WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.

                           10        20        30
                   ....*....|....*....|....*....|
gi 1191844490   12 LPRGWEEARDYDGKVFYIDHNTRRTSWIDP 41
Cdd:pfam00397    1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191844490  176 KKLKRELSQMKQELLYKEQGFATLKQidkkmsggqsgyelsEAKAILTELKSIRKAISSGEKEKQDLMQSLAKLQERFhl 255
Cdd:COG4942     23 AEAEAELEQLQQEIAELEKELAALKK---------------EEKALLKQLAALERRIAALARRIRALEQELAALEAEL-- 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191844490  256 dQSTGTSEPDLRSSPVNSHLSLSRQTLDAGSQTSISGDIGVRSRSNLAEKVRLSLQYEEAKRSMANLKIELSKLDSEawp 335
Cdd:COG4942     86 -AELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE--- 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191844490  336 galdIEKEKLMLINEKEELLKELQFITPQRRtqdELESLDAERQRLEEELLSVRGAPSRALAERLKLEERRKELLQKLEE 415
Cdd:COG4942    162 ----LAALRAELEAERAELEALLAELEEERA---ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA 234

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.

                           10        20        30
                   ....*....|....*....|....*....|
gi 1191844490   12 LPRGWEEARDYDGKVFYIDHNTRRTSWIDP 41
Cdd:pfam00397    1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30

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        30
                   ....*....|....*....|....*....|.
gi 1191844490   13 PRGWEEARDYDGKVFYIDHNTRRTSWIDPRD 43
Cdd:cd00201      1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31

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 1191844490   62 GWEAGFDPQIGVYYIDHINKTTQIEDPR 89
Cdd:cd00201      3 GWEERWDPDGRVYYYNHNTKETQWEDPR 30

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191844490  176 KKLKRELSQMKQELLYKEQGFATLKQidkkmsggqsgyelsEAKAILTELKSIRKAISSGEKEKQDLMQSLAKLQERFhl 255
Cdd:COG4942     23 AEAEAELEQLQQEIAELEKELAALKK---------------EEKALLKQLAALERRIAALARRIRALEQELAALEAEL-- 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191844490  256 dQSTGTSEPDLRSSPVNSHLSLSRQTLDAGSQTSISGDIGVRSRSNLAEKVRLSLQYEEAKRSMANLKIELSKLDSEawp 335
Cdd:COG4942     86 -AELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE--- 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191844490  336 galdIEKEKLMLINEKEELLKELQFITPQRRtqdELESLDAERQRLEEELLSVRGAPSRALAERLKLEERRKELLQKLEE 415
Cdd:COG4942    162 ----LAALRAELEAERAELEALLAELEEERA---ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA 234

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191844490  137 DAYKEKSSSRTSLFSGSSSSTKYDPDILKAEISTTRLRVKKLKRELSQMKqeLLYKEQGfatlkQIDKKMSGGQSGYELS 216
Cdd:pfam15905   34 AAESQPNLNNSKDASTPATARKVKSLELKKKSQKNLKESKDQKELEKEIR--ALVQERG-----EQDKRLQALEEELEKV 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191844490  217 EAK--AILTELKSIRKAISSGEKEKQDLMQSLAKLQERFHLDqstGTSEpdlRSSPVNSHLSLSRQTLDAGSQTSISGDI 294
Cdd:pfam15905  107 EAKlnAAVREKTSLSASVASLEKQLLELTRVNELLKAKFSED---GTQK---KMSSLSMELMKLRNKLEAKMKEVMAKQE 180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191844490  295 GVRSRSNLAEKvrlslQYEEAKRSMANLKIELSkldseawpgalDIEKEKlmlINEKEELLKELQFITPQRRTQDELESL 374
Cdd:pfam15905  181 GMEGKLQVTQK-----NLEHSKGKVAQLEEKLV-----------STEKEK---IEEKSETEKLLEYITELSCVSEQVEKY 241

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1191844490  375 DAERQRLEE-------ELLSVRGAPSRALAERLKLEERRKELLQKLE-ETTKLTTYLHSQLKNLSA 432
Cdd:pfam15905  242 KLDIAQLEEllkekndEIESLKQSLEEKEQELSKQIKDLNEKCKLLEsEKEELLREYEEKEQTLNA 307

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.

                           10        20        30
                   ....*....|....*....|....*....|
gi 1191844490   12 LPRGWEEARDYDGKVFYIDHNTRRTSWIDP 41
Cdd:pfam00397    1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30

C2 domain third repeat present in uncharacterized human KIAA1228-like proteins; KIAA proteins are uncharacterized human proteins. They were compiled by the Kazusa mammalian cDNA project which identified more than 2000 human genes. They are identified by 4 digit codes that precede the KIAA designation. Many KIAA genes are still functionally uncharacterized including KIAA1228. 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. This cd contains the third C2 repeat, C2C, and has a type-II topology.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191844490  697 ETAQVQIGLRYDAKSSSFLVIIAQLRNLHVFLIPHTSKVYFRVALLPSSTdVSCLFRTKVHPAMESMLFNDPFRVAISQT 776
Cdd:cd04030      1 PLGRIQLTIRYSSQRQKLIVTVHKCRNLPPCDSSDIPDPYVRLYLLPDKS-KSTRRKTSVKKDNLNPVFDETFEFPVSLE 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1191844490  777 ALQQKTLRVDLC-SVSRHRREECLAGT-QISLADLPFSNEiFTLWYNL 822
Cdd:cd04030     80 ELKRRTLDVAVKnSKSFLSREKKLLGQvLIDLSDLDLSKG-FTQWYDL 126

C2A domain first repeat present in Synaptotagmin 8; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. 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. This cd contains the first C2 repeat, C2A, and has a type-I topology.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191844490  698 TAQVQIGLRYDAKSSSFLVIIAQLRNLHVFLIPHTSKVYFRVALLPsstDVSCLFRTKVHPAMESMLFNDPFRVAISQTA 777
Cdd:cd08387      2 RGELHFSLEYDKDMGILNVKLIQARNLQPRDFSGTADPYCKVRLLP---DRSNTKQSKIHKKTLNPEFDESFVFEVPPQE 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1191844490  778 LQQKTLRVDLCSVSRHRREECLAGTQISLADLPFSNEIfTLW 819
Cdd:cd08387     79 LPKRTLEVLLYDFDQFSRDECIGVVELPLAEVDLSEKL-DLW 119

C2 domain first repeat present in Synaptotagmin-like proteins; All Slp members basically share an N-terminal Slp homology domain (SHD) and C-terminal tandem C2 domains (named the C2A domain and the C2B domain) with the SHD and C2 domains being separated by a linker sequence of various length. Slp1/JFC1 and Slp2/exophilin 4 promote granule docking to the plasma membrane. Additionally, their C2A domains are both Ca2+ independent, unlike the case in Slp3 and Slp4/granuphilin in which their C2A domains are Ca2+ dependent. It is thought that SHD (except for the Slp4-SHD) functions as a specific Rab27A/B-binding domain. In addition to Slps, rabphilin, Noc2, and Munc13-4 also function as Rab27-binding proteins. It has been demonstrated that Slp3 and Slp4/granuphilin promote dense-core vesicle exocytosis. Slp5 mRNA has been shown to be restricted to human placenta and liver suggesting a role in Rab27A-dependent membrane trafficking in specific tissues. 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. This cd contains the first C2 repeat, C2A, and has a type-I topology.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191844490  700 QVQIGLRYDAKSSSFLVIIAQLRNL-HVFLIPHTSKVYFRVALLPSSTDVSCLfRTKVHPAMESMLFNDPFRVAISQTAL 778
Cdd:cd08521      2 EIEFSLSYNYKTGSLEVHIKECRNLaYADEKKKRSNPYVKVYLLPDKSKQSKR-KTSVKKNTTNPVFNETLKYHISKSQL 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1191844490  779 QQKTLRVdlcSVSRHR---REECLAGTQISLADLPFSNEIFtLWYNL 822
Cdd:cd08521     81 ETRTLQL---SVWHHDrfgRNTFLGEVEIPLDSWDLDSQQS-EWYPL 123

Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.

                            10        20        30
                    ....*....|....*....|....*....|.
gi 1191844490    59 LPWGWEAGFDPQIGVYYIDHINKTTQIEDPR 89
Cdd:smart00456    2 LPPGWEERKDPDGRPYYYNHETKETQWEKPR 32

C2A domain first repeat present in Synaptotagmins 1, 5, 6, 9, and 10; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Synaptotagmin 1, a member of class 1 synaptotagmins, is located in the brain and endocranium and localized to the synaptic vesicles and secretory granules. It functions as a Ca2+ sensor for fast exocytosis as do synaptotagmins 5, 6, and 10. It is distinguished from the other synaptotagmins by having an N-glycosylated N-terminus. Synaptotagmins 5, 6, and 10, members of class 3 synaptotagmins, are located primarily in the brain and localized to the active zone and plasma membrane. They is distinguished from the other synaptotagmins by having disulfide bonds at its N-terminus. Synaptotagmin 6 also regulates the acrosome reaction, a unique Ca2+-regulated exocytosis, in sperm. Synaptotagmin 9, a class 5 synaptotagmins, is located in the brain and localized to the synaptic vesicles. It is thought to be a Ca2+-sensor for dense-core vesicle exocytosis. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. 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. This cd contains the first C2 repeat, C2A, and has a type-I topology.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191844490  701 VQIGLRYDAKSSSFLVIIAQLRNLHVFLIPHTSKVYFRVALLPsstDVSCLFRTKVHPAMESMLFNDPFRVAISQTALQQ 780
Cdd:cd08385      5 LQFSLDYDFQSNQLTVGIIQAADLPAMDMGGTSDPYVKVYLLP---DKKKKFETKVHRKTLNPVFNETFTFKVPYSELGN 81

                           90
                   ....*....|....*.
gi 1191844490  781 KTLRV---DLCSVSRH 793
Cdd:cd08385     82 KTLVFsvyDFDRFSKH 97

C2 domain; The C2 domain was first identified in PKC. 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 1191844490  716 VIIAQLRNLHVFLIPHTSKVYFRVALLPSSTdvsclFRTKVHPAMESMLFNDPFRVAISQTalQQKTLRVDLCSVSRHRR 795
Cdd:cd00030      3 VTVIEARNLPAKDLNGKSDPYVKVSLGGKQK-----FKTKVVKNTLNPVWNETFEFPVLDP--ESDTLTVEVWDKDRFSK 75

                           90       100
                   ....*....|....*....|....*..
gi 1191844490  796 EECLAGTQISLADLPFSNEIFTLWYNL 822
Cdd:cd00030     76 DDFLGEVEIPLSELLDSGKEGELWLPL 102

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191844490  206 MSGG--QSGYELSEAKAILTELKSIRKAISSGEKEKQDLMQSLAKL-QERFHLDQSTGTSEPDLRSspvnshLSLSRQTL 282
Cdd:TIGR02169  655 MTGGsrAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIeNRLDELSQELSDASRKIGE------IEKEIEQL 728

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191844490  283 DAGSQTSisgdigvrsrSNLAEKVRLSLQYEEAKRsmANLKIELSKLDSEAWPGALDIEKEKLMLINEKEELLKElqfit 362
Cdd:TIGR02169  729 EQEEEKL----------KERLEELEEDLSSLEQEI--ENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHS----- 791

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1191844490  363 PQRRTQDELESLDAERQRLEEELLSVRGAPSRALAERLKLEERRKELLQKLEETT 417
Cdd:TIGR02169  792 RIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLK 846

C2 domain first repeat present in Synaptotagmin-like proteins 1 and 2; All Slp members basically share an N-terminal Slp homology domain (SHD) and C-terminal tandem C2 domains (named the C2A domain and the C2B domain) with the SHD and C2 domains being separated by a linker sequence of various length. Slp1/JFC1 and Slp2/exophilin 4 promote granule docking to the plasma membrane. Additionally, their C2A domains are both Ca2+ independent, unlike Slp3 and Slp4/granuphilin which are Ca2+ dependent. It is thought that SHD (except for the Slp4-SHD) functions as a specific Rab27A/B-binding domain. In addition to Slps, rabphilin, Noc2, and Munc13-4 also function as Rab27-binding proteins. 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. This cd contains the first C2 repeat, C2A, and has a type-I topology.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191844490  701 VQIGLRYDAKSSSFLVIIAQLRNLHVFLI-PHTSKVYFRVALLPSSTDVSCLfRTKVHPAMESMLFNDPFRVAISQTALQ 779
Cdd:cd08393      4 VQFALDYDPKLRELHVHVIQCQDLAAADPkKQRSDPYVKTYLLPDKSNRGKR-KTSVKKKTLNPVFNETLRYKVEREELP 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1191844490  780 QKTLRVDLCSVSRHRREECLAGTQISLADLPFSNEIFTlWYNL 822
Cdd:cd08393     83 TRVLNLSVWHRDSLGRNSFLGEVEVDLGSWDWSNTQPT-WYPL 124

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191844490  119 HVKEQRL*LALDEYVRLNDayKEKSSSRTSlfsgsssstkydpDILKAEISTTRLRVKKLKRELSQMKQELlykeQGfat 198
Cdd:pfam15921  387 HKREKELSLEKEQNKRLWD--RDTGNSITI-------------DHLRRELDDRNMEVQRLEALLKAMKSEC----QG--- 444

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191844490  199 lkQIDKKMSGGQSGYELSEAKAILT---------------ELKSIRKAISSGEKEKQDLMQSLA---------------- 247
Cdd:pfam15921  445 --QMERQMAAIQGKNESLEKVSSLTaqlestkemlrkvveELTAKKMTLESSERTVSDLTASLQekeraieatnaeitkl 522

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191844490  248 ------KLQERFHLDQ--------STGTSEPDLRSSPVNSHLSLSRQTLDagSQTSISGDIGVRSRSNLAEKVRLSLQYE 313
Cdd:pfam15921  523 rsrvdlKLQELQHLKNegdhlrnvQTECEALKLQMAEKDKVIEILRQQIE--NMTQLVGQHGRTAGAMQVEKAQLEKEIN 600

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191844490  314 EAKRSMANLKIELSKLDS---EAWPGALDIEKEKLMLINEKEELLKELQFITpQRRTQ--DELESLDAERQRLEEELlsv 388
Cdd:pfam15921  601 DRRLELQEFKILKDKKDAkirELEARVSDLELEKVKLVNAGSERLRAVKDIK-QERDQllNEVKTSRNELNSLSEDY--- 676

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 1191844490  389 rgapsralaERLKLEERRKEllqklEETTKLTTYLHSQLKN 429
Cdd:pfam15921  677 ---------EVLKRNFRNKS-----EEMETTTNKLKMQLKS 703

C2 domain second repeat present in Synaptotagmin; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. There are several classes of Synaptotagmins. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. 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. This cd contains the second C2 repeat, C2B, and has a type-I topology.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191844490  699 AQVQIGLRYDAKSSSFLVIIAQLRNLHVFLIPHTSKVYFRVALLPSSTDVSClFRTKVHPAMESMLFNDPFRVAISQTAL 778
Cdd:cd00276      1 GELLLSLSYLPTAERLTVVVLKARNLPPSDGKGLSDPYVKVSLLQGGKKLKK-KKTSVKKGTLNPVFNEAFSFDVPAEQL 79

                           90       100
                   ....*....|....*....|.
gi 1191844490  779 QQKTLRVDLCSVSRHRREECL 799
Cdd:cd00276     80 EEVSLVITVVDKDSVGRNEVI 100

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191844490  164 LKAEISTTRLRVKKLKrelsqmkqelLYKEQGFATLKQIDKKMSGGQ--------SGYEL--------SEAKAILTELKS 227
Cdd:pfam15921  595 LEKEINDRRLELQEFK----------ILKDKKDAKIRELEARVSDLElekvklvnAGSERlravkdikQERDQLLNEVKT 664

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191844490  228 IRKAISSGEKEKQDLMQSLAKLQErfhlDQSTGTSEPDLRSSPVNSHLSLSRQTLdagsqTSISGDIGvrsrsnLAEKVR 307
Cdd:pfam15921  665 SRNELNSLSEDYEVLKRNFRNKSE----EMETTTNKLKMQLKSAQSELEQTRNTL-----KSMEGSDG------HAMKVA 729

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191844490  308 LSLQYE-EAKRSMANLKIELSKLDSEAWPGAldiEKEKLMLINEKEELLKELQFI-TPQRRTQDELESLDAERQRLEEEL 385
Cdd:pfam15921  730 MGMQKQiTAKRGQIDALQSKIQFLEEAMTNA---NKEKHFLKEEKNKLSQELSTVaTEKNKMAGELEVLRSQERRLKEKV 806

                          250       260       270
                   ....*....|....*....|....*....|....
gi 1191844490  386 LSVRGAPSRAlaeRLKLEERRKELLQKLEETTKL 419
Cdd:pfam15921  807 ANMEVALDKA---SLQFAECQDIIQRQEQESVRL 837