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Conserved domains on  [gi|569006009|ref|XP_006531913|]
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E3 ubiquitin-protein ligase synoviolin isoform X1 [Mus musculus]

Protein Classification

HRD1 family E3 ubiquitin-protein ligase( domain architecture ID 1004582)

HRD1 family E3 ubiquitin-protein ligase accepts ubiquitin specifically from endoplasmic reticulum-associated UBC7 E2 ligase and transfers it to substrates, promoting their degradation; similar to Drosophila melanogaster E3 ubiquitin-protein ligase HRD1 and Danio rerio E3 ubiquitin-protein ligase synoviolin

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HRD1 super family cl34953
HRD ubiquitin ligase complex, ER membrane component [Posttranslational modification, protein ...
10-333 8.45e-51

HRD ubiquitin ligase complex, ER membrane component [Posttranslational modification, protein turnover, chaperones];


The actual alignment was detected with superfamily member COG5243:

Pssm-ID: 227568 [Multi-domain]  Cd Length: 491  Bit Score: 182.86  E-value: 8.45e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006009  10 ASLALTGAVVAHAYYLKHQFYPTVVYLTKSSP-SMAVLYIQAFVLVFLLGKVMGKVFFGQLRAAEMEHLLERSWYAVTET 88
Cdd:COG5243    9 ASLVLFGLSVLLSLYSSATVYSALVMTSQLSPvHITIGLNVILLLFFLIANALKTLLFGSLRTFELELLYEQLWITLTEI 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006009  89 CLAFTVFRDDFSPRFVALFTLLLFLKCFHWLAEDRVdfmERSPNIS--WLFH--CRIVSLMFLLGILDFLFVSHAYHSIL 164
Cdd:COG5243   89 LLAISVFREAISFSFFMLLSTLLFAKVFHWILSFRT---ERLQIQStdQRFHifSRFSCAYFLLSILDASLIYLCISSEH 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006009 165 TRGASVQLVF--GFEYAILmtmVLTIfIKYVLHSVDLQSENPWDNKAVYMLYTELFTGFIKVLLYMAFMTIMIKVHTFPL 242
Cdd:COG5243  166 LIDKSTLFLFvcEFSVLLL---NLTS-EANKLCVYNYEARDDDDERSTYLFRLEVCYDGLTLLAYSLLFMYQFPYVRVPI 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006009 243 FAIRPMYLAMRQFKKAVTDAIMSRRAIRNMNTLYPDATPEELQAMDNVCIICREEMV------------TGAKRLPCNHI 310
Cdd:COG5243  242 YLIRQMYTCFYALFRRIREHARFRRATKDLNAMYPTATEEQLTNSDRTCTICMDEMFhpdheplprgldMTPKRLPCGHI 321
                        330       340
                 ....*....|....*....|...
gi 569006009 311 FHTSCLRSWFQRQQTCPTCRMDV 333
Cdd:COG5243  322 LHLHCLKNWLERQQTCPICRRPV 344
PHA03291 super family cl30053
envelope glycoprotein I; Provisional
530-601 3.05e-04

envelope glycoprotein I; Provisional


The actual alignment was detected with superfamily member PHA03291:

Pssm-ID: 223033 [Multi-domain]  Cd Length: 401  Bit Score: 43.40  E-value: 3.05e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569006009 530 PATSVNPTEETASTVVSAAPSTSAPSSEAPTPSPGASPPIP------EAEKPPAPESVGIVEELPEDGEPDAAELRRR 601
Cdd:PHA03291 205 PATPRPTPRTTASPETTPTPSTTTSPPSTTIPAPSTTIAAPqagttpEAEGTPAPPTPGGGEAPPANATPAPEASRYE 282
PRK06975 super family cl35524
bifunctional uroporphyrinogen-III synthetase/uroporphyrin-III C-methyltransferase; Reviewed
476-582 4.60e-03

bifunctional uroporphyrinogen-III synthetase/uroporphyrin-III C-methyltransferase; Reviewed


The actual alignment was detected with superfamily member PRK06975:

Pssm-ID: 235899 [Multi-domain]  Cd Length: 656  Bit Score: 40.09  E-value: 4.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006009 476 AGLTPEELRALEG------HERQHLEARLQSLRNIhTLLDAAMLQI-NQYLTVLASLGPPRPATSVNPTEETASTVVSAa 548
Cdd:PRK06975 214 AHLNPAEIDALKHaplvapHARIAEQARALGFDRI-TLTGAGDERIvRAFLTWADAAAQPATAAPAPSRMTDTNDSKSV- 291
                         90       100       110
                 ....*....|....*....|....*....|....
gi 569006009 549 psTSAPSSEAPTPSPGASPPIPEAEKPPAPESVG 582
Cdd:PRK06975 292 --TSQPAAAAAAPAPPPNPPATPPEPPARRGRGS 323
 
Name Accession Description Interval E-value
HRD1 COG5243
HRD ubiquitin ligase complex, ER membrane component [Posttranslational modification, protein ...
10-333 8.45e-51

HRD ubiquitin ligase complex, ER membrane component [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227568 [Multi-domain]  Cd Length: 491  Bit Score: 182.86  E-value: 8.45e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006009  10 ASLALTGAVVAHAYYLKHQFYPTVVYLTKSSP-SMAVLYIQAFVLVFLLGKVMGKVFFGQLRAAEMEHLLERSWYAVTET 88
Cdd:COG5243    9 ASLVLFGLSVLLSLYSSATVYSALVMTSQLSPvHITIGLNVILLLFFLIANALKTLLFGSLRTFELELLYEQLWITLTEI 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006009  89 CLAFTVFRDDFSPRFVALFTLLLFLKCFHWLAEDRVdfmERSPNIS--WLFH--CRIVSLMFLLGILDFLFVSHAYHSIL 164
Cdd:COG5243   89 LLAISVFREAISFSFFMLLSTLLFAKVFHWILSFRT---ERLQIQStdQRFHifSRFSCAYFLLSILDASLIYLCISSEH 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006009 165 TRGASVQLVF--GFEYAILmtmVLTIfIKYVLHSVDLQSENPWDNKAVYMLYTELFTGFIKVLLYMAFMTIMIKVHTFPL 242
Cdd:COG5243  166 LIDKSTLFLFvcEFSVLLL---NLTS-EANKLCVYNYEARDDDDERSTYLFRLEVCYDGLTLLAYSLLFMYQFPYVRVPI 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006009 243 FAIRPMYLAMRQFKKAVTDAIMSRRAIRNMNTLYPDATPEELQAMDNVCIICREEMV------------TGAKRLPCNHI 310
Cdd:COG5243  242 YLIRQMYTCFYALFRRIREHARFRRATKDLNAMYPTATEEQLTNSDRTCTICMDEMFhpdheplprgldMTPKRLPCGHI 321
                        330       340
                 ....*....|....*....|...
gi 569006009 311 FHTSCLRSWFQRQQTCPTCRMDV 333
Cdd:COG5243  322 LHLHCLKNWLERQQTCPICRRPV 344
RING-H2_synoviolin cd16479
RING finger, H2 subclass, found in synoviolin and similar proteins; Synoviolin, also known as ...
288-330 1.27e-31

RING finger, H2 subclass, found in synoviolin and similar proteins; Synoviolin, also known as synovial apoptosis inhibitor 1 (Syvn1), Hrd1, or Der3, is an endoplasmic reticulum (ER)-anchoring E3 ubiquitin ligase that functions as a suppressor of ER stress-induced apoptosis and plays a role in homeostasis maintenance. It also targets tumor suppressor gene p53 for proteasomal degradation, suggesting crosstalk between ER associated degradation (ERAD) and p53 mediated apoptotic pathway under ER stress. Moreover, synoviolin controls body weight and mitochondrial biogenesis through negative regulation of the thermogenic coactivator peroxisome proliferator-activated receptor coactivator (PGC)-1beta. It upregulates amyloid beta production by targeting a negative regulator of gamma-secretase, Retention in endoplasmic reticulum 1 (Rer1), for degradation. It is also involved in the degradation of endogenous immature nicastrin, and affects amyloid beta-protein generation. Moreover, synoviolin is highly expressed in rheumatoid synovial cells and may be involved in the pathogenesis of rheumatoid arthritis (RA). It functions as an anti-apoptotic factor that is responsible for the outgrowth of synovial cells during the development of RA. It promotes inositol-requiring enzyme 1 (IRE1) ubiquitination and degradation in synovial fibroblasts with collagen-induced arthritis. Furthermore, the upregulation of synoviolin may represent a protective response against neurodegeneration in Parkinson's disease (PD). In addition, synoviolin is involved in liver fibrogenesis. Synoviolin contains a C3H2C2-type RING-H2 finger.


Pssm-ID: 438142 [Multi-domain]  Cd Length: 43  Bit Score: 116.30  E-value: 1.27e-31
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 569006009 288 DNVCIICREEMVTGAKRLPCNHIFHTSCLRSWFQRQQTCPTCR 330
Cdd:cd16479    1 DNTCIICREEMTVGAKKLPCGHIFHLSCLRSWLQRQQTCPTCR 43
zf-RING_2 pfam13639
Ring finger domain;
291-330 1.89e-14

Ring finger domain;


Pssm-ID: 433370 [Multi-domain]  Cd Length: 44  Bit Score: 67.43  E-value: 1.89e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 569006009  291 CIICREEMVTGAK--RLPCNHIFHTSCLRSWFQRQQTCPTCR 330
Cdd:pfam13639   3 CPICLEEFEEGDKvvVLPCGHHFHRECLDKWLRSSNTCPLCR 44
RING smart00184
Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and ...
291-329 6.89e-12

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: 60.22  E-value: 6.89e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 569006009   291 CIICREEMVTGAKRLPCNHIFHTSCLRSWF-QRQQTCPTC 329
Cdd:smart00184   1 CPICLEEYLKDPVILPCGHTFCRSCIRKWLeSGNNTCPIC 40
PHA03291 PHA03291
envelope glycoprotein I; Provisional
530-601 3.05e-04

envelope glycoprotein I; Provisional


Pssm-ID: 223033 [Multi-domain]  Cd Length: 401  Bit Score: 43.40  E-value: 3.05e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569006009 530 PATSVNPTEETASTVVSAAPSTSAPSSEAPTPSPGASPPIP------EAEKPPAPESVGIVEELPEDGEPDAAELRRR 601
Cdd:PHA03291 205 PATPRPTPRTTASPETTPTPSTTTSPPSTTIPAPSTTIAAPqagttpEAEGTPAPPTPGGGEAPPANATPAPEASRYE 282
PRK06975 PRK06975
bifunctional uroporphyrinogen-III synthetase/uroporphyrin-III C-methyltransferase; Reviewed
476-582 4.60e-03

bifunctional uroporphyrinogen-III synthetase/uroporphyrin-III C-methyltransferase; Reviewed


Pssm-ID: 235899 [Multi-domain]  Cd Length: 656  Bit Score: 40.09  E-value: 4.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006009 476 AGLTPEELRALEG------HERQHLEARLQSLRNIhTLLDAAMLQI-NQYLTVLASLGPPRPATSVNPTEETASTVVSAa 548
Cdd:PRK06975 214 AHLNPAEIDALKHaplvapHARIAEQARALGFDRI-TLTGAGDERIvRAFLTWADAAAQPATAAPAPSRMTDTNDSKSV- 291
                         90       100       110
                 ....*....|....*....|....*....|....
gi 569006009 549 psTSAPSSEAPTPSPGASPPIPEAEKPPAPESVG 582
Cdd:PRK06975 292 --TSQPAAAAAAPAPPPNPPATPPEPPARRGRGS 323
SepH NF040712
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ...
528-602 8.30e-03

septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces venezuelae, and homologs were identified in Mycobacterium smegmatis. SepH contains a N-terminal DUF3071 domain and a conserved C-terminal region. It binds directly to cell division protein FtsZ to stimulate the assembly of FtsZ protofilaments.


Pssm-ID: 468676 [Multi-domain]  Cd Length: 346  Bit Score: 38.98  E-value: 8.30e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569006009 528 PRPATSVNPTEETASTVVSAAPSTSAPSSEAPTPSPGASPPIPEAEKPPAPEsvgiveelpedgEPDAAELRRRR 602
Cdd:NF040712 266 PAAEPDEATRDAGEPPAPGAAETPEAAEPPAPAPAAPAAPAAPEAEEPARPE------------PPPAPKPKRRR 328
 
Name Accession Description Interval E-value
HRD1 COG5243
HRD ubiquitin ligase complex, ER membrane component [Posttranslational modification, protein ...
10-333 8.45e-51

HRD ubiquitin ligase complex, ER membrane component [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227568 [Multi-domain]  Cd Length: 491  Bit Score: 182.86  E-value: 8.45e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006009  10 ASLALTGAVVAHAYYLKHQFYPTVVYLTKSSP-SMAVLYIQAFVLVFLLGKVMGKVFFGQLRAAEMEHLLERSWYAVTET 88
Cdd:COG5243    9 ASLVLFGLSVLLSLYSSATVYSALVMTSQLSPvHITIGLNVILLLFFLIANALKTLLFGSLRTFELELLYEQLWITLTEI 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006009  89 CLAFTVFRDDFSPRFVALFTLLLFLKCFHWLAEDRVdfmERSPNIS--WLFH--CRIVSLMFLLGILDFLFVSHAYHSIL 164
Cdd:COG5243   89 LLAISVFREAISFSFFMLLSTLLFAKVFHWILSFRT---ERLQIQStdQRFHifSRFSCAYFLLSILDASLIYLCISSEH 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006009 165 TRGASVQLVF--GFEYAILmtmVLTIfIKYVLHSVDLQSENPWDNKAVYMLYTELFTGFIKVLLYMAFMTIMIKVHTFPL 242
Cdd:COG5243  166 LIDKSTLFLFvcEFSVLLL---NLTS-EANKLCVYNYEARDDDDERSTYLFRLEVCYDGLTLLAYSLLFMYQFPYVRVPI 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006009 243 FAIRPMYLAMRQFKKAVTDAIMSRRAIRNMNTLYPDATPEELQAMDNVCIICREEMV------------TGAKRLPCNHI 310
Cdd:COG5243  242 YLIRQMYTCFYALFRRIREHARFRRATKDLNAMYPTATEEQLTNSDRTCTICMDEMFhpdheplprgldMTPKRLPCGHI 321
                        330       340
                 ....*....|....*....|...
gi 569006009 311 FHTSCLRSWFQRQQTCPTCRMDV 333
Cdd:COG5243  322 LHLHCLKNWLERQQTCPICRRPV 344
RING-H2_synoviolin cd16479
RING finger, H2 subclass, found in synoviolin and similar proteins; Synoviolin, also known as ...
288-330 1.27e-31

RING finger, H2 subclass, found in synoviolin and similar proteins; Synoviolin, also known as synovial apoptosis inhibitor 1 (Syvn1), Hrd1, or Der3, is an endoplasmic reticulum (ER)-anchoring E3 ubiquitin ligase that functions as a suppressor of ER stress-induced apoptosis and plays a role in homeostasis maintenance. It also targets tumor suppressor gene p53 for proteasomal degradation, suggesting crosstalk between ER associated degradation (ERAD) and p53 mediated apoptotic pathway under ER stress. Moreover, synoviolin controls body weight and mitochondrial biogenesis through negative regulation of the thermogenic coactivator peroxisome proliferator-activated receptor coactivator (PGC)-1beta. It upregulates amyloid beta production by targeting a negative regulator of gamma-secretase, Retention in endoplasmic reticulum 1 (Rer1), for degradation. It is also involved in the degradation of endogenous immature nicastrin, and affects amyloid beta-protein generation. Moreover, synoviolin is highly expressed in rheumatoid synovial cells and may be involved in the pathogenesis of rheumatoid arthritis (RA). It functions as an anti-apoptotic factor that is responsible for the outgrowth of synovial cells during the development of RA. It promotes inositol-requiring enzyme 1 (IRE1) ubiquitination and degradation in synovial fibroblasts with collagen-induced arthritis. Furthermore, the upregulation of synoviolin may represent a protective response against neurodegeneration in Parkinson's disease (PD). In addition, synoviolin is involved in liver fibrogenesis. Synoviolin contains a C3H2C2-type RING-H2 finger.


Pssm-ID: 438142 [Multi-domain]  Cd Length: 43  Bit Score: 116.30  E-value: 1.27e-31
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 569006009 288 DNVCIICREEMVTGAKRLPCNHIFHTSCLRSWFQRQQTCPTCR 330
Cdd:cd16479    1 DNTCIICREEMTVGAKKLPCGHIFHLSCLRSWLQRQQTCPTCR 43
RING-H2_AMFR cd16455
RING finger, H2 subclass, found in autocrine motility factor receptor (AMFR) and similar ...
291-331 8.77e-16

RING finger, H2 subclass, found in autocrine motility factor receptor (AMFR) and similar proteins; AMFR, also known as AMF receptor, or RING finger protein 45, or ER-protein gp78, is an internalizing cell surface glycoprotein localized in both plasma membrane caveolae and the endoplasmic reticulum (ER). It is involved in the regulation of cellular adhesion, proliferation, motility and apoptosis, as well as in the process of learning and memory. AMFR also functions as a RING finger-dependent ubiquitin protein ligase (E3) implicated in the degradation from the ER. AMFR contains an N-terminal RING-H2 finger and a C-terminal ubiquitin-associated (UBA)-like CUE domain.


Pssm-ID: 438119 [Multi-domain]  Cd Length: 44  Bit Score: 71.33  E-value: 8.77e-16
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 569006009 291 CIICREEMVTgAKRLPCNHIFHTSCLRSWFQRQQTCPTCRM 331
Cdd:cd16455    3 CAICWESMQS-ARKLPCGHLFHNSCLRSWLEQDTSCPTCRM 42
RING-H2 cd16448
H2 subclass of RING (RING-H2) fingers and its variants; The RING finger is a specialized type ...
291-330 1.72e-15

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: 70.51  E-value: 1.72e-15
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 569006009 291 CIICREEMVTGAK--RLPCNHIFHTSCLRSWFQ-RQQTCPTCR 330
Cdd:cd16448    1 CVICLEEFEEGDVvrLLPCGHVFHLACILRWLEsGNNTCPLCR 43
zf-RING_2 pfam13639
Ring finger domain;
291-330 1.89e-14

Ring finger domain;


Pssm-ID: 433370 [Multi-domain]  Cd Length: 44  Bit Score: 67.43  E-value: 1.89e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 569006009  291 CIICREEMVTGAK--RLPCNHIFHTSCLRSWFQRQQTCPTCR 330
Cdd:pfam13639   3 CPICLEEFEEGDKvvVLPCGHHFHRECLDKWLRSSNTCPLCR 44
RING-H2_PA-TM-RING cd16454
RING finger, H2 subclass, found in the PA-TM-RING ubiquitin ligase family; The PA-TM-RING ...
290-330 1.76e-13

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: 64.60  E-value: 1.76e-13
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 569006009 290 VCIICREEMVTGAK--RLPCNHIFHTSCLRSWFQRQQTCPTCR 330
Cdd:cd16454    1 TCAICLEEFKEGEKvrVLPCNHLFHKDCIDPWLEQHNTCPLCR 43
RING-H2_RNF139 cd16683
RING finger, H2 subclass, found in RING finger protein 139 (RNF139) and similar proteins; ...
285-333 4.01e-13

RING finger, H2 subclass, found in RING finger protein 139 (RNF139) 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. RNF139 physically and functionally interacts with von Hippel-Lindau (VHL), which is part of an SCF related E3-ubiquitin ligase complex with "gatekeeper" function in renal carcinoma and is defective in most sporadic clear-cell renal cell carcinomas (ccRCC). It suppresses growth and functions with VHL in a common pathway. RNF139 also suppresses tumorigenesis by targeting heme oxygenase-1 for ubiquitination and degradation. Moreover, RNF139 is a target of Translin (TSN), a posttranscriptional regulator of genes transcribed by the transcription factor CREM-tau in postmeiotic male germ cells, suggesting a role of RNF139 in dysgerminoma. In addition, RNF139 forms an integral part of a novel multi-protein ER complex, containing MHC I, US2, and signal peptide peptidase, which is associated with the ER-associated degradation (ERAD) pathway. It is required for the ubiquitination of MHC class I molecules before dislocation from the ER. As a novel sterol-sensing ER membrane protein, RNF139 hinders sterol regulatory element-binding protein-2 (SREBP-2) processing through interaction with SREBP-2 and SREBP cleavage-activated protein (SCAP), regulating its own turnover rate via its E3 ubiquitin ligase activity. RNF139 shows two regions of similarity with the receptor for sonic hedgehog (SHH), Patched. The first region corresponds to the second extracellular domain of Patched, which is involved in binding SHH. The second region is a putative sterol-sensing domain (SSD). The C-terminal half of RNF139 contains a C3H2C3-type RING-H2 finger with E3-ubiquitin ligase activity in vitro.


Pssm-ID: 438345 [Multi-domain]  Cd Length: 54  Bit Score: 64.21  E-value: 4.01e-13
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 569006009 285 QAMDNVCIICREEMVTGAKRLPCNHIFHTSCLRSWFQRQQTCPTCRMDV 333
Cdd:cd16683    1 REIDDVCAICYQEFTTSARITPCNHYFHALCLRKWLYIQDTCPMCHQKV 49
RING-H2_DZIP3 cd16460
RING finger, H2 subclass, found in DAZ (deleted in azoospermia)-interacting protein 3 (DZIP3) ...
291-333 9.53e-13

RING finger, H2 subclass, found in DAZ (deleted in azoospermia)-interacting protein 3 (DZIP3) and similar proteins; DZIP3, also known as RNA-binding ubiquitin ligase of 138 kDa (RUL138) or 2A-HUB protein, is an RNA-binding E3 ubiquitin-protein ligase that interacts with coactivator-associated arginine methyltransferase 1 (CARM1) and acts as a transcriptional coactivator of estrogen receptor (ER) alpha. It is also a histone H2A ubiquitin ligase that catalyzes monoubiquitination of H2A at lysine 119, functioning as a combinatorial component of the repression machinery required for repressing a specific chemokine gene expression program, critically modulating migratory responses to Toll-like receptors (TLR) activation. DZIP3 contains a C3H2C3-type RING-H2 finger at the C-terminus.


Pssm-ID: 438123 [Multi-domain]  Cd Length: 47  Bit Score: 62.94  E-value: 9.53e-13
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 569006009 291 CIICREEMVTG--AKRLPCNHIFHTSCLRSWFQRQQTCPTCRMDV 333
Cdd:cd16460    3 CVICHEAFSDGdrLLVLPCAHKFHTQCIGPWLDGQQTCPTCRLHV 47
RING-H2_RNF126-like cd16667
RING finger, H2 subclass, found in RING finger proteins RNF126, RNF115, and similar proteins; ...
291-330 2.09e-12

RING finger, H2 subclass, found in RING finger proteins RNF126, RNF115, and similar proteins; This subfamily includes RING finger proteins RNF126, RNF115, and similar proteins. RNF126 is a Bag6-dependent E3 ubiquitin ligase that is involved in the mislocalized protein (MLP) pathway of quality control. It regulates the retrograde sorting of the cation-independent mannose 6-phosphate receptor (CI-MPR). RNF126 promotes cancer cell proliferation by targeting the tumor suppressor p21 for ubiquitin-mediated degradation, and could be a novel therapeutic target in breast and prostate cancers. It is also able to ubiquitylate cytidine deaminase (AID), a poorly soluble protein that is essential for antibody diversification. RNF115, also known as Rab7-interacting ring finger protein (Rabring 7), or zinc finger protein 364 (ZNF364), or breast cancer-associated gene 2 (BCA2), is an E3 ubiquitin-protein ligase that is an endogenous inhibitor of adenosine monophosphate-activated protein kinase (AMPK) activation; this inhibition increases the efficacy of metformin in breast cancer cells. It also functions as a cofactor in the restriction imposed by tetherin on HIV-1, and targets HIV-1 Gag for lysosomal degradation, impairing virus assembly and release, in a tetherin-independent manner. Moreover, RNF115 is a Rab7-binding protein that stimulates c-Myc degradation through mono-ubiquitination of MM-1. It also plays crucial roles as a Rab7 target protein in vesicle traffic to late endosome/lysosome and lysosome biogenesis. RNF115 and RNF126 associate with the epidermal growth factor receptor (EGFR) and promote ubiquitylation of EGFR, suggesting they play a role in the ubiquitin-dependent sorting and downregulation of membrane receptors. Both of them contain an N-terminal BCA2 Zinc-finger domain (BZF), AKT-phosphorylation sites, and a C-terminal C3H2C3-type RING-H2 finger.


Pssm-ID: 438329 [Multi-domain]  Cd Length: 43  Bit Score: 61.55  E-value: 2.09e-12
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 569006009 291 CIICREEMVTG--AKRLPCNHIFHTSCLRSWFQRQQTCPTCR 330
Cdd:cd16667    2 CAVCKEDFEVGeeVRQLPCKHLFHPDCIVPWLELHNSCPVCR 43
mRING-CH-C4HC2H_ZNRF cd16489
Modified RING-CH finger, H2 subclass (C4HC2H-type), found in the ZNRF family; The ZNRF family ...
291-327 6.58e-12

Modified RING-CH finger, H2 subclass (C4HC2H-type), found in the ZNRF family; The ZNRF family includes zinc/RING finger proteins ZNRF1, ZNRF2, and similar proteins. It has been characterized by containing a unique combination of zinc finger-RING finger motifs in the C-terminal region, which is evolutionarily conserved in a wide range of species, including Caenorhabditis elegans and Drosophila. ZNRF proteins function as E3 ubiquitin ligases and are highly expressed in central nervous system (CNS) and peripheral nervous system (PNS) neurons, particularly during development and in adulthood. ZNRF1 and ZNRF2 are differentially localized within the synaptic region. ZNRF1 is associated with synaptic vesicle membranes, whereas ZNRF2 is present in presynaptic plasma membranes. They are N-myrisotoylated and also located in the endosome-lysosome compartment in fibroblasts. ZNRF proteins may play a role in the establishment and maintenance of neuronal transmission and plasticity via their ubiquitin ligase activity, as well as in regulating Ca2+-dependent exocytosis. The RING fingers found in ZNRF proteins are modified as C4HC2H-type RING-CH finger, rather than the typical C4HC3-type RING-CH finger, which is a variant of the RING-H2 finger.


Pssm-ID: 438152 [Multi-domain]  Cd Length: 43  Bit Score: 60.39  E-value: 6.58e-12
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 569006009 291 CIICREEMVTGAK--RLPCNHIFHTSCLRSWFQRQQTCP 327
Cdd:cd16489    2 CVICLEELEAGDTiaRLPCLCIYHKKCIDDWFEVNRSCP 40
RING smart00184
Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and ...
291-329 6.89e-12

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: 60.22  E-value: 6.89e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 569006009   291 CIICREEMVTGAKRLPCNHIFHTSCLRSWF-QRQQTCPTC 329
Cdd:smart00184   1 CPICLEEYLKDPVILPCGHTFCRSCIRKWLeSGNNTCPIC 40
RING-H2_RNF111-like cd16474
RING finger, H2 subclass, found in RING finger proteins RNF111, RNF165, and similar proteins; ...
291-332 8.18e-12

RING finger, H2 subclass, found in RING finger proteins RNF111, RNF165, and similar proteins; The family includes RING finger proteins RNF111, RNF165, and similar proteins. RNF111, also known as Arkadia, is a nuclear E3 ubiquitin-protein ligase that targets intracellular effectors and modulators of transforming growth factor beta (TGF-beta)/Nodal-related signaling for polyubiquitination and proteasome-dependent degradation. It also interacts with the clathrin-adaptor 2 (AP2) complex and regulates endocytosis of certain cell surface receptors, leading to modulation of epidermal growth factor (EGF) and possibly other signaling pathways. The N-terminal half of RNF111 harbors three SUMO-interacting motifs (SIMs). It thus functions as a SUMO-targeted ubiquitin ligase (STUbL) that directly links nonproteolytic ubiquitylation and SUMOylation in the DNA damage response, as well as triggers degradation of signal-induced polysumoylated proteins, such as the promyelocytic leukemia protein (PML). RNF165, also known as Arkadia-like 2, Arkadia2, or Ark2C, is an E3 ubiquitin ligase with homology to the C-terminal half of RNF111. It is expressed specifically in the nervous system, and can serve to amplify neuronal responses to specific signals. It acts as a positive regulator of bone morphogenetic protein (BMP)-Smad signaling that is involved in motor neuron (MN) axon elongation. Both RNF165 and RNF111 contain a C-terminal C3H2C3-type RING-H2 finger.


Pssm-ID: 438137 [Multi-domain]  Cd Length: 46  Bit Score: 60.12  E-value: 8.18e-12
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 569006009 291 CIICREEMVTG--AKRLPCNHIFHTSCLRSWFQRQQTCPTCRMD 332
Cdd:cd16474    3 CTICLSDFEEGedVRRLPCMHLFHQECVDQWLSTNKRCPICRVD 46
RING-H2_TTC3 cd16481
RING finger, H2 subclass, found in Tetratricopeptide repeat protein 3 (TTC3) and similar ...
290-333 1.22e-11

RING finger, H2 subclass, found in Tetratricopeptide repeat protein 3 (TTC3) and similar proteins; TTC3, also known as protein DCRR1, TPR repeat protein D, TPR repeat protein 3, or RING finger protein 105 (RNF105), is an E3 ubiquitin-protein ligase encoded by a gene within the Down syndrome (DS) critical region on chromosome 21. It affects differentiation and Golgi compactness in neurons through specific actin-regulating pathways. It inhibits the neuronal-like differentiation of pheocromocytoma cells by activating RhoA and by binding to Citron proteins. TTC3 is an Akt-specific E3 ligase that binds to phosphorylated Akt and facilitates its ubiquitination and degradation within the nucleus. It contains four N-terminal TPR motifs, a potential coiled-coil region and a Citron binding region in the central part, and a C-terminal C3H2C2-type RING-H2 finger.


Pssm-ID: 438144 [Multi-domain]  Cd Length: 45  Bit Score: 59.67  E-value: 1.22e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 569006009 290 VCIICREEMV--TGAKrLPCNHIFHTSCLRSWFQRQQTCPTCRMDV 333
Cdd:cd16481    1 PCIICHDDLKpdQLAK-LECGHIFHKECIKQWLKEQSTCPTCRVHV 45
RING-H2_RNF126 cd16801
RING finger, H2 subclass, found in RING finger protein 126 (RNF126) and similar proteins; ...
291-330 2.05e-11

RING finger, H2 subclass, found in RING finger protein 126 (RNF126) and similar proteins; RNF126 is a Bag6-dependent E3 ubiquitin ligase that is involved in the mislocalized protein (MLP) pathway of quality control. It regulates the retrograde sorting of the cation-independent mannose 6-phosphate receptor (CI-MPR). Moreover, RNF126 promotes cancer cell proliferation by targeting the tumor suppressor p21 for ubiquitin-mediated degradation, and could be a novel therapeutic target in breast and prostate cancers. It is also able to ubiquitylate cytidine deaminase (AID), a poorly soluble protein that is essential for antibody diversification. In addition, RNF126 and the related protein, RNF115 associate with the epidermal growth factor receptor (EGFR) and promote ubiquitylation of EGFR, suggesting they play a role in the ubiquitin-dependent sorting and downregulation of membrane receptors. RNF126 contains an N-terminal BCA2 Zinc-finger domain (BZF), the AKT-phosphorylation sites, and the C-terminal C3H2C3-type RING-H2 finger.


Pssm-ID: 438453 [Multi-domain]  Cd Length: 44  Bit Score: 58.85  E-value: 2.05e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 569006009 291 CIICREEMVTG--AKRLPCNHIFHTSCLRSWFQRQQTCPTCR 330
Cdd:cd16801    2 CPVCKEDYTVGenVRQLPCNHLFHNDCIVPWLEQHDTCPVCR 43
RING-HC_RNFT1-like cd16532
RING finger, HC subclass, found in RING finger and transmembrane domain-containing protein ...
289-330 3.66e-11

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: 58.08  E-value: 3.66e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 569006009 289 NVCIICREEMVTGAKrLPCNHIFHTSCLRSWFQRQQTCPTCR 330
Cdd:cd16532    1 DICPICQDEFKDPVV-LRCKHIFCEDCVSEWFERERTCPLCR 41
RING-H2_RNF139-like cd16476
RING finger, H2 subclass, found in RING finger proteins RNF139, RNF145, and similar proteins; ...
289-329 4.45e-11

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: 57.85  E-value: 4.45e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 569006009 289 NVCIICREEMVTgAKRLPCNHIFHTSCLRSWFQRQQTCPTC 329
Cdd:cd16476    1 DVCAICYQEMKE-ARITPCNHFFHGLCLRKWLYVQDTCPLC 40
RING-H2_RNF11 cd16468
RING finger, H2 subclass, found in RING finger protein 11 (RNF11) and similar proteins; RNF11 ...
291-329 5.01e-11

RING finger, H2 subclass, found in RING finger protein 11 (RNF11) and similar proteins; RNF11 is an E3 ubiquitin-protein ligase that acts both as an adaptor and a modulator of itch-mediated control of ubiquitination events underlying membrane traffic. It acts downstream of an enzymatic cascade for the ubiquitination of specific substrates. It is also a molecular adaptor of homologous to E6-associated protein C-terminus (HECT)-type ligases. RNF11 has been implicated in the regulation of several signaling pathways. It enhances transforming growth factor receptor (TGFR) signaling by both abrogating Smurf2-mediated receptor ubiquitination and by promoting the Smurf2-mediated degradation of AMSH (associated molecule with the SH3 domain of STAM), a de-ubiquitinating enzyme that enhances TGF-beta signaling and epidermal growth factor receptor (EGFR) endosomal recycling. It also acts directly on Smad4 to enhance Smad4 function, and plays a role in prolonged TGF-beta signaling. RNF11 also functions as a critical component of the A20 ubiquitin-editing protein complex that negatively regulates tumor necrosis factor (TNF)-mediated nuclear factor (NF)-kappaB activation. It interacts with Smad anchor for receptor activation (SARA) and the endosomal sorting complex required for transport (ESCRT)-0 complex, thus participating in the regulation of lysosomal degradation of EGFR. RNF11 acts as a novel GGA cargo actively participating in regulating the ubiquitination of the GGA protein family. RNF11 functions together with TAX1BP1 to target TANK-binding kinase 1 (TBK1)/IkappaB kinase IKKi, and further restricts antiviral signaling and type I interferon (IFN)-beta production. RNF11 contains an N-terminal PPPY motif that binds WW domain-containing proteins such as AIP4/itch, Nedd4 and Smurf1/2 (SMAD-specific E3 ubiquitin-protein ligase 1/2), and a C-terminal C3H2C3-type RING-H2 finger that functions as a scaffold for the coordinated transfer of ubiquitin to substrate proteins together with the E2 enzymes UbcH527 and Ubc13.


Pssm-ID: 438131 [Multi-domain]  Cd Length: 43  Bit Score: 57.76  E-value: 5.01e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 569006009 291 CIICREEMVTGA--KRLPCNHIFHTSCLRSWFQRQQTCPTC 329
Cdd:cd16468    2 CVICMADFVVGDpiRYLPCMHIYHVDCIDDWLMRSFTCPSC 42
RING-HC_RNF213 cd16561
RING finger, HC subclass, found in RING finger protein 213 (RNF213) and similar proteins; ...
291-333 9.61e-11

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: 57.29  E-value: 9.61e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 569006009 291 CIICREEMVTGAKrLPCNHIFHTSCLRSWFQRQQTCPTCRMDV 333
Cdd:cd16561    5 CSICLEDLNDPVK-LPCDHVFCEECIRQWLPGQMSCPLCRTEL 46
zf-rbx1 pfam12678
RING-H2 zinc finger domain; There are 8 cysteine/ histidine residues which are proposed to be ...
290-330 1.55e-10

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


Pssm-ID: 463669 [Multi-domain]  Cd Length: 55  Bit Score: 56.56  E-value: 1.55e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 569006009  290 VCIICREEMV--------TGAKRLP-----CNHIFHTSCLRSWFQRQQTCPTCR 330
Cdd:pfam12678   2 TCAICRNPFMepcpecqaPGDDECPvvwgeCGHAFHLHCISRWLKTNNTCPLCR 55
RING-H2_RNF103 cd16473
RING finger, H2 subclass, found in RING finger protein 103 (RNF103) and similar proteins; ...
291-336 1.66e-10

RING finger, H2 subclass, found in RING finger protein 103 (RNF103) and similar proteins; RNF103, also known as KF-1 or zinc finger protein 103 homolog (Zfp-103), is an endoplasmic reticulum (ER)-resident E3 ubiquitin-protein ligase that is widely expressed in many different organs, including brain, heart, kidney, spleen, and lung. It is involved in the ER-associated degradation (ERAD) pathway by interacting with components of the ERAD pathway, including Derlin-1 and VCP. RNF103 contains several hydrophobic regions at its N-terminal and middle regions, as well as a C-terminal C3H2C3-type RING-H2 finger.


Pssm-ID: 438136 [Multi-domain]  Cd Length: 55  Bit Score: 56.51  E-value: 1.66e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 569006009 291 CIICREEMVTGA--KRLPCNHIFHTSCLRSWFQR-QQTCPTCRMDVLRA 336
Cdd:cd16473    7 CAICLENYQNGDllRGLPCGHVFHQNCIDVWLERdNHCCPVCRWPVYKD 55
RING-H2_RNF6 cd16673
RING finger, H2 subclass, found in E3 ubiquitin-protein ligase RNF6 and similar proteins; RNF6 ...
290-337 1.96e-10

RING finger, H2 subclass, found in E3 ubiquitin-protein ligase RNF6 and similar proteins; RNF6 is an androgen receptor (AR)-associated protein that induces AR ubiquitination and promotes AR transcriptional activity. RNF6-induced ubiquitination may regulate AR transcriptional activity and specificity by modulating cofactor recruitment. RNF6 is overexpressed in hormone-refractory human prostate cancer tissues and required for prostate cancer cell growth under androgen-depleted conditions. Moreover, RNF6 regulates local serine/threonine kinase LIM kinase 1 (LIMK1) levels in axonal growth cones. RNF6-induced LIMK1 polyubiquitination is mediated via K48 of ubiquitin and leads to proteasomal degradation of the kinase. RNF6 also binds and upregulates the Inha promoter, and functions as a transcription regulatory protein in the mouse sertoli cell. RNF6 also acts as a potential tumor suppressor gene involved in the pathogenesis of esophageal squamous cell carcinoma (ESCC). RNF6 contains an N-terminal coiled-coil domain, a Lys-X-X-Leu/Ile-X-X-Leu/Ile (KIL) motif, and a C-terminal C3H2C3-type RING-H2 finger which is responsible for its ubiquitin ligase activity. The KIL motif is present in a subset of RING-H2 proteins from organisms as evolutionarily diverse as human, mouse, chicken, Drosophila, Caenorhabditis elegans, and Arabidopsis thaliana.


Pssm-ID: 438335 [Multi-domain]  Cd Length: 52  Bit Score: 56.50  E-value: 1.96e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 569006009 290 VCIICREEMVTGAK--RLPCNHIFHTSCLRSWFQRQQTCPTCRMDVLRAS 337
Cdd:cd16673    2 TCSVCINEYATGNKlrRLPCAHEFHIHCIDRWLSENSTCPICRQPVLGSN 51
RING-H2_PJA1_2 cd16465
RING finger, H2 subclass, found in protein E3 ubiquitin-protein ligase Praja-1, Praja-2, and ...
291-330 2.14e-10

RING finger, H2 subclass, found in protein E3 ubiquitin-protein ligase Praja-1, Praja-2, and similar proteins; This family includes two highly similar E3 ubiquitin-protein ligases, Praja-1 and Praja-2. Praja-1, also known as RING finger protein 70, is a RING-H2 finger ubiquitin ligase encoded by gene PJA1, a novel human X chromosome gene abundantly expressed in the brain. It has been implicated in bone and liver development, as well as memory formation and X-linked mental retardation (MRX). Praja-1 interacts with and activates the ubiquitin-conjugating enzyme UbcH5B, and shows E2-dependent E3 ubiquitin ligase activity. It is a 3-deazaneplanocin A (DZNep)-induced ubiquitin ligase that directly ubiquitinates individual polycomb repressive complex 2 (PRC2) subunits in a cell free system, which leads to their proteasomal degradation. It also plays an important role in neuronal plasticity, which is the basis for learning and memory. Moreover, Praja-1 ubiquitinates embryonic liver fodrin (ELF) and Smad3, but not Smad4, in a transforming growth factor-beta (TGF-beta)-dependent manner. It controls ELF abundance through ubiquitin-mediated degradation, and further regulates TGF-beta signaling, which plays a key role in the suppression of gastric carcinoma. Praja-1 also regulates the transcription function of the homeodomain protein Dlx5 by controlling the stability of Dlxin-1, via a ubiquitin-dependent degradation pathway. Praja-2, also known as RING finger protein 131, NEURODAP1, or KIAA0438, is an E2-dependent E3 ubiquitin ligase that interacts with and activates the ubiquitin-conjugating enzyme UbcH5B. It functions as an A-kinase anchoring protein (AKAP)-like E3 ubiquitin ligase that plays a critical role in controlling cyclic AMP (cAMP)-dependent PKA activity and pro-survival signaling, and further promotes cell proliferation and growth. Praja-2 is also involved in protein sorting at the postsynaptic density region of axosomatic synapses and possibly plays a role in synaptic communication and plasticity. Together with the AMPK-related kinase SIK2 and the CDK5 activator CDK5R1/p35, it forms a SIK2-p35-PJA2 complex that plays an essential role for glucose homeostasis in pancreatic beta cell functional compensation. Praja-2 ubiquitylates and degrades Mob, a core component of NDR/LATS kinase and a positive regulator of the tumor-suppressor Hippo signaling. Both Praja-1 and Praja-2 contain a potential nuclear localization signal (NLS) and a C-terminal C3H2C3-type RING-H2 motif.


Pssm-ID: 438128 [Multi-domain]  Cd Length: 46  Bit Score: 55.92  E-value: 2.14e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 569006009 291 CIICREEMVTG--AKRLPCNHIFHTSCLRSWFQRQQTCPTCR 330
Cdd:cd16465    2 CPICCSEYVKDeiATELPCHHLFHKPCITAWLQKSGTCPVCR 43
RING-H2_RNF115 cd16800
RING finger, H2 subclass, found in RING finger protein 115 (RNF115) and similar proteins; ...
291-330 2.61e-10

RING finger, H2 subclass, found in RING finger protein 115 (RNF115) and similar proteins; RNF115, also known as Rab7-interacting ring finger protein (Rabring 7), or zinc finger protein 364 (ZNF364), or breast cancer-associated gene 2 (BCA2), is an E3 ubiquitin-protein ligase that is an endogenous inhibitor of adenosine monophosphate-activated protein kinase (AMPK) activation and its inhibition increases the efficacy of metformin in breast cancer cells. It also functions as a co-factor in the restriction imposed by tetherin on HIV-1, and targets HIV-1 Gag for lysosomal degradation, impairing virus assembly and release, in a tetherin-independent manner. Moreover, RNF115 is a Rab7-binding protein that stimulates c-Myc degradation through mono-ubiquitination of MM-1. It also plays crucial roles as a Rab7 target protein in vesicle traffic to late endosome/lysosome and lysosome biogenesis. Furthermore, RNF115 and the related protein, RNF126 associate with the epidermal growth factor receptor (EGFR) and promote ubiquitylation of EGFR, suggesting they play a role in the ubiquitin-dependent sorting and downregulation of membrane receptors. RNF115 contains an N-terminal BCA2 Zinc-finger domain (BZF), the AKT-phosphorylation sites, and the C-terminal C3H2C3-type RING-H2 finger.


Pssm-ID: 438452 [Multi-domain]  Cd Length: 50  Bit Score: 56.11  E-value: 2.61e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 569006009 291 CIICREEMVTG--AKRLPCNHIFHTSCLRSWFQRQQTCPTCR 330
Cdd:cd16800    3 CPVCKEDYTVGeqVRQLPCNHFFHSDCIVPWLELHDTCPVCR 44
RING-H2_TUL1-like cd23117
RING finger, H2 subclass, found in Saccharomyces cerevisiae transmembrane E3 ubiquitin-protein ...
285-330 2.83e-10

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: 56.25  E-value: 2.83e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 569006009 285 QAMDNVCIICREE-------------MVTgakrlPCNHIFHTSCLRSWFQRQQTCPTCR 330
Cdd:cd23117    1 ENGSVDCVICMSDielpstnsvrrdyMVT-----PCNHIFHTNCLERWMDIKLECPTCR 54
RING-H2_RNF6-like cd16467
RING finger, H2 subclass, found in E3 ubiquitin-protein ligase RNF6, RNF12, and similar ...
291-330 3.49e-10

RING finger, H2 subclass, found in E3 ubiquitin-protein ligase RNF6, RNF12, and similar proteins; RNF6 is an androgen receptor (AR)-associated protein that induces AR ubiquitination and promotes AR transcriptional activity. RNF6-induced ubiquitination may regulate AR transcriptional activity and specificity by modulating cofactor recruitment. RNF6 is overexpressed in hormone-refractory human prostate cancer tissues and required for prostate cancer cell growth under androgen-depleted conditions. RNF6 also regulates local serine/threonine kinase LIM kinase 1 (LIMK1) levels in axonal growth cones. RNF6-induced LIMK1 polyubiquitination is mediated via K48 of ubiquitin and leads to proteasomal degradation of the kinase. RNF6 binds and upregulates the Inha promoter, and functions as a transcription regulatory protein in the mouse sertoli cell. It acts as a potential tumor suppressor gene involved in the pathogenesis of esophageal squamous cell carcinoma (ESCC). RNF12, also known as LIM domain-interacting RING finger protein, or RING finger LIM domain-binding protein (R-LIM), is an E3 ubiquitin-protein ligase encoded by gene RLIM that is crucial for normal embryonic development in some species and for normal X inactivation in mice. It thus functions as a major sex-specific epigenetic regulator of female mouse nurturing tissues. RNF12 is widely expressed during embryogenesis, and mainly localizes to the cell nucleus, where it regulates the levels of many proteins, including CLIM, LMO, HDAC2, TRF1, SMAD7, and REX1, by proteasomal degradation. Both RNF6 and RNF12 contain a well conserved C3H2C3-type RING-H2 finger.


Pssm-ID: 438130 [Multi-domain]  Cd Length: 43  Bit Score: 55.54  E-value: 3.49e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 569006009 291 CIICREEMVTGAK--RLPCNHIFHTSCLRSWFQRQQTCPTCR 330
Cdd:cd16467    2 CTICLGEYETGEKlrRLPCSHEFHSECVDRWLKENSSCPICR 43
zf-C3HC4 pfam00097
Zinc finger, C3HC4 type (RING finger); The C3HC4 type zinc-finger (RING finger) is a ...
291-329 3.86e-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: 55.05  E-value: 3.86e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 569006009  291 CIICREEMVTGAKRLPCNHIFHTSCLRSWFQ-RQQTCPTC 329
Cdd:pfam00097   1 CPICLEEPKDPVTLLPCGHLFCSKCIRSWLEsGNVTCPLC 40
RING-HC_RNF151 cd16547
RING finger, HC subclass, found in RING finger protein 151 (RNF151) and similar proteins; ...
288-333 7.18e-10

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: 54.77  E-value: 7.18e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 569006009 288 DNVCIICREEMVTGAkRLPCNHIFHTSCLRSWFQRQQTCPTCRMDV 333
Cdd:cd16547    3 DLICSICHGVLRCPV-RLSCSHIFCKKCILQWLKRQETCPCCRKEV 47
RING-H2_SIS3 cd23118
RING finger, H2 subclass, found in Arabidopsis thaliana protein SUGAR INSENSITIVE 3 (SIS3) and ...
291-333 1.04e-09

RING finger, H2 subclass, found in Arabidopsis thaliana protein SUGAR INSENSITIVE 3 (SIS3) and similar proteins; SIS3 is an E3 ubiquitin-protein ligase that acts as a positive regulator of sugar signaling during early seedling development. SIS3 contains a C3H2C3-type RING-H2 finger.


Pssm-ID: 438480 [Multi-domain]  Cd Length: 47  Bit Score: 54.29  E-value: 1.04e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 569006009 291 CIICREEMVTGAKR--LPCNHIFHTSCLRSWFQRQQTCPTCRMDV 333
Cdd:cd23118    3 CTICLEDFEDGEKLrvLPCQHQFHSECVDQWLRRNPKCPVCRRDA 47
mRING-CH-C4HC2H_ZNRF1 cd16694
Modified RING-CH finger, H2 subclass (C4HC2H-type), found in zinc/RING finger protein 1 (ZNRF1) ...
291-327 1.52e-09

Modified RING-CH finger, H2 subclass (C4HC2H-type), found in zinc/RING finger protein 1 (ZNRF1) and similar proteins; ZNRF1, also known as Nerve injury-induced gene 283 protein (nin283), or peripheral nerve injury protein (PNIP), is an E3 ubiquitin-protein ligase that is highly expressed in the nervous system during development and is associated with synaptic vesicle membranes. It is N-myrisotoylated and is also located in the endosome-lysosome compartment in fibroblasts, suggesting it may participate in ubiquitin-mediated protein modification. It contains an N-terminal MAGE domain, and a special C-terminal domain that combines a zinc finger and a modified C4HC2H-type RING-CH finger, rather than the typical C4HC3-type RING-CH finger, which is a variant of the RING-H2 finger. Only the RING finger of the zinc finger-RING finger motif is required for its E3 ubiquitin ligase activity. ZNRF1 regulates Schwann cell differentiation by proteasomal degradation of glutamine synthetase (GS). It also mediates regulation of neuritogenesis via interaction with beta-tubulin type 2 (Tubb2). Moreover, ZNRF1 promotes Wallerian degeneration by degrading AKT to induce glycogen synthase kinase-3beta (GSK3B)-dependent CRMP2 phosphorylation. Furthermore, ZNRF1 and its sister protein ZNRF2 regulate the ubiquitous Na+/K+ pump (Na+/K+ATPase). In addition, ZNRF1 may be associated with leukemogenesis of acute lymphoblastic leukemia (ALL) with paired box domain gene 5 (PAX5) alteration.


Pssm-ID: 438355 [Multi-domain]  Cd Length: 45  Bit Score: 53.88  E-value: 1.52e-09
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 569006009 291 CIICREEMVTG--AKRLPCNHIFHTSCLRSWFQRQQTCP 327
Cdd:cd16694    2 CVICLEELLQGdtIARLPCLCIYHKSCIDSWFEVNRSCP 40
RING-H2_BB-like cd23115
RING finger, H2 subclass, found in Arabidopsis thaliana RING-type E3 ubiquitin transferase BIG ...
291-333 2.18e-09

RING finger, H2 subclass, found in Arabidopsis thaliana RING-type E3 ubiquitin transferase BIG BROTHER (BB) and similar proteins; BB (also known as protein ENHANCER OF DA1-1 or EOD1) is an E3 ubiquitin-protein ligase that limits organ size, and possibly seed size, in a dose-dependent manner. It negatively regulates the duration of cell proliferation in leaves and petals independently of the major phytohormones (e.g. auxin, cytokinin, gibberellin, brassinosteroids, ethylene, abscisic acid, jasmonic acid), probably by targeting growth stimulators for degradation. It limits the proliferation of root meristematic cells. BB polyubiquitinates DA1. It is involved in the promotion of leaf senescence, in addition to its function in restricting plant growth. BB-related is an E3 ubiquitin-ligase probably involved in organ size regulation. Members of this subfamily contain a C3H2C3-type RING-H2 finger.


Pssm-ID: 438477 [Multi-domain]  Cd Length: 52  Bit Score: 53.60  E-value: 2.18e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 569006009 291 CIICREEMVTG--AKRLPCNHIFHTSCLRSWFQRQQTCPTCRMDV 333
Cdd:cd23115    7 CVICRLEYEEGedLLTLPCKHCYHSECIQQWLQINKVCPVCSAEV 51
RING-H2_RNF44 cd16680
RING finger, H2 subclass, found in RING finger protein 44 (RNF44) and similar proteins; RNF44 ...
282-332 3.11e-09

RING finger, H2 subclass, found in RING finger protein 44 (RNF44) and similar proteins; RNF44 is an uncharacterized RING finger protein that shows high sequence similarity with RNF38, which is a nuclear E3 ubiquitin protein ligase that plays a role in regulating p53. RNF44 contains a coiled-coil motif, a KIL motif (Lys-X2-Ile/Leu-X2-Ile/Leu, X can be any amino acid), and a C3H2C2-type RING-H2 finger.


Pssm-ID: 438342 [Multi-domain]  Cd Length: 62  Bit Score: 53.15  E-value: 3.11e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 569006009 282 EELQAMDNVCIICREEMVTGA--KRLPCNHIFHTSCLRSWFQRQQTCPTCRMD 332
Cdd:cd16680    1 ENHQSEQTLCVVCFSDFESRQllRVLPCNHEFHTKCVDKWLKTNRTCPICRAD 53
RING-H2_RNF165 cd16682
RING finger, H2 subclass, found in RING finger protein 165 (RNF165) and similar proteins; ...
282-333 3.55e-09

RING finger, H2 subclass, found in RING finger protein 165 (RNF165) and similar proteins; RNF165, also known as Arkadia-like 2, Arkadia2, or Ark2C, is an E3 ubiquitin ligase with homology to the C-terminal half of RNF111. It is expressed specifically in the nervous system, and can serve to amplify neuronal responses to specific signals. It acts as a positive regulator of bone morphogenetic protein (BMP)-Smad signaling that is involved in motor neuron (MN) axon elongation. RNF165 contains two serine rich domains, a nuclear localization signal, an NRG-TIER domain, and a C-terminal C3H2C3-type RING-H2 finger that is responsible for the enhancement of BMP-Smad1/5/8 signaling in the spinal cord.


Pssm-ID: 438344 [Multi-domain]  Cd Length: 59  Bit Score: 53.16  E-value: 3.55e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 569006009 282 EELQAMDNVCIICREEMVTG--AKRLPCNHIFHTSCLRSWFQRQQTCPTCRMDV 333
Cdd:cd16682    1 GEESDTDEKCTICLSMLEDGedVRRLPCMHLFHQLCVDQWLAMSKKCPICRVDI 54
RING-H2_EL5-like cd16461
RING finger, H2 subclass, found in rice E3 ubiquitin-protein ligase EL5 and similar proteins; ...
291-330 3.69e-09

RING finger, H2 subclass, found in rice E3 ubiquitin-protein ligase EL5 and similar proteins; EL5, also known as protein ELICITOR 5, is an E3 ubiquitin-protein ligase containing an N-terminal transmembrane domain and a C3H2C3-type RING-H2 finger that is a binding site for ubiquitin-conjugating enzyme (E2). It can be rapidly induced by N-acetylchitooligosaccharide elicitor. EL5 catalyzes polyubiquitination via the Lys48 residue of ubiquitin, and thus plays a crucial role as a membrane-anchored E3 in the maintenance of cell viability after the initiation of root primordial formation in rice. It also acts as an anti-cell death enzyme that might be responsible for mediating the degradation of cytotoxic proteins produced in root cells after the actions of phytohormones. Moreover, EL5 interacts with UBC5b, a rice ubiquitin carrier protein, through its RING-H2 finger. EL5 is an unstable protein, and its degradation is regulated by the C3H2C3-type RING-H2 finger in a proteasome-independent manner.


Pssm-ID: 438124 [Multi-domain]  Cd Length: 44  Bit Score: 52.65  E-value: 3.69e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 569006009 291 CIICREEMVTGAK--RLP-CNHIFHTSCLRSWFQRQQTCPTCR 330
Cdd:cd16461    2 CAICLSDYENGEElrRLPeCKHAFHKECIDEWLKSNSTCPLCR 44
RING-H2_RNF181 cd16669
RING finger, H2 subclass, found in RING finger protein 181 (RNF181) and similar proteins; ...
291-332 5.08e-09

RING finger, H2 subclass, found in RING finger protein 181 (RNF181) and similar proteins; RNF181, also known as HSPC238, is a platelet E3 ubiquitin-protein ligase containing a C3H2C3-type RING-H2 finger. It interacts with the KVGFFKR motif of platelet integrin alpha(IIb)beta3, suggesting a role for RNF181-mediated ubiquitination in integrin and platelet signaling. It also suppresses the tumorigenesis of hepatocellular carcinoma (HCC) through the inhibition of extracellular signal-regulated kinase/mitogen-activated protein kinase (ERK/MAPK) signaling in the liver.


Pssm-ID: 438331 [Multi-domain]  Cd Length: 46  Bit Score: 52.37  E-value: 5.08e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 569006009 291 CIICRE--EMVTGAKRLPCNHIFHTSCLRSWFQRQQTCPTCRMD 332
Cdd:cd16669    2 CPICLLefEEGETVKQLPCKHSFHSDCILPWLGKTNSCPLCRHE 45
RING-H2_RNF32_rpt1 cd16677
first RING finger, H2 subclass, found in RING finger protein 32 (RNF32) and similar proteins; ...
290-331 7.05e-09

first 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. This model corresponds to the first RING-H2 finger.


Pssm-ID: 438339 [Multi-domain]  Cd Length: 49  Bit Score: 51.92  E-value: 7.05e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 569006009 290 VCIICREEMVTGAK-RLPCNHIFHTSCLRSW--FQRQQTCPTCRM 331
Cdd:cd16677    1 PCPICLEDFGLQQQvLLSCSHVFHRACLESFerFSGKKTCPMCRK 45
RING-H2_RNF121-like cd16475
RING finger, H2 subclass, found in RING finger proteins RNF121, RNF175 and similar proteins; ...
289-330 9.49e-09

RING finger, H2 subclass, found in RING finger proteins RNF121, RNF175 and similar proteins; This subfamily includes RNF121, RNF175 and similar proteins. RNF121 is an E3-ubiquitin ligase present in the endoplasmic reticulum (ER) and cis-Golgi compartments. It is a novel regulator of apoptosis. It also facilitates the degradation and membrane localization of voltage-gated sodium (NaV) channels, and thus plays a role in the quality control of NaV channels during their synthesis and subsequent transport to the membrane. Moreover, RNF121 acts as a broad regulator of nuclear factor kappaB (NF-kappaB) signaling since its silencing also dampens NF-kappaB activation following stimulation of toll-like receptors (TLRs), nod-like receptors (NLRs), RIG-I-like Receptors (RLRs) or after DNA damage. RNF121 contains five conserved transmembrane (TM) domains and a C3H2C2-type RING-H2 finger. RNF175 is an uncharacterized RING finger protein that shows high sequence similarity with RNF121. This family also includes Arabidopsis RING finger E3 ligase RHA2A, RHA2B, and their homologs. RHA2A is a positive regulator of abscisic acid (ABA) signaling during seed germination and early seedling development. RHA2B may play a role in the ubiquitin-dependent proteolysis pathway that respond to proteasome inhibition. All subfamily members contain a C3H2C3-type RING-H2 finger, which is responsible for E3-ubiquitin ligase activity.


Pssm-ID: 438138 [Multi-domain]  Cd Length: 55  Bit Score: 51.53  E-value: 9.49e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 569006009 289 NVCIICR---------EEMVTGAKRLPCNHIFHTSCLRSW--FQRQQTCPTCR 330
Cdd:cd16475    1 NVCAVCGqkldvddneEGIIEKTYKLSCNHVFHEFCIRGWciVGKKQTCPYCK 53
RING-H2_RNF149 cd16804
RING finger, H2 subclass, found in RING finger protein 149 (RNF149) and similar proteins; ...
291-335 9.79e-09

RING finger, H2 subclass, found in RING finger protein 149 (RNF149) and similar proteins; RNF149, also known as DNA polymerase-transactivated protein 2, is an E3 ubiquitin-protein ligase that interacts with wild-type v-Raf murine sarcoma viral oncogene homolog B1 (BRAF), a RING domain-containing E3 ubiquitin ligase involved in control of gene transcription, translation, cytoskeletal organization, cell adhesion, and epithelial development. RNF149 induces the ubiquitination of wild-type BRAF and promotes its proteasome-dependent degradation. Mutated RNF149 has been found in some human breast, ovarian, and colorectal cancers. RNF149 contains an N-terminal signal peptide, a protease-associated (PA) domain, a transmembrane (TM) domain and a C-terminal C3H2C3-type RING-H2 finger domain followed by a putative PEST sequence.


Pssm-ID: 438455 [Multi-domain]  Cd Length: 48  Bit Score: 51.44  E-value: 9.79e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 569006009 291 CIICREEMVTG--AKRLPCNHIFHTSCLRSWFQRQQTCPTCRMDVLR 335
Cdd:cd16804    2 CAVCIENYKSKdvVRILPCKHVFHRICIDPWLLEHRTCPMCKLDVIK 48
RING-H2_BRAP2 cd16457
RING finger, H2 subclass, found in BRCA1-associated protein (BRAP2) and similar proteins; ...
291-330 1.09e-08

RING finger, H2 subclass, found in BRCA1-associated protein (BRAP2) and similar proteins; BRAP2, also known as impedes mitogenic signal propagation (IMP), RING finger protein 52, or renal carcinoma antigen NY-REN-63, is a novel cytoplasmic protein interacting with the two functional nuclear localization signal (NLS) motifs of BRCA1, a nuclear protein linked to breast cancer. It also binds to the SV40 large T antigen NLS motif and the bipartite NLS motif found in mitosin. BRAP2 serves as a cytoplasmic retention protein and plays a role in the regulation of nuclear protein transport. It contains an N-terminal RNA recognition motif (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain), followed by a C3H2C3-type RING-H2 finger and a UBP-type zinc finger.


Pssm-ID: 438121 [Multi-domain]  Cd Length: 44  Bit Score: 51.13  E-value: 1.09e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 569006009 291 CIICREEM---VTGAKRLPCNHIFHTSCLRSWFQRqqTCPTCR 330
Cdd:cd16457    3 CPVCLERMdesVSGILTILCNHSFHCSCLSKWGDS--SCPVCR 43
RING-H2_TRAIP cd16480
RING finger, H2 subclass, found in TRAF-interacting protein (TRAIP) and similar proteins; ...
291-330 1.10e-08

RING finger, H2 subclass, found in TRAF-interacting protein (TRAIP) and similar proteins; TRAIP, also known as RING finger protein 206 (RNF206) or TRIP, is a ubiquitously expressed nucleolar E3 ubiquitin ligase important for cellular proliferation and differentiation. It is found near mitotic chromosomes and functions as a regulator of the spindle assembly checkpoint. TRAIP interacts with tumor necrosis factor (TNF)-receptor-associated factor (TRAF) proteins and inhibits TNF-alpha-mediated nuclear factor (NF)-kappaB activation. It also interacts with two tumor suppressors CYLD and spleen tyrosine kinase (Syk), and DNA polymerase eta, which facilitates translesional synthesis after DNA damage. TRAIP contains an N-terminal C3H2C2-type RING-H2 finger and an extended coiled-coil domain.


Pssm-ID: 438143 [Multi-domain]  Cd Length: 43  Bit Score: 51.27  E-value: 1.10e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 569006009 291 CIICREEMVTG--AKRLPCNHIFHTSCLRSWFQRQQTCPTCR 330
Cdd:cd16480    2 CTICSDFFDNSrdVAAIHCGHTFHYDCLLQWFDTSRTCPQCR 43
RING-H2_RNF12 cd16674
RING finger, H2 subclass, found in RING finger protein 12 (RNF12) and similar proteins; RNF12, ...
291-337 1.15e-08

RING finger, H2 subclass, found in RING finger protein 12 (RNF12) and similar proteins; RNF12, also known as LIM domain-interacting RING finger protein or RING finger LIM domain-binding protein (R-LIM), is an E3 ubiquitin-protein ligase encoded by gene RLIM that is crucial for normal embryonic development in some species and for normal X inactivation in mice. It thus functions as a major sex-specific epigenetic regulator of female mouse nurturing tissues. RNF12 is widely expressed during embryogenesis, and mainly localizes to the cell nucleus, where it regulates the levels of many proteins, including CLIM, LMO, HDAC2, TRF1, SMAD7, and REX1, by proteasomal degradation. Its functional activity is regulated by phosphorylation-dependent nucleocytoplasmic shuttling. It is negatively regulated by pluripotency factors in embryonic stem cells. p53 represses its transcription through Sp1. RNF12 is the primary factor responsible for X chromosome inactivation (XCI) in female placental mammals. It is an indispensable factor in up-regulation of Xist transcription, thereby leading to initiation of random XCI. It also targets REX1, an inhibitor of XCI, for proteasomal degradation. RNF12 also acts as a co-regulator for a range of transcription factors, particularly those containing a LIM homeodomain, and modulates the formation of transcriptional multiprotein complexes. It is a negative regulator of Smad7, which in turn negatively regulates the signaling of type I receptors from the transforming growth factor beta (TGF-beta) superfamily. In addition, paternal RNF12 is a critical survival factor for milk-producing alveolar cells. RNF12 contains an nuclear localization signal (NLS) and a C3H2C3-type RING-H2 finger.


Pssm-ID: 438336 [Multi-domain]  Cd Length: 51  Bit Score: 51.26  E-value: 1.15e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 569006009 291 CIICREEMVTGAK--RLPCNHIFHTSCLRSWFQRQQTCPTCRMDVLRAS 337
Cdd:cd16674    3 CSVCITEYTEGNKlrKLPCSHEYHVHCIDRWLSENSTCPICRRAVLASG 51
RING-H2_RNF167 cd16797
RING finger, H2 subclass, found in RING finger protein 167 (RNF167) and similar proteins; ...
289-330 1.99e-08

RING finger, H2 subclass, found in RING finger protein 167 (RNF167) and similar proteins; RNF167, also known as RING105, is an endosomal/lysosomal E3 ubiquitin-protein ligase involved in alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR) ubiquitination. It ubiquitinates AMPA-type glutamate receptor subunit GluA2 and regulates its surface expression, and thus acts as a selective regulator of AMPAR-mediated neurotransmission. It acts as an endosomal membrane protein which ubiquitylates vesicle-associated membrane protein 3 (VAMP3) and regulates endosomal trafficking. Moreover, RNF167 plays a role in the regulation of TSSC5 (tumor-suppressing subchromosomal transferable fragment cDNA, also known as ORCTL2/IMPT1/BWR1A/SLC22A1L), which can function in concert with the ubiquitin-conjugating enzyme UbcH6. RNF167 is widely conserved in metazoans and contains an N-terminal signal peptide, a protease-associated (PA) domain, two transmembrane domains (TM1 and TM2), and a C-terminal C3H2C3-type RING-H2 finger domain followed by a putative PEST sequence.


Pssm-ID: 319711 [Multi-domain]  Cd Length: 46  Bit Score: 50.43  E-value: 1.99e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 569006009 289 NVCIICREEMVTGAKR--LPCNHIFHTSCLRSWFQR-QQTCPTCR 330
Cdd:cd16797    1 DVCAICLDEYEEGDKLrvLPCSHAYHSKCVDPWLTQtKKTCPVCK 45
RING-H2_ASR1 cd23120
RING finger, H2 subclass, found in Saccharomyces cerevisiae alcohol-sensitive RING finger ...
290-334 2.18e-08

RING finger, H2 subclass, found in Saccharomyces cerevisiae alcohol-sensitive RING finger protein 1 (ASR1) and similar proteins; ASR1 is required for tolerance to alcohol. It signals alcohol stress to the nucleus. ASR1 contains a C3H2C3-type RING-H2 finger.


Pssm-ID: 438482 [Multi-domain]  Cd Length: 54  Bit Score: 50.61  E-value: 2.18e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 569006009 290 VCIICREEMVTGAKRL-PCNHIFHTSCLRSWFQR--QQTCPTCRMDVL 334
Cdd:cd23120    3 ECPICLEEMNSGTGYLaDCGHEFHLTCIREWHNKsgNLDCPICRVESL 50
RING-H2_RNF24-like cd16469
RING finger, H2 subclass, found in RING finger proteins RNF24, RNF122, and similar proteins; ...
290-333 2.23e-08

RING finger, H2 subclass, found in RING finger proteins RNF24, RNF122, and similar proteins; This subfamily includes RNF24, RNF122, and similar proteins. RNF24 is an intrinsic membrane protein localized in the Golgi apparatus. It specifically interacts with the ankyrin-repeats domains (ARDs) of TRPC1, -3, -4, -5, -6, and -7, and affects TRPC intracellular trafficking without affecting their activity. RNF122 is a RING finger protein associated with HEK 293T cell viability. It is localized to the endoplasmic reticulum (ER) and the Golgi apparatus, and overexpressed in anaplastic thyroid cancer cells. RNF122 functions as an E3 ubiquitin ligase that can ubiquitinate itself and undergo degradation through its RING finger in a proteasome-dependent manner. Both RNF24 and RNF122 contain an N-terminal transmembrane domain and a C-terminal C3H2C3-type RING-H2 finger.


Pssm-ID: 438132 [Multi-domain]  Cd Length: 47  Bit Score: 50.46  E-value: 2.23e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 569006009 290 VCIICREEMVTGAK--RLPCNHIFHTSCLRSWFQRQQTCPTCRMDV 333
Cdd:cd16469    2 TCAVCLEEFKLKEElgVCPCGHAFHTKCLKKWLEVRNSCPICKSPV 47
RING-H2_RNF145 cd16684
RING finger, H2 subclass, found in RING finger protein 145 (RNF145) and similar proteins; ...
288-329 2.49e-08

RING finger, H2 subclass, found in RING finger protein 145 (RNF145) and similar proteins; 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, 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. Like RNF139, RNF145 contains a C3H2C3-type RING-H2 finger with possible E3-ubiquitin ligase activity.


Pssm-ID: 319598 [Multi-domain]  Cd Length: 43  Bit Score: 50.06  E-value: 2.49e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 569006009 288 DNVCIICREEMvTGAKRLPCNHIFHTSCLRSWFQRQQTCPTC 329
Cdd:cd16684    2 NDICSICYQDM-KSAVITPCSHFFHAGCLKKWLYVQETCPLC 42
RING-H2_RNF111 cd16681
RING finger, H2 subclass, found in RING finger protein 111 (RNF111) and similar proteins; ...
291-333 3.70e-08

RING finger, H2 subclass, found in RING finger protein 111 (RNF111) and similar proteins; RNF111, also known as Arkadia, is a nuclear E3 ubiquitin-protein ligase that targets intracellular effectors and modulators of transforming growth factor beta (TGF-beta)/Nodal-related signaling for polyubiquitination and proteasome-dependent degradation. It acts as an amplifier of Nodal signals, and enhances the dorsalizing activity of limiting amounts of Xnr1, a Nodal homolog, and requires Nodal signaling for its function. The loss of RNF111 results in early embryonic lethality, with defects attributed to compromised Nodal signaling. RNF111 also regulates tumor metastasis by modulation of the TGF-beta pathway. Its ubiquitination can be modulated by the four and a half LIM-only protein 2 (FHL2) that activates TGF-beta signal transduction. Furthermore, RNF111 interacts with the clathrin-adaptor 2 (AP2) complex and regulates endocytosis of certain cell surface receptors, leading to modulation of epidermal growth factor (EGF) and possibly other signaling pathways. In addition, RNF111 has been identified as a small ubiquitin-like modifier (SUMO)-binding protein with clustered SUMO-interacting motifs (SIMs) that together form a SUMO-binding domain (SBD). It thus functions as a SUMO-targeted ubiquitin ligase (STUbL) that directly links nonproteolytic ubiquitylation and SUMOylation in the DNA damage response, as well as triggers degradation of signal-induced polysumoylated proteins, such as the promyelocytic leukemia protein (PML). The N-terminal half of RNF111 harbors three SIMs. Its C-terminal half show high sequence similarity with RING finger protein 165 (RNF165), where it contains two serine rich domains, two nuclear localization signals, an NRG-TIER domain, and a C-terminal C3H2C3-type RING-H2 finger that is required for polyubiqutination and proteasome-dependent degradation of phosphorylated forms of Smad2/3 and three major negative regulators of TGF-beta signaling, Smad7, SnoN and c-Ski.


Pssm-ID: 438343 [Multi-domain]  Cd Length: 61  Bit Score: 50.45  E-value: 3.70e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 569006009 291 CIICREEMVTG--AKRLPCNHIFHTSCLRSWFQRQQTCPTCRMDV 333
Cdd:cd16681   13 CTICLSILEEGedVRRLPCMHLFHQVCVDQWLITNKKCPICRVDI 57
RING-HC_RNFT1 cd16741
RING finger, HC subclass, found in RING finger and transmembrane domain-containing protein 1 ...
279-330 4.19e-08

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: 49.88  E-value: 4.19e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 569006009 279 ATPEELQAMDNVCIICREEMvTGAKRLPCNHIFHTSCLRSWFQRQQTCPTCR 330
Cdd:cd16741    5 ASKRQCSEADDICAICQAEF-RKPILLICQHVFCEECISLWFNREKTCPLCR 55
RING-H2_RNF38-like cd16472
RING finger, H2 subclass, found in RING finger proteins RNF38, RNF44, and similar proteins; ...
291-330 4.78e-08

RING finger, H2 subclass, found in RING finger proteins RNF38, RNF44, and similar proteins; This subfamily includes RING finger proteins RNF38, RNF44, and similar proteins. RNF38 is a nuclear E3 ubiquitin protein ligase that plays a role in regulating p53. RNF44 is an uncharacterized RING finger protein that shows high sequence similarity to RNF38. Both RNF38 and RNF44 contain a coiled-coil motif, a KIL motif (Lys-X2-Ile/Leu-X2-Ile/Leu, X can be any amino acid), and a C3H2C3-type RING-H2 finger. In addition, RNF38 harbors two potential nuclear localization signals.


Pssm-ID: 438135 [Multi-domain]  Cd Length: 46  Bit Score: 49.25  E-value: 4.78e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 569006009 291 CIICREEMVTGAK--RLPCNHIFHTSCLRSWFQRQQTCPTCR 330
Cdd:cd16472    5 CVVCMCDYEKRQLlrVLPCSHEFHAKCIDKWLKTNRTCPICR 46
RING-H2_RNF130 cd16803
RING finger, H2 subclass, found in RING finger protein 130 (RNF130) and similar proteins; ...
291-335 5.20e-08

RING finger, H2 subclass, found in RING finger protein 130 (RNF130) and similar proteins; RNF130, also known as Goliath homolog (H-Goliath), is a paralog of RNF128, also known as gene related to anergy in lymphocytes protein (GRAIL). It is a transmembrane E3 ubiquitin-protein ligase expressed in leukocytes. It has a self-ubiquitination property, and controls the development of T cell clonal anergy by ubiquitination. RNF130 contains an N-terminal signal peptide, a protease-associated (PA) domain, a transmembrane (TM) domain and a C-terminal C3H2C3-type RING-H2 finger domain followed by a putative PEST sequence.


Pssm-ID: 319717 [Multi-domain]  Cd Length: 49  Bit Score: 49.59  E-value: 5.20e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 569006009 291 CIICREEMVTG--AKRLPCNHIFHTSCLRSWFQRQQTCPTCRMDVLR 335
Cdd:cd16803    3 CAVCIEGYKQNdvVRILPCKHVFHKSCVDPWLNEHCTCPMCKLNILK 49
RING-HC_EHV1-like cd23130
RING finger, HC subclass, found in Equid alphaherpesvirus 1 (Equine herpesvirus 1/EHV-1) ...
289-330 5.97e-08

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: 49.27  E-value: 5.97e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 569006009 289 NVCIICREEMVTGAKRLPCNHIFHTSCLRSWFQRQQTCPTCR 330
Cdd:cd23130    1 DVCPICLDDPEDEAITLPCLHQFCYTCILRWLQTSPTCPLCK 42
RING-H2_RHA1-like cd23121
RING finger, H2 subclass, found in Arabidopsis thaliana RING-H2 finger A1a (RHA1A), A1b (RHA1B) ...
288-332 5.98e-08

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: 49.41  E-value: 5.98e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 569006009 288 DNVCIICREEMVTGAK--RLP-CNHIFHTSCLRSWF-QRQQTCPTCRMD 332
Cdd:cd23121    1 DDCCAICLSDFNSDEKlrQLPkCGHIFHHHCLDRWIrYNKITCPLCRAD 49
RING-H2_RHA2B cd23123
RING finger, H2 subclass, found in Saccharomyces cerevisiae RING-H2 zinc finger protein RHA2B ...
291-330 6.51e-08

RING finger, H2 subclass, found in Saccharomyces cerevisiae RING-H2 zinc finger protein RHA2B and similar proteins; RHA2B is an E3 ubiquitin-protein ligase involved in the positive regulation of abscisic acid (ABA) signaling and responses to salt and osmotic stresses during seed germination and early seedling development. It acts additively with RHA2A in regulating ABA signaling and drought response. RHA2B contains a C3H2C3-type RING-H2 finger.


Pssm-ID: 438485 [Multi-domain]  Cd Length: 47  Bit Score: 49.12  E-value: 6.51e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 569006009 291 CIICREEMVTG--AKRLPCNHIFHTSCLRSWFQRQQ-TCPTCR 330
Cdd:cd23123    3 CCICLDKLKTGeeVKKLDCRHKFHKQCIEGWLKHLNfNCPLCR 45
mRING-C3HGC3_RFWD3 cd16450
Modified RING finger, C3HGC3-type, found in RING finger and WD repeat domain-containing ...
288-330 1.11e-07

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: 48.77  E-value: 1.11e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 569006009 288 DNVCIICREEMVT-GAKR---LPCNHIFHTSCLRSWFQRQQ-TCPTCR 330
Cdd:cd16450    2 GNTCPICFEPWTSsGEHRlvsLKCGHLFGYSCIEKWLKGKGkKCPQCN 49
RING-HC_CHFR cd16503
RING finger, HC subclass, found in checkpoint with forkhead and RING finger domains protein ...
290-337 1.12e-07

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: 48.52  E-value: 1.12e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 569006009 290 VCIICRE---EMVTGAkrlPCNHIFHTSCLRSWFQRQ-QTCPTCRMDVLRAS 337
Cdd:cd16503    4 TCSICQDllhDCVSLQ---PCMHNFCAACYSDWMERSnTECPTCRATVQRVN 52
RING-H2_RNF130-like cd16668
RING finger, H2 subclass, found in RING finger proteins, RNF130, RNF149, RNF150 and similar ...
291-333 1.20e-07

RING finger, H2 subclass, found in RING finger proteins, RNF130, RNF149, RNF150 and similar proteins; This subfamily includes RING finger proteins, RNF130, RNF149 and RNF150, which belong to a larger PA-TM-RING ubiquitin ligase family that has been characterized by an N-terminal signal peptide, a protease-associated (PA) domain, a transmembrane (TM) domain and a C-terminal C3H2C3-type RING-H2 finger domain followed by a putative PEST sequence. RNF130, also known as Goliath homolog (H-Goliath), is a paralog of RNF128. It is a transmembrane E3 ubiquitin-protein ligase expressed in leukocytes. It has a self-ubiquitination property and controls the development of T cell clonal anergy by ubiquitination. RNF133 is a testis-specific endoplasmic reticulum-associated E3 ubiquitin ligase that may play a role in sperm maturation through an ER-associated degradation (ERAD) pathway. RNF149, also known as DNA polymerase-transactivated protein 2, is an E3 ubiquitin-protein ligase that induces the ubiquitination of wild-type v-Raf murine sarcoma viral oncogene homolog B1 (BRAF) and promotes its proteasome-dependent degradation. RNF150 polymorphisms may be associated with chronic obstructive pulmonary disease (COPD) risk in the Chinese population. This subfamily also includes Drosophila melanogaster protein goliath (d-goliath), also known as protein g1, which is one of the founding members of the group. It was originally identified as a transcription factor involved in the embryo mesoderm formation.


Pssm-ID: 438330 [Multi-domain]  Cd Length: 46  Bit Score: 48.16  E-value: 1.20e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 569006009 291 CIICREEMVTG--AKRLPCNHIFHTSCLRSWFQRQQTCPTCRMDV 333
Cdd:cd16668    2 CAVCIEPYKPSdvIRILPCKHIFHKSCVDPWLLEHRTCPMCKLDI 46
RING-H2_MBR cd23113
RING finger, H2 subclass, found in Arabidopsis thaliana MED25-binding RING-H2 protein (MBR) ...
291-334 1.21e-07

RING finger, H2 subclass, found in Arabidopsis thaliana MED25-binding RING-H2 protein (MBR) and similar proteins; This subfamily includes MBR1 and MBR2 (also called HAL3-interacting protein 1 or AtHIP1). They are E3 ubiquitin-protein ligases that function as regulators of MED25 stability by targeting MED25 for degradation in a RING-H2-dependent manner. Proteasome-dependent degradation of MED25 seems to activate its function as a positive regulator of FLOWERING LOCUS T (FT) and is important to induce the expression of FT, and consequently to promote flowering. MBR2 may also function downstream of HAL3 and be required for HAL3-regulated plant growth. Activation of MBR2 by HAL3 may lead to the degradation of cell cycle suppressors, resulting in enhancement of cell division and plant growth. Both MBR1 and MBR2 contain a C3H2C3-type RING-H2 finger.


Pssm-ID: 438475 [Multi-domain]  Cd Length: 50  Bit Score: 48.33  E-value: 1.21e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 569006009 291 CIICREEMVTGAK--RLPCNHIFHTSCLRSWFQRQQTCPTCRMDVL 334
Cdd:cd23113    5 CCICQEEYEEGDElgTIECGHEYHSDCIKQWLVQKNLCPICKATAL 50
RING-H2_RNF38 cd16679
RING finger, H2 subclass, found in RING finger protein 38 (RNF38) and similar proteins; RNF38 ...
281-332 1.22e-07

RING finger, H2 subclass, found in RING finger protein 38 (RNF38) and similar proteins; RNF38 is a nuclear E3 ubiquitin protein ligase that is widely expressed throughout the human body, and is especially highly expressed in the heart, brain, placenta and the testis. It recognizes p53 as a substrate for ubiquitination, and thus plays a role in regulating p53. The overexpression of RNF38 increases p53 ubiquitination and alters p53 localization. It is also capable of autoubiquitination. RNF38 expression is negatively regulated by the serotonergic system. Induction of RNF38 may be involved in the anxiety-like behavior or non-cell autonomy in Oryzias latipes by the decline of serotonin (5-HT) levels. RNF38 contains a coiled-coil motif, a KIL motif (Lys-X2-Ile/Leu-X2-Ile/Leu, X can be any amino acid), a C3H2C3-type RING-H2 finger, as well as two potential nuclear localization signals.


Pssm-ID: 438341 [Multi-domain]  Cd Length: 67  Bit Score: 48.90  E-value: 1.22e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 569006009 281 PEELQAMDNVCIICREEMVTGA--KRLPCNHIFHTSCLRSWFQRQQTCPTCRMD 332
Cdd:cd16679   13 PNNHQSEQTLCVVCMCDFESRQllRVLPCNHEFHAKCVDKWLKANRTCPICRAD 66
RING-H2_RNF13 cd16796
RING finger, H2 subclass, found in RING finger protein 13 (RNF13) and similar proteins; RNF13 ...
289-336 1.79e-07

RING finger, H2 subclass, found in RING finger protein 13 (RNF13) and similar proteins; RNF13 is a widely expressed membrane-associated E3 ubiquitin-protein ligase that is functionally significant in the regulation of cancer development, muscle cell growth, and neuronal development. Its expression is developmentally regulated during myogenesis and is upregulated in various tumors. RNF13 negatively regulates cell proliferation through its E3 ligase activity. It functions as an important regulator of inositol-requiring transmembrane kinase/endonuclease IRE1alpha, mediating endoplasmic reticulum (ER) stress-induced apoptosis through the activation of the IRE1alpha-TRAF2-JNK signaling pathway. Moreover, RNF13 is involved in the regulation of the soluble N-ethylmaleimide-sensitive fusion protein attachment protein receptor (SNARE) complex via the ubiquitination of snapin, a SNAP25-interacting protein, which thereby controls synaptic function. In addition, RNF13 participates in regulating the function of satellite cells by modulating cytokine composition. RNF13 is evolutionarily conserved among many metazoans and contains an N-terminal signal peptide, a protease-associated (PA) domain, a transmembrane (TM) domain and a C-terminal C3H2C3-type RING-H2 finger domain followed by a putative PEST sequence.


Pssm-ID: 438450 [Multi-domain]  Cd Length: 59  Bit Score: 48.12  E-value: 1.79e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 569006009 289 NVCIICREEMVTGAKR--LPCNHIFHTSCLRSWFQR-QQTCPTCRMDVLRA 336
Cdd:cd16796    9 DVCAICLDEYEEGDKLriLPCSHAYHCKCVDPWLTKtKKTCPVCKQKVVPS 59
RING-H2_RNF13-like cd16665
RING finger, H2 subclass, found in RING finger protein 13 (RNF13), RING finger protein 167 ...
289-330 2.02e-07

RING finger, H2 subclass, found in RING finger protein 13 (RNF13), RING finger protein 167 (RNF167), and similar proteins; This subfamily includes RING finger protein 13 (RNF13), RING finger protein 167 (RNF167), Zinc/RING finger protein 4 (ZNRF4), and similar proteins, which belong to a larger PA-TM-RING ubiquitin ligase family that has been characterized by containing an N-terminal signal peptide, a protease-associated (PA) domain, a transmembrane domain (TM), and a C-terminal C3H2C3-type RING-H2 finger followed by a putative PEST sequence. RNF13 is a widely expressed membrane-associated E3 ubiquitin-protein ligase that functions in the regulation of cancer development, muscle cell growth, and neuronal development. Its expression is developmentally regulated during myogenesis and is upregulated in various tumors. RNF13 negatively regulates cell proliferation through its E3 ligase activity. RNF167, also known as RING105, is an endosomal/lysosomal E3 ubiquitin-protein ligase involved in the ubiquitination of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR). It acts as an endosomal membrane protein which ubiquitylates vesicle-associated membrane protein 3 (VAMP3) and regulates endosomal trafficking. Moreover, RNF167 plays a role in the regulation of TSSC5 (tumor-suppressing subchromosomal transferable fragment cDNA, also known as ORCTL2/IMPT1/BWR1A/SLC22A1L), which can function in concert with the ubiquitin-conjugating enzyme UbcH6. ZNRF4, also known as RING finger protein 204 (RNF204), or Nixin, is an endoplasmic reticulum (ER) membrane-anchored ubiquitin ligase that physically interacts with the ER-localized chaperone calnexin in a glycosylation-independent manner, inducing calnexin ubiquitination, and p97-dependent degradation. The murine protein sperizin (spermatid-specific ring zinc finger) is a homolog of human ZNRF4. It is specifically expressed in Haploid germ cells and is involved in spermatogenesis.


Pssm-ID: 438327 [Multi-domain]  Cd Length: 46  Bit Score: 47.81  E-value: 2.02e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 569006009 289 NVCIICREEMVTGAKR--LPCNHIFHTSCLRSWFQRQ-QTCPTCR 330
Cdd:cd16665    1 DVCAICLDDYEEGDKLriLPCSHAYHCKCIDPWLTKNkRTCPVCK 45
RING-H2_NIPL1-like cd23119
RING finger, H2 subclass, found in Arabidopsis thaliana NEP1-interacting protein-like 1 (NIPL1) ...
291-330 2.07e-07

RING finger, H2 subclass, found in Arabidopsis thaliana NEP1-interacting protein-like 1 (NIPL1) and similar proteins; This subfamily includes Arabidopsis thaliana NIPL1 and MISFOLDED PROTEIN SENSING RING E3 LIGASE 1 (MPSR1). NIPL1, also called RING-H2 finger protein ATL27, may be involved in the early steps of the plant defense signaling pathway. MPSR1 is a cytoplasmic E3 ubiquitin-protein ligase involved in protein quality control (PQC) under proteotoxic stress. It is essential for plant survival under proteotoxic stress. It functions by removing damaged proteins before they form cytotoxic aggregates. It recognizes misfolded proteins selectively and tethers polyubiquitin chains to the proteins directly for subsequent degradation by the 26S proteasome pathway. Members of this subfamily contain a C3H2C3-type RING-H2 finger.


Pssm-ID: 438481 [Multi-domain]  Cd Length: 44  Bit Score: 47.49  E-value: 2.07e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 569006009 291 CIICREEMVTG--AKRLP-CNHIFHTSCLRSWFQRQQTCPTCR 330
Cdd:cd23119    2 CTICLQDLQVGeiARSLPhCHHTFHLGCVDKWLGRHGSCPVCR 44
RING-HC_ScPSH1-like cd16568
RING finger, HC subclass, found in Saccharomyces cerevisiae POB3/SPT16 histone-associated ...
290-333 2.66e-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: 47.75  E-value: 2.66e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 569006009 290 VCIICREEMVTGAKrLPCNHIFHTSCLRSWF--QRQQTCPTCRMDV 333
Cdd:cd16568    6 ECIICHEYLYEPMV-TTCGHTYCYTCLNTWFksNRSLSCPDCRTKI 50
RING-H2_RNF24 cd16675
RING finger, H2 subclass, found in RING finger protein 24 (RNF24) and similar proteins; RNF24 ...
290-335 2.97e-07

RING finger, H2 subclass, found in RING finger protein 24 (RNF24) and similar proteins; RNF24 is an intrinsic membrane protein localized in the Golgi apparatus. It specifically interacts with the ankyrin-repeats domains (ARDs) of TRPC1, -3, -4, -5, -6, and -7, and affects TRPC intracellular trafficking without affecting their activity. RNF24 contains an N-terminal transmembrane domain and a C-terminal C3H2C3-type RING-H2 finger.


Pssm-ID: 438337 [Multi-domain]  Cd Length: 54  Bit Score: 47.31  E-value: 2.97e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 569006009 290 VCIICREEMVTGAKR--LPCNHIFHTSCLRSWFQRQQTCPTCRMDVLR 335
Cdd:cd16675    2 ICAVCLEEFKPKDELgiCPCKHAFHRKCLIKWLEVRKVCPLCNMPVLQ 49
RING-H2_RNF128-like cd16802
RING finger, H2 subclass, found in RING finger protein 128 (RNF128) and similar proteins; This ...
291-335 4.06e-07

RING finger, H2 subclass, found in RING finger protein 128 (RNF128) and similar proteins; This subfamily includes RING finger proteins RNF128, RNF133, RNF148, and similar proteins, which belong to a larger PA-TM-RING ubiquitin ligase family that has been characterized by containing an N-terminal signal peptide, a protease-associated (PA) domain, a transmembrane (TM) domain and a C-terminal C3H2C3-type RING-H2 finger followed by a putative PEST sequence. RNF128, also known as gene related to anergy in lymphocytes protein (GRAIL), is a type 1 transmembrane E3 ubiquitin-protein ligase that is a critical regulator of adaptive immunity and development. It inhibits cytokine gene transcription, is expressed in anergic CD4+ T cells, and has been implicated in primary T cell activation, survival, and differentiation, as well as in T cell anergy and oral tolerance. It induces T cell anergy through the ubiquitination activity of its cytosolic RING finger. It regulates expression of the costimulatory molecule CD40L on CD4 T cells, and ubiquitinates the costimulatory molecule CD40 ligand (CD40L) during the induction of T cell anergy. Moreover, RNF128 interacts with the luminal/extracellular portion of both CD151 and the related tetraspanin CD81 via its PA domain, which promoted ubiquitination of cytosolic lysine residues. It also down-modulates the expression of CD83 (previously described as a cell surface marker for mature dendritic cells) on CD4 T cells. Furthermore, Rho guanine dissociation inhibitor (RhoGDI) has been identified as a potential substrate of RNF128, suggesting a role for Rho effector molecules in T cell anergy. In addition, RNF128 plays a role in environmental stress responses. It promotes environmental salinity tolerance in euryhaline tilapia. RNF133 is a testis-specific endoplasmic reticulum-associated E3 ubiquitin ligase that is mainly present in the cytoplasm of elongated spermatids. It may play a role in sperm maturation through an ER-associated degradation (ERAD) pathway. RNF148 is a testis-specific E3 ubiquitin ligase that is abundantly expressed in testes and slightly expressed in pancreas. Its expression is regulated by histone deacetylases.


Pssm-ID: 438454 [Multi-domain]  Cd Length: 49  Bit Score: 47.04  E-value: 4.06e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 569006009 291 CIICREEMVTG--AKRLPCNHIFHTSCLRSWFQRQQTCPTCRMDVLR 335
Cdd:cd16802    3 CAVCIEPYKPNdvVRILTCNHLFHKNCIDPWLLEHRTCPMCKCDILK 49
RING-HC_IRC20-like cd23135
RING finger, HC subclass, found in Saccharomyces cerevisiae increased recombination centers ...
291-330 4.39e-07

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: 46.74  E-value: 4.39e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 569006009 291 CIICREEMVTGAKrLPCNHIFHTSCLRSWFQRQQTCPTCR 330
Cdd:cd23135    6 CSICFSEIRSGAI-LKCGHFFCLSCIASWLREKSTCPLCK 44
RING-H2_RNF43-like cd16666
RING finger, H2 subclass, found in RING finger proteins RNF43, ZNRF3, and similar proteins; ...
290-332 6.26e-07

RING finger, H2 subclass, found in RING finger proteins RNF43, ZNRF3, and similar proteins; RNF43 and ZNRF3 (also known as RNF203) are transmembrane E3 ubiquitin-protein ligases that belong to the PA-TM-RING ubiquitin ligase family, characterized by containing an N-terminal signal peptide, a protease-associated (PA) domain, a transmembrane (TM) domain and a C3H2C3-type RING-H2 finger followed by a long C-terminal region. Both RNF43 and RNF203 function as tumor suppressors involved in the regulation of Wnt/beta-catenin signaling. They negatively regulate Wnt signaling by interacting with complexes of frizzled (FZD) receptors and low-density lipoprotein receptor-related protein (LRP) 5/6, which leads to ubiquitination of FZD and endocytosis of the Wnt receptor. Dishevelled (DVL), a positive Wnt regulator, is required for ZNRF3/RNF43-mediated ubiquitination and degradation of FZD. They also associate with R-spondin 1 (RSPO1). This interaction may block FZD ubiquitination and enhances Wnt signaling.


Pssm-ID: 438328 [Multi-domain]  Cd Length: 45  Bit Score: 46.30  E-value: 6.26e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 569006009 290 VCIICREEMVTGA--KRLPCNHIFHTSCLRSWFQRQQTCPTCRMD 332
Cdd:cd16666    1 VCAICLEEYEEGQelRVLPCQHEFHRKCVDPWLLQNHTCPLCLFN 45
RING-HC_RNF8 cd16535
RING finger, HC subclass, found in RING finger protein 8 (RNF8) and similar proteins; RNF8 is ...
283-333 6.95e-07

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: 46.62  E-value: 6.95e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 569006009 283 ELQamdnvCIICREEMVTgAKRLPCNHIFHTSCLRSWFQRQQTCPTCRMDV 333
Cdd:cd16535    1 ELQ-----CSICSELFIE-AVTLNCSHSFCSYCITEWMKRKKECPICRKPI 45
RING-H2_RNF215 cd16670
RING finger, H2 subclass, found in RING finger protein 215 (RNF215) and similar proteins; This ...
291-334 7.52e-07

RING finger, H2 subclass, found in RING finger protein 215 (RNF215) and similar proteins; This family includes uncharacterized protein RNF215 and similar proteins. Although its biological function remains unclear, RNF215 shares high sequence similarity with PA-TM-RING ubiquitin ligases, which have been characterized by containing an N-terminal signal peptide, a protease-associated (PA) domain, a transmembrane (TM) domain and a C-terminal C3H2C3-type RING-H2 finger.


Pssm-ID: 438332 [Multi-domain]  Cd Length: 50  Bit Score: 46.29  E-value: 7.52e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 569006009 291 CIICREEMVTGA--KRLPCNHIFHTSCLRSWFQRQQTCPTCRMDVL 334
Cdd:cd16670    3 CAVCLDQFYKNQclRVLPCLHEFHRDCVDPWLLLQQTCPLCKRNIL 48
RING-HC_RNFT2 cd16742
RING finger, HC subclass, found in RING finger and transmembrane domain-containing protein 2 ...
279-330 7.61e-07

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: 46.80  E-value: 7.61e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 569006009 279 ATPEELQAMDNVCIIC----REEMVtgakrLPCNHIFHTSCLRSWFQRQQTCPTCR 330
Cdd:cd16742    4 ATSQQCSEAGDICAICqaefREPLI-----LICQHVFCEECLCLWFDRERTCPLCR 54
RING-HC_MKRN cd16521
RING finger, HC subclass, found in the makorin (MKRN) proteins; The MKRN protein subfamily ...
290-330 1.89e-06

RING finger, HC subclass, found in the makorin (MKRN) proteins; The MKRN protein subfamily includes ribonucleoproteins that are characterized by a variety of zinc-finger motifs, including typical arrays of one to four C3H1-type zinc fingers and a C3HC4-type RING-HC finger. Another motif rich in Cys and His residues (CH), with so far unknown function, is also generally present in MKRN proteins. MKRN proteins may have E3 ubiquitin ligase activity.


Pssm-ID: 438184 [Multi-domain]  Cd Length: 53  Bit Score: 44.96  E-value: 1.89e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 569006009 290 VCIICREEMVTGAKR---LP-CNHIFHTSCLRSWFQRQQ-------TCPTCR 330
Cdd:cd16521    2 ECGICMEVVLEKERRfgiLSnCNHVFCLECIREWRSSKDfensivrSCPICR 53
RING-H2_RNF43 cd16798
RING finger, H2 subclass, found in RING finger protein 43 (RNF43) and similar proteins; RNF43 ...
290-334 2.03e-06

RING finger, H2 subclass, found in RING finger protein 43 (RNF43) and similar proteins; RNF43 is a transmembrane E3 ubiquitin-protein ligase that plays an important role in frizzled (FZD)-dependent regulation of the Wnt/beta-catenin pathway. It functions as a tumor suppressor that inhibits Wnt/beta-catenin signaling by ubiquitinating FZD receptor and targeting it to the lysosomal pathway for degradation. miR-550a-5p directly targeted the 3'-UTR of gene RNF43 and regulated its expression. Moreover, RNF43 interacts with NEDD-4-like ubiquitin-protein ligase-1 (NEDL1) and regulates p53-mediated transcription. It may also be involved in cell growth control through the interaction with HAP95, a chromatin-associated protein interfacing the nuclear envelope. Mutations of RNF43 have been identified in various tumors, including colorectal cancer (CRC), endometrial cancer, mucinous ovarian tumors, gastric adenocarcinoma, pancreatic ductal adenocarcinoma, liver fluke-associated cholangiocarcinoma, hepatocellular carcinoma, and glioma. RNF43 contains an N-terminal signal peptide, a protease-associated (PA) domain, a transmembrane (TM) domain and a C3H2C3-type RING-H2 finger followed by a long C-terminal region.


Pssm-ID: 438451 [Multi-domain]  Cd Length: 53  Bit Score: 45.24  E-value: 2.03e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 569006009 290 VCIICREEMVTGA--KRLPCNHIFHTSCLRSWFQRQQTCPTCRMDVL 334
Cdd:cd16798    5 VCAICLEEFSEGQelRIISCSHEFHRECVDPWLHQHRTCPLCMFNII 51
RING_Ubox cd00162
RING finger (Really Interesting New Gene) domain and U-box domain superfamily; The RING finger ...
291-329 2.24e-06

RING finger (Really Interesting New Gene) domain and U-box domain superfamily; 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). C4C4-, C3HC3D-, C2H2C4-, and C3HC5-type RING fingers are closely related to RING-HC fingers. In contrast, C4HC3- (RING-CH alias RINGv), C3H3C2-, C3H2C2D-, C3DHC3-, and C4HC2H-type RING fingers are more closely related to RING-H2 fingers. However, not all RING finger-containing proteins display regular RING finger features, and the RING finger family has turned out to be multifarious. The degenerate RING fingers of the Siz/PIAS RING (SP-RING) family proteins and sporulation protein RMD5, are characterized by lacking the second, fifth, and sixth Zn2+ ion-coordinating residues. They bind only one Zn2+ ion. On the other hand, the RING fingers of the human APC11 and RBX1 proteins can bind a third Zn atom since they harbor four additional Zn ligands. U-box is a modified form of the RING finger domain that lacks metal chelating Cys and His residues. It resembles the cross-brace RING structure consisting of three beta-sheets and a single alpha-helix, which would be stabilized by salt bridges instead of chelated metal ions. U-box proteins are widely distributed among eukaryotic organisms and show a higher prevalence in plants than in other organisms. RING finger/U-box-containing proteins are 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 enable efficient transfer of ubiquitin from E2 to the substrates.


Pssm-ID: 438111 [Multi-domain]  Cd Length: 42  Bit Score: 44.76  E-value: 2.24e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 569006009 291 CIICREEMvTGAKRL---PCNHIFHTSCLRSWFQ-RQQTCPTC 329
Cdd:cd00162    1 CPICREEM-NDRRPVvllSCGHTFSRSAIARWLEgSKQKCPFC 42
RING-H2_RNF150 cd16805
RING finger, H2 subclass, found in RING finger protein 150 (RNF150) and similar proteins; ...
305-335 2.41e-06

RING finger, H2 subclass, found in RING finger protein 150 (RNF150) and similar proteins; RNF150 is a RING finger protein and its polymorphisms may be associated with chronic obstructive pulmonary disease (COPD) risk in the Chinese population. Further studies with larger numbers of participants worldwide are needed for validation of the relationships between RNF150 genetic variants and the pathogenesis of COPD. RNF150 contains an N-terminal signal peptide, a protease-associated (PA) domain, a transmembrane (TM) domain and a C-terminal C3H2C3-type RING-H2 finger domain followed by a putative PEST sequence.


Pssm-ID: 438456 [Multi-domain]  Cd Length: 55  Bit Score: 45.05  E-value: 2.41e-06
                         10        20        30
                 ....*....|....*....|....*....|.
gi 569006009 305 LPCNHIFHTSCLRSWFQRQQTCPTCRMDVLR 335
Cdd:cd16805   25 LPCRHLFHKSCVDPWLLDHRTCPMCKMNILK 55
RING-H2_ZNRF3 cd16799
RING finger, H2 subclass, found in zinc/RING finger protein 3 (ZNRF3) and similar proteins; ...
291-330 2.50e-06

RING finger, H2 subclass, found in zinc/RING finger protein 3 (ZNRF3) and similar proteins; ZNRF3, also known as RING finger protein 203 (RNF203), is a homolog of Ring finger protein 43 (RNF43). It is a transmembrane E3 ubiquitin-protein ligase that is associated with the Wnt receptor complex, and negatively regulates Wnt signaling by promoting the turnover of frizzled and lipoprotein receptor-related protein LRP6 in an R-spondin-sensitive manner. It inhibits gastric cancer cell growth and promotes cell apoptosis by affecting the Wnt/beta-catenin/TCF signaling pathway. ZNRF3 contains an N-terminal signal peptide, a protease-associated (PA) domain, a transmembrane (TM) domain and a C3H2C3-type RING-H2 finger followed by a long C-terminal region.


Pssm-ID: 319713 [Multi-domain]  Cd Length: 45  Bit Score: 44.63  E-value: 2.50e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 569006009 291 CIICREEMVTGA--KRLPCNHIFHTSCLRSWFQRQQTCPTCR 330
Cdd:cd16799    2 CAICLEKYIDGEelRVIPCTHRFHKKCVDPWLLQHHTCPHCR 43
mRING-H2-C3H3C2_Mio-like cd16488
Modified RING finger, H2 subclass (C3H3C2-type), found in WD repeat-containing protein mio and ...
291-328 3.45e-06

Modified RING finger, H2 subclass (C3H3C2-type), found in WD repeat-containing protein mio and its homologs; This subfamily contains Mio, WDR24, WDR59, and their counterparts Sea4, Sea2, and Sea3 from yeast, respectively. Mio/Sea4, Sea2/WDR24, and Sea3/WDR59 are components of the GATOR2 complex, which also includes another two subunits, Seh1and Sec13. GATOR2 and GATOR1, which is composed of three subunits, DEPDC5, Nprl2, and Nprl3, form the Rag-interacting complex GATOR (GAP Activity Towards Rags). Inhibition of GATOR1 subunits makes mTORC1 signaling resistant to amino acid deprivation. In contrast, inhibition of GATOR2 subunits suppresses mTORC1 signaling and GATOR2 negatively regulates DEPDC5. All subfamily members contain an N-terminal WD40 domain and a C-terminal RING-H2 finger with an unusual arrangement of zinc-coordinating residues. The cysteines and histidines in the RING-H2 finger are arranged as a modified C3H3C2-type, rather than the canonical C3H2C3-type.


Pssm-ID: 438151 [Multi-domain]  Cd Length: 44  Bit Score: 44.24  E-value: 3.45e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 569006009 291 CIICrEEMVTGAKR--LPCNHIFHTSCLRSWFQRQQTCPT 328
Cdd:cd16488    2 CAIC-HLPVKGLSSfcLNCGHGGHAECIREWFEDHTECPT 40
zf-RING_UBOX pfam13445
RING-type zinc-finger; This zinc-finger is a typical RING-type of plant ubiquitin ligases.
291-327 5.78e-06

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


Pssm-ID: 463881 [Multi-domain]  Cd Length: 38  Bit Score: 43.16  E-value: 5.78e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 569006009  291 CIICREEMVTgaKRLPCNHIFHTSCLR---SWFQRQQTCP 327
Cdd:pfam13445   1 CPICLELFTD--PVLPCGHTFCRECLEemsQKKGGKFKCP 38
COG5540 COG5540
RING-finger-containing ubiquitin ligase [Posttranslational modification, protein turnover, ...
291-333 6.98e-06

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


Pssm-ID: 227827 [Multi-domain]  Cd Length: 374  Bit Score: 48.45  E-value: 6.98e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 569006009 291 CIICREEMVTGAKR--LPCNHIFHTSCLRSWF-QRQQTCPTCRMDV 333
Cdd:COG5540  326 CAICMSNFIKNDRLrvLPCDHRFHVGCVDKWLlGYSNKCPVCRTAI 371
RING-HC_RNF141 cd16545
RING finger, HC subclass, found in RING finger protein 141 (RNF141) and similar proteins; ...
289-330 9.18e-06

RING finger, HC subclass, found in RING finger protein 141 (RNF141) and similar proteins; RNF141, also known as zinc finger protein 230 (ZNF230), is a RING finger protein present primarily in the nuclei of spermatogonia, the acrosome, and the tail of spermatozoa. It may have a broad function during early development of vertebrates. It plays an important role in spermatogenesis, including spermatogenic cell proliferation and sperm maturation, as well as motility and fertilization. It also exhibits DNA binding activity. RNF141/ZNF230 gene mutations may be associated with azoospermia. RNF141 contains a C3HC4-type RING finger domain that may function as an activator module in transcription.


Pssm-ID: 438207 [Multi-domain]  Cd Length: 40  Bit Score: 42.85  E-value: 9.18e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 569006009 289 NVCIIC---REEMVtgakrLPCNHIFHTSCLRSWFQRQQTCPTCR 330
Cdd:cd16545    1 EECCICmdrKADLI-----LPCAHSYCQKCIDKWSDRHRTCPICR 40
RING-HC cd16449
HC subclass of RING (RING-HC) finger and its variants; The RING finger is a specialized type ...
291-329 9.78e-06

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: 42.86  E-value: 9.78e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 569006009 291 CIICREEMVTgAKRLPCNHIFHTSCLRSWFQ-RQQTCPTC 329
Cdd:cd16449    3 CPICLERLKD-PVLLPCGHVFCRECIRRLLEsGSIKCPIC 41
RING-H2_RNF122 cd16676
RING finger, H2 subclass, found in RING finger protein 122 (RNF122) and similar proteins; ...
291-329 9.80e-06

RING finger, H2 subclass, found in RING finger protein 122 (RNF122) and similar proteins; RNF122 is a RING finger protein associated with HEK 293T cell viability. It is localized to the endoplasmic reticulum (ER) and the Golgi apparatus, and overexpressed in anaplastic thyroid cancer cells. RNF122 functions as an E3 ubiquitin ligase that can ubiquitinate itself and undergo degradation through its RING finger in a proteasome-dependent manner. It interacts with calcium-modulating cyclophilin ligand (CAML), which is not a substrate, but a stabilizer of RNF122. RNF122 contains an N-terminal transmembrane domain and a C-terminal C3H2C3-type RING-H2 finger.


Pssm-ID: 438338 [Multi-domain]  Cd Length: 47  Bit Score: 43.03  E-value: 9.80e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 569006009 291 CIICREEMVTGAKR--LPCNHIFHTSCLRSWFQRQQTCPTC 329
Cdd:cd16676    3 CAVCLEDFKTKDELgvLPCQHAFHRKCLVKWLEIRCVCPMC 43
RING-H2_AIRP1-like cd23116
RING finger, H2 subclass, found in Arabidopsis thaliana protein ABA INSENSITIVE RING PROTEIN 1 ...
288-329 1.10e-05

RING finger, H2 subclass, found in Arabidopsis thaliana protein ABA INSENSITIVE RING PROTEIN 1 (AIRP1) and similar proteins; This subfamily includes Arabidopsis thaliana AIRP1 and RING-H2 finger B1a (RHB1A). AIRP1, also known as RING-type E3 ubiquitin transferase AIRP1, possesses E3 ubiquitin-protein ligase activity in vitro when associated with the E2 enzyme UBC8. It plays combinatory roles with AIRP2 in the positive regulation of the abscisic acid-mediated drought stress response. RHB1A is a probable E3 ubiquitin-protein ligase. Members of this subfamily contain a C3H2C3-type RING-H2 finger.


Pssm-ID: 438478 [Multi-domain]  Cd Length: 49  Bit Score: 42.84  E-value: 1.10e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 569006009 288 DNVCIICREEMVTGAKRL--PCNHIFHTSCLRSWFQRQQTCPTC 329
Cdd:cd23116    2 EDVCPTCLEGYTEENPKLltKCGHHFHLACIYEWMERSERCPVC 45
mRING-CH-C4HC2H_ZNRF2 cd16695
Modified RING-CH finger, H2 subclass (C4HC2H-type), found in zinc/RING finger protein 2 (ZNRF2) ...
291-327 1.24e-05

Modified RING-CH finger, H2 subclass (C4HC2H-type), found in zinc/RING finger protein 2 (ZNRF2) and similar proteins; ZNRF2, also known as protein Ells2 or RING finger protein 202 (RNF202), is an E3 ubiquitin-protein ligase that is highly expressed in the nervous system during development and is present in presynaptic plasma membranes. It is N-myrisotoylated and is also located in the endosome-lysosome compartment in fibroblasts. It contains an N-terminal MAGE domain, and a special C-terminal domain that combines a zinc finger and a modified C4HC2H-type RING-CH finger, rather than the typical C4HC3-type RING-CH finger, which is a variant of RING-H2 finger. Only the RING finger of the zinc finger-RING finger motif is required for its E3 ubiquitin ligase activity. Together with its sister protein ZNRF1, ZNRF2 regulates the ubiquitous Na+/K+ pump (Na+/K+ATPase).


Pssm-ID: 438356 [Multi-domain]  Cd Length: 56  Bit Score: 43.10  E-value: 1.24e-05
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 569006009 291 CIICREEMVTG--AKRLPCNHIFHTSCLRSWFQRQQTCP 327
Cdd:cd16695   13 CAICLEELQQGdtIARLPCLCIYHKGCIDEWFEVNRSCP 51
mRING-H2-C3H2C2D_ZSWM2 cd16486
Modified RING finger, H2 subclass (C3H2C2D-type), found in zinc finger SWIM domain-containing ...
290-330 1.25e-05

Modified RING finger, H2 subclass (C3H2C2D-type), found in zinc finger SWIM domain-containing protein 2 (ZSWIM2) and similar proteins; ZSWIM2, also known as MEKK1-related protein X (MEX) or ZZ-type zinc finger-containing protein 2, is a testis-specific E3 ubiquitin ligase that promotes death receptor-induced apoptosis through Fas, death receptor (DR) 3 and DR4 signaling. ZSWIM2 is self-ubiquitinated and targeted for degradation through the proteasome pathway. It acts as an E3 ubiquitin ligase, through the E2, Ub-conjugating enzymes UbcH5a, UbcH5c, or UbcH6. ZSWIM2 contains four putative zinc-binding domains including an N-terminal SWIM (SWI2/SNF2 and MuDR) domain critical for its ubiquitination, and two modified RING-H2 fingers separated by a ZZ zinc finger domain, which was required for interaction with UbcH5a and its self-association. This model corresponds to the second RING-H2 finger, which is not a canonical C3H2C3-type, but a modified C3H2C2D-type.


Pssm-ID: 438149 [Multi-domain]  Cd Length: 49  Bit Score: 42.75  E-value: 1.25e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 569006009 290 VCIICREEMVTGAK--RLPCNHIFHTSCLRSWFQRQQ-TCPTCR 330
Cdd:cd16486    1 QCRICLKAFQLGQHvrTLPCRHKFHRDCIDNWLLHSRnSCPIDG 44
RING-HC_RNF219 cd16562
RING finger, HC subclass, found in RING finger protein 219 (RNF219) and similar proteins; ...
291-330 4.52e-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: 40.88  E-value: 4.52e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 569006009 291 CIIC----REEMVTgakrlPCNHIFHTSCLRSWFQRQQTCPTCR 330
Cdd:cd16562    4 CHIClgkvRQPVIC-----SNNHVFCSSCMDVWLKNNNQCPACR 42
zf-C3HC4_3 pfam13920
Zinc finger, C3HC4 type (RING finger);
288-335 4.58e-05

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 464042 [Multi-domain]  Cd Length: 50  Bit Score: 41.21  E-value: 4.58e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 569006009  288 DNVCIICREE---MVTgakrLPCNH-IFHTSCLRSWFQRQQTCPTCRMDVLR 335
Cdd:pfam13920   2 DLLCVICLDRprnVVL----LPCGHlCLCEECAERLLRKKKKCPICRQPIES 49
RING-HC_RNF138 cd16544
RING finger, HC subclass, found in RING finger protein 138 (RNF138) and similar proteins; ...
291-330 5.94e-05

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: 40.85  E-value: 5.94e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 569006009 291 CIICREEMVTGAKRLPCNHIFHTSCLRSWFQRQQT-CPTCR 330
Cdd:cd16544    5 CPVCQEVLKDPVELPPCRHIFCKACILLALRSSGArCPLCR 45
RING-CH-C4HC3_LTN1 cd16491
RING-CH finger, H2 subclass (C4HC3-type), found in E3 ubiquitin-protein ligase listerin and ...
291-330 5.96e-05

RING-CH finger, H2 subclass (C4HC3-type), found in E3 ubiquitin-protein ligase listerin and similar proteins; Listerin, also known as RING finger protein 160 or zinc finger protein 294, is the mammalian homolog of yeast Ltn1. It is widely expressed in all tissues, but motor and sensory neurons and neuronal processes in the brainstem and spinal cord are primarily affected in the mutant. Listerin is required for embryonic development and plays an important role in neurodegeneration. It also functions as a critical E3 ligase involving quality control of nonstop proteins. It mediates ubiquitylation of aberrant proteins that become stalled on ribosomes during translation. Ltn1 works with several cofactors to form a large ribosomal subunit-associated quality control complex (RQC), which mediates the ubiquitylation and extraction of ribosome-stalled nascent polypeptide chains for proteasomal degradation. It appears to first associate with nascent chain-stalled 60S subunits together with two proteins of unknown function, Tae2 and Rqc1. Listerin contains a long stretch of HEAT (Huntingtin, Elongation factor 3, PR65/A subunit of protein phosphatase 2A, and TOR) or ARM (Armadillo) repeats in the N terminus and middle region, and a catalytic RING-CH finger, also known as vRING or RINGv, with an unusual arrangement of zinc-coordinating residues in the C-terminus . Its cysteines and histidines are arranged in the sequence as C4HC3-type, rather than the C3H2C3-type in canonical RING-H2 finger.


Pssm-ID: 438154 [Multi-domain]  Cd Length: 50  Bit Score: 40.71  E-value: 5.96e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 569006009 291 CIICREEMVTGAKRLP------CNHIFHTSCLRSWFQ--RQQTCPTCR 330
Cdd:cd16491    3 CPICYSVIHGSNHSLPklkcktCKNKFHSACLYKWFRssNKSTCPLCR 50
zf-C3HC4_2 pfam13923
Zinc finger, C3HC4 type (RING finger);
290-329 5.97e-05

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 404756 [Multi-domain]  Cd Length: 40  Bit Score: 40.50  E-value: 5.97e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 569006009  290 VCIICREEMVTGAKRLPCNHIFHTSCLRSWFQRQQTCPTC 329
Cdd:pfam13923   1 MCPICMDMLKDPSTTTPCGHVFCQDCILRALRAGNECPLC 40
RING-HC_Topors cd16574
RING finger, HC subclass, found in topoisomerase I-binding arginine/serine-rich protein ...
288-330 7.42e-05

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: 40.35  E-value: 7.42e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 569006009 288 DNVCIICREEMVTGAKRL-PCNHIFHTSCLRSWFQRQQTCPTCR 330
Cdd:cd16574    1 DSSCPICLDRFENEKAFLdGCFHAFCFTCILEWSKVKNECPLCK 44
RING-H2_APC11 cd16456
RING finger, H2 subclass, found in anaphase-promoting complex subunit 11 (APC11) and similar ...
288-330 7.68e-05

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: 40.73  E-value: 7.68e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569006009 288 DNVCIICREE----------------MVTGAkrlpCNHIFHTSCLRSWFQRQ---QTCPTCR 330
Cdd:cd16456    1 DDVCGICRMAfdgccpdckfpgddcpLVWGK----CSHCFHMHCILKWLNSQqvqQHCPMCR 58
RING-HC_CeBARD1-like cd23143
RING finger, HC subclass, found in Caenorhabditis elegans BRCA1-associated RING domain protein ...
291-330 9.27e-05

RING finger, HC subclass, found in Caenorhabditis elegans BRCA1-associated RING domain protein 1 (CeBARD1) and similar proteins; CeBARD1, also called Ce-BRD-1, Cebrd-1, or RING-type E3 ubiquitin transferase BARD1, is a constituent of the CeBCD complex that possesses E3 ubiquitin-protein ligase activity. It plays a role in triggering cellular responses at damage sites in response to DNA damage that may be induced by ionizing radiation. It protects against chromosome non-disjunction and nuclear fragmentation during meiotic double-strand break repair to ensure sister chromatid recombination and aid chromosome stability. CeBARD1 contains a typical C3HC4-type RING-HC finger.


Pssm-ID: 438505 [Multi-domain]  Cd Length: 47  Bit Score: 40.22  E-value: 9.27e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 569006009 291 CIICREEMVTGAKRLPCNHIFHTSCLRSWFQRQQTCPTCR 330
Cdd:cd23143    4 CVICSEPQIDTFLLSSCGHIYCWECFTEFIEKRHMCPSCR 43
RING-H2_Rapsyn cd16478
RING finger, H2 subclass, found in 43 kDa receptor-associated protein of the synapse (Rapsyn) ...
291-330 9.97e-05

RING finger, H2 subclass, found in 43 kDa receptor-associated protein of the synapse (Rapsyn) and similar proteins; Rapsyn, also known as acetylcholine receptor (AChR)-associated 43 kDa protein or RING finger protein 205 (RNF205), is a 43 kDa postsynaptic protein that plays an essential role in the clustering and maintenance of AChR in the postsynaptic membrane of the motor endplate. AChRs enable the transport of rapsyn from the Golgi complex to the plasma membrane through a molecule-specific interaction. Rapsyn also mediates subsynaptic anchoring of protein kinase A (PKA) type I in close proximity to the postsynaptic membrane, which is essential for synapse maintenance. Its mutations in humans cause endplate AChR deficiency and myasthenic syndrome. Rapsyn contains an N-terminal myristoylation signal required for membrane association, seven tetratricopeptide repeats (TPRs) that subserve rapsyn self-association, a coiled-coil domain responsible for the binding of determinants within the long cytoplasmic loop of each AChR subunit, a C3H2C3-type RING-H2 finger that binds to the cytoplasmic domain of beta-dystroglycan and to S-NRAP and links rapsyn to the subsynaptic cytoskeleton, and a serine phosphorylation site.


Pssm-ID: 438141 [Multi-domain]  Cd Length: 48  Bit Score: 40.14  E-value: 9.97e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 569006009 291 CIICREEMvtGAKR-----LPCNHIFHTSCLRSWFQRQ-QTCPTCR 330
Cdd:cd16478    4 CGMCGESI--GEKNeqlqaLPCSHIFHLKCLQTNLRGGtRGCPNCR 47
mRING-HC-C3HC3D_Nrdp1 cd16634
Modified RING finger, HC subclass (C3HC3D-type), found in neuregulin receptor degradation ...
290-330 1.07e-04

Modified RING finger, HC subclass (C3HC3D-type), found in neuregulin receptor degradation protein-1 (Nrdp1) and similar proteins; Nrdp1 (referred to as FLRF in mice), also known as RING finger protein 41 (RNF41), is an E3 ubiquitin-protein ligase that plays a critical role in the regulation of cell growth and apoptosis, inflammation and production of reactive oxygen species (ROS), as well as in doxorubicin (DOX)-induced cardiac injury. It promotes the degradation of the epidermal growth factor receptor (EGFR/ErbB) family member, ErbB3, which is independent of growth factor stimulation. It also promotes M2 macrophage polarization by ubiquitinating and activating transcription factor CCAAT/enhancer-binding protein beta (C/EBPbeta) via Lys-63-linked ubiquitination. Moreover, Nrdp1 interacts with and modulates the activity of Parkin, a causative protein for early onset recessive juvenile parkinsonism (AR-JP). It also interacts with ubiquitin-specific protease 8 (USP8), which is involved in trafficking of various transmembrane proteins. Furthermore, Nrdp1 inhibits basal lysosomal degradation and enhances ectodomain shedding of JAK2-associated cytokine receptors. Its phosphorylation by the kinase Par-1b (also known as MARK2) is required for epithelial cell polarity. Nrdp1 contains an N-terminal modified C3HC3D-type RING-HC finger required for enhancing ErbB3 degradation, a B-box, a coiled-coil domain responsible for Nrdp1 oligomerization, and a C-terminal ErbB3-binding domain.


Pssm-ID: 438296 [Multi-domain]  Cd Length: 43  Bit Score: 39.71  E-value: 1.07e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 569006009 290 VCIICR---EEMVTGAKrlpCNHIFHTSCLRSWFQRQQTCPTCR 330
Cdd:cd16634    3 ICPICSgvlEEPLQAPH---CEHAFCNACITEWLSRQQTCPVDR 43
RING-HC_DTX3-like cd16506
RING finger, HC subclass, found in E3 ubiquitin-protein ligase Deltex3 (DTX3), Deltex-3-like ...
290-330 1.23e-04

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: 39.65  E-value: 1.23e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 569006009 290 VCIICREEMVTgAKRLP-CNHIFHTSCLRSWFQRQQTCPTCR 330
Cdd:cd16506    2 TCPICLDEIQN-KKTLEkCKHSFCEDCIDRALQVKPVCPVCG 42
RING-HC_SH3RF2 cd16749
RING finger, HC subclass, found in SH3 domain-containing RING finger protein 2 (SH3RF2) and ...
291-330 1.39e-04

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: 39.53  E-value: 1.39e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 569006009 291 CIICREEMVTGAKRLPCNHIFHTSCLRSWF--QRQQTCPTCR 330
Cdd:cd16749    3 CPVCFEKLDVTAKVLPCQHTFCKPCLQRIFkaRKELRCPECR 44
RING-HC_ScRAD18-like cd23148
RING finger, HC subclass, found in Saccharomyces cerevisiae radiation sensitivity protein 18 ...
291-338 1.96e-04

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: 39.44  E-value: 1.96e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 569006009 291 CIICREeMVTGAKRLPCNHIFHTSCLRSWFQRQQTCPTCRMDVLRASL 338
Cdd:cd23148    6 CHICKD-LLKAPMRTPCNHTFCSFCIRTHLNNDARCPLCKAEVTESGL 52
RING-HC_Cbl cd16708
RING finger, HC subclass, found in E3 ubiquitin-protein ligase Cbl and similar proteins; Cbl, ...
283-333 1.98e-04

RING finger, HC subclass, found in E3 ubiquitin-protein ligase Cbl and similar proteins; Cbl, also known as Casitas B-lineage lymphoma proto-oncogene, proto-oncogene c-Cbl, RING finger protein 55 (RNF55), or signal transduction protein Cbl, is a multi-domain protein that acts as a key negative regulator of various receptor and non-receptor tyrosine kinase signaling. It contains a tyrosine kinase-binding domain (TKB, also known as the phosphotyrosine binding PTB domain, composed of a four helix-bundle, a Ca2+ binding EF-hand and a highly variant SH2 domain), a proline-rich domain, a C3HC4-type RING-HC finger, and an ubiquitin-associated (UBA) domain. TKB is responsible for the interactions with many tyrosine kinases, such as the colony-stimulating factor-1 (CSF-1) receptor, Syk/ZAP-70, and Src-family of protein tyrosine kinases. The proline-rich domain can recruit proteins with a SH3 domain. Moreover, Cbl functions as an E3 ubiquitin ligase that can bind ubiquitin-conjugating enzymes (E2s) through the RING-HC finger.


Pssm-ID: 438368 [Multi-domain]  Cd Length: 77  Bit Score: 40.07  E-value: 1.98e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 569006009 283 ELQAMDNVCIICREEMvTGAKRLPCNHIFHTSCLRSWFQRQ-QTCPTCRMDV 333
Cdd:cd16708   16 EMGSTFQLCKICAEND-KDVKIEPCGHLMCTSCLTSWQESEgQGCPFCRCEI 66
RING-H2_Pirh2-like cd16464
RING finger, H2 subclass, found in p53-induced RING-H2 protein (Pirh2) and similar proteins; ...
291-330 2.13e-04

RING finger, H2 subclass, found in p53-induced RING-H2 protein (Pirh2) and similar proteins; Pirh2, also known as RING finger and CHY zinc finger domain-containing protein 1 (Rchy1), androgen receptor N-terminal-interacting protein, CH-rich-interacting match with PLAG1, RING finger protein 199 (RNF199), or zinc finger protein 363 (ZNF363), is a p53 inducible E3 ubiquitin-protein ligase that functions as a negative regulator of p53. It preferably ubiquitylates the tetrameric form of p53 in vitro and in vivo, suggesting a role of Pirh2 in downregulating the transcriptionally active form of p53 in the cell. Moreover, Pirh2 inhibits the transcriptional activity of p73, a homolog of the tumor suppressor p53, by promoting its ubiquitination. It also monoubiquitinates DNA polymerase eta (PolH) to suppress translesion DNA synthesis. Furthermore, Pirh2 functions as a negative regulator of the cyclin-dependent kinase inhibitor p27(Kip1) function by promoting ubiquitin-dependent proteasomal degradation. Pirh2 enhances androgen receptor (AR) signaling through inhibition of histone deacetylase 1 (HDAC1) and is overexpressed in prostate cancer. It interacts with TIP60 and this association may regulate Pirh2 stability. In addition, the oncoprotein pleomorphic adenoma gene like 2 (PLAGL2) can bind to the Pirh2 dimer and therefore control the stability of Pirh2. Pirh2 contains a total of nine zinc-binding sites with six located at the N-terminal region, two in the C3H2C3-type RING-H2 domain, and one in the C-terminal region. Nine zinc binding sites comprise three different zinc coordination schemes, including RING type cross-brace zinc coordination, C4 zinc finger, and a novel left-handed beta-spiral zinc-binding motif formed by three recurrent CCHC sequence motifs. This subfamily also includes Drosophila melanogaster Deltex, a ubiquitously expressed cytoplasmic ubiquitin E3 ligase that mediates Notch activation in Drosophila. It selectively suppresses T-cell activation through degradation of a key signaling molecule, MAP kinase kinase kinase 1 (MEKK1). It also inhibits Jun-mediated transcription at the stage of Ras-dependent Jun N-terminal protein kinase (JNK) activation. Deltex contains N-terminal two Notch-binding WWE domains that physically interact with the Notch ankyrin domains, a proline-rich motif that shares homology with SH3-binding domains, and a RING finger at the C-terminus.


Pssm-ID: 438127 [Multi-domain]  Cd Length: 45  Bit Score: 39.18  E-value: 2.13e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 569006009 291 CIICREEMVT---GAKRLPCNHIFHTSCLRSwFQRQQ--TCPTCR 330
Cdd:cd16464    2 CPVCLEDLFTsrePVHVLPCGHLMHSTCFEE-YLKSGnyRCPLCS 45
PEX10 COG5574
RING-finger-containing E3 ubiquitin ligase [Posttranslational modification, protein turnover, ...
288-330 2.13e-04

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


Pssm-ID: 227861 [Multi-domain]  Cd Length: 271  Bit Score: 43.34  E-value: 2.13e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 569006009 288 DNVCIICREEMVTgAKRLPCNHIFHTSCLRSWFQRQQT--CPTCR 330
Cdd:COG5574  215 DYKCFLCLEEPEV-PSCTPCGHLFCLSCLLISWTKKKYefCPLCR 258
RING-CH-C4HC3_ZSWM2 cd16494
RING-CH finger, H2 subclass (C4HC3-type), found in zinc finger SWIM domain-containing protein ...
288-332 2.36e-04

RING-CH finger, H2 subclass (C4HC3-type), found in zinc finger SWIM domain-containing protein 2 (ZSWIM2) and similar proteins; ZSWIM2, also known as MEKK1-related protein X (MEX) or ZZ-type zinc finger-containing protein 2, is a testis-specific E3 ubiquitin ligase that promotes death receptor-induced apoptosis through Fas, death receptor (DR) 3, and DR4 signaling. ZSWIM2 is self-ubiquitinated and targeted for degradation through the proteasome pathway. It also acts as an E3 ubiquitin ligase, through the E2, Ub-conjugating enzymes UbcH5a, UbcH5c, or UbcH6. ZSWIM2 contains four putative zinc-binding domains including an N-terminal SWIM (SWI2/SNF2 and MuDR) domain critical for its ubiquitination and two RING fingers separated by a ZZ zinc finger domain, which was required for interaction with UbcH5a and its self-association. This model corresponds to the first RING finger, which is a C4HC3-type RING-CH finger, also known as vRING or RINGv, rather than the canonical C3H2C3-type RING-H2 finger.


Pssm-ID: 438157 [Multi-domain]  Cd Length: 57  Bit Score: 39.24  E-value: 2.36e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 569006009 288 DNVCIICREEMVTGAKRLP-----CNHIFHTSCLRSW--FQRQQ----TCPTCRMD 332
Cdd:cd16494    1 EDDCPICYEEMLEKGEPLTycrfgCGNNVHIHCMKVWaeHQRQSdepvTCPLCRSD 56
RING-HC_UHRF cd16613
RING finger, HC subclass, found in ubiquitin-like PHD and RING finger domain-containing ...
291-332 2.56e-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: 38.87  E-value: 2.56e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 569006009 291 CIICrEEMVTGAKRLPCNHIFHTSCLRSWFQRQ-QTCPTCRMD 332
Cdd:cd16613    3 CICC-QELVYKPITTPCKHNICKSCLQRSFKAEvYTCPACRHD 44
RING-HC_Cbl-c cd16710
RING finger, HC subclass, found in E3 ubiquitin-protein ligase Cbl-c and similar proteins; ...
285-333 2.73e-04

RING finger, HC subclass, found in E3 ubiquitin-protein ligase Cbl-c and similar proteins; Cbl-c, also known as RING finger protein 57 (RNF57), SH3-binding protein Cbl-3, SH3-binding protein Cbl-c, or signal transduction protein Cbl-c, is an E3 ubiquitin-protein ligase expressed exclusively in epithelial cells. It contains a tyrosine-kinase-binding domain (TKB, also known as the phosphotyrosine binding PTB domain, composed of a four helix-bundle, a Ca2+ binding EF-hand and a highly variant SH2 domain), a C3HC4-type RING-HC finger, and a short proline-rich region, but lacks the ubiquitin-associated (UBA) leucine zipper motif that are present in Cbl and Cbl-b. Cbl-c acts as a regulator of epidermal growth factor receptor (EGFR)-mediated signal transduction. It also suppresses v-Src-induced transformation through ubiquitin-dependent protein degradation. Moreover, Cbl-c ubiquitinates and downregulates RETMEN2A and implicates Enigma (PDLIM7) as a positive regulator of RETMEN2A by blocking Cbl-mediated ubiquitination and degradation. The ubiquitin ligase activity of Cbl-c is increased via the interaction of its RING-HC finger domain with a LIM domain of the paxillin homolog, hydrogen peroxide induced construct 5 (Hic-5).


Pssm-ID: 438370 [Multi-domain]  Cd Length: 65  Bit Score: 39.30  E-value: 2.73e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 569006009 285 QAMDN---VCIICREEMvTGAKRLPCNHIFHTSCLRSW-FQRQQTCPTCRMDV 333
Cdd:cd16710    7 QAMNStfeLCKICAERD-KDVRIEPCGHLLCSCCLAAWqHSDSQTCPFCRCEI 58
RING-HC_BAR cd16497
RING finger, HC subclass, found in bifunctional apoptosis regulator (BAR); BAR, also known as ...
291-335 2.73e-04

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: 39.03  E-value: 2.73e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 569006009 291 CIICREEMVTgAKRLPCNHIFHTSCLRSWFQ--RQQTCPTCRMDVLR 335
Cdd:cd16497    4 CHCCYDLLVN-PTTLNCGHSFCRHCLALWWKssKKTECPECRQKWEG 49
mRING-HC-C4C4_TRIM37_C-VIII cd16619
Modified RING finger, HC subclass (C4C4-type), found in tripartite motif-containing protein 37 ...
291-330 2.89e-04

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: 38.49  E-value: 2.89e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 569006009 291 CIICREEmVTGAKRLP-CNHIFHTSCLRSWFQRQQ-TCPTCR 330
Cdd:cd16619    3 CFICMEK-LRDPRLCPhCSKLFCKGCIRRWLSEQRsSCPHCR 43
PHA03291 PHA03291
envelope glycoprotein I; Provisional
530-601 3.05e-04

envelope glycoprotein I; Provisional


Pssm-ID: 223033 [Multi-domain]  Cd Length: 401  Bit Score: 43.40  E-value: 3.05e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569006009 530 PATSVNPTEETASTVVSAAPSTSAPSSEAPTPSPGASPPIP------EAEKPPAPESVGIVEELPEDGEPDAAELRRR 601
Cdd:PHA03291 205 PATPRPTPRTTASPETTPTPSTTTSPPSTTIPAPSTTIAAPqagttpEAEGTPAPPTPGGGEAPPANATPAPEASRYE 282
RING-HC_Cbl-like cd16502
RING finger, HC subclass, found in Casitas B-lineage lymphoma (Cbl) proteins; The Cbl adaptor ...
289-330 3.28e-04

RING finger, HC subclass, found in Casitas B-lineage lymphoma (Cbl) proteins; The Cbl adaptor protein family contains a small class of RING-type E3 ubiquitin ligases with oncogenic activity, which is represented by three mammalian members, c-Cbl, Cbl-b and Cbl-c, as well as two invertebrate Cbl-family proteins, D-Cbl in Drosophila and Sli-1 in C. elegans. Cbl proteins function as potent negative regulators of various signaling cascades in a wide range of cell types. They play roles in ubiquitinating activated tyrosine kinases and targeting them for degradation. D-Cbl associates with the Drosophila epidermal growth factor receptor (EGFR) and overexpression of D-Cbl in the eye of Drosophila embryos inhibits EGFR-dependent photoreceptor cell development. Sli-1 is a negative regulator of the Let-23 receptor tyrosine kinase, an EGFR homolog, in vulva development. Cbl proteins in this subfamily consist of a highly conserved N-terminal half that includes a tyrosine-kinase-binding domain (TKB, also known as the phosphotyrosine binding PTB domain, composed of a four helix-bundle, a Ca2+ binding EF-hand and a highly variant SH2 domain) and a C3HC4-type RING-HC finger, both of which are required for Cbl-mediated downregulation of RTKs, and a divergent C-terminal region.


Pssm-ID: 438165 [Multi-domain]  Cd Length: 43  Bit Score: 38.48  E-value: 3.28e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 569006009 289 NVCIICREEMvTGAKRLPCNHIFHTSCLRSWfQRQ--QTCPTCR 330
Cdd:cd16502    2 QLCKICAEND-KDVRIEPCGHLLCTPCLTSW-QDSdgQTCPFCR 43
APC11 COG5194
Component of SCF ubiquitin ligase and anaphase-promoting complex [Posttranslational ...
288-330 3.38e-04

Component of SCF ubiquitin ligase and anaphase-promoting complex [Posttranslational modification, protein turnover, chaperones / Cell division and chromosome partitioning];


Pssm-ID: 227521 [Multi-domain]  Cd Length: 88  Bit Score: 39.82  E-value: 3.38e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 569006009 288 DNVCIICREEMVTGaKRLP-----CNHIFHTSCLRSWFQRQQTCPTCR 330
Cdd:COG5194   31 MGTCPECQFGMTPG-DECPvvwgvCNHAFHDHCIYRWLDTKGVCPLDR 77
RING-H2_RHF2A cd23122
RING finger, H2 subclass, found in Arabidopsis thaliana RING-H2 zinc finger protein RHF2A and ...
285-329 3.40e-04

RING finger, H2 subclass, found in Arabidopsis thaliana RING-H2 zinc finger protein RHF2A and similar proteins; RHF2A is an E3 ubiquitin-protein ligase involved in the positive regulation of the gametogenesis progression. It is required for the degradation of KRP6, a cyclin-dependent kinase inhibitor which accumulates during meiosis and blocks the progression of subsequent mitoses during gametophytes development. It functions in association with RHF1A. Members of this subfamily contain a C3H2C3-type RING-H2 finger.


Pssm-ID: 438484 [Multi-domain]  Cd Length: 63  Bit Score: 39.19  E-value: 3.40e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 569006009 285 QAMDNVCIICREEMVTG--AKRLPCNHIFHTSCLRSWFQRQQTCPTC 329
Cdd:cd23122    8 DACEDACSICLESFCEAdpATVTSCKHEYHLQCILEWSQRSKECPMC 54
mRING-HC-C3HC3D_LNX1-like cd16637
Modified RING finger, HC subclass (C3HC3D-type), found in ligand of Numb protein LNX1, LNX2, ...
288-327 3.45e-04

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: 38.53  E-value: 3.45e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 569006009 288 DNVCIICREEMVTGAKrLPCNHIFHTSCLRSWFQRQQTCP 327
Cdd:cd16637    1 DLTCHICLQPLVEPLD-TPCGHTFCYKCLTNYLKIQQCCP 39
RING-HC_RNF4 cd16533
RING finger, HC subclass, found in RING finger protein 4 (RNF4) and similar proteins; RNF4, ...
291-330 5.12e-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: 38.34  E-value: 5.12e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 569006009 291 CIICRE---EMVTGAKRL---PCNHIFHTSCLRSWFQRQQTCPTCR 330
Cdd:cd16533    6 CPICMDgysEIVQSGRLIvstECGHVFCSQCLRDSLKNANTCPTCR 51
RING-HC_PCGF3 cd16735
RING finger found in polycomb group RING finger protein 3 (PCGF3) and similar proteins; PCGF3, ...
290-341 5.51e-04

RING finger found in polycomb group RING finger protein 3 (PCGF3) and similar proteins; PCGF3, also known as RING finger protein 3A (RNF3A), is one of six PcG RING finger (PCGF) homologs (PCGF1, PCGF2/Mel-18, PCGF3, PCGF4/BMI1, PCGF5, and PCGF6) and serves as the core component of a Polycomb repressive complex 1 (PRC1). Like other PCGF homologs, PCGF3 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. PCGF3 contains a C3HC4-type RING-HC finger.


Pssm-ID: 438393 [Multi-domain]  Cd Length: 66  Bit Score: 38.59  E-value: 5.51e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 569006009 290 VCIICREEMVTGAKRLPCNHIFHTSCLRSWFQRQQTCPTCRMdVLRASLPAQ 341
Cdd:cd16735   13 TCRLCKGYLIDATTITECLHTFCKSCLVKYLEENNTCPTCGI-VIHQSHPLQ 63
mRING-H2-C3H2C2D_RBX1 cd16485
modified RING finger, H2 subclass (C3H2C2D-type), found in RING-box protein 1 (RBX1) and ...
307-329 6.67e-04

modified RING finger, H2 subclass (C3H2C2D-type), found in RING-box protein 1 (RBX1) and similar proteins; RBX1, also known as Hrt1, protein ZYP, RING finger protein 75 (RNF75), or regulator of cullins 1 (ROC1), is an E3 ubiquitin-protein ligase necessary for ubiquitin ligation activity of multimeric cullin (Cul)-RING E3 ligases (CRLs). RBX1-containing CRLs are involved in the NEDD8 pathway; RBX1 specifically regulates NEDD8ylation of Cul1-4. It can also bind and activate HIV-1 Vif-Cullin5 E3 ligase complex in vitro. Moreover, RBX1 is an essential element of Skp1/Cullin/F-box (SCF) E3-ubiquitin ligase complexes that target diverse proteins for proteasome-mediated degradation. It is a direct functional target of miR-194 and plays an important role in proliferation and migration of gastric cancer (GC) cells. RBX1 is also an essential component of KEAP1/CUL3/RBX1 E3-ubiquitin ligase complex that functions as a regulator of NFE2-related factor 2 (NRF2) and plays a key role in NRF2 pathway deregulation in multiple tumor types, including ovarian carcinomas (OVCA) and papillary thyroid carcinoma (PTC). Furthermore, RBX1 associates with DDB1, Cul4A, and Fbxw5 to form the Fbxw5-DDB1-Cul4A-Rbx1 complex that may function as a dual SUMO/ubiquitin ligase suppressing c-Myb activity through sumoylation or ubiquitination. RBX1 contains a C-terminal modified RING-H2 finger that is of C3H2C2D-type, rather than the canonical C3H2C3-type. The modified RING-H2 finger is essential for its ligase activity.


Pssm-ID: 438148 [Multi-domain]  Cd Length: 62  Bit Score: 38.15  E-value: 6.67e-04
                         10        20
                 ....*....|....*....|...
gi 569006009 307 CNHIFHTSCLRSWFQRQQTCPTC 329
Cdd:cd16485   36 CNHAFHFHCISRWLKTRQVCPLD 58
RING-HC_SH3RF3 cd16750
RING finger, HC subclass, found in SH3 domain-containing RING finger protein 3 (SH3RF3) and ...
291-330 6.98e-04

RING finger, HC subclass, found in SH3 domain-containing RING finger protein 3 (SH3RF3) and similar proteins; 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 a screen for interacting partners of p21-activated kinase 2 (PAK2). It may play a role in regulating c-Jun N-terminal kinase (JNK) mediated apoptosis in certain conditions. It also interacts with GTP-loaded Rac1. SH3RF3 is highly homologous to SH3RF1. Both 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: 438408 [Multi-domain]  Cd Length: 46  Bit Score: 37.79  E-value: 6.98e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 569006009 291 CIICREEMVTGAKRLPCNHIFHTSCLRSWF--QRQQTCPTCR 330
Cdd:cd16750    5 CSVCLERLDTTSKVLPCQHTFCRRCLESIVssRKELRCPECR 46
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
528-595 8.26e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 42.36  E-value: 8.26e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569006009 528 PRPATsVNPteETASTVVSAAPSTSAPSSEAPTPSPgaSPPIPEAEKPPAPESVGIV--------EELPEDGEPDA 595
Cdd:PRK14959 398 PTPGT-QGP--QGTAPAAGMTPSSAAPATPAPSAAP--SPRVPWDDAPPAPPRSGIPprpaprmpEASPVPGAPDS 468
RING-H2_DTX1-like cd16459
RING finger, H2 subclass, found in E3 ubiquitin-protein ligase Deltex1 (DTX1), Deltex2 (DTX2), ...
290-330 9.11e-04

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: 37.89  E-value: 9.11e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006009 290 VCIICREEMVT----------GAKRL----PCNHIFHTSCLRSWFQRQQ-----TCPTCR 330
Cdd:cd16459    1 DCPICCEPLCVasgyeeskleGSKVVvrlkKCSHMYHKACLVAMYSNGAkdgslQCPTCK 60
RING-HC_MKRN1_3 cd16730
RING finger, HC subclass, found in makorin-1 (MKRN1), makorin-3 (MKRN3), and similar proteins; ...
288-331 9.13e-04

RING finger, HC subclass, found in makorin-1 (MKRN1), makorin-3 (MKRN3), and similar proteins; MKRN1, also known as makorin RING finger protein 1 or RING finger protein 61 (RNF61), is an E3 ubiquitin-protein ligase targeting the telomerase catalytic subunit (TERT) for proteasome processing. It regulates the ubiquitination and degradation of peroxisome-proliferator-activated receptor gamma (PPARgamma), a nuclear receptor that is linked to obesity and metabolic diseases. It also mediates the posttranslational regulation of p14ARF, and thus potentially regulates cellular senescence and tumorigenesis in gastric cancer. Moreover, MKRN1 functions as a differentially negative regulator of p53 and p21, and controls cell cycle arrest and apoptosis. It induces degradation of West Nile virus (WNV) capsid protein to protect cells from WNV. It is a RNA-binding protein involved in the modulation of cellular stress and apoptosis. It predominantly associates with proteins involved in mRNA metabolism including regulators of mRNA turnover, transport, and/or translation, and acts as a component of a ribonucleoprotein complex in embryonic stem cells (ESCs) that is recruited to stress granules upon exposure to environmental stress. MKRN1 interacts with poly(A)-binding protein (PABP), a key component of different ribonucleoprotein complexes, in an RNA-independent manner, and stimulates translation in nerve cells. In addition, MKRN1 is a novel SEREX (serological identification of antigens by recombinant cDNA expression cloning) antigen of esophageal squamous cell carcinoma (SCC). It may be involved in carcinogenesis of the well-differentiated type of tumors possibly via ubiquitination of filamin A interacting protein 1 (L-FILIP). Human MKRN1 contains three N-terminal C3H1-type zinc fingers, a motif rich in Cys and His residues (CH), a C3HC4-type RING-HC finger, and another C3H1-type zinc finger at the C-terminus. MKRN3, also known as makorin RING finger protein 3, RING finger protein 63 (RNF63), or zinc finger protein 127 (ZNF127), is a therian mammal-specific retrocopy of MKRN1. It acts as a putative E3 ubiquitin-protein ligase involved in ubiquitination and cell signaling. MKRN3 shows a potential inhibitory effect on hypothalamic gonadotropin-releasing hormone (GnRH) secretion. Its defects represent the most frequent known genetic cause of familial central precocious puberty (CPP). In contrast to human MKRN1, human MKRN3 lacks the second C3H1-type zinc finger at the N-terminal region. The RING-HC finger of mammalian MKRN4 shows high sequence similarity with that of MKRN3, and is also included in this model.


Pssm-ID: 319644 [Multi-domain]  Cd Length: 61  Bit Score: 37.86  E-value: 9.13e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 569006009 288 DNVCIICRE---EMVTGAKR----LP-CNHIFHTSCLRSWFQRQQ-------TCPTCRM 331
Cdd:cd16730    1 DKVCGICMEvvyEKANPSERrfgiLSnCNHTYCLKCIRKWRSAKQfeskiikSCPECRI 59
RING-HC_ORTHRUS_rpt1 cd23138
first RING finger, HC subclass, found in Arabidopsis thaliana ORTHRUS and similar proteins; ...
291-330 9.99e-04

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: 37.42  E-value: 9.99e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 569006009 291 CIICR---EEMVTgakrLPCNHIFHTSCLRSWF-QRQQTCPTCR 330
Cdd:cd23138    5 CSFCMqlpERPVT----TPCGHNFCLKCFQKWMgQGKKTCGTCR 44
RING-HC_PEX10 cd16527
RING finger, HC subclass, found in peroxin-10 (PEX10) and similar proteins; PEX10, also known ...
291-330 1.07e-03

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: 37.21  E-value: 1.07e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 569006009 291 CIICREEMVTGAKrLPCNHIFHTSCLRSWFQRQQTCPTCR 330
Cdd:cd16527    3 CSLCLEERRHPTA-TPCGHLFCWSCITEWCNEKPECPLCR 41
RING-H2_Vps cd16484
RING finger, H2 subclass, found in vacuolar protein sorting-associated proteins Vps8, Vps11, ...
305-330 1.10e-03

RING finger, H2 subclass, found in vacuolar protein sorting-associated proteins Vps8, Vps11, Vps18, Vps41, and similar proteins; This subfamily corresponds to a group of vacuolar protein sorting-associated proteins containing a C-terminal C3H2C3-type RING-H2 finger, which includes Vps8, Vps11, Vps18, and Vps41. Vps11 and Vps18 associate with Vps16 and Vps33 to form a Class C Vps core complex that is required for soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNARE)-mediated membrane fusion at the lysosome-like yeast vacuole. The core complex, together with two additional compartment-specific subunits, forms the tethering complexes HOPS (homotypic vacuole fusion and protein sorting) and CORVET (class C core vacuole/endosome transport). CORVET contains the additional Vps3 and Vps8 subunits. It operates at endosomes, controls traffic into late endosomes and interacts with the Rab5/Vps21-GTP form. HOPS contains the additional Vps39 and Vps41 subunits. It operates at the lysosomal vacuole, controls all traffic from late endosomes into the vacuole and interacts with the Rab7/Ypt7-GTP form.


Pssm-ID: 438147  Cd Length: 48  Bit Score: 37.10  E-value: 1.10e-03
                         10        20
                 ....*....|....*....|....*.
gi 569006009 305 LPCNHIFHTSCLRSWFQRQQTCPTCR 330
Cdd:cd16484   23 FFCGHMFHKFCLPELSMTEAACPICL 48
zf-ANAPC11 pfam12861
Anaphase-promoting complex subunit 11 RING-H2 finger; Apc11 is one of the subunits of the ...
286-330 1.11e-03

Anaphase-promoting complex subunit 11 RING-H2 finger; Apc11 is one of the subunits of the anaphase-promoting complex or cyclosome. The APC subunits are cullin family proteins with ubiquitin ligase activity. Polyubiquitination marks proteins for degradation by the 26S proteasome and is carried out by a cascade of enzymes that includes ubiquitin-activating enzymes (E1s), ubiquitin-conjugating enzymes (E2s), and ubiquitin ligases (E3s). Apc11 acts as an E3 enzyme and is responsible for recruiting E2s to the APC and for mediating the subsequent transfer of ubiquitin to APC substrates in vivo. In Saccharomyces cerevisiae this RING-H2 finger protein defines the minimal ubiquitin ligase activity of the APC, and the integrity of the RING-H2 finger is essential for budding yeast cell viability.


Pssm-ID: 403920 [Multi-domain]  Cd Length: 85  Bit Score: 38.23  E-value: 1.11e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569006009  286 AMDNVCIICREE----------------MVTGAkrlpCNHIFHTSCLRSWFQRQQT---CPTCR 330
Cdd:pfam12861  19 PSDDVCGICRVSfdgtcpdckfpgddcpLVWGK----CSHNFHMHCILKWLHTETSkglCPMCR 78
PHA03247 PHA03247
large tegument protein UL36; Provisional
527-602 1.13e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 1.13e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569006009  527 PPRPATSVNPTEETASTVVSAAPSTSAPSSEAPTPspgASPPIPEAEKPPAPESVGiVEELPEDGEPDAAE-LRRRR 602
Cdd:PHA03247  409 APVPASVPTPAPTPVPASAPPPPATPLPSAEPGSD---DGPAPPPERQPPAPATEP-APDDPDDATRKALDaLRERR 481
RING-H2_WAVH2 cd23114
RING finger, H2 subclass, found in Arabidopsis thaliana protein WAV3 homolog 2 (WAVH2) and ...
291-332 1.24e-03

RING finger, H2 subclass, found in Arabidopsis thaliana protein WAV3 homolog 2 (WAVH2) and similar proteins; WAVH2, also known as RING-type E3 ubiquitin transferase WAVH2, is a probable E3 ubiquitin-protein ligase involved in the regulation of root growth. It acts as a positive regulator of root gravitropism. WAVH2 contains a C3H2C3-type RING-H2 finger.


Pssm-ID: 438476 [Multi-domain]  Cd Length: 56  Bit Score: 37.17  E-value: 1.24e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 569006009 291 CIICREEM----VTGAKRLPCNHIFHTSCLRSWFQ-RQQTCPTCRMD 332
Cdd:cd23114    7 CSICLETMkpgsGHAIFTAECSHSFHFECIAGNVRhGNLRCPVCRAK 53
RING-H2_RNF32 cd16471
RING finger, H2 subclass, found in RING finger protein 32 (RNF32) and similar proteins; RNF32 ...
291-330 1.25e-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: 36.84  E-value: 1.25e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 569006009 291 CIICREEMvTGAKR--LPCNHIFHTSCLRSWFQ----RQQTCPTCR 330
Cdd:cd16471    2 CPICLCAF-KGRKCtlLSCSHVFHEACLSAFEKfiesKNQKCPLCR 46
RING-HC_TRIM69_C-IV cd16611
RING finger, HC subclass, found in tripartite motif-containing protein 69 (TRIM69) and similar ...
305-340 1.28e-03

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: 37.43  E-value: 1.28e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 569006009 305 LPCNHIFHTSCLRSWFQRQQ---TCPTCRMDVLRASLPA 340
Cdd:cd16611   20 LSCGHNFCQSCITGFWELQAedtTCPECRELCQYRNLTP 58
PHA03247 PHA03247
large tegument protein UL36; Provisional
527-602 1.33e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 1.33e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569006009  527 PPRPATSVNPTEETASTVVSAAPSTSAPSSEAPTPSPgaSPPIPEAEKPPAPESVGIVEELPEDGEPDAAELRRRR 602
Cdd:PHA03247 2592 PPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPP--PSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPR 2665
RING-HC_Cbl-b cd16709
RING finger, HC subclass, found in E3 ubiquitin-protein ligase Cbl-b and similar proteins; ...
283-333 1.37e-03

RING finger, HC subclass, found in E3 ubiquitin-protein ligase Cbl-b and similar proteins; Cbl-b, also known as Casitas B-lineage lymphoma proto-oncogene b, RING finger protein 56 (RNF56), SH3-binding protein Cbl-b, or signal transduction protein Cbl-b, has been identified as a regulator of antigen-specific, T cell-intrinsic, peripheral immune tolerance, a state also known as clonal anergy. It may inhibit activation of the p85 subunit of phosphoinositide 3-kinase (PI3K), protein kinase C-theta (PKC-theta), and phospholipase C-gamma1 (PLC-gamma1) and negatively regulates T-cell receptor-induced transcription factor nuclear factor kappaB (NF-kappaB) activation. In addition, Cbl-b may target multiple signaling molecules involved in transforming growth factor (TGF)-beta-mediated transactivation pathways. Cbl-b contains a tyrosine-kinase-binding domain (TKB, also known as the phosphotyrosine binding PTB domain, is composed of a four helix-bundle, a Ca2+ binding EF-hand and a highly variant SH2 domain), a proline rich domain, a nuclear localization signal, a C3HC4-type RING-HC finger and an ubiquitin-associated (UBA) domain.


Pssm-ID: 438369 [Multi-domain]  Cd Length: 76  Bit Score: 37.74  E-value: 1.37e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 569006009 283 ELQAMDNVCIICREEMvTGAKRLPCNHIFHTSCLRSWFQRQ-QTCPTCRMDV 333
Cdd:cd16709   15 EMGSTFQLCKICAEND-KDVKIEPCGHLMCTSCLTAWQESDgQGCPFCRCEI 65
RING-HC_TRIM65_C-IV cd16609
RING finger, HC subclass, found in tripartite motif-containing protein TRIM65 and similar ...
282-331 1.45e-03

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: 36.97  E-value: 1.45e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 569006009 282 EELqamdnVCIICREeMVTGAKRLPCNHIFHTSCLRSWFQR----QQTCPTCRM 331
Cdd:cd16609    2 EEL-----TCSICLG-LYQDPVTLPCQHSFCRACIEDHWRQkdegSFSCPECRA 49
zf-RING_11 pfam17123
RING-like zinc finger;
291-316 1.57e-03

RING-like zinc finger;


Pssm-ID: 465355 [Multi-domain]  Cd Length: 29  Bit Score: 36.36  E-value: 1.57e-03
                          10        20
                  ....*....|....*....|....*...
gi 569006009  291 CIICREEMVTGAKR--LPCNHIFHTSCL 316
Cdd:pfam17123   2 CSICLDEFKPGQALfvLPCSHVFHYKCI 29
RING-HC_DTX3L cd16712
RING finger, HC subclass, found in protein Deltex-3-like (DTX3L) and similar proteins; DTX3L, ...
291-329 1.58e-03

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: 37.03  E-value: 1.58e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 569006009 291 CIICREEMVTgAKRLP-CNHIFHTSCLRSWFQRQQTCPTC 329
Cdd:cd16712    6 CPICMDRISN-KKVLPkCKHVFCAACIDKAMKYKPVCPVC 44
mRING-H2-C3DHC3_ZFPL1 cd16487
Modified RING finger, H2 subclass (C3DHC3-type), found in zinc finger protein-like 1 (ZFPL1) ...
288-329 1.60e-03

Modified RING finger, H2 subclass (C3DHC3-type), found in zinc finger protein-like 1 (ZFPL1) and similar proteins; ZFPL1, also known as zinc finger protein MCG4, is a novel mitotic Golgi phosphoprotein required for cis-Golgi integrity and efficient endoplasmic reticulum (ER)-to-Golgi transport via directly interacting with the cis-Golgi matrix protein GM130. ZFPL1 is a widely expressed integral membrane protein with two predicted zinc fingers at its N-terminus. One is a novel type of zinc finger, and the other is a modified RING-H2 finger that lacks the fourth zinc-binding residue of the consensus C3H2C3-type RING-H2 finger. It also contains a bipartite nuclear localization signal (NLS), and a leucine zipper at the C-terminus.


Pssm-ID: 438150 [Multi-domain]  Cd Length: 57  Bit Score: 36.89  E-value: 1.60e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 569006009 288 DNVCIICREEMVTG-AKRLPCNHIFHTSCLRSWFQRQQ--------TCPTC 329
Cdd:cd16487    1 DPNCTLCNTSLANGdVVRLVCYDLFHWSCLNEYAAQLPantapagyTCPQC 51
RING-H2_RBX2 cd16466
RING finger, H2 subclass, found in RING-box protein 2 (RBX2) and similar proteins; RBX2, also ...
289-332 1.70e-03

RING finger, H2 subclass, found in RING-box protein 2 (RBX2) and similar proteins; RBX2, also known as CKII beta-binding protein 1 (CKBBP1), RING finger protein 7 (RNF7), regulator of cullins 2 (ROC2), or sensitive to apoptosis gene protein (SAG), is an E3 ubiquitin-protein ligase that protects cells from apoptosis, confers radioresistance, and plays an essential and non-redundant role in embryogenesis and vasculogenesis. It promotes ubiquitination and degradation of a number of protein substrates, including c-JUN, DEPTOR, HIF-1alpha, IkappaBalpha, NF1, NOXA, p27, and procaspase-3, thus regulating various signaling pathways and biological processes. RBX2 is necessary for ubiquitin ligation activity of the multimeric cullin (Cul)-RING E3 ligases (CRLs). RBX2-containing CRLs are involved in the NEDD8 pathway and RBX2 specifically regulates NEDD8ylation of Cul5. It can bind and activate the HIV-1 Vif-Cullin5 E3 ligase complex in vitro. It is also a substrate of NEDD4-1 E3 ubiquitin ligase and mediates NEDD4-1 induced chemosensitization. The inactivation of RBX2 E3 ubiquitin ligase activity triggers senescence and inhibits Kras-induced immortalization. Endothelial deletion of RBX2 causes embryonic lethality and blocks tumor angiogenesis, and may have potential use in anti-angiogenesis therapy of human cancers. Moreover, as a component of the Cullin 5-RING E3 ubiquitin ligase (CRL5) complex, RBX2 regulates neuronal migration through different CRL5 adaptors, such as SOCS7. RBX2 also functions as a redox inducible antioxidant protein that scavenges oxygen radicals by forming inter- and intra-molecular disulfide bonds when acting alone. It contains a C-terminal C3H2C3-type RING-H2 finger that is essential for its ligase activity.


Pssm-ID: 438129 [Multi-domain]  Cd Length: 60  Bit Score: 37.14  E-value: 1.70e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 569006009 289 NVCIICREEMVTGAKRL--------------PCNHIFHTSCLRSWFQRQQTCPTCRMD 332
Cdd:cd16466    2 DTCAICRVQVMDACLRCqaenkqedcvvvwgECNHSFHNCCMSLWVKQNNRCPLCQQD 59
zf-RING_5 pfam14634
zinc-RING finger domain;
291-330 1.79e-03

zinc-RING finger domain;


Pssm-ID: 434085 [Multi-domain]  Cd Length: 43  Bit Score: 36.64  E-value: 1.79e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 569006009  291 CIICREEMVT--GAKRLPCNHIFHTSCLRSwFQRQQTCPTCR 330
Cdd:pfam14634   2 CNKCFKELSKtrPFYLTSCGHIFCEECLTR-LLQERQCPICK 42
RING-HC_RAD18 cd16529
RING finger, HC subclass, found in postreplication repair protein RAD18 and similar proteins; ...
291-333 2.22e-03

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


Pssm-ID: 438192 [Multi-domain]  Cd Length: 54  Bit Score: 36.51  E-value: 2.22e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 569006009 291 CIICREEMVTGAKRLPCNHIFHTSCLRSWFQRQQTCPTCRMDV 333
Cdd:cd16529    7 CPICFEYFNTAMMITQCSHNYCSLCIRRFLSYKTQCPTCRAAV 49
mRING-H2-C3H3C2_WDR59 cd16692
Modified RING finger, H2 subclass (C3H3C2-type), found in WD repeat-containing protein 59 ...
291-328 2.41e-03

Modified RING finger, H2 subclass (C3H3C2-type), found in WD repeat-containing protein 59 (WDR59) and similar proteins; WDR59 is a component of the GATOR2 complex, which also includes another four subunits, Seh1, Sec13, Sea2/WDR24, and Mio/Sea4. GATOR2 and GATOR1, which is composed of three subunits, DEPDC5, Nprl2, and Nprl3, form the Rag-interacting complex GATOR (GAP Activity Towards Rags). Inhibition of GATOR1 subunits makes mTORC1 signaling resistant to amino acid deprivation. In contrast, inhibition of GATOR2 subunits suppresses mTORC1 signaling and GATOR2 negatively regulates DEPDC5. WDR59 contains an N-terminal WD40 domain followed by a RWD domain, and a C-terminal RING-H2 finger with an unusual arrangement of zinc-coordinating residues. The cysteines and histidines in the RING-H2 finger are arranged as a modified C3H3C2-type, rather than the canonical C3H2C3-type. Sea3 is the yeast counterpart of WDR59. It is not included in this subfamily.


Pssm-ID: 438353  Cd Length: 47  Bit Score: 36.21  E-value: 2.41e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 569006009 291 CIICREEmVTGAKR--LPCNHIFHTSCLRSWFQRQQTCPT 328
Cdd:cd16692    3 CAICHVA-VRGSSNfcLACGHGGHTSHMMEWFRTQDVCPT 41
RING-HC_DTX3 cd16711
RING finger, HC subclass, found in E3 ubiquitin-protein ligase Deltex3 (DTX3) and similar ...
288-330 2.86e-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: 36.24  E-value: 2.86e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 569006009 288 DNVCIICREEMVTGAKRLPCNHIFHTSCLRSWFQRQQTCPTCR 330
Cdd:cd16711    1 EETCPICLGEIQNKKTLDKCKHSFCEDCITRALQVKKACPMCG 43
RING-HC_RNF5-like cd16534
RING finger, HC subclass, found in RING finger protein RNF5, RNF185 and similar proteins; RNF5 ...
291-330 3.31e-03

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: 35.74  E-value: 3.31e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 569006009 291 CIIC----REEMVTgakrlPCNHIFHTSCLRSWFQRQQ---TCPTCR 330
Cdd:cd16534    3 CNICldtaSDPVVT-----MCGHLFCWPCLYQWLETRPdrqTCPVCK 44
PLN02226 PLN02226
2-oxoglutarate dehydrogenase E2 component
530-580 3.44e-03

2-oxoglutarate dehydrogenase E2 component


Pssm-ID: 177871 [Multi-domain]  Cd Length: 463  Bit Score: 40.12  E-value: 3.44e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 569006009 530 PATSVNPTEETASTVVSAAPSTSAPSSEAPTPSPGASPP-------IPEAEKPPAPES 580
Cdd:PLN02226 158 PGTKVAIISKSEDAASQVTPSQKIPETTDPKPSPPAEDKqkpkvesAPVAEKPKAPSS 215
RING-HC_RAD5 cd23131
RING finger, HC subclass, found in radiation sensitivity protein 5 (RAD5) and similar proteins; ...
291-338 3.58e-03

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: 36.27  E-value: 3.58e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 569006009 291 CIICREEMVTGAKRL--PCNHIFHTSCLRSWFQRQQT------CPTCRMDVLRASL 338
Cdd:cd23131    6 CSICTQEPIEVGEVVftECGHSFCEDCLLEYIEFQNKkkldlkCPNCREPISKYRL 61
RING-HC_TRIM35_C-IV cd16599
RING finger, HC subclass, found in tripartite motif-containing protein 35 (TRIM35) and similar ...
282-339 4.12e-03

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: 36.28  E-value: 4.12e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569006009 282 EELQamdnvCIICRE---EMVTgakrLPCNHIFHTSCL-RSW-FQRQQTCPTCRMDVLRASLP 339
Cdd:cd16599    3 EELL-----CPICYEpfrEAVT----LRCGHNFCKGCVsRSWeRQPRAPCPVCKEASSSDDLR 56
RING-HC_MKRN2 cd16731
RING finger, HC subclass, found in makorin-2 (MKRN2) and similar proteins; MKRN2, also known ...
288-330 4.23e-03

RING finger, HC subclass, found in makorin-2 (MKRN2) and similar proteins; MKRN2, also known as makorin RING finger protein 2, RING finger protein 62 (RNF62), or HSPC070, is a putative ribonucleoprotein that acts as a neurogenesis inhibitor acting upstream of glycogen synthase kinase-3beta (GSK-3beta) in the phosphatidylinositol 3-kinase (PI3K)/Akt pathway. It also functions in promoting cell proliferation of primary CD34+ progenitor cells and K562 cells, indicating its possible involvement in normal and malignant hematopoiesis. Mammalian MKRN2 contains three N-terminal C3H1-type zinc fingers, a motif rich in Cys and His residues (CH), a C3HC4-type RING-HC finger, and another C3H1-type zinc finger at the C-terminus. The third C3H1-type zinc finger, the CH motif, as well as the RING zinc finger are necessary for its anti-neurogenic activity.


Pssm-ID: 319645 [Multi-domain]  Cd Length: 58  Bit Score: 36.03  E-value: 4.23e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 569006009 288 DNVCIICRE---EMVTGAKRL-----PCNHIFHTSCLRSW-----FQRQ--QTCPTCR 330
Cdd:cd16731    1 DKVCSICMEvvyEKASASERRfgilsNCNHTYCLSCIRQWrcakqFENPiiKSCPECR 58
PRK06975 PRK06975
bifunctional uroporphyrinogen-III synthetase/uroporphyrin-III C-methyltransferase; Reviewed
476-582 4.60e-03

bifunctional uroporphyrinogen-III synthetase/uroporphyrin-III C-methyltransferase; Reviewed


Pssm-ID: 235899 [Multi-domain]  Cd Length: 656  Bit Score: 40.09  E-value: 4.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006009 476 AGLTPEELRALEG------HERQHLEARLQSLRNIhTLLDAAMLQI-NQYLTVLASLGPPRPATSVNPTEETASTVVSAa 548
Cdd:PRK06975 214 AHLNPAEIDALKHaplvapHARIAEQARALGFDRI-TLTGAGDERIvRAFLTWADAAAQPATAAPAPSRMTDTNDSKSV- 291
                         90       100       110
                 ....*....|....*....|....*....|....
gi 569006009 549 psTSAPSSEAPTPSPGASPPIPEAEKPPAPESVG 582
Cdd:PRK06975 292 --TSQPAAAAAAPAPPPNPPATPPEPPARRGRGS 323
RING-HC_RNF146 cd16546
RING finger, HC subclass, found in RING finger protein 146 (RNF146) and similar proteins; ...
291-333 4.61e-03

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: 35.44  E-value: 4.61e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 569006009 291 CIICREEMVTGAKrLPCNHIFHTSCLRSWFQRQQTCPTCRMDV 333
Cdd:cd16546    3 CPICLQTCIHPVK-LPCGHIFCYLCVKGVAWQSKRCALCRQEI 44
RING-HC_XBAT35-like cd23129
RING finger, HC subclass, found in Arabidopsis thaliana protein XB3 homolog 5 (XBAT35) and ...
291-333 4.82e-03

RING finger, HC subclass, found in Arabidopsis thaliana protein XB3 homolog 5 (XBAT35) and similar proteins; XBAT35, also known as ankyrin repeat domain and RING finger-containing protein XBAT35, or RING-type E3 ubiquitin transferase XBAT35, has no E3 ubiquitin-protein ligase activity observed when associated with the E2 enzyme UBC8 in vitro. It contains a typical C3HC4-type RING-HC finger.


Pssm-ID: 438491 [Multi-domain]  Cd Length: 54  Bit Score: 35.70  E-value: 4.82e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 569006009 291 CIICREEmVTGAKRLPCNHIFH-TSCLRSWFQRQQTCPTCRMDV 333
Cdd:cd23129    5 CVVCMDA-PRDAVCVPCGHVAGcMSCLKALMQSSPLCPICRAPV 47
PRK14965 PRK14965
DNA polymerase III subunits gamma and tau; Provisional
496-582 4.98e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237871 [Multi-domain]  Cd Length: 576  Bit Score: 39.72  E-value: 4.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006009 496 ARLQSLRNIHTLLD-AAMLQINQYLTVLASLGPPRPATSVNPTEETASTVVSAAPSTSAPSSEAPTPSPGASPPIPEAE- 573
Cdd:PRK14965 359 ATLAPGAPVSELLDrLEALERGAPAPPSAAWGAPTPAAPAAPPPAAAPPVPPAAPARPAAARPAPAPAPPAAAAPPARSa 438

                 ....*....
gi 569006009 574 KPPAPESVG 582
Cdd:PRK14965 439 DPAAAASAG 447
RING-HC_SH3RF1 cd16748
RING finger, HC subclass, found in SH3 domain-containing RING finger protein 1 (SH3RF1) and ...
291-330 5.33e-03

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: 35.37  E-value: 5.33e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 569006009 291 CIICREEMVTGAKRLPCNHIFHTSCLRSWF--QRQQTCPTCR 330
Cdd:cd16748    5 CPVCLERLDATAKVLPCQHTFCRRCLLGIVgsRSELRCPECR 46
PRK14952 PRK14952
DNA polymerase III subunits gamma/tau;
549-599 5.89e-03

DNA polymerase III subunits gamma/tau;


Pssm-ID: 237866 [Multi-domain]  Cd Length: 584  Bit Score: 39.48  E-value: 5.89e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 569006009 549 PSTSAPSSEAPTPSPGASPPIPEAEKPPAPESVgiVEELPEDGEPDAAELR 599
Cdd:PRK14952 388 PANLLHNAPQAAPAPSAAAPEPKHQPAPEPRPV--LAPTPASGEPNAAAVR 436
RING-HC_PCGF1 cd16733
RING finger, HC subclass, found in polycomb group RING finger protein 1 (PCGF1) and similar ...
290-333 6.35e-03

RING finger, HC subclass, found in polycomb group RING finger protein 1 (PCGF1) and similar proteins; PCGF1, also known as nervous system Polycomb-1 (NSPc1) or RING finger protein 68 (RNF68), is one of six PcG RING finger (PCGF) homologs (PCGF1/NSPc1, PCGF2/Mel-18, PCGF3, PCGF4/BMI1, PCGF5, and PCGF6/MBLR). It serves as the core component of a noncanonical Polycomb repressive complex 1 (PRC1)-like BCOR complex that also contains RING1, RNF2, RYBP, SKP1, as well as the BCL6 co-repressor BCOR and the histone demethylase KDM2B, and is required to maintain the transcriptionally repressive state of some genes, such as Hox genes, BCL6 and the cyclin-dependent kinase inhibitor, CDKN1A. PCGF1 promotes cell cycle progression and enhances cell proliferation as well. It is a cell growth regulator that acts as a transcriptional repressor of p21Waf1/Cip1 via the retinoid acid response element (RARE element). Moreover, PCGF1 functions as an epigenetic regulator involved in hematopoietic cell differentiation. It cooperates with the transcription factor runt-related transcription factor 1 (Runx1) in regulating differentiation and self-renewal of hematopoietic cells. Furthermore, PCGF1 represents a physical and functional link between Polycomb function and pluripotency. PCGF1 contains a C3HC4-type RING-HC finger.


Pssm-ID: 438391 [Multi-domain]  Cd Length: 71  Bit Score: 35.70  E-value: 6.35e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 569006009 290 VCIICREEMVTGAKRLPCNHIFHTSCLRSWFQRQQTCPTCRMDV 333
Cdd:cd16733   11 VCYLCAGYFIDATTITECLHTFCKSCIVKYLQTSKYCPMCNIKI 54
RING-HC_SH3RFs cd16570
RING finger, HC subclass, found in SH3 domain-containing RING finger proteins SH3RF1, SH3RF2, ...
291-330 6.92e-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: 34.71  E-value: 6.92e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 569006009 291 CIICREEMVTGAKRLPCNHIFHTSCLRSWFQRQQT--CPTCR 330
Cdd:cd16570    3 CPVCLERLDVSAKVLPCQHTFCKRCLQIIVASRGElrCPECR 44
RING-HC_TRIM77_C-IV cd16543
RING finger, HC subclass, found in tripartite motif-containing protein 77 (TRIM77) and similar ...
291-331 7.21e-03

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: 35.06  E-value: 7.21e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 569006009 291 CIICREEM---VTgakrLPCNHIFHTSCLRSWFQRQQT---CPTCRM 331
Cdd:cd16543    6 CSICLDLLkdpVT----IPCGHSFCMNCITLLWDRKQGvpsCPQCRE 48
RING-H2_RNF32_rpt2 cd16678
second RING finger, H2 subclass, found in RING finger protein 32 (RNF32) and similar proteins; ...
305-330 7.74e-03

second 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. This model corresponds to the second RING-H2 finger.


Pssm-ID: 438340 [Multi-domain]  Cd Length: 61  Bit Score: 35.04  E-value: 7.74e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 569006009 305 LPCNHIFHTSCLRSwFQR-----QQTCPTCR 330
Cdd:cd16678   29 LSCSHVFHATCLEA-FEEfsvgeELVCPVCR 58
SepH NF040712
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ...
528-602 8.30e-03

septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces venezuelae, and homologs were identified in Mycobacterium smegmatis. SepH contains a N-terminal DUF3071 domain and a conserved C-terminal region. It binds directly to cell division protein FtsZ to stimulate the assembly of FtsZ protofilaments.


Pssm-ID: 468676 [Multi-domain]  Cd Length: 346  Bit Score: 38.98  E-value: 8.30e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569006009 528 PRPATSVNPTEETASTVVSAAPSTSAPSSEAPTPSPGASPPIPEAEKPPAPEsvgiveelpedgEPDAAELRRRR 602
Cdd:NF040712 266 PAAEPDEATRDAGEPPAPGAAETPEAAEPPAPAPAAPAAPAAPEAEEPARPE------------PPPAPKPKRRR 328
COG5219 COG5219
Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];
291-333 8.42e-03

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


Pssm-ID: 227544 [Multi-domain]  Cd Length: 1525  Bit Score: 39.27  E-value: 8.42e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 569006009  291 CIICREEMVTGAKRLP------CNHIFHTSCLRSWFQR--QQTCPTCRMDV 333
Cdd:COG5219  1472 CAICYSVLDMVDRSLPskrcatCKNKFHTRCLYKWFASsaRSNCPLCRSEI 1522
RING-HC_LONFs_rpt2 cd16514
second RING finger, HC subclass, found in the LON peptidase N-terminal domain and RING finger ...
291-333 8.94e-03

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: 34.55  E-value: 8.94e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 569006009 291 CIICRE---EMVTgakrLPCNHIFHTSCLRSWFQRQQTCPTCRMDV 333
Cdd:cd16514    4 CSLCLRllyEPVT----TPCGHTFCRACLERCLDHSPKCPLCRTSL 45
RING-HC_MKRN4 cd16732
RING finger, HC subclass, found in makorin-4 (MKRN4) and similar proteins; MKRN4, also known ...
288-331 8.97e-03

RING finger, HC subclass, found in makorin-4 (MKRN4) and similar proteins; MKRN4, also known as makorin RING finger protein pseudogene 4, makorin RING finger protein pseudogene 5, RING finger protein 64 (RNF64), zinc finger protein 127-Xp (ZNF127-Xp), or zinc finger protein 127-like 1, is a new divergent member of the makorin protein family in vertebrates. It may have an ancestral gonad-specific function and maternal embryonic expression before duplication in vertebrates. MKRN4 contains typical arrays of one to four C3H1-type zinc fingers, a motif rich in Cys and His residues (CH) and a C3HC4-type RING-HC finger. The RING-HC finger of mammalian MKRN4 shows high sequence similarity with that of MKRN3, and is not included in this model.


Pssm-ID: 438390 [Multi-domain]  Cd Length: 61  Bit Score: 35.17  E-value: 8.97e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 569006009 288 DNVCIICRE---EMVTGAKR----LP-CNHIFHTSCLRSW-----FQRQ--QTCPTCRM 331
Cdd:cd16732    1 DVACGICMDkvyEKAHAKERvfgiLPnCNHAFCVGCIKKWrkskdFQNEviKACPQCRV 59
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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