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Conserved domains on  [gi|568997450|ref|XP_006523054|]
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E3 ubiquitin-protein ligase TTC3 isoform X9 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TTC3_DZIP3_dom pfam19179
E3 ubiquitin-protein ligase TTC3/DZIP3 domain; This domain is found in E3 ubiquitin-protein ...
492-607 1.30e-65

E3 ubiquitin-protein ligase TTC3/DZIP3 domain; This domain is found in E3 ubiquitin-protein ligases TTC3 and DZIP3 and its function is unknown. TTC3 mediates ubiquitination and degradation of phosphorylated Akt, apparently its preferable target. DZIP3 is also able to bind RNA through a Lys-rich region which enhances is ubiquitination activity. It is suggested that RNA-binding proteins or ribonucleoprotein particles might be physiological targets for this enzyme, which could be important during viral infections, especially for those replicating through RNA intermediates. This domain is also found in uncharacterized proteins found in viruses.


:

Pssm-ID: 465988  Cd Length: 116  Bit Score: 217.50  E-value: 1.30e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997450   492 IEESKPEKVKVMLEKFVEECKFPPVPDAVCCYQKCRGYSKIQIYLTDPDFKGFIRISCCQYCKVEFHMNCWKKLKTTTFN 571
Cdd:pfam19179    1 IEETQPEKLKELLESLIELCKFPPKPDAVCRYQKCLGHSKIEIYFTDPDFKGFIRVSCCQSCKVEFHINCWKKLKTTSFS 80
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 568997450   572 DKIDKDFLQGICLTPDCEGIISKIIIYSSGGQVKCE 607
Cdd:pfam19179   81 DKNDKDFLQESCLTPDCRGQICKIVIFGSTGLVKCE 116
RING-H2_TTC3 cd16481
RING finger, H2 subclass, found in Tetratricopeptide repeat protein 3 (TTC3) and similar ...
1800-1840 2.28e-19

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: 82.78  E-value: 2.28e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 568997450 1800 SCEICHEIFKSKNMRVLKCGHKFHKGCFKQWLKGQSTCPTC 1840
Cdd:cd16481     1 PCIICHDDLKPDQLAKLECGHIFHKECIKQWLKEQSTCPTC 41
PLN03088 super family cl33632
SGT1, suppressor of G2 allele of SKP1; Provisional
107-251 2.29e-11

SGT1, suppressor of G2 allele of SKP1; Provisional


The actual alignment was detected with superfamily member PLN03088:

Pssm-ID: 215568 [Multi-domain]  Cd Length: 356  Bit Score: 67.50  E-value: 2.29e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997450  107 RGNEEFSKEKFEIAVIYYTRAIEYRPENHLLYGNRALCFLRMGQFRNALSDGKRAIVLKNTWPKGHYRYCDAlCM-LGEY 185
Cdd:PLN03088    8 KAKEAFVDDDFALAVDLYTQAIDLDPNNAELYADRAQANIKLGNFTEAVADANKAIELDPSLAKAYLRKGTA-CMkLEEY 86
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568997450  186 DWALQANIKAQKLCKNDPEgIKDLIQQ-HVKLQKQIEDLQGRTSNKNPIKAFYESRAYIPRNSSAPA 251
Cdd:PLN03088   87 QTAKAALEKGASLAPGDSR-FTKLIKEcDEKIAEEEKDLVQPVPSDLPSSVTAPPVEEADATPVVPP 152
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
360-472 5.98e-07

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 50.58  E-value: 5.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997450  360 LRSLIQDGYTALLEQRCRSAAQAFTELLNgLDPqkikqlnlamiNYVLVVYGLAVSLLGIGRPEElseAENQFKRIIEHY 439
Cdd:COG4783     4 AEALYALAQALLLAGDYDEAEALLEKALE-LDP-----------DNPEAFALLGEILLQLGDLDE---AIVLLHEALELD 68
                          90       100       110
                  ....*....|....*....|....*....|...
gi 568997450  440 PNEGLdclAYCGIGKVYLKKNRFLEALNHFEKA 472
Cdd:COG4783    69 PDEPE---ARLNLGLALLKAGDYDEALALLEKA 98
PTZ00121 super family cl31754
MAEBL; Provisional
1330-1564 4.94e-05

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.60  E-value: 4.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997450 1330 EVNTEPYEPFETQQGDLSQKEKECHLLREQLKVACE---NCEQIELRSSQEIKDLEEkLQRHTEENKISKTELDWFLQDL 1406
Cdd:PTZ00121 1595 EEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEekkKVEQLKKKEAEEKKKAEE-LKKAEEENKIKAAEEAKKAEED 1673
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997450 1407 DR---EIKKWQQEKKEIQE---RLKALKKKIKKVINTSEMPAQKNDGFDKECEPHPDQSlgfssalTDEKTKVEESVRKG 1480
Cdd:PTZ00121 1674 KKkaeEAKKAEEDEKKAAEalkKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKA-------EEAKKEAEEDKKKA 1746
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997450 1481 KELYEESHQRAVAAEVSVLENWKEREVCKLQGVASQSEAYLKSLKLMSSDSATYPDVE---------------YDILSWE 1545
Cdd:PTZ00121 1747 EEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFdnfaniieggkegnlVINDSKE 1826
                         250
                  ....*....|....*....
gi 568997450 1546 SFLSTVREEIESKKSQFEE 1564
Cdd:PTZ00121 1827 MEDSAIKEVADSKNMQLEE 1845
 
Name Accession Description Interval E-value
TTC3_DZIP3_dom pfam19179
E3 ubiquitin-protein ligase TTC3/DZIP3 domain; This domain is found in E3 ubiquitin-protein ...
492-607 1.30e-65

E3 ubiquitin-protein ligase TTC3/DZIP3 domain; This domain is found in E3 ubiquitin-protein ligases TTC3 and DZIP3 and its function is unknown. TTC3 mediates ubiquitination and degradation of phosphorylated Akt, apparently its preferable target. DZIP3 is also able to bind RNA through a Lys-rich region which enhances is ubiquitination activity. It is suggested that RNA-binding proteins or ribonucleoprotein particles might be physiological targets for this enzyme, which could be important during viral infections, especially for those replicating through RNA intermediates. This domain is also found in uncharacterized proteins found in viruses.


Pssm-ID: 465988  Cd Length: 116  Bit Score: 217.50  E-value: 1.30e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997450   492 IEESKPEKVKVMLEKFVEECKFPPVPDAVCCYQKCRGYSKIQIYLTDPDFKGFIRISCCQYCKVEFHMNCWKKLKTTTFN 571
Cdd:pfam19179    1 IEETQPEKLKELLESLIELCKFPPKPDAVCRYQKCLGHSKIEIYFTDPDFKGFIRVSCCQSCKVEFHINCWKKLKTTSFS 80
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 568997450   572 DKIDKDFLQGICLTPDCEGIISKIIIYSSGGQVKCE 607
Cdd:pfam19179   81 DKNDKDFLQESCLTPDCRGQICKIVIFGSTGLVKCE 116
RING-H2_TTC3 cd16481
RING finger, H2 subclass, found in Tetratricopeptide repeat protein 3 (TTC3) and similar ...
1800-1840 2.28e-19

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: 82.78  E-value: 2.28e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 568997450 1800 SCEICHEIFKSKNMRVLKCGHKFHKGCFKQWLKGQSTCPTC 1840
Cdd:cd16481     1 PCIICHDDLKPDQLAKLECGHIFHKECIKQWLKEQSTCPTC 41
PLN03088 PLN03088
SGT1, suppressor of G2 allele of SKP1; Provisional
107-251 2.29e-11

SGT1, suppressor of G2 allele of SKP1; Provisional


Pssm-ID: 215568 [Multi-domain]  Cd Length: 356  Bit Score: 67.50  E-value: 2.29e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997450  107 RGNEEFSKEKFEIAVIYYTRAIEYRPENHLLYGNRALCFLRMGQFRNALSDGKRAIVLKNTWPKGHYRYCDAlCM-LGEY 185
Cdd:PLN03088    8 KAKEAFVDDDFALAVDLYTQAIDLDPNNAELYADRAQANIKLGNFTEAVADANKAIELDPSLAKAYLRKGTA-CMkLEEY 86
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568997450  186 DWALQANIKAQKLCKNDPEgIKDLIQQ-HVKLQKQIEDLQGRTSNKNPIKAFYESRAYIPRNSSAPA 251
Cdd:PLN03088   87 QTAKAALEKGASLAPGDSR-FTKLIKEcDEKIAEEEKDLVQPVPSDLPSSVTAPPVEEADATPVVPP 152
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
107-224 2.04e-10

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 63.10  E-value: 2.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997450  107 RGNEEFSKEKFEIAVIYYTRAIEYRPENHLLYGNRALCFLRMGQFRNALSDGKRAIVLKNTWPKGHYRYCDALCMLGEYD 186
Cdd:COG0457    48 LGLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLALQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYD 127
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 568997450  187 WALQANIKAQKLCKNDPEGIKDLIQQHVKLQKQIEDLQ 224
Cdd:COG0457   128 EAIEAYERALELDPDDADALYNLGIALEKLGRYEEALE 165
zf-RING_2 pfam13639
Ring finger domain;
1799-1840 3.21e-10

Ring finger domain;


Pssm-ID: 433370 [Multi-domain]  Cd Length: 44  Bit Score: 57.03  E-value: 3.21e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 568997450  1799 NSCEICHEIF-KSKNMRVLKCGHKFHKGCFKQWLKGQSTCPTC 1840
Cdd:pfam13639    1 DECPICLEEFeEGDKVVVLPCGHHFHRECLDKWLRSSNTCPLC 43
RING smart00184
Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and ...
1801-1840 7.20e-10

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: 55.98  E-value: 7.20e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 568997450   1801 CEICHEIFkSKNMRVLKCGHKFHKGCFKQWLK-GQSTCPTC 1840
Cdd:smart00184    1 CPICLEEY-LKDPVILPCGHTFCRSCIRKWLEsGNNTCPIC 40
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
360-472 5.98e-07

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 50.58  E-value: 5.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997450  360 LRSLIQDGYTALLEQRCRSAAQAFTELLNgLDPqkikqlnlamiNYVLVVYGLAVSLLGIGRPEElseAENQFKRIIEHY 439
Cdd:COG4783     4 AEALYALAQALLLAGDYDEAEALLEKALE-LDP-----------DNPEAFALLGEILLQLGDLDE---AIVLLHEALELD 68
                          90       100       110
                  ....*....|....*....|....*....|...
gi 568997450  440 PNEGLdclAYCGIGKVYLKKNRFLEALNHFEKA 472
Cdd:COG4783    69 PDEPE---ARLNLGLALLKAGDYDEALALLEKA 98
3a0801s09 TIGR00990
mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) ...
104-189 4.06e-06

mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) (mitochondrial import receptor for the ADP/ATP carrier) (translocase of outermembrane tom70); [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 273380 [Multi-domain]  Cd Length: 615  Bit Score: 51.91  E-value: 4.06e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997450   104 MKMRGNEEFSKEKFEIAVIYYTRAIEYRPENhLLYGNRALCFLRMGQFRNALSDGKRAIVLKNTWPKGHYRYCDALCMLG 183
Cdd:TIGR00990  130 LKEKGNKAYRNKDFNKAIKLYSKAIECKPDP-VYYSNRAACHNALGDWEKVVEDTTAALELDPDYSKALNRRANAYDGLG 208

                   ....*.
gi 568997450   184 EYDWAL 189
Cdd:TIGR00990  209 KYADAL 214
COG5540 COG5540
RING-finger-containing ubiquitin ligase [Posttranslational modification, protein turnover, ...
1798-1842 2.41e-05

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


Pssm-ID: 227827 [Multi-domain]  Cd Length: 374  Bit Score: 48.84  E-value: 2.41e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 568997450 1798 GNSCEICHEIF-KSKNMRVLKCGHKFHKGCFKQWLKGQS-TCPTCGS 1842
Cdd:COG5540   323 GVECAICMSNFiKNDRLRVLPCDHRFHVGCVDKWLLGYSnKCPVCRT 369
PTZ00121 PTZ00121
MAEBL; Provisional
1330-1564 4.94e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.60  E-value: 4.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997450 1330 EVNTEPYEPFETQQGDLSQKEKECHLLREQLKVACE---NCEQIELRSSQEIKDLEEkLQRHTEENKISKTELDWFLQDL 1406
Cdd:PTZ00121 1595 EEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEekkKVEQLKKKEAEEKKKAEE-LKKAEEENKIKAAEEAKKAEED 1673
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997450 1407 DR---EIKKWQQEKKEIQE---RLKALKKKIKKVINTSEMPAQKNDGFDKECEPHPDQSlgfssalTDEKTKVEESVRKG 1480
Cdd:PTZ00121 1674 KKkaeEAKKAEEDEKKAAEalkKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKA-------EEAKKEAEEDKKKA 1746
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997450 1481 KELYEESHQRAVAAEVSVLENWKEREVCKLQGVASQSEAYLKSLKLMSSDSATYPDVE---------------YDILSWE 1545
Cdd:PTZ00121 1747 EEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFdnfaniieggkegnlVINDSKE 1826
                         250
                  ....*....|....*....
gi 568997450 1546 SFLSTVREEIESKKSQFEE 1564
Cdd:PTZ00121 1827 MEDSAIKEVADSKNMQLEE 1845
rad18 TIGR00599
DNA repair protein rad18; All proteins in this family for which functions are known are ...
1801-1844 5.30e-03

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


Pssm-ID: 273165 [Multi-domain]  Cd Length: 397  Bit Score: 41.14  E-value: 5.30e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 568997450  1801 CEICHEIFKSKnmRVLKCGHKFHKGCFKQWLKGQSTCPTCGSSD 1844
Cdd:TIGR00599   29 CHICKDFFDVP--VLTSCSHTFCSLCIRRCLSNQPKCPLCRAED 70
TPR_1 pfam00515
Tetratricopeptide repeat;
448-475 8.70e-03

Tetratricopeptide repeat;


Pssm-ID: 459840 [Multi-domain]  Cd Length: 34  Bit Score: 35.47  E-value: 8.70e-03
                           10        20
                   ....*....|....*....|....*...
gi 568997450   448 AYCGIGKVYLKKNRFLEALNHFEKAKTL 475
Cdd:pfam00515    3 ALYNLGNAYFKLGKYDEALEYYEKALEL 30
 
Name Accession Description Interval E-value
TTC3_DZIP3_dom pfam19179
E3 ubiquitin-protein ligase TTC3/DZIP3 domain; This domain is found in E3 ubiquitin-protein ...
492-607 1.30e-65

E3 ubiquitin-protein ligase TTC3/DZIP3 domain; This domain is found in E3 ubiquitin-protein ligases TTC3 and DZIP3 and its function is unknown. TTC3 mediates ubiquitination and degradation of phosphorylated Akt, apparently its preferable target. DZIP3 is also able to bind RNA through a Lys-rich region which enhances is ubiquitination activity. It is suggested that RNA-binding proteins or ribonucleoprotein particles might be physiological targets for this enzyme, which could be important during viral infections, especially for those replicating through RNA intermediates. This domain is also found in uncharacterized proteins found in viruses.


Pssm-ID: 465988  Cd Length: 116  Bit Score: 217.50  E-value: 1.30e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997450   492 IEESKPEKVKVMLEKFVEECKFPPVPDAVCCYQKCRGYSKIQIYLTDPDFKGFIRISCCQYCKVEFHMNCWKKLKTTTFN 571
Cdd:pfam19179    1 IEETQPEKLKELLESLIELCKFPPKPDAVCRYQKCLGHSKIEIYFTDPDFKGFIRVSCCQSCKVEFHINCWKKLKTTSFS 80
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 568997450   572 DKIDKDFLQGICLTPDCEGIISKIIIYSSGGQVKCE 607
Cdd:pfam19179   81 DKNDKDFLQESCLTPDCRGQICKIVIFGSTGLVKCE 116
RING-H2_TTC3 cd16481
RING finger, H2 subclass, found in Tetratricopeptide repeat protein 3 (TTC3) and similar ...
1800-1840 2.28e-19

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: 82.78  E-value: 2.28e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 568997450 1800 SCEICHEIFKSKNMRVLKCGHKFHKGCFKQWLKGQSTCPTC 1840
Cdd:cd16481     1 PCIICHDDLKPDQLAKLECGHIFHKECIKQWLKEQSTCPTC 41
PLN03088 PLN03088
SGT1, suppressor of G2 allele of SKP1; Provisional
107-251 2.29e-11

SGT1, suppressor of G2 allele of SKP1; Provisional


Pssm-ID: 215568 [Multi-domain]  Cd Length: 356  Bit Score: 67.50  E-value: 2.29e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997450  107 RGNEEFSKEKFEIAVIYYTRAIEYRPENHLLYGNRALCFLRMGQFRNALSDGKRAIVLKNTWPKGHYRYCDAlCM-LGEY 185
Cdd:PLN03088    8 KAKEAFVDDDFALAVDLYTQAIDLDPNNAELYADRAQANIKLGNFTEAVADANKAIELDPSLAKAYLRKGTA-CMkLEEY 86
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568997450  186 DWALQANIKAQKLCKNDPEgIKDLIQQ-HVKLQKQIEDLQGRTSNKNPIKAFYESRAYIPRNSSAPA 251
Cdd:PLN03088   87 QTAKAALEKGASLAPGDSR-FTKLIKEcDEKIAEEEKDLVQPVPSDLPSSVTAPPVEEADATPVVPP 152
RING-H2_DZIP3 cd16460
RING finger, H2 subclass, found in DAZ (deleted in azoospermia)-interacting protein 3 (DZIP3) ...
1801-1840 4.81e-11

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: 59.48  E-value: 4.81e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 568997450 1801 CEICHEIFKSK-NMRVLKCGHKFHKGCFKQWLKGQSTCPTC 1840
Cdd:cd16460     3 CVICHEAFSDGdRLLVLPCAHKFHTQCIGPWLDGQQTCPTC 43
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
107-224 2.04e-10

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 63.10  E-value: 2.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997450  107 RGNEEFSKEKFEIAVIYYTRAIEYRPENHLLYGNRALCFLRMGQFRNALSDGKRAIVLKNTWPKGHYRYCDALCMLGEYD 186
Cdd:COG0457    48 LGLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLALQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYD 127
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 568997450  187 WALQANIKAQKLCKNDPEGIKDLIQQHVKLQKQIEDLQ 224
Cdd:COG0457   128 EAIEAYERALELDPDDADALYNLGIALEKLGRYEEALE 165
RING-H2 cd16448
H2 subclass of RING (RING-H2) fingers and its variants; The RING finger is a specialized type ...
1801-1840 2.39e-10

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: 57.41  E-value: 2.39e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 568997450 1801 CEICHEIFKSKN-MRVLKCGHKFHKGCFKQWLK-GQSTCPTC 1840
Cdd:cd16448     1 CVICLEEFEEGDvVRLLPCGHVFHLACILRWLEsGNNTCPLC 42
zf-RING_2 pfam13639
Ring finger domain;
1799-1840 3.21e-10

Ring finger domain;


Pssm-ID: 433370 [Multi-domain]  Cd Length: 44  Bit Score: 57.03  E-value: 3.21e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 568997450  1799 NSCEICHEIF-KSKNMRVLKCGHKFHKGCFKQWLKGQSTCPTC 1840
Cdd:pfam13639    1 DECPICLEEFeEGDKVVVLPCGHHFHRECLDKWLRSSNTCPLC 43
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
107-224 5.12e-10

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 61.95  E-value: 5.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997450  107 RGNEEFSKEKFEIAVIYYTRAIEYRPENHLLYGNRALCFLRMGQFRNALSDGKRAIVLKNTWPKGHYRYCDALCMLGEYD 186
Cdd:COG0457    82 LGLALQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLGIALEKLGRYE 161
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 568997450  187 WALQANIKAQKLCKNDPEGIKDLIQQHVKLQKQIEDLQ 224
Cdd:COG0457   162 EALELLEKLEAAALAALLAAALGEAALALAAAEVLLAL 199
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
107-224 5.45e-10

Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 61.47  E-value: 5.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997450  107 RGNEEFSKEKFEIAVIYYTRAIEYRPENHLLYGNRALCFLRMGQFRNALSDGKRAIVLKntwPKGHYRYCD---ALCMLG 183
Cdd:COG4785    79 RGVAYDSLGDYDLAIADFDQALELDPDLAEAYNNRGLAYLLLGDYDAALEDFDRALELD---PDYAYAYLNrgiALYYLG 155
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 568997450  184 EYDWALQANIKAQKLCKNDPEGI--KDLIQQHVKLQKQIEDLQ 224
Cdd:COG4785   156 RYELAIADLEKALELDPNDPERAlwLYLAERKLDPEKALALLL 198
RING smart00184
Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and ...
1801-1840 7.20e-10

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: 55.98  E-value: 7.20e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 568997450   1801 CEICHEIFkSKNMRVLKCGHKFHKGCFKQWLK-GQSTCPTC 1840
Cdd:smart00184    1 CPICLEEY-LKDPVILPCGHTFCRSCIRKWLEsGNNTCPIC 40
RING-H2_PA-TM-RING cd16454
RING finger, H2 subclass, found in the PA-TM-RING ubiquitin ligase family; The PA-TM-RING ...
1800-1840 7.38e-10

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: 55.74  E-value: 7.38e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 568997450 1800 SCEICHEIFKSKNM-RVLKCGHKFHKGCFKQWLKGQSTCPTC 1840
Cdd:cd16454     1 TCAICLEEFKEGEKvRVLPCNHLFHKDCIDPWLEQHNTCPLC 42
RING-H2_synoviolin cd16479
RING finger, H2 subclass, found in synoviolin and similar proteins; Synoviolin, also known as ...
1799-1840 2.97e-09

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: 54.28  E-value: 2.97e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 568997450 1799 NSCEICHEIFKSKNMRvLKCGHKFHKGCFKQWLKGQSTCPTC 1840
Cdd:cd16479     2 NTCIICREEMTVGAKK-LPCGHIFHLSCLRSWLQRQQTCPTC 42
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
112-191 3.30e-09

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 57.66  E-value: 3.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997450  112 FSKEKFEIAVIYYTRAIEYRPENHLLYGNRALCFLRMGQFRNALSDGKRAIVLKNTWPKGHYRYCDALCMLGEYDWALQA 191
Cdd:COG5010    65 NKLGDFEESLALLEQALQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAA 144
mRING-C3HGC3_RFWD3 cd16450
Modified RING finger, C3HGC3-type, found in RING finger and WD repeat domain-containing ...
1797-1840 4.03e-09

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: 54.16  E-value: 4.03e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 568997450 1797 DGNSCEICHEIFKSK-NMRV--LKCGHKFHKGCFKQWLKGQS-TCPTC 1840
Cdd:cd16450     1 EGNTCPICFEPWTSSgEHRLvsLKCGHLFGYSCIEKWLKGKGkKCPQC 48
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
107-204 9.48e-09

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 58.09  E-value: 9.48e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997450  107 RGNEEFSKEKFEIAVIYYTRAIEYRPENHLLYGNRALCFLRMGQFRNALSDGKRAIVLKNTWPKGHYRYCDALCMLGEYD 186
Cdd:COG0457    14 LGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLALQALGRYE 93
                          90
                  ....*....|....*...
gi 568997450  187 WALQANIKAQKLCKNDPE 204
Cdd:COG0457    94 EALEDYDKALELDPDDAE 111
RING-H2_TRAIP cd16480
RING finger, H2 subclass, found in TRAF-interacting protein (TRAIP) and similar proteins; ...
1801-1840 1.23e-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: 52.43  E-value: 1.23e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 568997450 1801 CEICHEIFK-SKNMRVLKCGHKFHKGCFKQWLKGQSTCPTC 1840
Cdd:cd16480     2 CTICSDFFDnSRDVAAIHCGHTFHYDCLLQWFDTSRTCPQC 42
RING-H2_EL5-like cd16461
RING finger, H2 subclass, found in rice E3 ubiquitin-protein ligase EL5 and similar proteins; ...
1800-1840 1.52e-08

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: 52.26  E-value: 1.52e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 568997450 1800 SCEICHEIFKSKNM--RVLKCGHKFHKGCFKQWLKGQSTCPTC 1840
Cdd:cd16461     1 ECAICLSDYENGEElrRLPECKHAFHKECIDEWLKSNSTCPLC 43
RING-H2_RNF24-like cd16469
RING finger, H2 subclass, found in RING finger proteins RNF24, RNF122, and similar proteins; ...
1801-1843 1.70e-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: 52.01  E-value: 1.70e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 568997450 1801 CEICHEIFKSKN-MRVLKCGHKFHKGCFKQWLKGQSTCPTCGSS 1843
Cdd:cd16469     3 CAVCLEEFKLKEeLGVCPCGHAFHTKCLKKWLEVRNSCPICKSP 46
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
108-204 2.97e-08

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 58.85  E-value: 2.97e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997450  108 GNEEFSKEKFEIAVIYYTRAIEYRPENHLLYGNRALCFLRMGQFRNALSDGKRAIVLKNTWPKGHYRYCDALCMLGEYDW 187
Cdd:COG3914   119 GNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNALQDLGRLEE 198
                          90
                  ....*....|....*..
gi 568997450  188 ALQAnikAQKLCKNDPE 204
Cdd:COG3914   199 AIAA---YRRALELDPD 212
RING-H2_RNF215 cd16670
RING finger, H2 subclass, found in RING finger protein 215 (RNF215) and similar proteins; This ...
1800-1840 3.15e-08

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: 51.30  E-value: 3.15e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 568997450 1800 SCEICHEIFKSKN-MRVLKCGHKFHKGCFKQWLKGQSTCPTC 1840
Cdd:cd16670     2 SCAVCLDQFYKNQcLRVLPCLHEFHRDCVDPWLLLQQTCPLC 43
RING-H2_RNF103 cd16473
RING finger, H2 subclass, found in RING finger protein 103 (RNF103) and similar proteins; ...
1796-1840 5.34e-08

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: 50.74  E-value: 5.34e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 568997450 1796 PDGNSCEICHEIFKSKNM-RVLKCGHKFHKGCFKQWL-KGQSTCPTC 1840
Cdd:cd16473     2 LECEECAICLENYQNGDLlRGLPCGHVFHQNCIDVWLeRDNHCCPVC 48
RING-H2_RNF139-like cd16476
RING finger, H2 subclass, found in RING finger proteins RNF139, RNF145, and similar proteins; ...
1801-1840 6.62e-08

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: 50.15  E-value: 6.62e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 568997450 1801 CEICHEIFKSknMRVLKCGHKFHKGCFKQWLKGQSTCPTC 1840
Cdd:cd16476     3 CAICYQEMKE--ARITPCNHFFHGLCLRKWLYVQDTCPLC 40
RING-H2_SIS3 cd23118
RING finger, H2 subclass, found in Arabidopsis thaliana protein SUGAR INSENSITIVE 3 (SIS3) and ...
1800-1840 7.82e-08

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: 50.06  E-value: 7.82e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 568997450 1800 SCEICHEIFKSKN-MRVLKCGHKFHKGCFKQWLKGQSTCPTC 1840
Cdd:cd23118     2 TCTICLEDFEDGEkLRVLPCQHQFHSECVDQWLRRNPKCPVC 43
RING-H2_RNF43-like cd16666
RING finger, H2 subclass, found in RING finger proteins RNF43, ZNRF3, and similar proteins; ...
1800-1840 8.89e-08

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: 50.15  E-value: 8.89e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 568997450 1800 SCEICHEIFKSKN-MRVLKCGHKFHKGCFKQWLKGQSTCPTC 1840
Cdd:cd16666     1 VCAICLEEYEEGQeLRVLPCQHEFHRKCVDPWLLQNHTCPLC 42
mRING-H2-C3H2C2D_ZSWM2 cd16486
Modified RING finger, H2 subclass (C3H2C2D-type), found in zinc finger SWIM domain-containing ...
1801-1841 1.26e-07

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: 49.68  E-value: 1.26e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 568997450 1801 CEICHEIFK-SKNMRVLKCGHKFHKGCFKQWLKGQS-TCPTCG 1841
Cdd:cd16486     2 CRICLKAFQlGQHVRTLPCRHKFHRDCIDNWLLHSRnSCPIDG 44
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
100-221 1.63e-07

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 52.12  E-value: 1.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997450  100 QGELMKMRGNEEFSKEKFEIAVIYYTRAIEYRPENHLLYGNRALCFLRMGQFRNALSDGKRAIVLKNTWPKGHYRYCDAL 179
Cdd:COG4783     3 CAEALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLAL 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 568997450  180 CMLGEYDWALQANIKAQKLCKNDPEGIKDLIQQHVKLQKQIE 221
Cdd:COG4783    83 LKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDE 124
RING-H2_RNF130 cd16803
RING finger, H2 subclass, found in RING finger protein 130 (RNF130) and similar proteins; ...
1799-1840 1.83e-07

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: 49.20  E-value: 1.83e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 568997450 1799 NSCEICHEIFKSKNM-RVLKCGHKFHKGCFKQWLKGQSTCPTC 1840
Cdd:cd16803     1 DHCAVCIEGYKQNDVvRILPCKHVFHKSCVDPWLNEHCTCPMC 43
RING-H2_RNF111-like cd16474
RING finger, H2 subclass, found in RING finger proteins RNF111, RNF165, and similar proteins; ...
1801-1840 1.89e-07

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: 48.94  E-value: 1.89e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 568997450 1801 CEICHEIFKSKN-MRVLKCGHKFHKGCFKQWLKGQSTCPTC 1840
Cdd:cd16474     3 CTICLSDFEEGEdVRRLPCMHLFHQECVDQWLSTNKRCPIC 43
RING-H2_RNF130-like cd16668
RING finger, H2 subclass, found in RING finger proteins, RNF130, RNF149, RNF150 and similar ...
1801-1840 2.33e-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: 48.93  E-value: 2.33e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 568997450 1801 CEICHEIFKSKN-MRVLKCGHKFHKGCFKQWLKGQSTCPTC 1840
Cdd:cd16668     2 CAVCIEPYKPSDvIRILPCKHIFHKSCVDPWLLEHRTCPMC 42
RING-H2_RNF32_rpt1 cd16677
first RING finger, H2 subclass, found in RING finger protein 32 (RNF32) and similar proteins; ...
1800-1840 2.93e-07

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: 48.83  E-value: 2.93e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 568997450 1800 SCEICHEIFKSKNMRVLKCGHKFHKGCFKQWLK--GQSTCPTC 1840
Cdd:cd16677     1 PCPICLEDFGLQQQVLLSCSHVFHRACLESFERfsGKKTCPMC 43
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
101-212 3.36e-07

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 51.16  E-value: 3.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997450  101 GELMKMRGNEEFSKEKFEIAVIYYTRAIEYRPENHLLYGNRALCFLRMGQFRNALSDGKRAIVLKNTWPKGHYRYCDALC 180
Cdd:COG4235    17 AEGWLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALALDPDNPEALYLLGLAAF 96
                          90       100       110
                  ....*....|....*....|....*....|....
gi 568997450  181 MLGEYDWALQANIKAQKLCKNDPE--GIKDLIQQ 212
Cdd:COG4235    97 QQGDYAEAIAAWQKLLALLPADAParLLEASIAE 130
RING-H2_RNF44 cd16680
RING finger, H2 subclass, found in RING finger protein 44 (RNF44) and similar proteins; RNF44 ...
1801-1840 3.45e-07

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: 48.91  E-value: 3.45e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 568997450 1801 CEICHEIFKSKNM-RVLKCGHKFHKGCFKQWLKGQSTCPTC 1840
Cdd:cd16680    10 CVVCFSDFESRQLlRVLPCNHEFHTKCVDKWLKTNRTCPIC 50
RING-H2_Pirh2-like cd16464
RING finger, H2 subclass, found in p53-induced RING-H2 protein (Pirh2) and similar proteins; ...
1801-1841 3.66e-07

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: 48.42  E-value: 3.66e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 568997450 1801 CEICHE-IFKSK-NMRVLKCGHKFHKGCFKQWLKGQS-TCPTCG 1841
Cdd:cd16464     2 CPVCLEdLFTSRePVHVLPCGHLMHSTCFEEYLKSGNyRCPLCS 45
RING-H2_RNF149 cd16804
RING finger, H2 subclass, found in RING finger protein 149 (RNF149) and similar proteins; ...
1800-1840 4.75e-07

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: 47.98  E-value: 4.75e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 568997450 1800 SCEICHEIFKSKNM-RVLKCGHKFHKGCFKQWLKGQSTCPTC 1840
Cdd:cd16804     1 NCAVCIENYKSKDVvRILPCKHVFHRICIDPWLLEHRTCPMC 42
RING-H2_MBR cd23113
RING finger, H2 subclass, found in Arabidopsis thaliana MED25-binding RING-H2 protein (MBR) ...
1801-1845 5.78e-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: 47.95  E-value: 5.78e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 568997450 1801 CEICHEIF-KSKNMRVLKCGHKFHKGCFKQWLKGQSTCPTCGSSDL 1845
Cdd:cd23113     5 CCICQEEYeEGDELGTIECGHEYHSDCIKQWLVQKNLCPICKATAL 50
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
360-472 5.98e-07

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 50.58  E-value: 5.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997450  360 LRSLIQDGYTALLEQRCRSAAQAFTELLNgLDPqkikqlnlamiNYVLVVYGLAVSLLGIGRPEElseAENQFKRIIEHY 439
Cdd:COG4783     4 AEALYALAQALLLAGDYDEAEALLEKALE-LDP-----------DNPEAFALLGEILLQLGDLDE---AIVLLHEALELD 68
                          90       100       110
                  ....*....|....*....|....*....|...
gi 568997450  440 PNEGLdclAYCGIGKVYLKKNRFLEALNHFEKA 472
Cdd:COG4783    69 PDEPE---ARLNLGLALLKAGDYDEALALLEKA 98
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
106-204 6.03e-07

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 50.58  E-value: 6.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997450  106 MRGNEEFSKEKFEIAVIYYTRAIEYRPENHLLYGNRALCFLRMGQFRNALSDGKRAIVLKNTWPKGHYRYCDALCMLGEY 185
Cdd:COG4783    43 LLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRP 122
                          90
                  ....*....|....*....
gi 568997450  186 DWALQAnikAQKLCKNDPE 204
Cdd:COG4783   123 DEAIAA---LEKALELDPD 138
RING-H2_RNF122 cd16676
RING finger, H2 subclass, found in RING finger protein 122 (RNF122) and similar proteins; ...
1800-1840 6.41e-07

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: 47.65  E-value: 6.41e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 568997450 1800 SCEICHEIFKSKN-MRVLKCGHKFHKGCFKQWLKGQSTCPTC 1840
Cdd:cd16676     2 TCAVCLEDFKTKDeLGVLPCQHAFHRKCLVKWLEIRCVCPMC 43
RING-H2_RNF38-like cd16472
RING finger, H2 subclass, found in RING finger proteins RNF38, RNF44, and similar proteins; ...
1797-1840 6.81e-07

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: 47.71  E-value: 6.81e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 568997450 1797 DGNSCEICHEIFKSK-NMRVLKCGHKFHKGCFKQWLKGQSTCPTC 1840
Cdd:cd16472     1 DQTQCVVCMCDYEKRqLLRVLPCSHEFHAKCIDKWLKTNRTCPIC 45
RING-H2_RNF126-like cd16667
RING finger, H2 subclass, found in RING finger proteins RNF126, RNF115, and similar proteins; ...
1801-1840 6.85e-07

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: 47.30  E-value: 6.85e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 568997450 1801 CEICHEIFK-SKNMRVLKCGHKFHKGCFKQWLKGQSTCPTC 1840
Cdd:cd16667     2 CAVCKEDFEvGEEVRQLPCKHLFHPDCIVPWLELHNSCPVC 42
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
112-198 1.10e-06

Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 48.63  E-value: 1.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997450  112 FSKEKFEIAVIYYTRAIEYRPENHLLYGNRALCFLRMGQFRNALsDGKRAIVLKNTWPKGHYRYCDALCMLGEYDWALQA 191
Cdd:COG3063     3 LKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAI-ALEKALKLDPNNAEALLNLAELLLELGDYDEALAY 81

                  ....*..
gi 568997450  192 NIKAQKL 198
Cdd:COG3063    82 LERALEL 88
RING-H2_RNF11 cd16468
RING finger, H2 subclass, found in RING finger protein 11 (RNF11) and similar proteins; RNF11 ...
1801-1840 1.16e-06

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: 46.97  E-value: 1.16e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 568997450 1801 CEICHEIFKSKN-MRVLKCGHKFHKGCFKQWLKGQSTCPTC 1840
Cdd:cd16468     2 CVICMADFVVGDpIRYLPCMHIYHVDCIDDWLMRSFTCPSC 42
zf-rbx1 pfam12678
RING-H2 zinc finger domain; There are 8 cysteine/ histidine residues which are proposed to be ...
1817-1840 1.46e-06

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: 46.93  E-value: 1.46e-06
                           10        20
                   ....*....|....*....|....
gi 568997450  1817 KCGHKFHKGCFKQWLKGQSTCPTC 1840
Cdd:pfam12678   31 ECGHAFHLHCISRWLKTNNTCPLC 54
RING-HC_RNF151 cd16547
RING finger, HC subclass, found in RING finger protein 151 (RNF151) and similar proteins; ...
1801-1840 1.53e-06

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


Pssm-ID: 438209 [Multi-domain]  Cd Length: 49  Bit Score: 46.68  E-value: 1.53e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 568997450 1801 CEICHEIFKSKNMrvLKCGHKFHKGCFKQWLKGQSTCPTC 1840
Cdd:cd16547     6 CSICHGVLRCPVR--LSCSHIFCKKCILQWLKRQETCPCC 43
RING-H2_AMFR cd16455
RING finger, H2 subclass, found in autocrine motility factor receptor (AMFR) and similar ...
1801-1840 1.68e-06

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: 46.29  E-value: 1.68e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 568997450 1801 CEICHEifKSKNMRVLKCGHKFHKGCFKQWLKGQSTCPTC 1840
Cdd:cd16455     3 CAICWE--SMQSARKLPCGHLFHNSCLRSWLEQDTSCPTC 40
RING-H2_BB-like cd23115
RING finger, H2 subclass, found in Arabidopsis thaliana RING-type E3 ubiquitin transferase BIG ...
1797-1843 2.09e-06

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: 46.29  E-value: 2.09e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 568997450 1797 DGNSCEIC-HEIFKSKNMRVLKCGHKFHKGCFKQWLKGQSTCPTCGSS 1843
Cdd:cd23115     3 DNERCVICrLEYEEGEDLLTLPCKHCYHSECIQQWLQINKVCPVCSAE 50
RING-H2_RNF43 cd16798
RING finger, H2 subclass, found in RING finger protein 43 (RNF43) and similar proteins; RNF43 ...
1801-1840 2.19e-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: 46.39  E-value: 2.19e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 568997450 1801 CEICHEIFKS-KNMRVLKCGHKFHKGCFKQWLKGQSTCPTC 1840
Cdd:cd16798     6 CAICLEEFSEgQELRIISCSHEFHRECVDPWLHQHRTCPLC 46
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
128-204 3.10e-06

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 50.39  E-value: 3.10e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568997450  128 IEYRPENHLLYGNRALCFLRMGQFRNALSDGKRAIVLKNTWPKGHYRYCDALCMLGEYDWALQANIKAQKLCKNDPE 204
Cdd:COG0457     1 LELDPDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAE 77
RING-H2_RNF139 cd16683
RING finger, H2 subclass, found in RING finger protein 139 (RNF139) and similar proteins; ...
1788-1840 3.82e-06

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: 45.72  E-value: 3.82e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568997450 1788 QKKDDVpapdgnsCEICHEIFKSkNMRVLKCGHKFHKGCFKQWLKGQSTCPTC 1840
Cdd:cd16683     1 REIDDV-------CAICYQEFTT-SARITPCNHYFHALCLRKWLYIQDTCPMC 45
3a0801s09 TIGR00990
mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) ...
104-189 4.06e-06

mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) (mitochondrial import receptor for the ADP/ATP carrier) (translocase of outermembrane tom70); [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 273380 [Multi-domain]  Cd Length: 615  Bit Score: 51.91  E-value: 4.06e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997450   104 MKMRGNEEFSKEKFEIAVIYYTRAIEYRPENhLLYGNRALCFLRMGQFRNALSDGKRAIVLKNTWPKGHYRYCDALCMLG 183
Cdd:TIGR00990  130 LKEKGNKAYRNKDFNKAIKLYSKAIECKPDP-VYYSNRAACHNALGDWEKVVEDTTAALELDPDYSKALNRRANAYDGLG 208

                   ....*.
gi 568997450   184 EYDWAL 189
Cdd:TIGR00990  209 KYADAL 214
RING-H2_RNF181 cd16669
RING finger, H2 subclass, found in RING finger protein 181 (RNF181) and similar proteins; ...
1800-1840 4.15e-06

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: 45.44  E-value: 4.15e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 568997450 1800 SCEICHEIF-KSKNMRVLKCGHKFHKGCFKQWLKGQSTCPTC 1840
Cdd:cd16669     1 KCPICLLEFeEGETVKQLPCKHSFHSDCILPWLGKTNSCPLC 42
RING-H2_RNF128-like cd16802
RING finger, H2 subclass, found in RING finger protein 128 (RNF128) and similar proteins; This ...
1799-1840 4.73e-06

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: 45.11  E-value: 4.73e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 568997450 1799 NSCEICHEIFKSKN-MRVLKCGHKFHKGCFKQWLKGQSTCPTC 1840
Cdd:cd16802     1 DSCAVCIEPYKPNDvVRILTCNHLFHKNCIDPWLLEHRTCPMC 43
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
117-204 5.22e-06

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 51.53  E-value: 5.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997450  117 FEIAVIYYTRAIEYRPENHLLYGNRALCFLRMGQFRNALSDGKRAIVLKNTWPKGHYRYCDALCMLGEYDWALQAnikAQ 196
Cdd:COG3914    94 YEEALALYRRALALNPDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAA---LR 170

                  ....*...
gi 568997450  197 KLCKNDPE 204
Cdd:COG3914   171 RALELDPD 178
RING-H2_RNF145 cd16684
RING finger, H2 subclass, found in RING finger protein 145 (RNF145) and similar proteins; ...
1801-1840 5.85e-06

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: 45.05  E-value: 5.85e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 568997450 1801 CEICHEIFKSKnmRVLKCGHKFHKGCFKQWLKGQSTCPTC 1840
Cdd:cd16684     5 CSICYQDMKSA--VITPCSHFFHAGCLKKWLYVQETCPLC 42
zf-C3HC4_2 pfam13923
Zinc finger, C3HC4 type (RING finger);
1801-1840 6.02e-06

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 404756 [Multi-domain]  Cd Length: 40  Bit Score: 44.74  E-value: 6.02e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 568997450  1801 CEICHEIFKSKnMRVLKCGHKFHKGCFKQWLKGQSTCPTC 1840
Cdd:pfam13923    2 CPICMDMLKDP-STTTPCGHVFCQDCILRALRAGNECPLC 40
RING-HC cd16449
HC subclass of RING (RING-HC) finger and its variants; The RING finger is a specialized type ...
1800-1840 6.38e-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: 44.78  E-value: 6.38e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 568997450 1800 SCEICHEIFKskNMRVLKCGHKFHKGCFKQWLK-GQSTCPTC 1840
Cdd:cd16449     2 ECPICLERLK--DPVLLPCGHVFCRECIRRLLEsGSIKCPIC 41
RING-H2_RHA2B cd23123
RING finger, H2 subclass, found in Saccharomyces cerevisiae RING-H2 zinc finger protein RHA2B ...
1799-1842 6.61e-06

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: 44.88  E-value: 6.61e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 568997450 1799 NSCEIC-HEIFKSKNMRVLKCGHKFHKGCFKQWLKGQS-TCPTCGS 1842
Cdd:cd23123     1 SDCCIClDKLKTGEEVKKLDCRHKFHKQCIEGWLKHLNfNCPLCRS 46
RING-HC_IRC20-like cd23135
RING finger, HC subclass, found in Saccharomyces cerevisiae increased recombination centers ...
1800-1840 6.84e-06

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


Pssm-ID: 438497 [Multi-domain]  Cd Length: 44  Bit Score: 44.81  E-value: 6.84e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 568997450 1800 SCEICHEIFKSKNmrVLKCGHKFHKGCFKQWLKGQSTCPTC 1840
Cdd:cd23135     5 SCSICFSEIRSGA--ILKCGHFFCLSCIASWLREKSTCPLC 43
RING-H2_RNF6-like cd16467
RING finger, H2 subclass, found in E3 ubiquitin-protein ligase RNF6, RNF12, and similar ...
1800-1840 7.25e-06

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: 44.37  E-value: 7.25e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 568997450 1800 SCEICHEIFKSKNM-RVLKCGHKFHKGCFKQWLKGQSTCPTC 1840
Cdd:cd16467     1 ECTICLGEYETGEKlRRLPCSHEFHSECVDRWLKENSSCPIC 42
RING-H2_RNF126 cd16801
RING finger, H2 subclass, found in RING finger protein 126 (RNF126) and similar proteins; ...
1801-1840 8.60e-06

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: 44.59  E-value: 8.60e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 568997450 1801 CEICHEIFK-SKNMRVLKCGHKFHKGCFKQWLKGQSTCPTC 1840
Cdd:cd16801     2 CPVCKEDYTvGENVRQLPCNHLFHNDCIVPWLEQHDTCPVC 42
RING-H2_RNF38 cd16679
RING finger, H2 subclass, found in RING finger protein 38 (RNF38) and similar proteins; RNF38 ...
1801-1840 8.76e-06

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: 45.05  E-value: 8.76e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 568997450 1801 CEICHEIFKSKNM-RVLKCGHKFHKGCFKQWLKGQSTCPTC 1840
Cdd:cd16679    23 CVVCMCDFESRQLlRVLPCNHEFHAKCVDKWLKANRTCPIC 63
RING-HC_ScPSH1-like cd16568
RING finger, HC subclass, found in Saccharomyces cerevisiae POB3/SPT16 histone-associated ...
1801-1840 1.29e-05

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: 44.28  E-value: 1.29e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 568997450 1801 CEICHEIFKSKNMrvLKCGHKFHKGCFKQWLKGQ--STCPTC 1840
Cdd:cd16568     7 CIICHEYLYEPMV--TTCGHTYCYTCLNTWFKSNrsLSCPDC 46
RING-H2_PJA1_2 cd16465
RING finger, H2 subclass, found in protein E3 ubiquitin-protein ligase Praja-1, Praja-2, and ...
1800-1840 1.55e-05

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: 43.60  E-value: 1.55e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 568997450 1800 SCEIC-HEIFKSKNMRVLKCGHKFHKGCFKQWLKGQSTCPTC 1840
Cdd:cd16465     1 CCPICcSEYVKDEIATELPCHHLFHKPCITAWLQKSGTCPVC 42
RING-HC_RNFT1-like cd16532
RING finger, HC subclass, found in RING finger and transmembrane domain-containing protein ...
1799-1840 2.07e-05

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: 43.06  E-value: 2.07e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 568997450 1799 NSCEICHEIFKSKnmRVLKCGHKFHKGCFKQWLKGQSTCPTC 1840
Cdd:cd16532     1 DICPICQDEFKDP--VVLRCKHIFCEDCVSEWFERERTCPLC 40
COG5540 COG5540
RING-finger-containing ubiquitin ligase [Posttranslational modification, protein turnover, ...
1798-1842 2.41e-05

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


Pssm-ID: 227827 [Multi-domain]  Cd Length: 374  Bit Score: 48.84  E-value: 2.41e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 568997450 1798 GNSCEICHEIF-KSKNMRVLKCGHKFHKGCFKQWLKGQS-TCPTCGS 1842
Cdd:COG5540   323 GVECAICMSNFiKNDRLRVLPCDHRFHVGCVDKWLLGYSnKCPVCRT 369
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
367-472 2.43e-05

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 47.69  E-value: 2.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997450  367 GYTALLEQRCRSAAQAFTELLNgLDPqkikqlnlamiNYVLVVYGLAVSLLGIGRPEElseAENQFKRIIEHYPNeglDC 446
Cdd:COG0457    15 GLAYRRLGRYEEAIEDYEKALE-LDP-----------DDAEALYNLGLAYLRLGRYEE---ALADYEQALELDPD---DA 76
                          90       100
                  ....*....|....*....|....*.
gi 568997450  447 LAYCGIGKVYLKKNRFLEALNHFEKA 472
Cdd:COG0457    77 EALNNLGLALQALGRYEEALEDYDKA 102
RING-H2_RNF6 cd16673
RING finger, H2 subclass, found in E3 ubiquitin-protein ligase RNF6 and similar proteins; RNF6 ...
1800-1840 2.60e-05

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: 43.41  E-value: 2.60e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 568997450 1800 SCEIC-HEIFKSKNMRVLKCGHKFHKGCFKQWLKGQSTCPTC 1840
Cdd:cd16673     2 TCSVCiNEYATGNKLRRLPCAHEFHIHCIDRWLSENSTCPIC 43
RING-H2_RNF115 cd16800
RING finger, H2 subclass, found in RING finger protein 115 (RNF115) and similar proteins; ...
1801-1843 2.63e-05

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: 43.40  E-value: 2.63e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 568997450 1801 CEICHEIFK-SKNMRVLKCGHKFHKGCFKQWLKGQSTCPTCGSS 1843
Cdd:cd16800     3 CPVCKEDYTvGEQVRQLPCNHFFHSDCIVPWLELHDTCPVCRKS 46
RING-H2_RNF12 cd16674
RING finger, H2 subclass, found in RING finger protein 12 (RNF12) and similar proteins; RNF12, ...
1800-1847 2.64e-05

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: 43.17  E-value: 2.64e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 568997450 1800 SCEICHEIFKSKN-MRVLKCGHKFHKGCFKQWLKGQSTCPTCGSSDLLS 1847
Cdd:cd16674     2 TCSVCITEYTEGNkLRKLPCSHEYHVHCIDRWLSENSTCPICRRAVLAS 50
RING-H2_AIRP1-like cd23116
RING finger, H2 subclass, found in Arabidopsis thaliana protein ABA INSENSITIVE RING PROTEIN 1 ...
1797-1842 2.72e-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: 43.23  E-value: 2.72e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 568997450 1797 DGNSCEICHEIFKSKNMRVL-KCGHKFHKGCFKQWLKGQSTCPTCGS 1842
Cdd:cd23116     1 DEDVCPTCLEGYTEENPKLLtKCGHHFHLACIYEWMERSERCPVCDK 47
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
347-472 2.77e-05

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 46.11  E-value: 2.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997450  347 RAAHQDFANIMKMLRSLIQDGYTALLEQRCRSAAQAFTELLNgLDPqkikqlnlamiNYVLVVYGLAVSLLGIGRPEEls 426
Cdd:COG5010    41 ELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQALQ-LDP-----------NNPELYYNLALLYSRSGDKDE-- 106
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 568997450  427 eAENQFKRIIEHYPNeglDCLAYCGIGKVYLKKNRFLEALNHFEKA 472
Cdd:COG5010   107 -AKEYYEKALALSPD---NPNAYSNLAALLLSLGQDDEAKAALQRA 148
RING-H2_RNF24 cd16675
RING finger, H2 subclass, found in RING finger protein 24 (RNF24) and similar proteins; RNF24 ...
1801-1840 3.74e-05

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: 43.08  E-value: 3.74e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 568997450 1801 CEICHEIFKSKN-MRVLKCGHKFHKGCFKQWLKGQSTCPTC 1840
Cdd:cd16675     3 CAVCLEEFKPKDeLGICPCKHAFHRKCLIKWLEVRKVCPLC 43
RING-HC_RNF213 cd16561
RING finger, HC subclass, found in RING finger protein 213 (RNF213) and similar proteins; ...
1801-1840 3.92e-05

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: 42.65  E-value: 3.92e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 568997450 1801 CEICHEIFKS--KnmrvLKCGHKFHKGCFKQWLKGQSTCPTC 1840
Cdd:cd16561     5 CSICLEDLNDpvK----LPCDHVFCEECIRQWLPGQMSCPLC 42
RING-H2_RNF167 cd16797
RING finger, H2 subclass, found in RING finger protein 167 (RNF167) and similar proteins; ...
1801-1840 4.06e-05

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: 42.72  E-value: 4.06e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 568997450 1801 CEICHEIFKSKN-MRVLKCGHKFHKGCFKQWL-KGQSTCPTC 1840
Cdd:cd16797     3 CAICLDEYEEGDkLRVLPCSHAYHSKCVDPWLtQTKKTCPVC 44
zf-C3HC4 pfam00097
Zinc finger, C3HC4 type (RING finger); The C3HC4 type zinc-finger (RING finger) is a ...
1801-1840 4.12e-05

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: 42.34  E-value: 4.12e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 568997450  1801 CEICHEIFKsKNMRVLKCGHKFHKGCFKQWLK-GQSTCPTC 1840
Cdd:pfam00097    1 CPICLEEPK-DPVTLLPCGHLFCSKCIRSWLEsGNVTCPLC 40
RING-H2_RNF150 cd16805
RING finger, H2 subclass, found in RING finger protein 150 (RNF150) and similar proteins; ...
1797-1840 4.19e-05

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: 42.73  E-value: 4.19e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 568997450 1797 DGNSCEICHEIFKSKNM-RVLKCGHKFHKGCFKQWLKGQSTCPTC 1840
Cdd:cd16805     5 DFDNCAVCIEGYKPNDVvRILPCRHLFHKSCVDPWLLDHRTCPMC 49
RING-HC_AtBRCA1-like cd23147
RING finger, HC subclass, found in Arabidopsis thaliana protein BREAST CANCER SUSCEPTIBILITY 1 ...
1800-1840 4.63e-05

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


Pssm-ID: 438509 [Multi-domain]  Cd Length: 54  Bit Score: 42.46  E-value: 4.63e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 568997450 1800 SCEICHEIFKSKnmRVLKCGHKFHKGCFKQWLKGQSTCPTC 1840
Cdd:cd23147     6 KCPICLSLFKSA--ANLSCNHCFCAGCIGESLKLSAICPVC 44
RING-CH-C4HC3_LTN1 cd16491
RING-CH finger, H2 subclass (C4HC3-type), found in E3 ubiquitin-protein ligase listerin and ...
1801-1840 4.81e-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: 42.25  E-value: 4.81e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 568997450 1801 CEICHEIFKSKNMRVLK-----CGHKFHKGCFKQWLK--GQSTCPTC 1840
Cdd:cd16491     3 CPICYSVIHGSNHSLPKlkcktCKNKFHSACLYKWFRssNKSTCPLC 49
PTZ00121 PTZ00121
MAEBL; Provisional
1330-1564 4.94e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.60  E-value: 4.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997450 1330 EVNTEPYEPFETQQGDLSQKEKECHLLREQLKVACE---NCEQIELRSSQEIKDLEEkLQRHTEENKISKTELDWFLQDL 1406
Cdd:PTZ00121 1595 EEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEekkKVEQLKKKEAEEKKKAEE-LKKAEEENKIKAAEEAKKAEED 1673
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997450 1407 DR---EIKKWQQEKKEIQE---RLKALKKKIKKVINTSEMPAQKNDGFDKECEPHPDQSlgfssalTDEKTKVEESVRKG 1480
Cdd:PTZ00121 1674 KKkaeEAKKAEEDEKKAAEalkKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKA-------EEAKKEAEEDKKKA 1746
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997450 1481 KELYEESHQRAVAAEVSVLENWKEREVCKLQGVASQSEAYLKSLKLMSSDSATYPDVE---------------YDILSWE 1545
Cdd:PTZ00121 1747 EEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFdnfaniieggkegnlVINDSKE 1826
                         250
                  ....*....|....*....
gi 568997450 1546 SFLSTVREEIESKKSQFEE 1564
Cdd:PTZ00121 1827 MEDSAIKEVADSKNMQLEE 1845
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
367-472 5.06e-05

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 46.92  E-value: 5.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997450  367 GYTALLEQRCRSAAQAFTELLNgLDPqkikqlnlamiNYVLVVYGLAVSLLGIGRPEElseAENQFKRIIEHYPNeglDC 446
Cdd:COG0457    49 GLAYLRLGRYEEALADYEQALE-LDP-----------DDAEALNNLGLALQALGRYEE---ALEDYDKALELDPD---DA 110
                          90       100
                  ....*....|....*....|....*.
gi 568997450  447 LAYCGIGKVYLKKNRFLEALNHFEKA 472
Cdd:COG0457   111 EALYNLGLALLELGRYDEAIEAYERA 136
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
347-472 5.10e-05

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 48.07  E-value: 5.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997450  347 RAAHQDFANIMKMLRSLIQDGYTALLEQRCRSAAQAFTELlnGLDPQKIKQLNLAMI---NYVLVVYGLAVSLLGIGRPE 423
Cdd:COG3914    52 AEAAAAALLALAAGEAAAAAAALLLLAALLELAALLLQAL--GRYEEALALYRRALAlnpDNAEALFNLGNLLLALGRLE 129
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 568997450  424 ElseAENQFKRIIEHYPNeglDCLAYCGIGKVYLKKNRFLEALNHFEKA 472
Cdd:COG3914   130 E---ALAALRRALALNPD---FAEAYLNLGEALRRLGRLEEAIAALRRA 172
HRD1 COG5243
HRD ubiquitin ligase complex, ER membrane component [Posttranslational modification, protein ...
1795-1843 6.18e-05

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


Pssm-ID: 227568 [Multi-domain]  Cd Length: 491  Bit Score: 47.66  E-value: 6.18e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997450 1795 APDGNSCEICHE---------IFKSKNM--RVLKCGHKFHKGCFKQWLKGQSTCPTCGSS 1843
Cdd:COG5243   284 TNSDRTCTICMDemfhpdhepLPRGLDMtpKRLPCGHILHLHCLKNWLERQQTCPICRRP 343
RING-H2_RHA1-like cd23121
RING finger, H2 subclass, found in Arabidopsis thaliana RING-H2 finger A1a (RHA1A), A1b (RHA1B) ...
1799-1840 7.17e-05

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: 42.09  E-value: 7.17e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 568997450 1799 NSCEICHEIFKS--KNMRVLKCGHKFHKGCFKQWLK-GQSTCPTC 1840
Cdd:cd23121     2 DCCAICLSDFNSdeKLRQLPKCGHIFHHHCLDRWIRyNKITCPLC 46
RING-H2_ASR1 cd23120
RING finger, H2 subclass, found in Saccharomyces cerevisiae alcohol-sensitive RING finger ...
1801-1840 7.57e-05

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: 42.14  E-value: 7.57e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 568997450 1801 CEICHEIFKSKNMRVLKCGHKFHKGCFKQWLK--GQSTCPTC 1840
Cdd:cd23120     4 CPICLEEMNSGTGYLADCGHEFHLTCIREWHNksGNLDCPIC 45
RING-H2_ZNRF3 cd16799
RING finger, H2 subclass, found in zinc/RING finger protein 3 (ZNRF3) and similar proteins; ...
1801-1840 8.72e-05

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: 41.55  E-value: 8.72e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 568997450 1801 CEICHEIF-KSKNMRVLKCGHKFHKGCFKQWLKGQSTCPTC 1840
Cdd:cd16799     2 CAICLEKYiDGEELRVIPCTHRFHKKCVDPWLLQHHTCPHC 42
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
116-213 1.22e-04

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 46.91  E-value: 1.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997450  116 KFEIAVIYYTRAIEYRPENHLLYGNRALCFLRMGQFRNALSDGKRAIVLKNTWPKGHYRYCDALCMLGEYDWAlQANIKA 195
Cdd:COG3914   161 RLEEAIAALRRALELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALELDPDNADAHSNLLFALRQACDWEVY-DRFEEL 239
                          90
                  ....*....|....*...
gi 568997450  196 QKLCKNDPEGIKDLIQQH 213
Cdd:COG3914   240 LAALARGPSELSPFALLY 257
RING-HC_DTX3-like cd16506
RING finger, HC subclass, found in E3 ubiquitin-protein ligase Deltex3 (DTX3), Deltex-3-like ...
1801-1841 1.44e-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: 40.81  E-value: 1.44e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 568997450 1801 CEICHEIFKskNMRVL-KCGHKFHKGCFKQWLKGQSTCPTCG 1841
Cdd:cd16506     3 CPICLDEIQ--NKKTLeKCKHSFCEDCIDRALQVKPVCPVCG 42
mRING-H2-C3H3C2_Mio-like cd16488
Modified RING finger, H2 subclass (C3H3C2-type), found in WD repeat-containing protein mio and ...
1800-1841 1.53e-04

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: 40.77  E-value: 1.53e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 568997450 1800 SCEICHEIFKSKNMRVLKCGHKFHKGCFKQWLKGQSTCPT-CG 1841
Cdd:cd16488     1 SCAICHLPVKGLSSFCLNCGHGGHAECIREWFEDHTECPTgCG 43
RING-HC_EHV1-like cd23130
RING finger, HC subclass, found in Equid alphaherpesvirus 1 (Equine herpesvirus 1/EHV-1) ...
1799-1840 1.70e-04

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: 40.80  E-value: 1.70e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 568997450 1799 NSCEICHEIFKSKNMrVLKCGHKFHKGCFKQWLKGQSTCPTC 1840
Cdd:cd23130     1 DVCPICLDDPEDEAI-TLPCLHQFCYTCILRWLQTSPTCPLC 41
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
379-472 1.72e-04

Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 42.08  E-value: 1.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997450  379 AAQAFTELLNgLDPqkikqlnlamiNYVLVVYGLAVSLLGIGRPEElseAEnQFKRIIEHYPNeglDCLAYCGIGKVYLK 458
Cdd:COG3063    11 AEEYYEKALE-LDP-----------DNADALNNLGLLLLEQGRYDE---AI-ALEKALKLDPN---NAEALLNLAELLLE 71
                          90
                  ....*....|....
gi 568997450  459 KNRFLEALNHFEKA 472
Cdd:COG3063    72 LGDYDEALAYLERA 85
RING-H2_TUL1-like cd23117
RING finger, H2 subclass, found in Saccharomyces cerevisiae transmembrane E3 ubiquitin-protein ...
1797-1840 2.35e-04

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: 40.84  E-value: 2.35e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568997450 1797 DGNSCEIC-------HEIFKSKNMRVLKCGHKFHKGCFKQWLKGQSTCPTC 1840
Cdd:cd23117     3 GSVDCVICmsdielpSTNSVRRDYMVTPCNHIFHTNCLERWMDIKLECPTC 53
RING-CH-C4HC3_NSE1 cd16493
RING-CH finger, H2 subclass (C4HC3-type), found in non-structural maintenance of chromosomes ...
1800-1843 2.90e-04

RING-CH finger, H2 subclass (C4HC3-type), found in non-structural maintenance of chromosomes (SMC) element 1 homolog (NSE1) and similar proteins; NSE1, also known as non-SMC element 1 homolog (NSMCE1), is an E3 ubiquitin ligase that contains a C4HC3-type RING-CH finger, also known as vRING or RINGv, a variant of C3H2C3-type RING-H2 finger. Together with its partner proteins NSE3 and NSE4, it forms a tight subcomplex of the SMC5-6 complex, which includes another two subcomplexes, SMC6-SMC5-NSE2 and NSE5-NSE6. The vRING finger is essential for normal NSE1-NSE3-NSE4 trimer formation in vitro and for damage-induced recruitment of NSE4 and SMC5 to subnuclear foci in vivo. Thus it functions as a protein-protein interaction domain required for SMC5-6 holocomplex integrity and recruitment to, or retention at, DNA lesions. The C-terminal half of NSE1, including the vRING finger, is required for DNA damage resistance and mitotic fidelity of SMC5-6 complex in the fission yeast Schizosaccharomyces pombe. The RING-CH finger may play an important role in Rad52-dependent post-replication repair of UV-damaged DNA in Saccharomyces cerevisiae.


Pssm-ID: 438156  Cd Length: 49  Bit Score: 40.12  E-value: 2.90e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 568997450 1800 SCEICHEI-FKSKNMRVLKCGHKFHKGCFKQWLKGQS--TCPTCGSS 1843
Cdd:cd16493     2 SCNICHEIvIQGQSCPNEDCGIRLHLYCAKRYFRRRAepRCPSCNTP 48
RING-H2_RNF165 cd16682
RING finger, H2 subclass, found in RING finger protein 165 (RNF165) and similar proteins; ...
1801-1840 3.18e-04

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: 40.45  E-value: 3.18e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 568997450 1801 CEICHEIFKS-KNMRVLKCGHKFHKGCFKQWLKGQSTCPTC 1840
Cdd:cd16682    10 CTICLSMLEDgEDVRRLPCMHLFHQLCVDQWLAMSKKCPIC 50
RING-HC_CHFR cd16503
RING finger, HC subclass, found in checkpoint with forkhead and RING finger domains protein ...
1801-1840 3.24e-04

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


Pssm-ID: 438166 [Multi-domain]  Cd Length: 55  Bit Score: 40.43  E-value: 3.24e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 568997450 1801 CEICHEIFkSKNMRVLKCGHKFHKGCFKQWL-KGQSTCPTC 1840
Cdd:cd16503     5 CSICQDLL-HDCVSLQPCMHNFCAACYSDWMeRSNTECPTC 44
RING-H2_RNF111 cd16681
RING finger, H2 subclass, found in RING finger protein 111 (RNF111) and similar proteins; ...
1801-1840 3.92e-04

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: 40.43  E-value: 3.92e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 568997450 1801 CEICHEIFKS-KNMRVLKCGHKFHKGCFKQWLKGQSTCPTC 1840
Cdd:cd16681    13 CTICLSILEEgEDVRRLPCMHLFHQVCVDQWLITNKKCPIC 53
RING-HC_RNF4 cd16533
RING finger, HC subclass, found in RING finger protein 4 (RNF4) and similar proteins; RNF4, ...
1800-1840 4.29e-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: 39.88  E-value: 4.29e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 568997450 1800 SCEIC----HEIFKSKNMRV-LKCGHKFHKGCFKQWLKGQSTCPTC 1840
Cdd:cd16533     5 SCPICmdgySEIVQSGRLIVsTECGHVFCSQCLRDSLKNANTCPTC 50
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
410-481 4.37e-04

Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane constriction [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 441335 [Multi-domain]  Cd Length: 113  Bit Score: 41.52  E-value: 4.37e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568997450  410 YGLAVSLLGIGRPEElseAENQFKRIIEHYPNEGLDCLAYCGIGKVYLKKNRFLEALNHFEKaktLISRLPG 481
Cdd:COG1729    34 YWLGEAYYALGDYDE---AAEAFEKLLKRYPDSPKAPDALLKLGLSYLELGDYDKARATLEE---LIKKYPD 99
RING-HC_COP1 cd16504
RING finger, HC subclass, found in constitutive photomorphogenesis protein 1 (COP1) and ...
1800-1842 4.85e-04

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


Pssm-ID: 438167 [Multi-domain]  Cd Length: 47  Bit Score: 39.53  E-value: 4.85e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 568997450 1800 SCEICHEIFKSKNMRvlKCGHKFHKGCFKQWLKGQSTCPTCGS 1842
Cdd:cd16504     4 LCPICFDIIKEAFVT--KCGHSFCYKCIVKHLEQKNRCPKCNF 44
zf-RING_UBOX pfam13445
RING-type zinc-finger; This zinc-finger is a typical RING-type of plant ubiquitin ligases.
1801-1838 5.58e-04

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: 38.92  E-value: 5.58e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 568997450  1801 CEICHEIFkskNMRVLKCGHKFHKGC---FKQWLKGQSTCP 1838
Cdd:pfam13445    1 CPICLELF---TDPVLPCGHTFCRECleeMSQKKGGKFKCP 38
RING-H2_RNF32 cd16471
RING finger, H2 subclass, found in RING finger protein 32 (RNF32) and similar proteins; RNF32 ...
1801-1840 1.02e-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: 38.77  E-value: 1.02e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 568997450 1801 CEICHEIFKSKNMRVLKCGHKFHKGC---FKQWLKGQS-TCPTC 1840
Cdd:cd16471     2 CPICLCAFKGRKCTLLSCSHVFHEAClsaFEKFIESKNqKCPLC 45
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
368-472 1.12e-03

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 43.83  E-value: 1.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997450  368 YTALLEQRCRSAAQAFTELLNGLDPQKIKQLNLAMINYVLVVYGLAVSLLGIGRPEElseAENQFKRIIEHYPNeglDCL 447
Cdd:COG3914    40 ALGLALLLLAALAEAAAAALLALAAGEAAAAAAALLLLAALLELAALLLQALGRYEE---ALALYRRALALNPD---NAE 113
                          90       100
                  ....*....|....*....|....*
gi 568997450  448 AYCGIGKVYLKKNRFLEALNHFEKA 472
Cdd:COG3914   114 ALFNLGNLLLALGRLEEALAALRRA 138
RING-HC_MmTRIM43-like cd23133
RING finger, HC subclass, found in Mus musculus tripartite motif-containing protein 43 (TRIM43) ...
1800-1840 1.13e-03

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


Pssm-ID: 438495 [Multi-domain]  Cd Length: 57  Bit Score: 38.74  E-value: 1.13e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 568997450 1800 SCEICHEIFKskNMRVLKCGHKFHKGC---FKQWLKGQSTCPTC 1840
Cdd:cd23133     5 TCSICQGIFM--NPVYLRCGHKFCEAClllFQEDIKFPAYCPMC 46
RING_Ubox cd00162
RING finger (Really Interesting New Gene) domain and U-box domain superfamily; The RING finger ...
1801-1840 1.34e-03

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: 38.21  E-value: 1.34e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 568997450 1801 CEICHEIFKSKNMRVLK-CGHKFHKGCFKQWLKGQS-TCPTC 1840
Cdd:cd00162     1 CPICREEMNDRRPVVLLsCGHTFSRSAIARWLEGSKqKCPFC 42
RING-HC_TRIM13_like_C-V cd16581
RING finger, HC subclass, found in tripartite motif-containing proteins TRIM13, TRIM59 and ...
1800-1840 1.36e-03

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


Pssm-ID: 438243 [Multi-domain]  Cd Length: 50  Bit Score: 38.26  E-value: 1.36e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 568997450 1800 SCEICHEIFKSKnmRVLKCGHKFHKGCFK-------QWLKGQSTCPTC 1840
Cdd:cd16581     4 TCSICYNIFDDP--KILPCSHTFCKNCLEkllaasgYYLLASLKCPTC 49
RING-H2_BRAP2 cd16457
RING finger, H2 subclass, found in BRCA1-associated protein (BRAP2) and similar proteins; ...
1818-1840 1.37e-03

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: 38.04  E-value: 1.37e-03
                          10        20
                  ....*....|....*....|...
gi 568997450 1818 CGHKFHKGCFKQWlkGQSTCPTC 1840
Cdd:cd16457    22 CNHSFHCSCLSKW--GDSSCPVC 42
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
144-218 1.45e-03

Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 39.77  E-value: 1.45e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568997450  144 CFLRMGQFRNALSDGKRAIVLKNTWPKGHYRYCDALCMLGEYDWALQANiKAQKLCKNDPEGIKDLIQQHVKLQK 218
Cdd:COG3063     1 LYLKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIALE-KALKLDPNNAEALLNLAELLLELGD 74
RING-HC_BAR cd16497
RING finger, HC subclass, found in bifunctional apoptosis regulator (BAR); BAR, also known as ...
1800-1840 1.49e-03

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


Pssm-ID: 438160 [Multi-domain]  Cd Length: 52  Bit Score: 38.26  E-value: 1.49e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 568997450 1800 SCEICHEIFKskNMRVLKCGHKFHKGCFKQWLKG--QSTCPTC 1840
Cdd:cd16497     3 LCHCCYDLLV--NPTTLNCGHSFCRHCLALWWKSskKTECPEC 43
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
112-164 1.51e-03

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 41.10  E-value: 1.51e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568997450  112 FSKEKFEIAVIYYTRAIEYRPENHLLYGNRALCFLRMGQFRNALSDGKRAIVL 164
Cdd:COG5010    99 SRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQRALGT 151
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
107-224 1.59e-03

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 42.30  E-value: 1.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997450  107 RGNEEFSKEKFEIAVIYYTRAIEYRPENHLLYGNRALCFLRMGQFRNALSDGKRAIVLKNTWPKGHYRYCDALCMLGEYD 186
Cdd:COG0457   116 LGLALLELGRYDEAIEAYERALELDPDDADALYNLGIALEKLGRYEEALELLEKLEAAALAALLAAALGEAALALAAAEV 195
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 568997450  187 WALQANIKAQKLCKNDPEGIKDLIQQHVKLQKQIEDLQ 224
Cdd:COG0457   196 LLALLLALEQALRKKLAILTLAALAELLLLALALLLAL 233
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
108-224 1.68e-03

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 42.41  E-value: 1.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997450  108 GNEEFSKEKFEIAVIYYTRAIEYRPENHLLYGNRALCFLRMGQFRNALSDGKRAIVLKNTWPKGHYRYCDALCMLGEYDW 187
Cdd:COG2956   151 AELYLEQGDYDEAIEALEKALKLDPDCARALLLLAELYLEQGDYEEAIAALERALEQDPDYLPALPRLAELYEKLGDPEE 230
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 568997450  188 ALQANIKAQKLCKNDPEGIK--DLIQQHVKLQKQIEDLQ 224
Cdd:COG2956   231 ALELLRKALELDPSDDLLLAlaDLLERKEGLEAALALLE 269
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
136-221 1.96e-03

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 40.71  E-value: 1.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997450  136 LLYGNRALCFLRMGQFRNALSDGKRAIVLKNTWPKGHYRYCDALCMLGEYDWALQANIKAQKLCKNDPEGIKDLIQQHVK 215
Cdd:COG5010    55 AIESPSDNLYNKLGDFEESLALLEQALQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLS 134

                  ....*.
gi 568997450  216 LQKQIE 221
Cdd:COG5010   135 LGQDDE 140
RING-H2_RNF13-like cd16665
RING finger, H2 subclass, found in RING finger protein 13 (RNF13), RING finger protein 167 ...
1801-1840 2.03e-03

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: 37.80  E-value: 2.03e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 568997450 1801 CEICHEIFKSKN-MRVLKCGHKFHKGCFKQWL-KGQSTCPTC 1840
Cdd:cd16665     3 CAICLDDYEEGDkLRILPCSHAYHCKCIDPWLtKNKRTCPVC 44
RING-HC_RAD18 cd16529
RING finger, HC subclass, found in postreplication repair protein RAD18 and similar proteins; ...
1801-1840 2.06e-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: 38.05  E-value: 2.06e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 568997450 1801 CEICHEIFKSKNMrVLKCGHKFHKGCFKQWLKGQSTCPTC 1840
Cdd:cd16529     7 CPICFEYFNTAMM-ITQCSHNYCSLCIRRFLSYKTQCPTC 45
RING-HC_TRIM69_C-IV cd16611
RING finger, HC subclass, found in tripartite motif-containing protein 69 (TRIM69) and similar ...
1800-1840 2.22e-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: 38.20  E-value: 2.22e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 568997450 1800 SCEICHEIFKSKNMrvLKCGHKFHKGCFKQWLKGQ---STCPTC 1840
Cdd:cd16611     6 HCPLCLDFFRDPVM--LSCGHNFCQSCITGFWELQaedTTCPEC 47
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
347-483 2.22e-03

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 40.71  E-value: 2.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997450  347 RAAHQDFANIMKMLRSLIQDGYTALLEQRCRSAAQAFTELLNGLDPQKIKQLNLAMINYVLVvyglavsLLGIGRPEEls 426
Cdd:COG5010     2 RALEGFDRLPLYLLLLTKLRTLVEKYEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNL-------YNKLGDFEE-- 72
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568997450  427 eAENQFKRIIEHYPNEGLdclAYCGIGKVYLKKNRFLEALNHFEKAKTLISRLPGIL 483
Cdd:COG5010    73 -SLALLEQALQLDPNNPE---LYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAY 125
RING-HC_DTX3 cd16711
RING finger, HC subclass, found in E3 ubiquitin-protein ligase Deltex3 (DTX3) and similar ...
1801-1841 2.22e-03

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


Pssm-ID: 438371 [Multi-domain]  Cd Length: 54  Bit Score: 37.78  E-value: 2.22e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 568997450 1801 CEICHEIFKskNMRVL-KCGHKFHKGCFKQWLKGQSTCPTCG 1841
Cdd:cd16711     4 CPICLGEIQ--NKKTLdKCKHSFCEDCITRALQVKKACPMCG 43
RING-HC_ORTHRUS_rpt1 cd23138
first RING finger, HC subclass, found in Arabidopsis thaliana ORTHRUS and similar proteins; ...
1818-1842 3.19e-03

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: 3.19e-03
                          10        20
                  ....*....|....*....|....*.
gi 568997450 1818 CGHKFHKGCFKQWL-KGQSTCPTCGS 1842
Cdd:cd23138    20 CGHNFCLKCFQKWMgQGKKTCGTCRS 45
RING-HC_TRIM50_like_C-IV cd16605
RING finger, HC subclass, found in tripartite motif-containing protein TRIM50, TRIM73, TRIM74 ...
1801-1840 3.53e-03

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


Pssm-ID: 438267 [Multi-domain]  Cd Length: 45  Bit Score: 37.04  E-value: 3.53e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 568997450 1801 CEICHEIFKSKNMrvLKCGHKFHKGCFKQW---LKGQSTCPTC 1840
Cdd:cd16605     3 CPICLEVFKEPLM--LQCGHSYCKSCLVSLsgeLDGQLLCPVC 43
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
427-472 3.75e-03

Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane constriction [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 441335 [Multi-domain]  Cd Length: 113  Bit Score: 38.82  E-value: 3.75e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 568997450  427 EAENQFKRIIEHYPNEGLDCLAYCGIGKVYLKKNRFLEALNHFEKA 472
Cdd:COG1729    11 EAIAAFKAFLKRYPNSPLAPDALYWLGEAYYALGDYDEAAEAFEKL 56
RING-HC_RNF8 cd16535
RING finger, HC subclass, found in RING finger protein 8 (RNF8) and similar proteins; RNF8 is ...
1801-1840 3.81e-03

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: 37.37  E-value: 3.81e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 568997450 1801 CEICHEIFKSKNmrVLKCGHKFHKGCFKQWLKGQSTCPTC 1840
Cdd:cd16535     4 CSICSELFIEAV--TLNCSHSFCSYCITEWMKRKKECPIC 41
RING-H2_RNF13 cd16796
RING finger, H2 subclass, found in RING finger protein 13 (RNF13) and similar proteins; RNF13 ...
1801-1840 4.76e-03

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: 37.33  E-value: 4.76e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 568997450 1801 CEIC-HEIFKSKNMRVLKCGHKFHKGCFKQWL-KGQSTCPTC 1840
Cdd:cd16796    11 CAIClDEYEEGDKLRILPCSHAYHCKCVDPWLtKTKKTCPVC 52
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
367-473 5.20e-03

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 40.76  E-value: 5.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997450  367 GYTALLEQRCRSAAQAFTELLNgLDPqkikqlnlamiNYVLVVYGLAVSLLGIGRPEElseAENQFKRIIEHYPNeglDC 446
Cdd:COG0457    83 GLALQALGRYEEALEDYDKALE-LDP-----------DDAEALYNLGLALLELGRYDE---AIEAYERALELDPD---DA 144
                          90       100
                  ....*....|....*....|....*..
gi 568997450  447 LAYCGIGKVYLKKNRFLEALNHFEKAK 473
Cdd:COG0457   145 DALYNLGIALEKLGRYEEALELLEKLE 171
mRING-HC-C3HC3D_Nrdp1 cd16634
Modified RING finger, HC subclass (C3HC3D-type), found in neuregulin receptor degradation ...
1801-1838 5.23e-03

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: 36.63  E-value: 5.23e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 568997450 1801 CEICHEIFKSKnMRVLKCGHKFHKGCFKQWLKGQSTCP 1838
Cdd:cd16634     4 CPICSGVLEEP-LQAPHCEHAFCNACITEWLSRQQTCP 40
rad18 TIGR00599
DNA repair protein rad18; All proteins in this family for which functions are known are ...
1801-1844 5.30e-03

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


Pssm-ID: 273165 [Multi-domain]  Cd Length: 397  Bit Score: 41.14  E-value: 5.30e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 568997450  1801 CEICHEIFKSKnmRVLKCGHKFHKGCFKQWLKGQSTCPTCGSSD 1844
Cdd:TIGR00599   29 CHICKDFFDVP--VLTSCSHTFCSLCIRRCLSNQPKCPLCRAED 70
zf-RING-like pfam08746
RING-like domain; This is a zinc finger domain that is related to the C3HC4 RING finger domain ...
1801-1840 6.11e-03

RING-like domain; This is a zinc finger domain that is related to the C3HC4 RING finger domain (pfam00097).


Pssm-ID: 430187  Cd Length: 43  Bit Score: 36.19  E-value: 6.11e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 568997450  1801 CEICHEI-FKSKNMRVLKCGHKFHKGCFKQWLKGQS--TCPTC 1840
Cdd:pfam08746    1 CEACKEIvTQGQRCPNEDCNVRLHDDCLRKYFRTRRspKCPKC 43
mRING-H2-C3H3C2_WDR59 cd16692
Modified RING finger, H2 subclass (C3H3C2-type), found in WD repeat-containing protein 59 ...
1801-1841 6.33e-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: 6.33e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 568997450 1801 CEICHEIFKSKNMRVLKCGHKFHKGCFKQWLKGQSTCPT-CG 1841
Cdd:cd16692     3 CAICHVAVRGSSNFCLACGHGGHTSHMMEWFRTQDVCPTgCG 44
RING-HC_Topors cd16574
RING finger, HC subclass, found in topoisomerase I-binding arginine/serine-rich protein ...
1798-1840 6.35e-03

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: 36.49  E-value: 6.35e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 568997450 1798 GNSCEICHEIFKSKNMRVLKCGHKFHKGCFKQWLKGQSTCPTC 1840
Cdd:cd16574     1 DSSCPICLDRFENEKAFLDGCFHAFCFTCILEWSKVKNECPLC 43
mRING-CH-C4HC2H_ZNRF cd16489
Modified RING-CH finger, H2 subclass (C4HC2H-type), found in the ZNRF family; The ZNRF family ...
1801-1838 6.72e-03

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: 36.13  E-value: 6.72e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 568997450 1801 CEICHEIF-KSKNMRVLKCGHKFHKGCFKQWLKGQSTCP 1838
Cdd:cd16489     2 CVICLEELeAGDTIARLPCLCIYHKKCIDDWFEVNRSCP 40
RING-H2_RNF121-like cd16475
RING finger, H2 subclass, found in RING finger proteins RNF121, RNF175 and similar proteins; ...
1799-1840 7.87e-03

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: 36.50  E-value: 7.87e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568997450 1799 NSCEICHEIFK--------SKNMRVLKCGHKFHKGCFKQWL---KGQsTCPTC 1840
Cdd:cd16475     1 NVCAVCGQKLDvddneegiIEKTYKLSCNHVFHEFCIRGWCivgKKQ-TCPYC 52
TPR_1 pfam00515
Tetratricopeptide repeat;
448-475 8.70e-03

Tetratricopeptide repeat;


Pssm-ID: 459840 [Multi-domain]  Cd Length: 34  Bit Score: 35.47  E-value: 8.70e-03
                           10        20
                   ....*....|....*....|....*...
gi 568997450   448 AYCGIGKVYLKKNRFLEALNHFEKAKTL 475
Cdd:pfam00515    3 ALYNLGNAYFKLGKYDEALEYYEKALEL 30
RING-HC_RAD16-like cd16567
RING finger, HC subclass, found in Saccharomyces cerevisiae DNA repair protein RAD16, ...
1800-1840 9.28e-03

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


Pssm-ID: 438229 [Multi-domain]  Cd Length: 48  Bit Score: 35.78  E-value: 9.28e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 568997450 1800 SCEICHEIfkSKNMRVLKCGHKFHKGCFKQWLK----GQSTCPTC 1840
Cdd:cd16567     2 VCGICHEE--AEDPVVARCHHVFCRACVKEYIEsapgGKVTCPTC 44
RING-H2_NIPL1-like cd23119
RING finger, H2 subclass, found in Arabidopsis thaliana NEP1-interacting protein-like 1 (NIPL1) ...
1800-1840 9.74e-03

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: 35.94  E-value: 9.74e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 568997450 1800 SCEICHEIFKSKNM-RVL-KCGHKFHKGCFKQWLKGQSTCPTC 1840
Cdd:cd23119     1 CCTICLQDLQVGEIaRSLpHCHHTFHLGCVDKWLGRHGSCPVC 43
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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