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Conserved domains on  [gi|164661227|ref|XP_001731736.1|]
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hypothetical protein MGL_1004 [Malassezia globosa CBS 7966]

Protein Classification

RING-HC and HELICc domain-containing protein (domain architecture ID 11852592)

protein containing domains SNF2_N, RING-HC, and HELICc

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SNF2_N super family cl26465
SNF2 family N-terminal domain; This domain is found in proteins involved in a variety of ...
316-621 4.11e-37

SNF2 family N-terminal domain; This domain is found in proteins involved in a variety of processes including transcription regulation (e.g., SNF2, STH1, brahma, MOT1), DNA repair (e.g., ERCC6, RAD16, RAD5), DNA recombination (e.g., RAD54), and chromatin unwinding (e.g., ISWI) as well as a variety of other proteins with little functional information (e.g., lodestar, ETL1).


The actual alignment was detected with superfamily member pfam00176:

Pssm-ID: 331286  Cd Length: 305  Bit Score: 145.23  E-value: 4.11e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164661227   316 RGAILAEEMGLGKTIEVLALILEQADpHRHEKHEAywdvqnevcvqpiGTTLIVSPETLRRQWLDEVATYAPSLRLYSYT 395
Cdd:pfam00176   17 RGGILADEMGLGKTLQTISLLLTLKY-LYHIKKLP-------------GPTLIVVPLSLLDNWMNEFERWVPSLRLVVLV 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164661227   396 GHKQASEHRGRTETWGQWASQYDVMVVSFEVLARDLAAshaapvralrhpsryerpRSPLVQLEFLRVVMDEVQLVGGNA 475
Cdd:pfam00176   83 GDGGSRMDKMNVRLLPKVLADYDVVITTYETLRRDKKN------------------RSLLKKLKWHRVILDEGHRLKNSK 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164661227   476 AKTIGMIRRQRS---LAVSGTPVRR-LADLRTSLWFLGlvPPSMTTPRAWKRILS------------AELApyvcELLAN 539
Cdd:pfam00176  145 SKLSEALSKLRTrnrWILTGTPIQNnLEELWALLNFLR--PGPFGSLQTFDKWFVrpiergggekgvARLH----KLLKP 218
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164661227   540 VGIRHTKAQVAHEmvLPPQTRFLVPVDFTHVETAFYRDVWQASL------------AALNLDADGAPMsdtwvlDTGILR 607
Cdd:pfam00176  219 FLLRRTKKDVEKS--LPPKVEEILFCRLSKGQRKLYQTALQALRgngilkllirnrAATKFSSKSFRG------KPGLLN 290
                          330
                   ....*....|....
gi 164661227   608 SqLLRLRQACTHPQ 621
Cdd:pfam00176  291 I-LLRLRKICNHPD 303
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination and ...
1345-1516 7.97e-24

Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination and repair];


:

Pssm-ID: 223627  Cd Length: 866  Bit Score: 109.05  E-value: 7.97e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164661227 1345 TSSNTFQVLPAEMRQALDNMALEGGSGSKLDLLIRHLVHIQCTTG--EKSLVFSSFARGLDLVASNLERHGLAYARVDG- 1421
Cdd:COG0553   665 TFDRIVLLLREDKDFDYLKKPLIQLSKGKLQALDELLLDKLLEEGhyHKVLIFSQFTPVLDLLEDYLKALGIKYVRLDGs 744
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164661227 1422 TGGKRSSAAVHAFQHKPDVRVLLLHSEAQSAGLNLLAATHMFLLEPLLNHAMELQAIGRVHRIGQTRPTYVYGYMVRDTV 1501
Cdd:COG0553   745 TPAKRRQELIDRFNADEEEKVFLLSLKAGGLGLNLTGADTVILFDPWWNPAVELQAIDRAHRIGQKRPVKVYRLITRGTI 824
                         170
                  ....*....|....*
gi 164661227 1502 EERIVALaAERKQSL 1516
Cdd:COG0553   825 EEKILEL-QEKKQEL 838
RING-HC cd16449
HC subclass of RING (RING-HC) finger and its variants; RING finger is a specialized type of ...
1276-1315 2.19e-08

HC subclass of RING (RING-HC) finger and its variants; 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 HC subclass of RING (RING-HC) finger proteins 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 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 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: 319363  Cd Length: 39  Bit Score: 53.63  E-value: 2.19e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 164661227 1276 CFICTNLIETGILTNaCGHLCCEACFHAWLSHGHRTCPMC 1315
Cdd:cd16449     1 CPICLELLKDPVLLP-CGHTFCRSCLRRLLKEGKKKCPIC 39
 
Name Accession Description Interval E-value
SNF2_N pfam00176
SNF2 family N-terminal domain; This domain is found in proteins involved in a variety of ...
316-621 4.11e-37

SNF2 family N-terminal domain; This domain is found in proteins involved in a variety of processes including transcription regulation (e.g., SNF2, STH1, brahma, MOT1), DNA repair (e.g., ERCC6, RAD16, RAD5), DNA recombination (e.g., RAD54), and chromatin unwinding (e.g., ISWI) as well as a variety of other proteins with little functional information (e.g., lodestar, ETL1).


Pssm-ID: 306645  Cd Length: 305  Bit Score: 145.23  E-value: 4.11e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164661227   316 RGAILAEEMGLGKTIEVLALILEQADpHRHEKHEAywdvqnevcvqpiGTTLIVSPETLRRQWLDEVATYAPSLRLYSYT 395
Cdd:pfam00176   17 RGGILADEMGLGKTLQTISLLLTLKY-LYHIKKLP-------------GPTLIVVPLSLLDNWMNEFERWVPSLRLVVLV 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164661227   396 GHKQASEHRGRTETWGQWASQYDVMVVSFEVLARDLAAshaapvralrhpsryerpRSPLVQLEFLRVVMDEVQLVGGNA 475
Cdd:pfam00176   83 GDGGSRMDKMNVRLLPKVLADYDVVITTYETLRRDKKN------------------RSLLKKLKWHRVILDEGHRLKNSK 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164661227   476 AKTIGMIRRQRS---LAVSGTPVRR-LADLRTSLWFLGlvPPSMTTPRAWKRILS------------AELApyvcELLAN 539
Cdd:pfam00176  145 SKLSEALSKLRTrnrWILTGTPIQNnLEELWALLNFLR--PGPFGSLQTFDKWFVrpiergggekgvARLH----KLLKP 218
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164661227   540 VGIRHTKAQVAHEmvLPPQTRFLVPVDFTHVETAFYRDVWQASL------------AALNLDADGAPMsdtwvlDTGILR 607
Cdd:pfam00176  219 FLLRRTKKDVEKS--LPPKVEEILFCRLSKGQRKLYQTALQALRgngilkllirnrAATKFSSKSFRG------KPGLLN 290
                          330
                   ....*....|....
gi 164661227   608 SqLLRLRQACTHPQ 621
Cdd:pfam00176  291 I-LLRLRKICNHPD 303
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination and ...
1345-1516 7.97e-24

Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination and repair];


Pssm-ID: 223627  Cd Length: 866  Bit Score: 109.05  E-value: 7.97e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164661227 1345 TSSNTFQVLPAEMRQALDNMALEGGSGSKLDLLIRHLVHIQCTTG--EKSLVFSSFARGLDLVASNLERHGLAYARVDG- 1421
Cdd:COG0553   665 TFDRIVLLLREDKDFDYLKKPLIQLSKGKLQALDELLLDKLLEEGhyHKVLIFSQFTPVLDLLEDYLKALGIKYVRLDGs 744
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164661227 1422 TGGKRSSAAVHAFQHKPDVRVLLLHSEAQSAGLNLLAATHMFLLEPLLNHAMELQAIGRVHRIGQTRPTYVYGYMVRDTV 1501
Cdd:COG0553   745 TPAKRRQELIDRFNADEEEKVFLLSLKAGGLGLNLTGADTVILFDPWWNPAVELQAIDRAHRIGQKRPVKVYRLITRGTI 824
                         170
                  ....*....|....*
gi 164661227 1502 EERIVALaAERKQSL 1516
Cdd:COG0553   825 EEKILEL-QEKKQEL 838
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination and ...
317-627 2.55e-18

Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination and repair];


Pssm-ID: 223627  Cd Length: 866  Bit Score: 91.33  E-value: 2.55e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164661227  317 GAILAEEMGLGKTIEVLALIleqadPHRHEKHEaywdvqnevcvQPIGTTLIVSPETLRRQWLDEVATYAPSLRLYsYTG 396
Cdd:COG0553   360 GGILADDMGLGKTVQTIALL-----LSLLESIK-----------VYLGPALIVVPASLLSNWKREFEKFAPDLRLV-LVY 422
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164661227  397 HKQASEHRGRTETWGQWASQ-----YDVMVVSFEVLARDLAashaapvralrhpsryerPRSPLVQLEFLRVVMDEVQLV 471
Cdd:COG0553   423 HGEKSELDKKREALRDLLKLhlviiFDVVITTYELLRRFLV------------------DHGGLKKIEWDRVVLDEAHRI 484
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164661227  472 G---GNAAKTIGMIRRQRSLAVSGTPV-RRLADLRTSLWF---LGLVPPSMTTPRAW-KRILSAE--------LAPYVCE 535
Cdd:COG0553   485 KndqSSEGKALQFLKALNRLDLTGTPLeNRLGELWSLLQEflnPGLLGTSFAIFTRLfEKPIQAEedigpleaRELGIEL 564
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164661227  536 LLANVG---IRHTKAQVAHEMVLPPQTRFLVPVDFTHVETAFYRDVWQASLAALNLDADGAPMSDTWVLDTGILRSQL-- 610
Cdd:COG0553   565 LRKLLSpfiLRRTKEDVEVLKELPPKIEKVLECELSEEQRELYEALLEGAEKNQQLLEDLEKADSDENRIGDSELNILal 644
                         330
                  ....*....|....*...
gi 164661227  611 -LRLRQACTHPQVAMRGG 627
Cdd:COG0553   645 lTRLRQICNHPALVDEGL 662
HELICc cd00079
Helicase superfamily c-terminal domain; associated with DEXDc-, DEAD-, and DEAH-box proteins, ...
1370-1493 1.37e-12

Helicase superfamily c-terminal domain; associated with DEXDc-, DEAD-, and DEAH-box proteins, yeast initiation factor 4A, Ski2p, and Hepatitis C virus NS3 helicases; this domain is found in a wide variety of helicases and helicase related proteins; may not be an autonomously folding unit, but an integral part of the helicase; 4 helicase superfamilies at present according to the organization of their signature motifs; all helicases share the ability to unwind nucleic acid duplexes with a distinct directional polarity; they utilize the free energy from nucleoside triphosphate hydrolysis to fuel their translocation along DNA, unwinding the duplex in the process


Pssm-ID: 238034  Cd Length: 131  Bit Score: 68.03  E-value: 1.37e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164661227 1370 SGSKLDLLIRhLVHIQCTTGEKSLVFSSFARGLDLVASNLERHGL--AYARVDGTGGKRSSAaVHAFQHKPdvRVLLLHS 1447
Cdd:cd00079    10 EDEKLEALLE-LLKEHLKKGGKVLIFCPSKKMLDELAELLRKPGIkvAALHGDGSQEEREEV-LKDFREGE--IVVLVAT 85
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 164661227 1448 EAQSAGLNLLAATHMFLLEPLLNHAMELQAIGRVHRIGQTRPTYVY 1493
Cdd:cd00079    86 DVIARGIDLPNVSVVINYDLPWSPSSYLQRIGRAGRAGQKGTAILL 131
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
1389-1509 5.86e-12

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601  Cd Length: 1033  Bit Score: 70.60  E-value: 5.86e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164661227 1389 GEKSLVFSSFARGLDLVASNLERHGLAYARVDG-TGGKRSSAAVHAFqHKPDVR--VLLLHSEAQSAGLNLLAATHMFLL 1465
Cdd:PLN03142  487 DSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGnTGGEDRDASIDAF-NKPGSEkfVFLLSTRAGGLGINLATADIVILY 565
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 164661227 1466 EPLLNHAMELQAIGRVHRIGQTRPTYVYGYMVRDTVEERIVALA 1509
Cdd:PLN03142  566 DSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERA 609
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
1372-1485 1.01e-09

Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.


Pssm-ID: 306726  Cd Length: 110  Bit Score: 59.14  E-value: 1.01e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164661227  1372 SKLDLLIRHLVHIQctTGEKSLVFSSFARGLDLVASnLERHGLAYARVDG--TGGKRSsAAVHAFQHKpDVRVLLlHSEA 1449
Cdd:pfam00271    1 EKLEALLELLKKKE--RGGKVLIFSQTKKRLEAELL-LEKEGIKVARLHGdlSQEERE-EILEDFRNG-KIDVLV-ATDV 74
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 164661227  1450 QSAGLNLLAATHMFLLEPLLNHAMELQAIGRVHRIG 1485
Cdd:pfam00271   75 AGRGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 110
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
319-620 3.74e-09

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601  Cd Length: 1033  Bit Score: 61.36  E-value: 3.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164661227  319 ILAEEMGLGKTIEVLALIleqadPHRHEkheaYWDVQnevcvqpiGTTLIVSPETLRRQWLDEVATYAPSLRLYSYTGHK 398
Cdd:PLN03142  192 ILADEMGLGKTLQTISLL-----GYLHE----YRGIT--------GPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFHGNP 254
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164661227  399 QASEHRgRTETWGqwASQYDVMVVSFEVLARDLAAshaapvraLRHPS-RYerprsplvqleflrVVMDEVQLVGGNA-- 475
Cdd:PLN03142  255 EERAHQ-REELLV--AGKFDVCVTSFEMAIKEKTA--------LKRFSwRY--------------IIIDEAHRIKNENsl 309
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164661227  476 -AKTIGMIRRQRSLAVSGTPVRR-LADLRTSLWFLglVPP---SMTTPRAWKRILSAELAPYVCELLANVG----IRHTK 546
Cdd:PLN03142  310 lSKTMRLFSTNYRLLITGTPLQNnLHELWALLNFL--LPEifsSAETFDEWFQISGENDQQEVVQQLHKVLrpflLRRLK 387
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164661227  547 AQVahEMVLPPQTRFLVPVDFTHVETAFYRDVWQASLAALNLDADgapmsdtwvldtgilRSQLL----RLRQACTHP 620
Cdd:PLN03142  388 SDV--EKGLPPKKETILKVGMSQMQKQYYKALLQKDLDVVNAGGE---------------RKRLLniamQLRKCCNHP 448
DEXDc smart00487
DEAD-like helicases superfamily;
311-508 1.83e-08

DEAD-like helicases superfamily;


Pssm-ID: 214692  Cd Length: 201  Bit Score: 56.35  E-value: 1.83e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164661227    311 VAGDVRGAILAEEMGLGKTIEVLALILEQADPHRHekheaywdvqnevcvqpiGTTLIVSP-ETLRRQWLDEVATYAPSL 389
Cdd:smart00487   20 LLSGLRDVILAAPTGSGKTLAALLPALEALKRGKG------------------GRVLVLVPtRELAEQWAEELKKLGPSL 81
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164661227    390 RL---YSYTGHKqasehrgRTETWGQWAS-QYDVMVVSFEVLARDLaashaapvralrhpsryERPRSPLVQLEFlrVVM 465
Cdd:smart00487   82 GLkvvGLYGGDS-------KREQLRKLESgKTDILVTTPGRLLDLL-----------------ENDKLSLSNVDL--VIL 135
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|....*....
gi 164661227    466 DEVQ--LVGGNAAKTIGMIRR----QRSLAVSGTPVRRLADLRTSLWFL 508
Cdd:smart00487  136 DEAHrlLDGGFGDQLEKLLKLlpknVQLLLLSATPPEEIENLLELFLND 184
RING-HC cd16449
HC subclass of RING (RING-HC) finger and its variants; RING finger is a specialized type of ...
1276-1315 2.19e-08

HC subclass of RING (RING-HC) finger and its variants; 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 HC subclass of RING (RING-HC) finger proteins 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 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 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: 319363  Cd Length: 39  Bit Score: 53.63  E-value: 2.19e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 164661227 1276 CFICTNLIETGILTNaCGHLCCEACFHAWLSHGHRTCPMC 1315
Cdd:cd16449     1 CPICLELLKDPVLLP-CGHTFCRSCLRRLLKEGKKKCPIC 39
RING smart00184
Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and ...
1276-1315 1.07e-07

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


Pssm-ID: 214546  Cd Length: 40  Bit Score: 51.74  E-value: 1.07e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 164661227   1276 CFICTNLIETGILTNACGHLCCEACFHAWLSHGHRTCPMC 1315
Cdd:smart00184    1 CPICLEEYLKDPVILPCGHTFCRSCIRKWLESGNNTCPIC 40
zf-C3HC4 pfam00097
Zinc finger, C3HC4 type (RING finger); The C3HC4 type zinc-finger (RING finger) is a ...
1276-1315 3.74e-07

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: 306580  Cd Length: 40  Bit Score: 50.05  E-value: 3.74e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 164661227  1276 CFICTNLIETGILTNACGHLCCEACFHAWLSHGHRTCPMC 1315
Cdd:pfam00097    1 CPICLEEPKDPVTLLPCGHLFCSKCIRSWLESGNVTCPLC 40
HELICc smart00490
helicase superfamily c-terminal domain;
1403-1485 1.54e-05

helicase superfamily c-terminal domain;


Pssm-ID: 197757  Cd Length: 82  Bit Score: 46.05  E-value: 1.54e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164661227   1403 DLVASNLERHGLAYARVDG--TGGKRSsAAVHAFqhKPDVRVLLLHSEAQSAGLNLLAATHMFLLEPLLNHAMELQAIGR 1480
Cdd:smart00490    1 EELAELLKELGIKVARLHGglSQEERE-EILDKF--NNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGR 77

                    ....*
gi 164661227   1481 VHRIG 1485
Cdd:smart00490   78 AGRAG 82
DEXDc cd00046
DEAD-like helicases superfamily. A diverse family of proteins involved in ATP-dependent RNA or ...
316-494 7.55e-04

DEAD-like helicases superfamily. A diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 238005  Cd Length: 144  Bit Score: 41.55  E-value: 7.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164661227  316 RGAILAEEMGLGKTIEVLALILEQADPHRHekheaywdvqnevcvqpiGTTLIVSP-ETLRRQWLDEVATYAP-SLRLYS 393
Cdd:cd00046     1 RDVLLAAPTGSGKTLAALLPILELLDSLKG------------------GQVLVLAPtRELANQVAERLKELFGeGIKVGY 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164661227  394 YTGHKQASEHRGRtetwgqWASQYDVMVVSFEVLARDLaashaapvralrhpsryERPRSPLVQLEFlrVVMDEVQLVGG 473
Cdd:cd00046    63 LIGGTSIKQQEKL------LSGKTDIVVGTPGRLLDEL-----------------ERLKLSLKKLDL--LILDEAHRLLN 117
                         170       180
                  ....*....|....*....|....*..
gi 164661227  474 NAAKTIGMIRRQRS------LAVSGTP 494
Cdd:cd00046   118 QGFGLLGLKILLKLpkdrqvLLLSATP 144
PEX10 COG5574
RING-finger-containing E3 ubiquitin ligase [Posttranslational modification, protein turnover, ...
1274-1324 2.14e-03

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


Pssm-ID: 227861  Cd Length: 271  Bit Score: 41.80  E-value: 2.14e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 164661227 1274 RRCFICTNLIETGILTnACGHLCCEAC-FHAWLSHGHRTCPMCKTRLAPRDV 1324
Cdd:COG5574   216 YKCFLCLEEPEVPSCT-PCGHLFCLSClLISWTKKKYEFCPLCRAKVYPKKV 266
 
Name Accession Description Interval E-value
SNF2_N pfam00176
SNF2 family N-terminal domain; This domain is found in proteins involved in a variety of ...
316-621 4.11e-37

SNF2 family N-terminal domain; This domain is found in proteins involved in a variety of processes including transcription regulation (e.g., SNF2, STH1, brahma, MOT1), DNA repair (e.g., ERCC6, RAD16, RAD5), DNA recombination (e.g., RAD54), and chromatin unwinding (e.g., ISWI) as well as a variety of other proteins with little functional information (e.g., lodestar, ETL1).


Pssm-ID: 306645  Cd Length: 305  Bit Score: 145.23  E-value: 4.11e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164661227   316 RGAILAEEMGLGKTIEVLALILEQADpHRHEKHEAywdvqnevcvqpiGTTLIVSPETLRRQWLDEVATYAPSLRLYSYT 395
Cdd:pfam00176   17 RGGILADEMGLGKTLQTISLLLTLKY-LYHIKKLP-------------GPTLIVVPLSLLDNWMNEFERWVPSLRLVVLV 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164661227   396 GHKQASEHRGRTETWGQWASQYDVMVVSFEVLARDLAAshaapvralrhpsryerpRSPLVQLEFLRVVMDEVQLVGGNA 475
Cdd:pfam00176   83 GDGGSRMDKMNVRLLPKVLADYDVVITTYETLRRDKKN------------------RSLLKKLKWHRVILDEGHRLKNSK 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164661227   476 AKTIGMIRRQRS---LAVSGTPVRR-LADLRTSLWFLGlvPPSMTTPRAWKRILS------------AELApyvcELLAN 539
Cdd:pfam00176  145 SKLSEALSKLRTrnrWILTGTPIQNnLEELWALLNFLR--PGPFGSLQTFDKWFVrpiergggekgvARLH----KLLKP 218
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164661227   540 VGIRHTKAQVAHEmvLPPQTRFLVPVDFTHVETAFYRDVWQASL------------AALNLDADGAPMsdtwvlDTGILR 607
Cdd:pfam00176  219 FLLRRTKKDVEKS--LPPKVEEILFCRLSKGQRKLYQTALQALRgngilkllirnrAATKFSSKSFRG------KPGLLN 290
                          330
                   ....*....|....
gi 164661227   608 SqLLRLRQACTHPQ 621
Cdd:pfam00176  291 I-LLRLRKICNHPD 303
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination and ...
1345-1516 7.97e-24

Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination and repair];


Pssm-ID: 223627  Cd Length: 866  Bit Score: 109.05  E-value: 7.97e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164661227 1345 TSSNTFQVLPAEMRQALDNMALEGGSGSKLDLLIRHLVHIQCTTG--EKSLVFSSFARGLDLVASNLERHGLAYARVDG- 1421
Cdd:COG0553   665 TFDRIVLLLREDKDFDYLKKPLIQLSKGKLQALDELLLDKLLEEGhyHKVLIFSQFTPVLDLLEDYLKALGIKYVRLDGs 744
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164661227 1422 TGGKRSSAAVHAFQHKPDVRVLLLHSEAQSAGLNLLAATHMFLLEPLLNHAMELQAIGRVHRIGQTRPTYVYGYMVRDTV 1501
Cdd:COG0553   745 TPAKRRQELIDRFNADEEEKVFLLSLKAGGLGLNLTGADTVILFDPWWNPAVELQAIDRAHRIGQKRPVKVYRLITRGTI 824
                         170
                  ....*....|....*
gi 164661227 1502 EERIVALaAERKQSL 1516
Cdd:COG0553   825 EEKILEL-QEKKQEL 838
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination and ...
317-627 2.55e-18

Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination and repair];


Pssm-ID: 223627  Cd Length: 866  Bit Score: 91.33  E-value: 2.55e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164661227  317 GAILAEEMGLGKTIEVLALIleqadPHRHEKHEaywdvqnevcvQPIGTTLIVSPETLRRQWLDEVATYAPSLRLYsYTG 396
Cdd:COG0553   360 GGILADDMGLGKTVQTIALL-----LSLLESIK-----------VYLGPALIVVPASLLSNWKREFEKFAPDLRLV-LVY 422
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164661227  397 HKQASEHRGRTETWGQWASQ-----YDVMVVSFEVLARDLAashaapvralrhpsryerPRSPLVQLEFLRVVMDEVQLV 471
Cdd:COG0553   423 HGEKSELDKKREALRDLLKLhlviiFDVVITTYELLRRFLV------------------DHGGLKKIEWDRVVLDEAHRI 484
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164661227  472 G---GNAAKTIGMIRRQRSLAVSGTPV-RRLADLRTSLWF---LGLVPPSMTTPRAW-KRILSAE--------LAPYVCE 535
Cdd:COG0553   485 KndqSSEGKALQFLKALNRLDLTGTPLeNRLGELWSLLQEflnPGLLGTSFAIFTRLfEKPIQAEedigpleaRELGIEL 564
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164661227  536 LLANVG---IRHTKAQVAHEMVLPPQTRFLVPVDFTHVETAFYRDVWQASLAALNLDADGAPMSDTWVLDTGILRSQL-- 610
Cdd:COG0553   565 LRKLLSpfiLRRTKEDVEVLKELPPKIEKVLECELSEEQRELYEALLEGAEKNQQLLEDLEKADSDENRIGDSELNILal 644
                         330
                  ....*....|....*...
gi 164661227  611 -LRLRQACTHPQVAMRGG 627
Cdd:COG0553   645 lTRLRQICNHPALVDEGL 662
HELICc cd00079
Helicase superfamily c-terminal domain; associated with DEXDc-, DEAD-, and DEAH-box proteins, ...
1370-1493 1.37e-12

Helicase superfamily c-terminal domain; associated with DEXDc-, DEAD-, and DEAH-box proteins, yeast initiation factor 4A, Ski2p, and Hepatitis C virus NS3 helicases; this domain is found in a wide variety of helicases and helicase related proteins; may not be an autonomously folding unit, but an integral part of the helicase; 4 helicase superfamilies at present according to the organization of their signature motifs; all helicases share the ability to unwind nucleic acid duplexes with a distinct directional polarity; they utilize the free energy from nucleoside triphosphate hydrolysis to fuel their translocation along DNA, unwinding the duplex in the process


Pssm-ID: 238034  Cd Length: 131  Bit Score: 68.03  E-value: 1.37e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164661227 1370 SGSKLDLLIRhLVHIQCTTGEKSLVFSSFARGLDLVASNLERHGL--AYARVDGTGGKRSSAaVHAFQHKPdvRVLLLHS 1447
Cdd:cd00079    10 EDEKLEALLE-LLKEHLKKGGKVLIFCPSKKMLDELAELLRKPGIkvAALHGDGSQEEREEV-LKDFREGE--IVVLVAT 85
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 164661227 1448 EAQSAGLNLLAATHMFLLEPLLNHAMELQAIGRVHRIGQTRPTYVY 1493
Cdd:cd00079    86 DVIARGIDLPNVSVVINYDLPWSPSSYLQRIGRAGRAGQKGTAILL 131
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
1389-1509 5.86e-12

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601  Cd Length: 1033  Bit Score: 70.60  E-value: 5.86e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164661227 1389 GEKSLVFSSFARGLDLVASNLERHGLAYARVDG-TGGKRSSAAVHAFqHKPDVR--VLLLHSEAQSAGLNLLAATHMFLL 1465
Cdd:PLN03142  487 DSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGnTGGEDRDASIDAF-NKPGSEkfVFLLSTRAGGLGINLATADIVILY 565
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 164661227 1466 EPLLNHAMELQAIGRVHRIGQTRPTYVYGYMVRDTVEERIVALA 1509
Cdd:PLN03142  566 DSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERA 609
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
1372-1485 1.01e-09

Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.


Pssm-ID: 306726  Cd Length: 110  Bit Score: 59.14  E-value: 1.01e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164661227  1372 SKLDLLIRHLVHIQctTGEKSLVFSSFARGLDLVASnLERHGLAYARVDG--TGGKRSsAAVHAFQHKpDVRVLLlHSEA 1449
Cdd:pfam00271    1 EKLEALLELLKKKE--RGGKVLIFSQTKKRLEAELL-LEKEGIKVARLHGdlSQEERE-EILEDFRNG-KIDVLV-ATDV 74
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 164661227  1450 QSAGLNLLAATHMFLLEPLLNHAMELQAIGRVHRIG 1485
Cdd:pfam00271   75 AGRGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 110
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
319-620 3.74e-09

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601  Cd Length: 1033  Bit Score: 61.36  E-value: 3.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164661227  319 ILAEEMGLGKTIEVLALIleqadPHRHEkheaYWDVQnevcvqpiGTTLIVSPETLRRQWLDEVATYAPSLRLYSYTGHK 398
Cdd:PLN03142  192 ILADEMGLGKTLQTISLL-----GYLHE----YRGIT--------GPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFHGNP 254
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164661227  399 QASEHRgRTETWGqwASQYDVMVVSFEVLARDLAAshaapvraLRHPS-RYerprsplvqleflrVVMDEVQLVGGNA-- 475
Cdd:PLN03142  255 EERAHQ-REELLV--AGKFDVCVTSFEMAIKEKTA--------LKRFSwRY--------------IIIDEAHRIKNENsl 309
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164661227  476 -AKTIGMIRRQRSLAVSGTPVRR-LADLRTSLWFLglVPP---SMTTPRAWKRILSAELAPYVCELLANVG----IRHTK 546
Cdd:PLN03142  310 lSKTMRLFSTNYRLLITGTPLQNnLHELWALLNFL--LPEifsSAETFDEWFQISGENDQQEVVQQLHKVLrpflLRRLK 387
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164661227  547 AQVahEMVLPPQTRFLVPVDFTHVETAFYRDVWQASLAALNLDADgapmsdtwvldtgilRSQLL----RLRQACTHP 620
Cdd:PLN03142  388 SDV--EKGLPPKKETILKVGMSQMQKQYYKALLQKDLDVVNAGGE---------------RKRLLniamQLRKCCNHP 448
DEXDc smart00487
DEAD-like helicases superfamily;
311-508 1.83e-08

DEAD-like helicases superfamily;


Pssm-ID: 214692  Cd Length: 201  Bit Score: 56.35  E-value: 1.83e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164661227    311 VAGDVRGAILAEEMGLGKTIEVLALILEQADPHRHekheaywdvqnevcvqpiGTTLIVSP-ETLRRQWLDEVATYAPSL 389
Cdd:smart00487   20 LLSGLRDVILAAPTGSGKTLAALLPALEALKRGKG------------------GRVLVLVPtRELAEQWAEELKKLGPSL 81
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164661227    390 RL---YSYTGHKqasehrgRTETWGQWAS-QYDVMVVSFEVLARDLaashaapvralrhpsryERPRSPLVQLEFlrVVM 465
Cdd:smart00487   82 GLkvvGLYGGDS-------KREQLRKLESgKTDILVTTPGRLLDLL-----------------ENDKLSLSNVDL--VIL 135
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|....*....
gi 164661227    466 DEVQ--LVGGNAAKTIGMIRR----QRSLAVSGTPVRRLADLRTSLWFL 508
Cdd:smart00487  136 DEAHrlLDGGFGDQLEKLLKLlpknVQLLLLSATPPEEIENLLELFLND 184
RING-HC cd16449
HC subclass of RING (RING-HC) finger and its variants; RING finger is a specialized type of ...
1276-1315 2.19e-08

HC subclass of RING (RING-HC) finger and its variants; 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 HC subclass of RING (RING-HC) finger proteins 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 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 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: 319363  Cd Length: 39  Bit Score: 53.63  E-value: 2.19e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 164661227 1276 CFICTNLIETGILTNaCGHLCCEACFHAWLSHGHRTCPMC 1315
Cdd:cd16449     1 CPICLELLKDPVLLP-CGHTFCRSCLRRLLKEGKKKCPIC 39
RING smart00184
Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and ...
1276-1315 1.07e-07

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


Pssm-ID: 214546  Cd Length: 40  Bit Score: 51.74  E-value: 1.07e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 164661227   1276 CFICTNLIETGILTNACGHLCCEACFHAWLSHGHRTCPMC 1315
Cdd:smart00184    1 CPICLEEYLKDPVILPCGHTFCRSCIRKWLESGNNTCPIC 40
zf-C3HC4 pfam00097
Zinc finger, C3HC4 type (RING finger); The C3HC4 type zinc-finger (RING finger) is a ...
1276-1315 3.74e-07

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: 306580  Cd Length: 40  Bit Score: 50.05  E-value: 3.74e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 164661227  1276 CFICTNLIETGILTNACGHLCCEACFHAWLSHGHRTCPMC 1315
Cdd:pfam00097    1 CPICLEEPKDPVTLLPCGHLFCSKCIRSWLESGNVTCPLC 40
zf-RING_2 pfam13639
Ring finger domain;
1276-1316 4.43e-07

Ring finger domain;


Pssm-ID: 316187  Cd Length: 44  Bit Score: 50.12  E-value: 4.43e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 164661227  1276 CFICTNLIETG--ILTNACGHLCCEACFHAWLSHgHRTCPMCK 1316
Cdd:pfam13639    3 CPICLEEFEDGdeVRVLPCGHHFHRECLDKWLRS-SNTCPLCR 44
zf-C3HC4_2 pfam13923
Zinc finger, C3HC4 type (RING finger);
1275-1315 6.01e-07

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 316445  Cd Length: 40  Bit Score: 49.73  E-value: 6.01e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 164661227  1275 RCFICTNLIETGILTNACGHLCCEACFHAWLSHGHRtCPMC 1315
Cdd:pfam13923    1 MCPICLDMLKDPSTTTPCGHVFCQKCILRALRSGNE-CPLC 40
RING-HC_COP1 cd16504
RING finger, HC subclass, found in constitutive photomorphogenesis protein 1 (COP1) and ...
1276-1319 1.45e-06

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), was defined as 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 14-3-3 delta 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: 319418  Cd Length: 46  Bit Score: 48.41  E-value: 1.45e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 164661227 1276 CFICTNLIETGILTnACGHLCCEACFHAWLSHGHRtCPMCKTRL 1319
Cdd:cd16504     5 CPICFDIIEEAYMT-KCGHSFCYKCIRTSLEQSNR-CPKCNFVL 46
mRING-HC-C4C4_TRIM37_C-VIII cd16619
Modified RING finger, HC subclass (C4C4-type), found in tripartite motif-containing protein 37 ...
1274-1316 1.36e-05

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


Pssm-ID: 319533  Cd Length: 43  Bit Score: 45.80  E-value: 1.36e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 164661227 1274 RRCFICTNLIETGILTNACGHLCCEACFHAWLSHGHRTCPMCK 1316
Cdd:cd16619     1 FRCFICMEKLRDARLCPHCSKLCCFSCIRRWLTEQRSQCPHCR 43
HELICc smart00490
helicase superfamily c-terminal domain;
1403-1485 1.54e-05

helicase superfamily c-terminal domain;


Pssm-ID: 197757  Cd Length: 82  Bit Score: 46.05  E-value: 1.54e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164661227   1403 DLVASNLERHGLAYARVDG--TGGKRSsAAVHAFqhKPDVRVLLLHSEAQSAGLNLLAATHMFLLEPLLNHAMELQAIGR 1480
Cdd:smart00490    1 EELAELLKELGIKVARLHGglSQEERE-EILDKF--NNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGR 77

                    ....*
gi 164661227   1481 VHRIG 1485
Cdd:smart00490   78 AGRAG 82
RING-HC_AtRMA_like cd16745
RING finger, HC subclass, found in Arabidopsis thaliana RING membrane-anchor proteins (AtRMAs) ...
1276-1316 1.80e-05

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


Pssm-ID: 319659  Cd Length: 45  Bit Score: 45.37  E-value: 1.80e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 164661227 1276 CFICTNLIETGILTnACGHLCCEACFHAWL--SHGHRTCPMCK 1316
Cdd:cd16745     3 CNICLDLASDPVVT-LCGHLFCWPCLYRWLqrHSENRECPVCK 44
zf-C3HC4_3 pfam13920
Zinc finger, C3HC4 type (RING finger);
1272-1317 8.17e-05

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 316442  Cd Length: 50  Bit Score: 43.53  E-value: 8.17e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 164661227  1272 EARRCFIC-TNLIETGILTnaCGHLC-CEACFHAWLShGHRTCPMCKT 1317
Cdd:pfam13920    1 EDRLCVIClDRPRNVVLLP--CGHLClCEECAERLLR-KKKKCPICRQ 45
RING-HC_RNF138 cd16544
RING finger, HC subclass, found in RING finger protein 138 (RNF138) and similar proteins; ...
1276-1316 1.44e-04

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


Pssm-ID: 319458  Cd Length: 46  Bit Score: 42.86  E-value: 1.44e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 164661227 1276 CFICTNLIETGILTNACGHLCCEACFHAWLSHGHRTCPMCK 1316
Cdd:cd16544     5 CPVCQEVLQTPIRTKKCRHVFCRKCFLLAMRRSGAHCPLCR 45
RING-HC_RNF5_like cd16534
RING finger, HC subclass, found in RING finger protein RNF5, RNF185 and similar proteins; RNF5 ...
1276-1316 2.05e-04

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


Pssm-ID: 319448  Cd Length: 43  Bit Score: 42.03  E-value: 2.05e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 164661227 1276 CFICTNLIETGILTnACGHLCCEACFHAWLSHG--HRTCPMCK 1316
Cdd:cd16534     2 CNICLDTAKDAVVS-MCGHLFCWPCLHQWLETRpdRPTCPVCK 43
RING-HC_RNF141 cd16545
RING finger, HC subclass, found in RING finger protein 141 (RNF141) and similar proteins; ...
1276-1316 2.26e-04

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


Pssm-ID: 319459  Cd Length: 39  Bit Score: 42.01  E-value: 2.26e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 164661227 1276 CFICTNLIETGILtnACGHLCCEACFHAWlSHGHRTCPMCK 1316
Cdd:cd16545     2 CCICMDRKPDTIL--PCAHSFCQKCIDKW-SVRHRTCPICR 39
Prok-RING_4 pfam14447
Prokaryotic RING finger family 4; RING finger family domain found sporadically in bacteria. ...
1276-1323 2.37e-04

Prokaryotic RING finger family 4; RING finger family domain found sporadically in bacteria. The finger is fused to an N-terminal alpha-helical domain, ROT/Trove-like repeats and a C-terminal TerD domain. The architecture suggests a possible role in an RNA-processing complex.


Pssm-ID: 316929  Cd Length: 46  Bit Score: 41.96  E-value: 2.37e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 164661227  1276 CFICTnLIETGILTNACGHLCCEACFHAWlshGHRTCPMCKTRLAPRD 1323
Cdd:pfam14447    1 CVLCG-RVGTVHILSPCGHLVCRDCFDGS---DYSGCPICHRRIDPDD 44
zf-RING_5 pfam14634
zinc-RING finger domain;
1275-1317 2.85e-04

zinc-RING finger domain;


Pssm-ID: 317082  Cd Length: 43  Bit Score: 41.65  E-value: 2.85e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 164661227  1275 RCFICTNLI---ETGILTNaCGHLCCEACFHAwlSHGHRTCPMCKT 1317
Cdd:pfam14634    1 HCNKCFKPLsetRPFYLTS-CGHIFCEECLSK--LLQERQCPICRK 43
RING-HC_RNF170 cd16553
RING finger, HC subclass, found in RING finger protein 170 (RNF170) and similar proteins; ...
1276-1316 3.98e-04

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


Pssm-ID: 319467  Cd Length: 44  Bit Score: 41.50  E-value: 3.98e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 164661227 1276 CFICTNLIETGILTNaCGHLCCEACFHAWLSHGHRT----CPMCK 1316
Cdd:cd16553     1 CPICLGDASYPVETN-CGHIFCGNCIITYWRHGRWLgaisCPMCR 44
RING-HC_Cbl_like cd16502
RING finger, HC subclass, found in Casitas B-lineage lymphoma (Cbl) proteins; The Cbl adaptor ...
1276-1316 4.79e-04

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


Pssm-ID: 319416  Cd Length: 43  Bit Score: 41.19  E-value: 4.79e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 164661227 1276 CFICT-NLIETGIltNACGHLCCEACFHAWLSHGHRTCPMCK 1316
Cdd:cd16502     4 CKICAeNDKDVRI--EPCGHLLCTPCLTSWQDSDGQTCPFCR 43
DEXDc cd00046
DEAD-like helicases superfamily. A diverse family of proteins involved in ATP-dependent RNA or ...
316-494 7.55e-04

DEAD-like helicases superfamily. A diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 238005  Cd Length: 144  Bit Score: 41.55  E-value: 7.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164661227  316 RGAILAEEMGLGKTIEVLALILEQADPHRHekheaywdvqnevcvqpiGTTLIVSP-ETLRRQWLDEVATYAP-SLRLYS 393
Cdd:cd00046     1 RDVLLAAPTGSGKTLAALLPILELLDSLKG------------------GQVLVLAPtRELANQVAERLKELFGeGIKVGY 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164661227  394 YTGHKQASEHRGRtetwgqWASQYDVMVVSFEVLARDLaashaapvralrhpsryERPRSPLVQLEFlrVVMDEVQLVGG 473
Cdd:cd00046    63 LIGGTSIKQQEKL------LSGKTDIVVGTPGRLLDEL-----------------ERLKLSLKKLDL--LILDEAHRLLN 117
                         170       180
                  ....*....|....*....|....*..
gi 164661227  474 NAAKTIGMIRRQRS------LAVSGTP 494
Cdd:cd00046   118 QGFGLLGLKILLKLpkdrqvLLLSATP 144
RING-HC_RNFT1_like cd16532
RING finger, HC subclass, found in RING finger and transmembrane domain-containing protein ...
1276-1316 8.51e-04

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: 319446  Cd Length: 40  Bit Score: 40.34  E-value: 8.51e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 164661227 1276 CFICTNLIETGILTnACGHLCCEACFHAWLSHgHRTCPMCK 1316
Cdd:cd16532     2 CPICQDEFKDPIKL-RCKHIFCEDCVSEWFDR-ERTCPLCR 40
RING-H2_GRAIL cd16668
RING finger, H2 subclass, found in the GRAIL transmembrane proteins family; The GRAIL ...
1276-1316 1.38e-03

RING finger, H2 subclass, found in the GRAIL transmembrane proteins family; The GRAIL transmembrane proteins family includes RING finger proteins RNF128 (also known as GRAIL), RNF130, RNF133, RNF148, 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. RNF128 is a type 1 transmembrane E3 ubiquitin-protein ligase that is a critical regulator of adaptive immunity and development. 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. RNF148 is a testis-specific E3 ubiquitin ligase that is abundantly expressed in testes and slightly expressed in pancreas. Its expression regulated by histone deacetylases. 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 is a RING finger protein that its polymorphisms may be associated with chronic obstructive pulmonary disease (COPD) risk in the Chinese population. The family also includes Drosophila melanogaster protein goliath (d-goliath), also known as protein g1, which is one of the funding members of the family. It was originally identified as a transcription factor involved in the embryo mesoderm formation.


Pssm-ID: 319582  Cd Length: 48  Bit Score: 39.64  E-value: 1.38e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 164661227 1276 CFICTNLIETG----ILTnaCGHLCCEACFHAWLsHGHRTCPMCK 1316
Cdd:cd16668     2 CAVCIEPYKPGdvvrILP--CKHIFHKSCVDPWL-LEHRTCPMCK 43
PEX10 COG5574
RING-finger-containing E3 ubiquitin ligase [Posttranslational modification, protein turnover, ...
1274-1324 2.14e-03

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


Pssm-ID: 227861  Cd Length: 271  Bit Score: 41.80  E-value: 2.14e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 164661227 1274 RRCFICTNLIETGILTnACGHLCCEAC-FHAWLSHGHRTCPMCKTRLAPRDV 1324
Cdd:COG5574   216 YKCFLCLEEPEVPSCT-PCGHLFCLSClLISWTKKKYEFCPLCRAKVYPKKV 266
RING-HC_RNF185 cd16744
RING finger, HC subclass, found in RING finger protein 185 (RNF185) and similar proteins; ...
1276-1316 2.37e-03

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


Pssm-ID: 319658  Cd Length: 43  Bit Score: 39.12  E-value: 2.37e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 164661227 1276 CFICTNLIETGILTnACGHLCCEACFHAWLSH--GHRTCPMCK 1316
Cdd:cd16744     2 CNICLDTAKDAVVS-LCGHLFCWPCLHQWLETrpNRQVCPVCK 43
RING-HC_RING1_like cd16531
RING finger, HC subclass, found in really interesting new gene proteins RING1, RING2 and ...
1276-1316 2.41e-03

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


Pssm-ID: 319445  Cd Length: 41  Bit Score: 38.95  E-value: 2.41e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 164661227 1276 CFICTNLIETGILTNACGHLCCEACFHAWLSHGHRTCPMCK 1316
Cdd:cd16531     1 CPICLDIIKNTMTTKECLHRFCAECITTALRSGNKECPTCR 41
zf-UDP pfam14569
Zinc-binding RING-finger; This RING/U-box type zinc-binding domain is frequently found in the ...
1276-1318 2.99e-03

Zinc-binding RING-finger; This RING/U-box type zinc-binding domain is frequently found in the catalytic subunit (irx3) of cellulose synthase. The enzymic class is EC:2.4.1.12, whereby the synthase removes the glucose from UDP-glucose and adds it to the growing cellulose, thereby releasing UDP. The domain-structure is treble-clef like (Structure 1weo).


Pssm-ID: 317028  Cd Length: 75  Bit Score: 38.91  E-value: 2.99e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 164661227  1276 CFICTN---LIETG---ILTNACGHLCCEACFHAWLSHGHRTCPMCKTR 1318
Cdd:pfam14569    8 CQICGDdvgLTEDGelfVACNECAFPVCRPCYEYERKDGNQSCPQCKTR 56
RING-H2 cd16448
H2 subclass of RING (RING-H2) finger and its variants; RING finger is a specialized type of ...
1276-1316 3.04e-03

H2 subclass of RING (RING-H2) finger and its variants; 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 as 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 pattern. Some lack a single Cys or His residues at typical Zn ligand positions. Especially, 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 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: 319362  Cd Length: 44  Bit Score: 38.59  E-value: 3.04e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 164661227 1276 CFICTNLIETG----ILTNaCGHlcceaCFHA-----WLSHGHRTCPMCK 1316
Cdd:cd16448     1 CAICLEEFEEGdcpvRLLP-CGH-----VFHKscidkWLESGNRTCPLCR 44
RING-H2_RNF128_like cd16802
RING finger, H2 subclass, found in RING finger protein 128 (RNF128) and similar proteins; This ...
1276-1316 3.85e-03

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 domain 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 regulated by histone deacetylases.


Pssm-ID: 319716  Cd Length: 49  Bit Score: 38.65  E-value: 3.85e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 164661227 1276 CFICTNLIETG----ILTnaCGHLCCEACFHAWLSHgHRTCPMCK 1316
Cdd:cd16802     3 CAVCIEPYKPNdvvrILT--CNHFFHKSCIDPWLLE-HRTCPMCK 44
RING-HC_Cbl-c cd16710
RING finger, HC subclass, found in E3 ubiquitin-protein ligase Cbl-c and similar proteins; ...
1276-1323 4.39e-03

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


Pssm-ID: 319624  Cd Length: 53  Bit Score: 38.53  E-value: 4.39e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 164661227 1276 CFICTNLiETGILTNACGHLCCEACFHAWLSHGHRTCPMCKTRLAPRD 1323
Cdd:cd16710     7 CKICAER-DKDVRIEPCGHLLCSCCLAAWQHSDSQTCPFCRCEIKGRE 53
RING_Ubox cd00162
The superfamily of RING finger (Really Interesting New Gene) domain and U-box domain; RING ...
1276-1315 5.82e-03

The superfamily of RING finger (Really Interesting New Gene) domain and U-box domain; 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 as 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 pattern. Some lack a single Cys or His residues at typical Zn ligand positions. Especially, 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 finger. In contrast, C4HC3- (RING-CH alias RINGv), C3H3C2-, C3H2C2D-, C3DHC3-, and C4HC2H-type RING fingers are close to RING-H2 finger. However, not all RING finger-containing proteins display regular RING finger features, and the RING finger family has turned out to be multifarious. The degenerated RING fingers from 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. 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 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: 319361  Cd Length: 40  Bit Score: 37.83  E-value: 5.82e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 164661227 1276 CFICTNLIETGILTNACGHLCCEACFHAWLSHGHRTCPMC 1315
Cdd:cd00162     1 CPICRELMKDPVVLPSCGHTFCYSCIARWLESSDQTCPFC 40
RING-H2_PA-TM-RING cd16454
RING finger, H2 subclass, found in the PA-TM-RING ubiquitin ligase family; The PA-TM-RING ...
1276-1316 6.18e-03

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: 319368  Cd Length: 43  Bit Score: 37.67  E-value: 6.18e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 164661227 1276 CFICTNLIETG--ILTNACGHLCCEACFHAWLSHgHRTCPMCK 1316
Cdd:cd16454     2 CAICLEEFEDGeeVRVLPCNHLFHSNCIDPWLEQ-HATCPLCR 43
mRING-HC-C3HC3D_Nrdp1 cd16634
Modified RING finger, HC subclass (C3HC3D-type), found in neuregulin receptor degradation ...
1276-1314 8.06e-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 promoten and 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 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: 319548  Cd Length: 43  Bit Score: 37.40  E-value: 8.06e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 164661227 1276 CFICTNLIETGILTNACGHLCCEACFHAWLSHgHRTCPM 1314
Cdd:cd16634     4 CPICSGVLEEPLQAPHCEHAFCNACITEWLSR-QQTCPV 41
RING-HC_CHFR cd16503
RING finger, HC subclass, found in checkpoint with forkhead and RING finger domains protein ...
1272-1316 9.24e-03

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) and a C3HC4-type RING-HC finger.


Pssm-ID: 319417  Cd Length: 44  Bit Score: 37.39  E-value: 9.24e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 164661227 1272 EARRCFICTNLIETGILTNACGHLCCEACFHAWLSHGHrTCPMCK 1316
Cdd:cd16503     1 ETLLCSICQDLLHDCVSLQPCMHNFCAGCYSEWMERSS-LCPQCR 44
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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