C2 domain present in E3 ubiquitin ligase; E3 ubiquitin ligase is part of the ubiquitylation mechanism responsible for controlling surface expression of membrane proteins. The sequential action of several enzymes are involved: ubiquitin-activating enzyme E1, ubiquitin-conjugating enzyme E2, and ubiquitin-protein ligase E3 which is responsible for substrate recognition and promoting the transfer of ubiquitin to the target protein. E3 ubiquitin ligase is composed of an N-terminal C2 domain, 4 WW domains, and a HECTc domain. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394581985  17 KSQLTLKVVSAKPKVHNRQPRINSYVEVAVDGLPSetKKTGKRIGSSELLWNEIIILNVTAQSHLDLKVWSCHTLR-NEL 95
Cdd:cd04021    1 KSQLQITVESAKLKSNSKSFKPDPYVEVTVDGQPP--KKTEVSKKTSNPKWNEHFTVLVTPQSTLEFKVWSHHTLKaDVL 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 394581985  96 LGTASVNLSNVLKNNGGKMENMQLTLNLQTENKGSVVSGGELTIFLD 142
Cdd:cd04021   79 LGEASLDLSDILKNHNGKLENVKLTLNLSSENKGSSVKVGELTVILD 125

DNA polymerase III subunit gamma/tau;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394581985 172 AVAPENRHQPPSTNCFGGRSRTHRHSGASARTTPATGEQSPGARSRH--RQPVKNSGHSGLANGTVNDEPTTATDPEEPS 249
Cdd:PRK07003 423 AEAPPAAPAPPATADRGDDAADGDAPVPAKANARASADSRCDERDAQppADSGSASAPASDAPPDAAFEPAPRAAAPSAA 502

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 394581985 250 VVGVTSPPAAPLSVtpnpnttslPAPATPAEGEEPSTSGTQQLPAAAQAP 299
Cdd:PRK07003 503 TPAAVPDARAPAAA---------SREDAPAAAAPPAPEARPPTPAAAAPA 543

C2 domain present in E3 ubiquitin ligase; E3 ubiquitin ligase is part of the ubiquitylation mechanism responsible for controlling surface expression of membrane proteins. The sequential action of several enzymes are involved: ubiquitin-activating enzyme E1, ubiquitin-conjugating enzyme E2, and ubiquitin-protein ligase E3 which is responsible for substrate recognition and promoting the transfer of ubiquitin to the target protein. E3 ubiquitin ligase is composed of an N-terminal C2 domain, 4 WW domains, and a HECTc domain. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394581985  17 KSQLTLKVVSAKPKVHNRQPRINSYVEVAVDGLPSetKKTGKRIGSSELLWNEIIILNVTAQSHLDLKVWSCHTLR-NEL 95
Cdd:cd04021    1 KSQLQITVESAKLKSNSKSFKPDPYVEVTVDGQPP--KKTEVSKKTSNPKWNEHFTVLVTPQSTLEFKVWSHHTLKaDVL 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 394581985  96 LGTASVNLSNVLKNNGGKMENMQLTLNLQTENKGSVVSGGELTIFLD 142
Cdd:cd04021   79 LGEASLDLSDILKNHNGKLENVKLTLNLSSENKGSSVKVGELTVILD 125

Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.

                         10        20
                 ....*....|....*....|....*....
gi 394581985 303 PAGWEQRELPNGRVYYVDHNTKTTTWERP 331
Cdd:cd00201    1 PPGWEERWDPDGRVYYYNHNTKETQWEDP 29

Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, protein kinases C, and synaptotagmins (among others). Some do not appear to contain Ca2+-binding sites. Particular C2s appear to bind phospholipids, inositol polyphosphates, and intracellular proteins. Unusual occurrence in perforin. Synaptotagmin and PLC C2s are permuted in sequence with respect to N- and C-terminal beta strands. SMART detects C2 domains using one or both of two profiles.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394581985    19 QLTLKVVSAKPKVHNRQPR-INSYVEVAVDGLPSETKKTGKRIGSSELLWNEIIILNVT--AQSHLDLKVWS-CHTLRNE 94
Cdd:smart00239   1 TLTVKIISARNLPPKDKGGkSDPYVKVSLDGDPKEKKKTKVVKNTLNPVWNETFEFEVPppELAELEIEVYDkDRFGRDD 80

                           90       100
                   ....*....|....*....|.
gi 394581985    95 LLGTASVNLSNVLKNNGGKME 115
Cdd:smart00239  81 FIGQVTIPLSDLLLGGRHEKL 101

C2 domain present in E3 ubiquitin ligase; E3 ubiquitin ligase is part of the ubiquitylation mechanism responsible for controlling surface expression of membrane proteins. The sequential action of several enzymes are involved: ubiquitin-activating enzyme E1, ubiquitin-conjugating enzyme E2, and ubiquitin-protein ligase E3 which is responsible for substrate recognition and promoting the transfer of ubiquitin to the target protein. E3 ubiquitin ligase is composed of an N-terminal C2 domain, 4 WW domains, and a HECTc domain. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394581985  17 KSQLTLKVVSAKPKVHNRQPRINSYVEVAVDGLPSetKKTGKRIGSSELLWNEIIILNVTAQSHLDLKVWSCHTLR-NEL 95
Cdd:cd04021    1 KSQLQITVESAKLKSNSKSFKPDPYVEVTVDGQPP--KKTEVSKKTSNPKWNEHFTVLVTPQSTLEFKVWSHHTLKaDVL 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 394581985  96 LGTASVNLSNVLKNNGGKMENMQLTLNLQTENKGSVVSGGELTIFLD 142
Cdd:cd04021   79 LGEASLDLSDILKNHNGKLENVKLTLNLSSENKGSSVKVGELTVILD 125

Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.

                         10        20
                 ....*....|....*....|....*....
gi 394581985 303 PAGWEQRELPNGRVYYVDHNTKTTTWERP 331
Cdd:cd00201    1 PPGWEERWDPDGRVYYYNHNTKETQWEDP 29

Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, protein kinases C, and synaptotagmins (among others). Some do not appear to contain Ca2+-binding sites. Particular C2s appear to bind phospholipids, inositol polyphosphates, and intracellular proteins. Unusual occurrence in perforin. Synaptotagmin and PLC C2s are permuted in sequence with respect to N- and C-terminal beta strands. SMART detects C2 domains using one or both of two profiles.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394581985    19 QLTLKVVSAKPKVHNRQPR-INSYVEVAVDGLPSETKKTGKRIGSSELLWNEIIILNVT--AQSHLDLKVWS-CHTLRNE 94
Cdd:smart00239   1 TLTVKIISARNLPPKDKGGkSDPYVKVSLDGDPKEKKKTKVVKNTLNPVWNETFEFEVPppELAELEIEVYDkDRFGRDD 80

                           90       100
                   ....*....|....*....|.
gi 394581985    95 LLGTASVNLSNVLKNNGGKME 115
Cdd:smart00239  81 FIGQVTIPLSDLLLGGRHEKL 101

large tegument protein UL36; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394581985  164 PSRDSSGTAVAPENRHqPPSTNCFGGRSRTHRHSGASARTTPATGEQ----SPGARSRHRQpVKNSGHSGLANGTVNDEP 239
Cdd:PHA03247 2607 DPRGPAPPSPLPPDTH-APDPPPPSPSPAANEPDPHPPPTVPPPERPrddpAPGRVSRPRR-ARRLGRAAQASSPPQRPR 2684

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 394581985  240 TTATDPEEPSVVGVTSPPAAPLSVTPNPNTTSLPAPATP----AEGEEPSTSGTQQLPAAAQAPdALPAGWEQRELP 312
Cdd:PHA03247 2685 RRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPgpaaARQASPALPAAPAPPAVPAGP-ATPGGPARPARP 2760

large tegument protein UL36; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394581985  135 GELTIFLDGPTVDLGNVPNGSALTDGSQLPSRDSSGTAVAPENRHQPPSTncfggrsrthrhSGASARTTPAtGEQSPGA 214
Cdd:PHA03247 2693 GSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPP------------AVPAGPATPG-GPARPAR 2759

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394581985  215 RSRHRQPVKNSGHSGLANGTVNDEPTTATDPEEPSVVGVTSPP-AAPLSVTPNPNTTSLPAPATPAEGEEPSTSGTQQLP 293
Cdd:PHA03247 2760 PPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWdPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAP 2839

                         170       180
                  ....*....|....*....|...
gi 394581985  294 AAAQAPDALPAGWEQRELPNGRV 316
Cdd:PHA03247 2840 PPPPGPPPPSLPLGGSVAPGGDV 2862