contain a C3HC4-type RING-HC finger.


Pssm-ID: 438188 [Multi-domain]  Cd Length: 42  Bit Score: 36.82  E-value: 3.87e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1958660160   22 LECPICLELIKEPVS-TKCDHIFCKFCMLKLLNQKKgpsQCPLC 64
Cdd:cd16525      1 LTCSLCKGYLIDATTiTECLHSFCKSCIVRHLETSK---NCPVC 41
BRCT_microcephalin_rpt3 cd17751
third BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA damage ...
1698-1792 3.88e-03

third BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA damage response protein involved in regulation of CHK1 and BRCA1. It has been implicated in chromosome condensation and DNA damage induced cellular responses. It may play a role in neurogenesis and regulation of the size of the cerebral cortex. Microcephalin contains three BRCT repeats. This family corresponds to the third repeat.


Pssm-ID: 349382  Cd Length: 75  Bit Score: 37.60  E-value: 3.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660160 1698 SRESQEKLFEGLQIYCCePFTNMPKDELERMLQLCGASVVKELplltRDTGahpIVLVQPSAwteDNDCPdigqlckgrL 1777
Cdd:cd17751      1 SRYRQNLFADGGPIYVS-SNSVPPKDKLEELVLLCGGKVVKSS----RKAD---ICIGKTPP---NPDKP---------S 60
                           90
                   ....*....|....*
gi 1958660160 1778 VMWDWVLDSISVYRC 1792
Cdd:cd17751     61 VSEKWLLDSITNHKL 75
RING-H2_TUL1-like cd23117
RING finger, H2 subclass, found in Saccharomyces cerevisiae transmembrane E3 ubiquitin-protein ...
23-67 4.63e-03

RING finger, H2 subclass, found in Saccharomyces cerevisiae transmembrane E3 ubiquitin-protein ligase 1 (TUL1) and similar proteins; This subfamily includes Saccharomyces cerevisiae TUL1, Schizosaccharomyces pombe DSC E3 ubiquitin ligase complex subunit 1 (DSC1), and Arabidopsis thaliana protein FLYING SAUCER 2 (FLY2). TUL1 is the catalytic component of DSC E3 ubiquitin ligase complexes that tag proteins present in Golgi, endosome and vacuole membranes and function in protein homeostasis under non-stress conditions, and support a role in protein quality control. It mediates ubiquitination of vacuolar proteins such as CPS1, PPN1, PEP12 and other proteins containing exposed hydrophilic residues within their transmembrane domains, leading to their sorting into internal vesicles in late endosomes. TUL1 also targets the unpalmitoylated endosomal SNARE TLG1 to the multivesicular body (MVB) pathway. DSC1, also known as defective for SREBP cleavage protein 1, is the catalytic component of the DSC E3 ubiquitin ligase complex required for the sre1 transcriptional activator proteolytic cleavage to release the soluble transcription factor from the membrane in low oxygen or sterol conditions. FLY2 acts as an E3 ubiquitin-protein ligase that may be involved in xylem development. Members of this subfamily contain a C3H2C3-type RING-H2 finger.


Pssm-ID: 438479 [Multi-domain]  Cd Length: 59  Bit Score: 36.99  E-value: 4.63e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958660160   23 ECPICLELI---------KEPVSTKCDHIFCKFCMLKLLNQKkgpSQCPLCKNE 67
Cdd:cd23117      6 DCVICMSDIelpstnsvrRDYMVTPCNHIFHTNCLERWMDIK---LECPTCRRP 56
zf-Nse pfam11789
Zinc-finger of the MIZ type in Nse subunit; Nse1 and Nse2 are novel non-SMC subunits of the ...
22-62 5.78e-03

Zinc-finger of the MIZ type in Nse subunit; Nse1 and Nse2 are novel non-SMC subunits of the fission yeast Smc5-6 DNA repair complex. This family is the zinc-finger domain similar to the MIZ type of zinc-finger.


Pssm-ID: 403098 [Multi-domain]  Cd Length: 57  Bit Score: 36.88  E-value: 5.78e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1958660160   22 LECPICLELIKEPV-STKCDHIFCKFCMLKLLNQKKGpSQCP 62
Cdd:pfam11789   12 LTCPLTLQPFVEPVtSKKCNHVFEKDAILEMLKRNPT-VKCP 52
RING-H2_RNF32 cd16471
RING finger, H2 subclass, found in RING finger protein 32 (RNF32) and similar proteins; RNF32 ...
23-65 6.11e-03

RING finger, H2 subclass, found in RING finger protein 32 (RNF32) and similar proteins; RNF32 is mainly expressed in testis spermatogenesis, most likely in spermatocytes and/or in spermatids, suggesting a possible role in sperm formation. RNF32 contains two C3H2C3-type RING-H2 fingers separated by an IQ domain of unknown function. Although the biological function of RNF32 remains unclear, proteins with double RING-H2 fingers may act as scaffolds for binding several proteins that function in the same pathway.


Pssm-ID: 438134 [Multi-domain]  Cd Length: 46  Bit Score: 36.45  E-value: 6.11e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1958660160   23 ECPICLELIK--EPVSTKCDHIFCKFCMLKLLNQKKGPSQ-CPLCK 65
Cdd:cd16471      1 ECPICLCAFKgrKCTLLSCSHVFHEACLSAFEKFIESKNQkCPLCR 46
RING-HC_RNF169 cd16551
RING finger, HC subclass, found in RING finger protein 169 (RNF169) and similar proteins; ...
22-65 6.55e-03

RING finger, HC subclass, found in RING finger protein 169 (RNF169) and similar proteins; RNF169 is an uncharacterized E3 ubiquitin-protein ligase paralogous to RNF168. It functions as a negative regulator of the DNA damage signaling cascade. RNF169 recognizes polyubiquitin structures but does not itself contribute to double-strand break (DSB)-induced chromatin ubiquitylation. It contributes to regulation of the DSB repair pathway utilization via functionally competing with recruiting repair factors, 53BP1 and RAP80-BRCA1, for association with RNF168-modified chromatin independent of its catalytic activity, limiting the magnitude of the RNF8/RNF168-dependent signaling response to DSBs. RNF169 contains an N-terminal C3HC4-type RING-HC finger and a C-terminal MIU (motif interacting with ubiquitin) domain.


Pssm-ID: 438213 [Multi-domain]  Cd Length: 55  Bit Score: 36.37  E-value: 6.55e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1958660160   22 LECPICLELIKEPVSTKCDHIFCKFCMLKLLNQKKGPSQCPLCK 65
Cdd:cd16551      2 LTCAGCLEVPVEPATLPCGHTLCRGCANRALDAAEAGPTCPRCR 45
RING-HC_BAR cd16497
RING finger, HC subclass, found in bifunctional apoptosis regulator (BAR); BAR, also known as ...
24-65 6.86e-03

RING finger, HC subclass, found in bifunctional apoptosis regulator (BAR); BAR, also known as RING finger protein 47, was originally identified as an inhibitor of Bax-induced apoptosis. It participates in the block of apoptosis induced by TNF-family death receptors (extrinsic pathway) and mitochondria-dependent apoptosis (intrinsic pathway). BAR is predominantly expressed by neurons in the central nervous system and is involved in the regulation of neuronal survival. It is an endoplasmic reticulum (ER)-associated RING-type E3 ubiquitin ligase that interacts with BI-1 protein and post-translationally regulates its stability, as well as functioning in ER stress. BAR contains an N-terminal C3HC4-type RING-HC finger, a SAM domain, a coiled-coil domain, and a C-terminal transmembrane (TM) domain. This model corresponds to the RING-HC finger responsible for the binding of ubiquitin conjugating enzymes (E2s).


Pssm-ID: 438160 [Multi-domain]  Cd Length: 52  Bit Score: 36.33  E-value: 6.86e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1958660160   24 CPICLELIKEPVSTKCDHIFCKFCM-LKLLNQKKgpSQCPLCK 65
Cdd:cd16497      4 CHCCYDLLVNPTTLNCGHSFCRHCLaLWWKSSKK--TECPECR 44
RING-H2_DTX2 cd16672
RING finger, H2 subclass, found in E3 ubiquitin-protein ligase Deltex2 (DTX2) and similar ...
37-65 6.96e-03

RING finger, H2 subclass, found in E3 ubiquitin-protein ligase Deltex2 (DTX2) and similar proteins; DTX2, also known as RING finger protein 58, together with DTX1 and DTX4, forms a family of related proteins that are the mammalian homologs of Drosophila Deltex, a known regulator of Notch signals. Like DTX1 and DTX4, DTX2 is expressed in thymocytes. It interacts with the intracellular domain of Notch receptors and acts as a negative regulator of Notch signals in T cells. However, the endogenous levels of DTX1 and DTX2 is not important for regulating Notch signals during thymocyte development. DTX2 contains two Notch-binding WWE domains at the N-terminus that physically interact with the Notch ankyrin domains, a proline-rich motif that shares homology with SH3-binding domains, and a C3H2C3-type RING-H2 finger at the C-terminus. It also harbors two nuclear localization signals.


Pssm-ID: 438334  Cd Length: 72  Bit Score: 37.11  E-value: 6.96e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1958660160   37 TKCDHIFCKFCMLKLLNQ--KKGPSQCPLCK 65
Cdd:cd16672     33 TKCGHTFHLLCMLAMYNNgnKDGSLQCPSCK 63
mRING-HC-C3HC3D_arc-1-like cd23124
Modified RING finger, HC subclass (C3HC3D-type), found in Caenorhabditis elegans putative ...
22-62 7.03e-03

Modified RING finger, HC subclass (C3HC3D-type), found in Caenorhabditis elegans putative GTP-binding protein trim-23 homolog (arc-1) and similar proteins; arc-1, also called RING-type E3 ubiquitin transferase arc-1, is an E3 ubiquitin-protein ligase that mediates E2-dependent protein ubiquitination. arc-1 contains a modified C3HC3D-type RING-HC finger.


Pssm-ID: 438486 [Multi-domain]  Cd Length: 55  Bit Score: 36.32  E-value: 7.03e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1958660160   22 LECPICLE-------LIKEPVSTKCDHIFCKFCMLKLLNQKKGPSQCP 62
Cdd:cd23124      2 LECGICQQeysaddpLLIPRILTECGHTICTNCAGTILGQSSGSIFCP 49
RING-HC_SH3RF2 cd16749
RING finger, HC subclass, found in SH3 domain-containing RING finger protein 2 (SH3RF2) and ...
22-65 7.53e-03

RING finger, HC subclass, found in SH3 domain-containing RING finger protein 2 (SH3RF2) and similar proteins; SH3RF2, also known as heart protein phosphatase 1-binding protein (HEPP1), plenty of SH3s (POSH)-eliminating RING protein (POSHER), protein phosphatase 1 regulatory subunit 39, or RING finger protein 158 (RNF158), is a putative E3 ubiquitin-protein ligase that acts as an anti-apoptotic regulator for the c-Jun N-terminal kinase (JNK) pathway by binding to and promoting the proteasomal degradation of SH3RF1 (or POSH), a scaffold protein that is required for pro-apoptotic JNK activation. It may also play a role in cardiac functions together with protein phosphatase 1. SH3RF2 contains an N-terminal C3HC4-type RING-HC finger responsible for the E3 ligase activity and four Src Homology 3 (SH3) domains, which are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs.


Pssm-ID: 438407 [Multi-domain]  Cd Length: 46  Bit Score: 36.07  E-value: 7.53e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1958660160   22 LECPICLEliKEPVSTK---CDHIFCKFCMLKLLNQKKgPSQCPLCK 65
Cdd:cd16749      1 LECPVCFE--KLDVTAKvlpCQHTFCKPCLQRIFKARK-ELRCPECR 44
SP-RING_PIAS-like cd16650
SP-RING finger found in the Siz/PIAS RING (SP-RING) family of SUMO E3 ligases; The SP-RING ...
22-66 7.54e-03

SP-RING finger found in the Siz/PIAS RING (SP-RING) family of SUMO E3 ligases; The SP-RING family includes PIAS (protein inhibitor of activated STAT) proteins, Zmiz proteins, and Siz proteins from plants and fungi. PIAS proteins modulate the activity of several transcription factors and act as E3 ubiquitin ligases in the sumoylation pathway. There are four members: PIAS1, PIAS2 (also known as PIASx), PIAS3, and PIAS4 (also known as PIASy). PIAS proteins were initially identified as inhibitors of activated STAT only, but are now known to interact with and modulate several other proteins, including androgen receptor (AR), tumor suppressor p53, and the transforming growth factor-beta (TGF-beta) signaling protein SMAD. They interact with STATs in a cytokine-dependent manner. PIAS proteins have SUMO E3-ligase activity and interaction of PIAS proteins with transcription factors often results in sumoylation of that protein. Zmiz1 (Zimp10) and its homolog Zmiz2 (Zimp7) were initially identified in humans as androgen receptor (AR) interacting proteins that function as transcriptional co-activators. They interact with BRG1, the catalytic subunit of the SWI-SNF remodeling complex. They also associate with other hormone nuclear receptors and transcription factors such as p53 and Smad3/Smad4, and regulate transcription of specific target genes by altering their chromatin structure. SIZ1 proteins from plants and fungi are also founding members of this family. SIZ1-mediated conjugation of SUMO1 and SUMO2 to other intracellular proteins is essential in Arabidopsis. Yeast SIZ proteins are SUMO E3 ligases involved in a novel pathway of chromosome maintenance. They enhance SUMO modification to many substrates in vivo, but also exhibit unique substrate specificity. PIAS proteins contain a specific RING finger known as Siz/PIAS (protein inhibitor of activated signal transducer and activator of transcription) RING (SP-RING) finger, which is essential for SUMO ligase activity. The SP-RING finger is a variant of the RING finger, which lacks the second, fifth, and sixth zinc-binding residues of the consensus C3H2C3-/C3HC4-type RING fingers. It binds a single Zn ion, instead of two ions bound by typical RING fingers.


Pssm-ID: 438312  Cd Length: 48  Bit Score: 36.09  E-value: 7.54e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1958660160   22 LECPICLELIKEPV-STKCDHIFCkFCMLKLL--NQKKGPSQCPLCKN 66
Cdd:cd16650      2 LRCPLSLKRIKTPArGKHCKHLQC-FDLDSYLefNKRKPTWKCPICDK 48
BRCT_Bard1_rpt2 cd17720
second (C-terminal) BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar ...
1705-1791 8.06e-03

second (C-terminal) BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar proteins; Bard1, also termed BARD-1, or RING-type E3 ubiquitin transferase BARD1, is a critical factor in BRCA1-mediated tumor suppression and may also serve as a target for tumorigenic lesions in some human cancers. It associates with BRCA1 (breast cancer-1) to form a heterodimeric BRCA1/BARD1 complex that is responsible for maintaining genomic stability through nuclear functions involving DNA damage signaling and repair, transcriptional regulation, and cell cycle control. The BRCA1/BARD1 complex catalyzes autoubiquitination of BRCA1 and trans ubiquitination of other protein substrates. Its E3 ligase activity is dramatically reduced in the presence of UBX domain protein 1 (UBXN1). BARD-1 contains an N-terminal C3HC4-type RING-HC finger that binds BRCA1, and a C-terminal region with three ankyrin repeats and tandem BRCT domains that bind CstF-50 (cleavage stimulation factor) to modulate mRNA processing and RNAP II stability in response to DNA damage. The family corresponds to the second BRCT domain.


Pssm-ID: 349352  Cd Length: 101  Bit Score: 37.73  E-value: 8.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660160 1705 LFEGLQIYCCEPFTN-MPKDELERMLQLCGASVVKELPllTRDTGAHPIVLVQPSAWtedndcPDIGQLCKGRLVMWD-- 1781
Cdd:cd17720      1 LFDGCHFYFHGTFKPpTTKDDLEQLVKAGGGTVLSREP--KPDSDVTQTINTVAYAR------PDSDLANCTHYIIYDkl 72
                           90       100
                   ....*....|....*....|....*....
gi 1958660160 1782 -------------------WVLDSISVYR 1791
Cdd:cd17720     73 ndkkpakvrqgkvrvvpvsWLLDCISQFK 101
PHA02929 PHA02929
N1R/p28-like protein; Provisional
15-67 8.15e-03

N1R/p28-like protein; Provisional


Pssm-ID: 222944  Cd Length: 238  Bit Score: 39.76  E-value: 8.15e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958660160   15 LHAMQKILECPICLELIKEP--------VSTKCDHIFCKFCMLKLlnqKKGPSQCPLCKNE 67
Cdd:PHA02929   168 LYNRSKDKECAICMEKVYDKeiknmyfgILSNCNHVFCIECIDIW---KKEKNTCPVCRTP 225
RING-HC_TRIM46_C-I cd16757
RING finger, HC subclass, found in tripartite motif-containing protein 46 (TRIM46) and similar ...
18-65 8.74e-03

RING finger, HC subclass, found in tripartite motif-containing protein 46 (TRIM46) and similar proteins; TRIM46, also known as gene Y protein (GeneY) or tripartite, fibronectin type-III and C-terminal SPRY motif protein (TRIFIC), is a microtubule-associated protein that specifically localizes to the proximal axon, partly overlaps with the axon initial segment (AIS) at later stages, and organizes uniform microtubule orientation in axons. It controls neuronal polarity and axon specification by driving the formation of parallel microtubule arrays. TRIM46 belongs to the C-I subclass of the TRIM (tripartite motif) family of proteins, which are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, a PRY domain and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438415 [Multi-domain]  Cd Length: 43  Bit Score: 35.94  E-value: 8.74e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1958660160   18 MQKILECPICLELIKEPVSTKCDHIFCKFCMLKLLnqkkgpSQCPLCK 65
Cdd:cd16757      1 MERELLCPVCKEMYKQPLVLPCMHNVCQVCASEVL------FPCPPCQ 42
RING-HC_TRIM2 cd16767
RING finger, HC subclass, found in tripartite motif-containing protein 2 (TRIM2); TRIM2, also ...
19-65 9.54e-03

RING finger, HC subclass, found in tripartite motif-containing protein 2 (TRIM2); TRIM2, also known as RING finger protein 86 (RNF86), is an E3 ubiquitin-protein ligase that ubiquitinates the neurofilament light chain, a component of the intermediate filament in axons. Loss of function of TRIM2 results in early-onset axonal neuropathy. TRIM2 also plays a role in mediating the p42/p44 MAPK-dependent ubiquitination of the cell death-promoting protein Bcl-2-interacting mediator of cell death (Bim) in rapid ischemic tolerance. TRIM2 belongs to the C-VII subclass of the TRIM (tripartite motif)-NHL family that is defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil domain, as well as a NHL (named after proteins NCL-1, HT2A and Lin-41 that contain repeats folded into a six-bladed beta propeller) repeat domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438423 [Multi-domain]  Cd Length: 51  Bit Score: 36.15  E-value: 9.54e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1958660160   19 QKILECPICLELIKEPVSTKCDHIFCKFCMLKLLNQKKGPSQCPLCK 65
Cdd:cd16767      4 KQFLICSICLDRYKNPKVLPCLHTFCERCLQNYIPAHSLTLSCPVCR 50
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH