transcription termination factor Rho; Provisional

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535613  822 PSSDLADEKVETVSQPSESPKDTIDKTKKPRTRRSRFHSPSTTWSPNKDTPQEKKRPQSPSPRRETGKESRKSQSPSPKN 901
Cdd:PRK12678    68 ATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARKAGE 147

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535613  902 ESARGRKKSRSQSPKKDIARERRQSQSRSPKRDTTRESRRSEslsprRETSRENKRSQPRVKDSSPGEKSRSQSRERESD 981
Cdd:PRK12678   148 GGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGE-----RGRREERGRDGDDRDRRDRREQGDRREERGRRD 222

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535613  982 RDGQRRERERrtrkwsrsrshsrspsrcrtkskSSSFGRIDRDSYSPRWKGRWANDGWRCPRGNDRYRKNDPEKQNENTR 1061
Cdd:PRK12678   223 GGDRRGRRRR-----------------------RDRRDARGDDNREDRGDRDGDDGEGRGGRRGRRFRDRDRRGRRGGDG 279

                          250
                   ....*....|..
gi 2462535613 1062 KEKNDIHLDADD 1073
Cdd:PRK12678   280 GNEREPELREDD 291

N1R/p28-like protein; Provisional

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535613   60 LFQREMKKKTVCTLNMgdkKYEDMEGEENG---------------DNTISTGL-----LY--SEADRCPICLNCLLEKEV 117
Cdd:PHA02929   113 EYNQKILKNKPSNDKI---NYIYMRKEEDMfyaiinkkgknykkfLKTIPSVLseyekLYnrSKDKECAICMEKVYDKEI 189

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2462535613  118 -----GFPESCNHVFCMTCILKWAETLASCPIDRKPFQAVFK 154
Cdd:PHA02929   190 knmyfGILSNCNHVFCIECIDIWKKEKNTCPVCRTPFISVIK 231

transcription termination factor Rho; Provisional

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535613  822 PSSDLADEKVETVSQPSESPKDTIDKTKKPRTRRSRFHSPSTTWSPNKDTPQEKKRPQSPSPRRETGKESRKSQSPSPKN 901
Cdd:PRK12678    68 ATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARKAGE 147

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535613  902 ESARGRKKSRSQSPKKDIARERRQSQSRSPKRDTTRESRRSEslsprRETSRENKRSQPRVKDSSPGEKSRSQSRERESD 981
Cdd:PRK12678   148 GGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGE-----RGRREERGRDGDDRDRRDRREQGDRREERGRRD 222

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535613  982 RDGQRRERERrtrkwsrsrshsrspsrcrtkskSSSFGRIDRDSYSPRWKGRWANDGWRCPRGNDRYRKNDPEKQNENTR 1061
Cdd:PRK12678   223 GGDRRGRRRR-----------------------RDRRDARGDDNREDRGDRDGDDGEGRGGRRGRRFRDRDRRGRRGGDG 279

                          250
                   ....*....|..
gi 2462535613 1062 KEKNDIHLDADD 1073
Cdd:PRK12678   280 GNEREPELREDD 291

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)

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 2462535613   105 CPICLNCLLEKEVGFPesCNHVFCMTCILKWAETL-ASCPI 144
Cdd:smart00184    1 CPICLEEYLKDPVILP--CGHTFCRSCIRKWLESGnNTCPI 39

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

                           10        20
                   ....*....|....*....|....*...
gi 2462535613  123 CNHVFCMTCILKWAETLASCPIDRKPFQ 150
Cdd:COG5194     54 CNHAFHDHCIYRWLDTKGVCPLDRQTWV 81

Modified RING finger, HC subclass (C3HC3D-type), found in PHD and RING finger domain-containing protein 1 (PHRF1) and similar proteins; PHRF1, also known as KIAA1542, or CTD-binding SR-like protein rA9, is a ubiquitin ligase which induces the ubiquitination of TGIF (TG-interacting factor) at lysine 130. It acts as a tumor suppressor that promotes the transforming growth factor (TGF)-beta cytostatic program through selective release of TGIF-driven promyelocytic leukemia protein (PML) inactivation. PHRF1 contains a plant homeodomain (PHD) finger and a modified C3HC3D-type RING-HC finger.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2462535613  101 EADRCPICLNCLLEKEVGFPESCNHVFCMTCILKWAETLASCPIDRKPF 149
Cdd:cd16635      3 ESESCPICLNTFRDQAVGTPESCDHIFCLDCILEWSKNANTCPVDRIVF 51

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.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 2462535613  103 DRCPICLNCLLEKEVGFPesCNHVFCMTCILKWAETLASCPIDRKPF 149
Cdd:cd23130      1 DVCPICLDDPEDEAITLP--CLHQFCYTCILRWLQTSPTCPLCKTPV 45

Ring finger domain;

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2462535613  103 DRCPICLNCLLEKEVGFPESCNHVFCMTCILKWAETLASCPIDR 146
Cdd:pfam13639    1 DECPICLEEFEEGDKVVVLPCGHHFHRECLDKWLRSSNTCPLCR 44

transcription termination factor Rho; Provisional

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535613  822 PSSDLADEKVETVSQPSESPKDTIDKTKKPRTRRSRFHSPSTTWSPNKDTPQEKKRPQSPSPRRETGKESRKSQSPSPKN 901
Cdd:PRK12678    68 ATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARKAGE 147

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535613  902 ESARGRKKSRSQSPKKDIARERRQSQSRSPKRDTTRESRRSEslsprRETSRENKRSQPRVKDSSPGEKSRSQSRERESD 981
Cdd:PRK12678   148 GGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGE-----RGRREERGRDGDDRDRRDRREQGDRREERGRRD 222

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535613  982 RDGQRRERERrtrkwsrsrshsrspsrcrtkskSSSFGRIDRDSYSPRWKGRWANDGWRCPRGNDRYRKNDPEKQNENTR 1061
Cdd:PRK12678   223 GGDRRGRRRR-----------------------RDRRDARGDDNREDRGDRDGDDGEGRGGRRGRRFRDRDRRGRRGGDG 279

                          250
                   ....*....|..
gi 2462535613 1062 KEKNDIHLDADD 1073
Cdd:PRK12678   280 GNEREPELREDD 291

U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of an N-terminal arginine-rich low complexity domain followed by three tandem RNA recognition motifs (pfam00076). The well-characterized members of this family are auxilliary components of the U2 small nuclear ribonuclearprotein splicing factor (U2AF). These proteins are closely related to the CC1-like subfamily of splicing factors (TIGR01622). Members of this subfamily are found in plants, metazoa and fungi.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535613  885 RETGKESRKSQSPSPKNESARGRKKSRSQSPKKDIARERRQSQSRSPKRDTTRESRRSESLSPRRETSRENKRSQP--RV 962
Cdd:TIGR01642    3 EEPDREREKSRGRDRDRSSERPRRRSRDRSRFRDRHRRSRERSYREDSRPRDRRRYDSRSPRSLRYSSVRRSRDRPrrRS 82

                           90       100
                   ....*....|....*....|
gi 2462535613  963 KDSSPGEKSRSQSRERESDR 982
Cdd:TIGR01642   83 RSVRSIEQHRRRLRDRSPSN 102

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.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2462535613  103 DRCPICLNCLLEKEVGFPESCNHVFCMTCILKWAETLASCPIDRKP 148
Cdd:cd16469      1 DTCAVCLEEFKLKEELGVCPCGHAFHTKCLKKWLEVRNSCPICKSP 46

splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors including the Pad-1 protein (N. crassa), CAPER (M. musculus) and CC1.3 (H.sapiens). These proteins are characterized by an N-terminal arginine-rich, low complexity domain followed by three (or in the case of 4 H. sapiens paralogs, two) RNA recognition domains (rrm: pfam00706). These splicing factors are closely related to the U2AF splicing factor family (TIGR01642). A homologous gene from Plasmodium falciparum was identified in the course of the analysis of that genome at TIGR and was included in the seed.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535613  885 RETGKESRKSQSPSPKNESARGRKKSRSQSPKKDIARERRQSQSRSPKRDTTRESR--------RSESLSPRRETSRENK 956
Cdd:TIGR01622    7 RERLRDSSSAGDRDRRRDKGRERSRDRSRDRERSRSRRRDRHRDRDYYRGRERRSRsrrpnrryRPREKRRRRGDSYRRR 86

                           90       100
                   ....*....|....*....|....*..
gi 2462535613  957 RSQPRVKDSSPGEKSRSQSRERESDRD 983
Cdd:TIGR01622   87 RDDRRSRREKPRARDGTPEPLTEDERD 113

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

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2462535613  105 CPICLNcLLEKEVGFPesCNHVFCMTCILK-WAET---LASCPIDRKPF 149
Cdd:cd16604      3 CPICLD-LLKDPVTLP--CGHSFCMGCLGAlWGAGrggRASCPLCRQTF 48

Zinc finger, C3HC4 type (RING finger);

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 2462535613  104 RCPICLNCLLEKEVGFPesCNHVFCMTCILKWAETLASCPI 144
Cdd:pfam13923    1 MCPICMDMLKDPSTTTP--CGHVFCQDCILRALRAGNECPL 39

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

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2462535613  104 RCPICLncllekevgfpES--------CNHVFCMTCILKWAETLASCPIDRKPFQ 150
Cdd:cd16527      2 KCSLCL-----------EErrhptatpCGHLFCWSCITEWCNEKPECPLCREPFQ 45

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

                           10        20        30
                   ....*....|....*....|....*....|.
gi 2462535613  123 CNHVFCMTCILKWAETLAS---CPIDRKPFQ 150
Cdd:cd16456     32 CSHCFHMHCILKWLNSQQVqqhCPMCRQEWK 62

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.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 2462535613  105 CPIClNCLLEKEVGFPEsCNHVFCMTCILKWAETLASCPIDR 146
Cdd:cd16634      4 CPIC-SGVLEEPLQAPH-CEHAFCNACITEWLSRQQTCPVDR 43

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

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 2462535613  105 CPICLNcLLEKEVGFPesCNHVFCMTCILKWAETLA----SCP 143
Cdd:pfam15227    1 CPICLD-YLEKPVSIE--CGHSFCLSCINSLQKEPDgeslLCP 40

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

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 2462535613  104 RCPICLNcLLEKEVGFPesCNHVFCMTCILKWAETLASCPIDRKPFQA 151
Cdd:cd16719      6 KCKLCGK-VLEEPLSTP--CGHVFCAGCLLPWAVQRRLCPLQCQPIAA 50

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.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 2462535613  105 CPICLNCLleKEVGFPESCNHVFCMTCILKWAETLA-SCPI 144
Cdd:pfam00097    1 CPICLEEP--KDPVTLLPCGHLFCSKCIRSWLESGNvTCPL 39

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.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2462535613  104 RCPICLNCLLEKE-VGFPESCNHVFCMTCILKWAETLASCPIDR 146
Cdd:cd16461      1 ECAICLSDYENGEeLRRLPECKHAFHKECIDEWLKSNSTCPLCR 44

U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of an N-terminal arginine-rich low complexity domain followed by three tandem RNA recognition motifs (pfam00076). The well-characterized members of this family are auxilliary components of the U2 small nuclear ribonuclearprotein splicing factor (U2AF). These proteins are closely related to the CC1-like subfamily of splicing factors (TIGR01622). Members of this subfamily are found in plants, metazoa and fungi.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535613  902 ESARGRKKSRSQSPKKDIARERRQSQSRSPKRDTTRESRRSESLSPRRETSRENKRS-QPRVKDSSPGEKSRSQSRERES 980
Cdd:TIGR01642    4 EPDREREKSRGRDRDRSSERPRRRSRDRSRFRDRHRRSRERSYREDSRPRDRRRYDSrSPRSLRYSSVRRSRDRPRRRSR 83

                   ...
gi 2462535613  981 DRD 983
Cdd:TIGR01642   84 SVR 86

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.

                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 2462535613  108 CLNCLLEKEVGFPESCNHVFCMTCILKWAETLASCPI 144
Cdd:cd23135      6 CSICFSEIRSGAILKCGHFFCLSCIASWLREKSTCPL 42

Dentin matrix protein 1 (DMP1); This family consists of several mammalian dentin matrix protein 1 (DMP1) sequences. The dentin matrix acidic phosphoprotein 1 (DMP1) gene has been mapped to human chromosome 4q21. DMP1 is a bone and teeth specific protein initially identified from mineralized dentin. DMP1 is primarily localized in the nuclear compartment of undifferentiated osteoblasts. In the nucleus, DMP1 acts as a transcriptional component for activation of osteoblast-specific genes like osteocalcin. During the early phase of osteoblast maturation, Ca(2+) surges into the nucleus from the cytoplasm, triggering the phosphorylation of DMP1 by a nuclear isoform of casein kinase II. This phosphorylated DMP1 is then exported out into the extracellular matrix, where it regulates nucleation of hydroxyapatite. DMP1 is a unique molecule that initiates osteoblast differentiation by transcription in the nucleus and orchestrates mineralized matrix formation extracellularly, at later stages of osteoblast maturation. The DMP1 gene has been found to be ectopically expressed in lung cancer although the reason for this is unknown.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535613  742 EKSLEEKNES-LTEHPRSTELPKTHI-EQIQKHFSEDNNEMIPMECDSfCSDQNESEVEPSVNADLKQMNENSVTHCSEN 819
Cdd:pfam07263  247 QASTQDSGDSqSVEYPSRKFFRKSRIsEEDDRGELDDSNTMEEVKSDS-TESTSSKEAGLSQSREDSKSESQEDSEESQS 325

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535613  820 NMPSSDLADEKVETVSQPSESPKDTIDKTKKPRTRRSRFHSPSTTWSPNKDTP-QEKKRPQSPSPRRETGKESRKSQSPS 898
Cdd:pfam07263  326 QEDSQNSQDPSSESSQEADLPSQESSSESQEEVVSESRGDNPDNTSSSEEDQEdSDSSEEDSLSTFSSSESESREEQADS 405

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535613  899 PKNESARGRKKSRSQSPKKDIA-RERRQSQSRSpkrdttRESRRSESLSPRRETSRENKRSqprvkDSSPGEKSRSQSRE 977
Cdd:pfam07263  406 ESNESLRSSEESPESSEDENSSsQEGLQSHSAS------TESQSEESQSEQDSQSEEDDES-----DSQDSSRSKEDSNS 474

                   ...
gi 2462535613  978 RES 980
Cdd:pfam07263  475 TES 477

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

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 2462535613  104 RCPICLNcLLEKEVGFPesCNHVFCMTCILKWAETLASCP 143
Cdd:cd16512      2 KCKLCLG-VLEEPLATP--CGHVFCAGCVLPWVVRNGSCP 38

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.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 2462535613  105 CPICLNCLLEKEVGFPES-CNHVFCMTCILKWAETlaSCPIDR 146
Cdd:cd16457      3 CPVCLERMDESVSGILTIlCNHSFHCSCLSKWGDS--SCPVCR 43

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

                           10        20
                   ....*....|....*....|....*...
gi 2462535613  123 CNHVFCMTCILKWAETLASCPIDRKPFQ 150
Cdd:COG5194     54 CNHAFHDHCIYRWLDTKGVCPLDRQTWV 81

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.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 2462535613  105 CPICLNCLLEKEVGfpeSCNHVFCMTCILKWAETLASCPI 144
Cdd:cd16504      5 CPICFDIIKEAFVT---KCGHSFCYKCIVKHLEQKNRCPK 41

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

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2462535613  104 RCPICLNcllekEVGFPESCNH---VFCMTCILKW-AETLASCP 143
Cdd:cd16619      2 RCFICME-----KLRDPRLCPHcskLFCKGCIRRWlSEQRSSCP 40

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

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2462535613  105 CPICLNCLLEKEVGfpeSCNHVFCMTCILKWAETLAS----CPI 144
Cdd:cd16536      3 CPICLEPPVAPRIT---RCGHIFCWPCILRYLSLSEKkwrkCPI 43

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

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2462535613  103 DRCPICLncllEKEVGFPESCNHVFCMTCILKWAETLASCPIDR 146
Cdd:cd16545      1 EECCICM----DRKADLILPCAHSYCQKCIDKWSDRHRTCPICR 40

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

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462535613  105 CPICLNCLLEKEV------GFPESCNHVFCMTCILKW-------AETLASCP 143
Cdd:cd16732      4 CGICMDKVYEKAHakervfGILPNCNHAFCVGCIKKWrkskdfqNEVIKACP 55

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

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462535613  101 EADRCPICLNCLLEkevGFPESCNHVFCMTCILKWAETLA-----SCPIDRKP 148
Cdd:cd16583      4 EEGVCPICQEPLKE---AVSTDCGHLFCRMCLTQHAKKASasgvfSCPVCRKP 53

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

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2462535613  105 CPICLNCLLEkevgfPES--CNHVFCMTCILK-W--AETLASCPIDRKPFQ 150
Cdd:cd16594      8 CPICLDYFTD-----PVTldCGHSFCRACIARcWeePETSASCPQCRETCP 53

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

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 2462535613  103 DRCPICLNCLLEKEVGFPESCNHVFCMTCILKWAETLASCPI 144
Cdd:cd23122     12 DACSICLESFCEADPATVTSCKHEYHLQCILEWSQRSKECPM 53

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

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2462535613  103 DRCPICLNcllekevgfpeSCNHVFCMTCILKWAETLAS---CPIDRKPFQ 150
Cdd:pfam12861   43 DDCPLVWG-----------KCSHNFHMHCILKWLHTETSkglCPMCRQTFK 82

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

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462535613  103 DRCPICLNcllekEVGFP--ESCNHVFCMTCILK-WAETLA----SCPIDRKPFQAVF 153
Cdd:cd16553      2 MECPICLQ-----DARFPveTNCGHLFCGPCIITyWRHGSWlgavSCPVCRQTVTLLL 54

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535613  852 RTRRSRfHSPSTTWSpnkdtpQEKKRPQSPSPR--------RETGKESRKSQSPSPKNESARGRKKSRSQ------SPKK 917
Cdd:pfam03154    6 RTRRSR-GSMSTLRS------GRKKQTASPDGRasptnedlRSSGRNSPSAASTSSNDSKAESMKKSSKKikeeapSPLK 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535613  918 DIARERRQ--SQSRSPKRDTTRESRRSESLSPRRETSRENKRSQPRV---------KDSSPGEKSRSQS----RERESDR 982
Cdd:pfam03154   79 SAKRQREKgaSDTEEPERATAKKSKTQEISRPNSPSEGEGESSDGRSvndegssdpKDIDQDNRSTSPSipspQDNESDS 158

                   .
gi 2462535613  983 D 983
Cdd:pfam03154  159 D 159

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.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 2462535613  105 CPIClncllEKEVGFPES-----CNHVFCMTCILKWAETLASCPIDRK 147
Cdd:cd16801      2 CPVC-----KEDYTVGENvrqlpCNHLFHNDCIVPWLEQHDTCPVCRK 44

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

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2462535613  105 CPICLNCLLEkevgfPES--CNHVFCMTCILKWAE---TLASCPIDRKPF 149
Cdd:cd16498     19 CPICLELLKE-----PVStkCDHQFCRFCILKLLQkkkKPAPCPLCKKSV 63