Putative zinc-RING and/or ribbon; This is a family of cysteine-rich proteins. Many members also carry a pleckstrin-homology domain, pfam00169

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595019 268 RQCDYTGQYYCSHCHWNDLAVIPARVVHNWDFEPRKVSRCSMRYLALMVSRPVLRLREINPLLFSYVEELVEIRKLRQDI 347
Cdd:pfam13901   1 RLCDYTGKYYCSGCHWNDTSVIPARILHNWDFKKYPVSKFAKQLLDSIYSQPLLNLSDLNPSLYSKVKELAKVRELREQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595019 348 LLMKPYFITCREAMEARLL--LQLQDRQHFVENDEMYSVQDLLDVHAGRLGCSLTEIHTLFAKHIKlDCERCQAKGFVCE 425
Cdd:pfam13901  81 KLLKDYLKTCRFAAEEELLklFRLRPRHHLLEDSHLYSLQDLVDIKNGSLLPFLEELVQFAEKHVT-NCELCQGKGFICE 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1034595019 426 LCREGDVLFPFDSH-TSVCADCSAVFHRDCYYDNSTTCPKCARL 468
Cdd:pfam13901 160 LCNSDDIIFPFDIDtTSRCEKCKAVFHKSCFRSGASPCPKCERL 203

Putative zinc-RING and/or ribbon; This is a family of cysteine-rich proteins. Many members also carry a pleckstrin-homology domain, pfam00169

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595019 268 RQCDYTGQYYCSHCHWNDLAVIPARVVHNWDFEPRKVSRCSMRYLALMVSRPVLRLREINPLLFSYVEELVEIRKLRQDI 347
Cdd:pfam13901   1 RLCDYTGKYYCSGCHWNDTSVIPARILHNWDFKKYPVSKFAKQLLDSIYSQPLLNLSDLNPSLYSKVKELAKVRELREQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595019 348 LLMKPYFITCREAMEARLL--LQLQDRQHFVENDEMYSVQDLLDVHAGRLGCSLTEIHTLFAKHIKlDCERCQAKGFVCE 425
Cdd:pfam13901  81 KLLKDYLKTCRFAAEEELLklFRLRPRHHLLEDSHLYSLQDLVDIKNGSLLPFLEELVQFAEKHVT-NCELCQGKGFICE 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1034595019 426 LCREGDVLFPFDSH-TSVCADCSAVFHRDCYYDNSTTCPKCARL 468
Cdd:pfam13901 160 LCNSDDIIFPFDIDtTSRCEKCKAVFHKSCFRSGASPCPKCERL 203

Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the Protein kinase C conserved region 1 (C1) domain.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1034595019 173 HRFyKEKSKSVKQTCDKCNTIIWGLIQTWYTCTGCYYRCHSKCLNLISKPCVSS 226
Cdd:pfam00130   1 HHF-VHRNFKQPTFCDHCGEFLWGLGKQGLKCSWCKLNVHKRCHEKVPPECGCD 53

Putative zinc-RING and/or ribbon; This is a family of cysteine-rich proteins. Many members also carry a pleckstrin-homology domain, pfam00169

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595019 268 RQCDYTGQYYCSHCHWNDLAVIPARVVHNWDFEPRKVSRCSMRYLALMVSRPVLRLREINPLLFSYVEELVEIRKLRQDI 347
Cdd:pfam13901   1 RLCDYTGKYYCSGCHWNDTSVIPARILHNWDFKKYPVSKFAKQLLDSIYSQPLLNLSDLNPSLYSKVKELAKVRELREQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595019 348 LLMKPYFITCREAMEARLL--LQLQDRQHFVENDEMYSVQDLLDVHAGRLGCSLTEIHTLFAKHIKlDCERCQAKGFVCE 425
Cdd:pfam13901  81 KLLKDYLKTCRFAAEEELLklFRLRPRHHLLEDSHLYSLQDLVDIKNGSLLPFLEELVQFAEKHVT-NCELCQGKGFICE 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1034595019 426 LCREGDVLFPFDSH-TSVCADCSAVFHRDCYYDNSTTCPKCARL 468
Cdd:pfam13901 160 LCNSDDIIFPFDIDtTSRCEKCKAVFHKSCFRSGASPCPKCERL 203

protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains. It contains the motif HX12CX2CXnCX2CX4HX2CX7C, where C and H are cysteine and histidine, respectively; X represents other residues; and n is either 13 or 14. C1 has a globular fold with two separate Zn(2+)-binding sites. It was originally discovered as lipid-binding modules in protein kinase C (PKC) isoforms. C1 domains that bind and respond to phorbol esters (PE) and diacylglycerol (DAG) are referred to as typical, and those that do not respond to PE and DAG are deemed atypical. A C1 domain may also be referred to as PKC or non-PKC C1, based on the parent protein's activity. Most C1 domain-containing non-PKC proteins act as lipid kinases and scaffolds, except PKD which acts as a protein kinase. PKC C1 domains play roles in membrane translocation and activation of the enzyme.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1034595019 173 HRFYKEKSKSVKqTCDKCNTIIWGLIQTWYTCTGCYYRCHSKCLNLISKPC 223
Cdd:cd00029     1 HRFVPTTFSSPT-FCDVCGKLIWGLFKQGLKCSDCGLVCHKKCLDKAPSPC 50

protein kinase C conserved region 1 (C1 domain) found in Schizosaccharomyces pombe protein BZZ1 and similar proteins; BZZ1 is a syndapin-like F-BAR protein that plays a role in endocytosis and trafficking to the vacuole. It functions with type I myosins to restore polarity of the actin cytoskeleton after NaCl stress. BZZ1 contains an N-terminal F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs), a central coiled-coil, and two C-terminal SH3 domains. Schizosaccharomyces pombe BZZ1 also harbors a C1 domain, but Saccharomyces cerevisiae BZZ1 doesn't have any. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1034595019 173 HRFyKEKSKSVKQTCDKCNTIIWGLIQTWYTCTGCYYRCHSKCLNLISKPC 223
Cdd:cd20824     2 HNF-KPHSFSIPTKCDYCGEKIWGLSKKGLSCKDCGFNCHIKCELKVPPEC 51

protein kinase C conserved region 1 (C1 domain) found in uncharacterized proteins similar to myotubularin-related proteins; The family includes a group of uncharacterized proteins that show high sequence similarity to vertebrate myotubularin-related proteins (MTMRs), such as MTMR5 and MTMR13. MTMRs may function as guanine nucleotide exchange factors (GEFs). Vertebrate MTMR5 and MTMR13 contain an N-terminal DENN domain, a PH-GRAM domain, an inactive PTP domain, a SET interaction domain, a coiled-coil domain, and a C-terminal PH domain. Members of this family contain these domains and have an additional C1 domain. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.

                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1034595019 185 QTCDKCNTIIWGLIQTWYTCTGCYYRCHSKCLNLISKPC 223
Cdd:cd20828    17 TNCDYCLQILWGIVKKGMKCSECGYNCHEKCQPQVPKQC 55

first protein kinase C conserved region 1 (C1 domain) found in classical (or conventional) protein kinase C (cPKC), novel protein kinase C (nPKC), and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domains. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. nPKCs are calcium-independent, but require DAG and PS for activity, while atypical PKCs (aPKCs) only require PS. PKCs phosphorylate and modify the activities of a wide variety of cellular proteins including receptors, enzymes, cytoskeletal proteins, transcription factors, and other kinases. They play a central role in signal transduction pathways that regulate cell migration and polarity, proliferation, differentiation, and apoptosis. This family includes classical PKCs (cPKCs) and novel PKCs (nPKCs). There are four cPKC isoforms (named alpha, betaI, betaII, and gamma) and four nPKC isoforms (delta, epsilon, eta, and theta). Members of this family contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.

                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1034595019 187 CDKCNTIIWGLIQTWYTCTGCYYRCHSKCLNLISKPC 223
Cdd:cd20792    15 CSHCKDFIWGLGKQGYQCQVCRFVVHKRCHEYVVFKC 51

second protein kinase C conserved region 1 (C1 domain) found in uncharacterized phosphatidylinositol 3-kinase regulatory subunit-like proteins; The family includes a group of uncharacterized proteins that show high sequence similarity to vertebrate phosphatidylinositol 3-kinase regulatory subunits (PIK3Rs), which bind to activated (phosphorylated) protein-tyrosine kinases through its SH2 domain and regulate their kinase activity. Unlike typical PIK3Rs, members of this family have two C1 domains. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1034595019 173 HRFyKEKSKSVKQTCDKCNTIIWGLIQTWYTCTGCYYRCHSKC 215
Cdd:cd20830     1 HRF-VEQSFSTLQWCDKCGKFLFGLVHQGLQCQDCGLVCHRTC 42

protein kinase C conserved region 1 (C1 domain) found in the RAS guanyl-releasing protein (RASGRP) family; The RASGRP family includes RASGRP1-4. They function as cation-, usually calcium-, and diacylglycerol (DAG)-regulated nucleotide exchange factor activating Ras through the exchange of bound GDP for GTP. RASGRP1, also called calcium and DAG-regulated guanine nucleotide exchange factor II (CalDAG-GEFII) or Ras guanyl-releasing protein, activates the Erk/MAP kinase cascade and regulates T-cell/B-cell development, homeostasis and differentiation by coupling T-lymphocyte/B-lymphocyte antigen receptors to Ras. RASGRP1 also regulates NK cell cytotoxicity and ITAM-dependent cytokine production by activation of Ras-mediated ERK and JNK pathways. RASGRP2, also called calcium and DAG-regulated guanine nucleotide exchange factor I (CalDAG-GEFI), Cdc25-like protein (CDC25L), or F25B3.3 kinase-like protein, specifically activates Rap and may also activate other GTPases such as RRAS, RRAS2, NRAS, KRAS but not HRAS. RASGRP2 is involved in aggregation of platelets and adhesion of T-lymphocytes and neutrophils probably through inside-out integrin activation, as well as in the muscarinic acetylcholine receptor M1/CHRM1 signaling pathway. RASGRP3, also called calcium and DAG-regulated guanine nucleotide exchange factor III (CalDAG-GEFIII), or guanine nucleotide exchange factor for Rap1, is a guanine nucleotide-exchange factor activating H-Ras, R-Ras and Ras-associated protein-1/2. It functions as an important mediator of signaling downstream from receptor coupled phosphoinositide turnover in B and T cells. RASGRP4 may function in mast cell differentiation. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1034595019 172 EHRFYKeksksvKQTCDKCNTIIWGLIQTWYTCTGCYYRCHSKCLNLISKPC 223
Cdd:cd20808     6 ETTYFK------PTFCDHCTGLLWGLIKQGYKCKDCGINCHKHCKDLVVVEC 51

protein kinase C conserved region 1 (C1 domain) found in the unconventional myosin-IX family; Myosins IX (Myo9) is a class of unique motor proteins with a common structure of an N-terminal extension preceding a myosin head homologous to the Ras-association (RA) domain, a head (motor) domain, a neck with IQ motifs that bind light chains, and a C-terminal tail containing cysteine-rich zinc binding (C1) and Rho-GTPase activating protein (RhoGAP) domains. There are two genes for myosins IX in humans, IXa and IXb, that are different in their expression and localization. IXa is expressed abundantly in brain and testis, and IXb is expressed abundantly in tissues of the immune system. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1034595019 171 LEHRFYKEKSkSVKQTCDKCNTIIWgLIQTWYTCTGCYYRCHSKCLNLISKPC 223
Cdd:cd20818     2 NGHKFATVQF-NIPTYCEVCNSFIW-LMEKGLVCQVCKFTCHKKCYSKITAPC 52

protein kinase C conserved region 1 (C1 domain) found in Munc13-1 and similar proteins; Munc13-1, also called protein unc-13 homolog A (Unc13A), is a diacylglycerol (DAG) receptor that plays a role in vesicle maturation during exocytosis as a target of the diacylglycerol second messenger pathway. It is involved in neurotransmitter release by acting in synaptic vesicle priming prior to vesicle fusion and participates in the activity-dependent refilling of readily releasable vesicle pool (RRP). Loss of MUNC13-1 function causes microcephaly, cortical hyperexcitability, and fatal myasthenia. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.

                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1034595019 187 CDKCNTIIWGLIQTWYTCTGCYYRCHSKCLNLISKPC 223
Cdd:cd20858    21 CYECEGLLWGIARQGMRCTECGVKCHEKCQDLLNADC 57

protein kinase C conserved region 1 (C1 domain) found in tensin-2 like (TNS2-like) proteins; The TNS2-like group includes TNS2, and variants of TNS1 and TNS3. Tensin-2 (TNS2), also called C1 domain-containing phosphatase and tensin (C1-TEN), or tensin-like C1 domain-containing phosphatase (TENC1), is an essential component for the maintenance of glomerular basement membrane (GBM) structures. It regulates cell motility and proliferation. It may have phosphatase activity. TNS2 reduces AKT1 phosphorylation, lowers AKT1 kinase activity and interferes with AKT1 signaling. Tensin-1 (TNS1) plays a role in fibrillar adhesion formation. It may be involved in cell migration, cartilage development and in linking signal transduction pathways to the cytoskeleton. Tensin-3 (TNS3), also called tensin-like SH2 domain-containing protein 1 (TENS1), or tumor endothelial marker 6 (TEM6), may play a role in actin remodeling. It is involved in the dissociation of the integrin-tensin-actin complex. Typical TNS1 and TNS3 do not contain C1 domains, but some isoforms/variants do. Members of this family contain an N-terminal region with a zinc finger (C1 domain), a protein tyrosine phosphatase (PTP)-like domain and a protein kinase 2 (C2) domain, and a C-terminal region with SH2 and pTyr binding (PTB) domains. This model corresponds to C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1034595019 173 HRFyKEKSKSVKQTCDKCNTIIWGliqTWYTCTGCYYRCHSKCLNLISKPCVSS 226
Cdd:cd20826     3 HSF-KEKSFRKPRTCDVCKQIIWN---EGSSCRVCKYACHRKCEPKVTAACSPS 52

protein kinase C conserved region 1 (C1 domain) found in the kinase suppressor of Ras (KSR) family; KSR is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases, but there is some debate in this designation as a few groups have reported detecting kinase catalytic activity for KSRs, specifically KSR1. Vertebrates contain two KSR proteins, KSR1 and KSR2. KSR proteins contain a SAM-like domain, a zinc finger cysteine-rich domain (C1), and a pseudokinase domain. This model describes the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1034595019 172 EHRFykEKSKSVKQTCDKCNTIIWGliqtWYTCTGCYYRCHSKCLNLISKPC 223
Cdd:cd20812     2 KHRF--SKKLFMRQTCDYCHKQMFF----GLKCKDCKYKCHKKCAKKAPPSC 47

second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) theta, delta, and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. Members of this family contain two copies of C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1034595019 173 HRFYKEKSKSvKQTCDKCNTIIWGLIQTWYTCTGCYYRCHSKCLNLISKPC 223
Cdd:cd20837     1 HRFKVYNYMS-PTFCDHCGSLLWGLFRQGLKCEECGMNVHHKCQKKVANLC 50

protein kinase C conserved region 1 (C1 domain) found in uncharacterized Rho guanine nucleotide exchange factor (ARHGEF)-like proteins; The family includes a group of uncharacterized proteins that show high sequence similarity to vertebrate Rho guanine nucleotide exchange factors ARHGEF11 and ARHGEF12, which may play a role in the regulation of RhoA GTPase by guanine nucleotide-binding alpha-12 (GNA12) and alpha-13 (GNA13). Unlike typical ARHGEF11 and ARHGEF12, members of this family contain a C1 domain. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.

                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1034595019 187 CDKCNTIIWGLIQTWYTCTGCYYRCHSKCLNLISKPCV 224
Cdd:cd20832    15 CNHCSGLLWGIGYQGYQCSDCEFNIHKQCIEVIEESCP 52

protein kinase C conserved region 1 (C1 domain) found in RAS guanyl-releasing protein 3 (RASGRP3) and similar proteins; RASGRP3, also called calcium and DAG-regulated guanine nucleotide exchange factor III (CalDAG-GEFIII), or guanine nucleotide exchange factor for Rap1, is a guanine nucleotide-exchange factor activating H-Ras, R-Ras and Ras-associated protein-1/2. It functions as an important mediator of signaling downstream from receptor coupled phosphoinositide turnover in B and T cells. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.

                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1034595019 187 CDKCNTIIWGLIQTWYTCTGCYYRCHSKCLNLISKPC 223
Cdd:cd20862    21 CEHCAGFLWGIIKQGYKCKDCGVNCHKQCKDLLVLAC 57

protein kinase C conserved region 1 (C1 domain) found in unconventional myosin-IXa and similar proteins; Myosin-IXa, also called unconventional myosin-9a (Myo9a), is a single-headed, actin-dependent motor protein of the unconventional myosin IX class. It is expressed in several tissues and is enriched in the brain and testes. Myosin-IXa contains a Ras-associating (RA) domain, a motor domain, a protein kinase C conserved region 1 (C1), and a Rho GTPase activating domain (RhoGAP). Myosin-IXa binds the alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptor (AMPAR) GluA2 subunit, and plays a key role in controlling the molecular structure and function of hippocampal synapses. Moreover, Myosin-IXa functions in epithelial cell morphology and differentiation, such that its knockout mice develop hydrocephalus and kidney dysfunction. Myosin-IXa regulates collective epithelial cell migration by targeting RhoGAP activity to cell-cell junctions. Myosin-IXa negatively regulates Rho GTPase signaling, and functions as a regulator of kidney tubule function. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1034595019 176 YKEKSKSVKQTCDKCNTIIWgLIQTWYTCTGCYYRCHSKCLNLISKPC 223
Cdd:cd20883     8 FKSTQYSIPTYCEYCSSLIW-MMDRAYVCKLCRYACHKKCCLKTTTKC 54