p28-like protein; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998156  157 DMDCPFAHGNYCDMCQQWSLHPYNAELRKKHENECVANHTTEMERafllqkteqKTCGICMENIFEKNLR---FGILNGC 233
Cdd:PHA03096 134 GKYCEYLHGDICDICEKYLLHPTDIKQRYNEQKTCLSYQLRLLLS---------KICGICLENIKAKYIIkkyYGILSEI 204

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71998156  234 QHCFCLDCIRQWRskdqeNVELATKTVRSCPECR----------QHSDYVIPSLFWVESGQEKDLLIEMYKENTKRKIC 302
Cdd:PHA03096 205 KHEFNIFCIKIWM-----TESLYKETEPENRRLNtvivfiekinEDLKNNIPSRYWIDDKYDKNLLSFRYKKMHIRKVC 278

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

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71998156 275 PSLFWVESGQEKDLLIEMYKENTKRKICKYYSNERSRG------ACPFGN-KCFYKHQLPDGSI 331
Cdd:COG5252 117 PDLYSDVRDKEEDVPLGKRPWINTDRVCKFFIEAMESGkygwgwTCPNGNmRCSYIHKLPDGYV 180

p28-like protein; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998156  157 DMDCPFAHGNYCDMCQQWSLHPYNAELRKKHENECVANHTTEMERafllqkteqKTCGICMENIFEKNLR---FGILNGC 233
Cdd:PHA03096 134 GKYCEYLHGDICDICEKYLLHPTDIKQRYNEQKTCLSYQLRLLLS---------KICGICLENIKAKYIIkkyYGILSEI 204

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71998156  234 QHCFCLDCIRQWRskdqeNVELATKTVRSCPECR----------QHSDYVIPSLFWVESGQEKDLLIEMYKENTKRKIC 302
Cdd:PHA03096 205 KHEFNIFCIKIWM-----TESLYKETEPENRRLNtvivfiekinEDLKNNIPSRYWIDDKYDKNLLSFRYKKMHIRKVC 278

Zinc-finger containing family; zf-CCCH_3 family is found in eukaryotes, and is typically between 155 and 169 amino acids in length.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 71998156     1 MPRHETDCRYFANGYCSKGNTCTFTH-DVATRNENICHFNLVGKCsYGRACRFLHTR 56
Cdd:pfam15663   1 MENKGDDCYFFYYSTCTKGDSCPFRHcEAALGNETVCTLWQEGRC-FRPVCRFRHME 56

Cleavage and polyadenylation specificity factor (CPSF) Clipper subunit and related makorin family Zn-finger proteins [General function prediction only];

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 71998156   8 CRYFANGYCSKGNTCTFTHDVATRNENI--CH-FNLVGKCSYGRACRFLHTRP 57
Cdd:COG5084 107 CKFFLRGLCKSGFSCEFLHEYDLRSSQGppCRsFSLKGSCSSGPSCGYSHIDP 159

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

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71998156 211 KTCGICMENIFEK----NLRFGILNGCQHCFCLDCIRQWRSKDQenveLATKTVRSCPECRQHS 270
Cdd:cd16730   2 KVCGICMEVVYEKanpsERRFGILSNCNHTYCLKCIRKWRSAKQ----FESKIIKSCPECRITS 61

N1R/p28-like protein; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998156  162 FAHGNYCDMCQQWSLhpYNAELRKKHEN-----ECVANHTTEMERAFLLQKTEQktCGICMENIFEKNLR---FGILNGC 233
Cdd:PHA02929 125 NDKINYIYMRKEEDM--FYAIINKKGKNykkflKTIPSVLSEYEKLYNRSKDKE--CAICMEKVYDKEIKnmyFGILSNC 200

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 71998156  234 QHCFCLDCIRQWRskdqenvelatKTVRSCPECRQHSDYVIPSLFW 279
Cdd:PHA02929 201 NHVFCIECIDIWK-----------KEKNTCPVCRTPFISVIKSRFF 235

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

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71998156 211 KTCGICMENIFEKNL----RFGILNGCQHCFCLDCIRQWRSKDQenveLATKTVRSCPECR 267
Cdd:cd16731   2 KVCSICMEVVYEKASaserRFGILSNCNHTYCLSCIRQWRCAKQ----FENPIIKSCPECR 58

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

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 71998156 212 TCGICMENIfeKNLRfGILNGCQHCFCLDCIRQWrskdqenvelaTKTVRSCPECRQH 269
Cdd:cd16574   3 SCPICLDRF--ENEK-AFLDGCFHAFCFTCILEW-----------SKVKNECPLCKQP 46

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

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71998156 275 PSLFWVESGQEKDLLIEMYKENTKRKICKYYSNERSRG------ACPFGN-KCFYKHQLPDGSI 331
Cdd:COG5252 117 PDLYSDVRDKEEDVPLGKRPWINTDRVCKFFIEAMESGkygwgwTCPNGNmRCSYIHKLPDGYV 180

Cleavage and polyadenylation specificity factor (CPSF) Clipper subunit and related makorin family Zn-finger proteins [General function prediction only];

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 71998156   8 CRYFANGYCSKGNTCTFTHDVATRNENI--CH-FNLVGKCSYGRACRFLHTRP 57
Cdd:COG5084 107 CKFFLRGLCKSGFSCEFLHEYDLRSSQGppCRsFSLKGSCSSGPSCGYSHIDP 159

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        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71998156 213 CGICMENIFEknlrFGILNGCQHCFCLDCIRQWrskdqenvelaTKTVRSCPECRQHSDYVI 274
Cdd:cd23130   3 CPICLDDPED----EAITLPCLHQFCYTCILRW-----------LQTSPTCPLCKTPVTSII 49

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

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998156 209 EQKTCGICMENifeknLRFGILNGCQHCFCLDCIRQWRSKDqenvelatktvRSCPECRQ 268
Cdd:cd16561   1 GEQECSICLED-----LNDPVKLPCDHVFCEECIRQWLPGQ-----------MSCPLCRT 44