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Conserved domains on  [gi|2032737686|ref|XP_041333638|]
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protein piccolo [Pyrgilauda ruficollis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
C2A_RIM1alpha cd04031
C2 domain first repeat contained in Rab3-interacting molecule (RIM) proteins; RIMs are ...
 4721-4855 3.42e-66

C2 domain first repeat contained in Rab3-interacting molecule (RIM) proteins; RIMs are believed to organize specialized sites of the plasma membrane called active zones. They also play a role in controlling neurotransmitter release, plasticity processes, as well as memory and learning. RIM contains an N-terminal zinc finger domain, a PDZ domain, and two C-terminal C2 domains (C2A, C2B). 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. Members here have a type-I topology and do not bind Ca2+.


:

Pssm-ID: 175997 [Multi-domain]  Cd Length: 125  Bit Score: 220.97  E-value: 3.42e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4721 ITGEIQLQINYDKHLGNLIIHILQARNLAPRDNNGYSDPFVKVYLLPGRgqvmvvqnaSAEYKRRTKYIQKSLNPEWNQT 4800
Cdd:cd04031      1 ITGRIQIQLWYDKVTSQLIVTVLQARDLPPRDDGSLRNPYVKVYLLPDR---------SEKSKRRTKTVKKTLNPEWNQT 71

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2032737686 4801 VIYKNISVEQLKKKTLEVTVWDYDRFSSNDFLGEVLIELSSiSQLDNTPRWYPLK 4855
Cdd:cd04031     72 FEYSNVRRETLKERTLEVTVWDYDRDGENDFLGEVVIDLAD-ALLDDEPHWYPLQ 125
PDZ_RIM-like cd06714
PDZ domain of Rab3-interacting molecule 1 (RIM), RIM2, piccolo and related domains; PDZ ...
 4520-4615 3.54e-49

PDZ domain of Rab3-interacting molecule 1 (RIM), RIM2, piccolo and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of RIM, RIM2, piccolo and related domains. RIM proteins and Gallus gallus protein piccolo (also called aczonin) are involved in neurotransmitter release at presynaptic active zones, the site of vesicle fusion. A protein complex containing RIM proteins positions synaptic vesicles containing synaptotagmin at the active zone. RIM proteins simultaneously activate docking and priming of synaptic vesicles and recruit Ca2+-channels to active zones, thereby connecting primed synaptic vesicles to Ca2+-channels. RIM binding to vesicular Rab proteins (Rab3 and Rab27 isoforms) mediates vesicle docking; RIM binding to Munc13 activates vesicle priming; RIM binding to the Ca2+-channel, both directly and indirectly via RIM-BP, recruits the Ca2+-channels. The RIM PDZ domain interacts with the C-termini of N- and P/Q-type voltage-gated Ca2+-channels. RIM1, RIM2 and piccolo also participate in regulated exocytosis through binding cAMP-GEFII (cAMP-binding protein-guanidine nucleotide exchange factor II). The piccolo PDZ domain binds cAMP-GEFII. RIM2 also plays a role in dendrite formation by melanocytes. Caenorhabditis elegans RIM (also known as unc-10) may be involved in the regulation of defecation and daumone response. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This RIM-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


:

Pssm-ID: 467198 [Multi-domain]  Cd Length: 95  Bit Score: 170.81  E-value: 3.54e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4520 FPHTRLKLLRDPKDHTVSGNGLGIRVVGGKEIPgsSGEIGAYIAKILPGGNAEQTGKLVEGMQVLEWNGIPLTGKTYEEV 4599
Cdd:cd06714      2 FLIGRIILQRDPKDGSVSGNGLGLKVVGGKMTE--SGRLGAYVTKVKPGSVADTVGHLREGDEVLEWNGISLQGKTFEEV 79

                           90
                   ....*....|....*.
gi 2032737686 4600 QSIIIQQSGEAEICVR 4615
Cdd:cd06714     80 QDIISQSKGEVELVVS 95
FYVE2_PCLO cd15776
FYVE-related domain 2 found in protein piccolo; Protein piccolo, also termed aczonin, is a ...
 919-982 2.68e-42

FYVE-related domain 2 found in protein piccolo; Protein piccolo, also termed aczonin, is a neuron-specific presynaptic active zone scaffolding protein that mainly interacts with a detergent-resistant cytoskeletal-like subcellular fraction and is involved in the organization of the interplay between neurotransmitter vesicles, the cytoskeleton, and the plasma membrane at synaptic active zones. It binds profilin, an actin-binding protein implicated in actin cytoskeletal dynamics. It also functions as a presynaptic low-affinity Ca2+ sensor and has been implicated in Ca2+ regulation of neurotransmitter release. Piccolo is a multi-domain protein containing two N-terminal FYVE zinc fingers, a polyproline tract, and a PDZ domain and two C-terminal C2 domains. This family corresponds to the second FYVE domain, which resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif.


:

Pssm-ID: 277315 [Multi-domain]  Cd Length: 64  Bit Score: 150.22  E-value: 2.68e-42
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2032737686  919 MSCPLCKTGLNIGSKDPPNFNTCTECKKVVCNLCGFNPMPHIAEVQEWLCLNCQTQRAMSGQLG 982
Cdd:cd15776      1 LLCPLCKTELNIGSKDPPNFNTCTECKKTVCNLCGFNPTPHLTEVKEWLCLNCQTQRAMSGQLG 64
FYVE1_PCLO cd15774
FYVE-related domain 1 found in protein piccolo; Protein piccolo, also termed aczonin, is a ...
 452-513 8.03e-42

FYVE-related domain 1 found in protein piccolo; Protein piccolo, also termed aczonin, is a neuron-specific presynaptic active zone scaffolding protein that mainly interacts with a detergent-resistant cytoskeletal-like subcellular fraction and is involved in the organization of the interplay between neurotransmitter vesicles, the cytoskeleton, and the plasma membrane at synaptic active zones. It binds profilin, an actin-binding protein implicated in actin cytoskeletal dynamics. It also functions as a presynaptic low-affinity Ca2+ sensor and has been implicated in Ca2+ regulation of neurotransmitter release. Piccolo is a multi-domain protein containing two N-terminal FYVE zinc fingers, a polyproline tract, and a PDZ domain and two C-terminal C2 domains. This family corresponds to the first FYVE domain, which resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif.


:

Pssm-ID: 277313 [Multi-domain]  Cd Length: 62  Bit Score: 148.64  E-value: 8.03e-42
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2032737686  452 TFCPLCTTTELLLHTPEKANYNTCTQCHTVVCSLCGFNPNPHITEISEWLCLNCQMQRTLGG 513
Cdd:cd15774      1 TICPLCKTTELLLHTPEKANYNTCTQCQTTVCSLCGFNPNPHITEKKEWLCLNCQMQRALGG 62
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 188-736 3.91e-24

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 113.49  E-value: 3.91e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  188 QKVAPKEQGKPEEQRSPAKHPTQP-QSPKPAVQQQGPVRPTVQQTESskqqqqpggpkqvqKPGhgqpADAKQDQAKQPA 266
Cdd:PHA03247  2541 EELASDDAGDPPPPLPPAAPPAAPdRSVPPPRPAPRPSEPAVTSRAR--------------RPD----APPQSARPRAPV 2602

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  267 QPRGPQKSQPQPSePTKPIQQQTSAKPSSG------------PTKPSPQQPDSTKVTSQTAPPTKPSSQ-QPGPAKQPSQ 333
Cdd:PHA03247  2603 DDRGDPRGPAPPS-PLPPDTHAPDPPPPSPspaanepdphppPTVPPPERPRDDPAPGRVSRPRRARRLgRAAQASSPPQ 2681

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  334 QPARQGAPVK----------PSPQQTGPPKQPSQQPGPEKPSAQQAGPAKQPPQPGSGKPPPQQTGLVKQVPPQAGPTkp 403
Cdd:PHA03247  2682 RPRRRAARPTvgsltsladpPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPAR-- 2759

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  404 PSQTVGPTKPLAQQAGPTKPPGQQPGPE-KPPQQTQAGANQPTETAPKKTFCPLCTTTELLLHTPEKANYNTCTQCHTVV 482
Cdd:PHA03247  2760 PPTTAGPPAPAPPAAPAAGPPRRLTRPAvASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAP 2839

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  483 CSLCGFNPNPhiteisewlclncqmqRTLGGDLAPG----LGPGPQPLAPKQKTPIPPSAKPSPQPQPVQKKDVTPKPDP 558
Cdd:PHA03247  2840 PPPPGPPPPS----------------LPLGGSVAPGgdvrRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPD 2903

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  559 SQAadskrPPPQkkqtqlPGSPPvkskQPRAEPTDISQQTDATPKSDQVKPtqaeDKQKQPSVQKPTADSVSTSVAAEQK 638
Cdd:PHA03247  2904 QPE-----RPPQ------PQAPP----PPQPQPQPPPPPQPQPPPPPPPRP----QPPLAPTTDPAGAGEPSGAVPQPWL 2964

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  639 QDLAGPRPPTQQKVTDSPKPELAKPSQDTHPagdkPDSKPVPQVSRQKSDPKFASQPGARPDAKAQK--PIDPTQTKDDP 716
Cdd:PHA03247  2965 GALVPGRVAVPRFRVPQPAPSREAPASSTPP----LTGHSLSRVSSWASSLALHEETDPPPVSLKQTlwPPDDTEDSDAD 3040

                          570       580
                   ....*....|....*....|....*.
gi 2032737686  717 KKLPTKP------APKPDTkPAPKGP 736
Cdd:PHA03247  3041 SLFDSDSersdleALDPLP-PEPHDP 3065
PTZ00121 super family cl31754
MAEBL; Provisional
 1029-1729 4.34e-15

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 83.27  E-value: 4.34e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1029 AKPKEEPGVQKEAPKLQQGRLEKTlsaDKIQQGIQKEDAKpKQGKLVKAPSADKIQHASQKEDPRiQQTKLTKTASYDRV 1108
Cdd:PTZ00121  1242 AKKAEEERNNEEIRKFEEARMAHF---ARRQAAIKAEEAR-KADELKKAEEKKKADEAKKAEEKK-KADEAKKKAEEAKK 1316

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1109 LQEVQKEDE----KLQEAKLAKTSSADKILHRVQKEDIKLQEAKLAKVPS-ADKILQGIQKEDPKLQQMKMAKALSADKI 1183
Cdd:PTZ00121  1317 ADEAKKKAEeakkKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAeAAEKKKEEAKKKADAAKKKAEEKKKADEA 1396

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1184 QLAAQREDTKLQEVKlpKAASVDKiqhgTQKDIKLQHEKIKKTSSVDKIQEEGQK-EETKLQRGKLSKTPSADKIPATAT 1262
Cdd:PTZ00121  1397 KKKAEEDKKKADELK--KAAAAKK----KADEAKKKAEEKKKADEAKKKAEEAKKaDEAKKKAEEAKKAEEAKKKAEEAK 1470

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1263 ADQKIPLSTLEEDKETVLPEKSTPHPEDKKEEITAEIKDRVAEEKAEVEAPYKGLQAKEEEDVKKEDLTTgisqvvlKAE 1342
Cdd:PTZ00121  1471 KADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAK-------KAE 1543

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1343 KAQEAEIPVQTAPLPGTDHVEAVREKIEKEDDKSDTSSSQQQKSPqglsdtgyssdgISSSLGEIPSHIPTDEKDLLKET 1422
Cdd:PTZ00121  1544 EKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKK------------AEEARIEEVMKLYEEEKKMKAEE 1611

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1423 SKKdtiSQESPPSPSDLAKLESTVLSILEAQASTLSDEKSAKSKEPSETYGEQTKDQLKTKplpvtpesyspDEEDLKAI 1502
Cdd:PTZ00121  1612 AKK---AEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKK-----------AEEDKKKA 1677

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1503 KEGEGTIAEEGKGAASSQADYKEEHEGDDMSARRQQRYDSVEDSSESENSpvprRKRRTSVGSSSSDEYKRDDSQGSGDE 1582
Cdd:PTZ00121  1678 EEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEE----NKIKAEEAKKEAEEDKKKAEEAKKDE 1753

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1583 EDfiRKQILEMSADEDASGSDDDEFIRNQLKE-ISAAESQKKEEVKSKAKGTagkhrrmaRKSSAGYDEDAGRRHSWHDD 1661
Cdd:PTZ00121  1754 EE--KKKIAHLKKEEEKKAEEIRKEKEAVIEEeLDEEDEKRRMEVDKKIKDI--------FDNFANIIEGGKEGNLVIND 1823

                          650       660       670       680       690       700
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2032737686 1662 DDETFDESPEPKYRESKSQDSEELAVSGggglRRFKTIELNSTITNKYSEVSEpQKGVLYFDEEPELE 1729
Cdd:PTZ00121  1824 SKEMEDSAIKEVADSKNMQLEEADAFEK----HKFNKNNENGEDGNKEADFNK-EKDLKEDDEEEIEE 1886
C2 super family cl14603
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 5097-5222 6.50e-15

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.


The actual alignment was detected with superfamily member cd04030:

Pssm-ID: 472691 [Multi-domain]  Cd Length: 127  Bit Score: 74.23  E-value: 6.50e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 5097 GEIKIALkkEMKTDGEQLIVEILQCRNITykFKSPDHLPDLYVKLYVvnISTQKRVIKKKTRVCRHDREPSFNETFRFSL 5176
Cdd:cd04030      3 GRIQLTI--RYSSQRQKLIVTVHKCRNLP--PCDSSDIPDPYVRLYL--LPDKSKSTRRKTSVKKDNLNPVFDETFEFPV 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2032737686 5177 SPAGHSLQILLVS--NGGKFM--KKTLIGEAYIWLDKVDLRKRIVNWHKL 5222
Cdd:cd04030     77 SLEELKRRTLDVAvkNSKSFLsrEKKLLGQVLIDLSDLDLSKGFTQWYDL 126
CCDC47 super family cl46382
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ...
 3782-3845 4.80e-03

PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of the PAT complex, an endoplasmic reticulum (ER)-resident membrane multiprotein complex that facilitates multi-pass membrane proteins insertion into membranes. The PAT complex, formed by CCDC47 and Asterix proteins, acts as an intramembrane chaperone by directly interacting with nascent transmembrane domains (TMDs), releasing its substrates upon correct folding, and is needed for optimal biogenesis of multi-pass membrane proteins. CCDC47 is required to maintain the stability of Asterix. CCDC47 is associated with various membrane-associated processes and is component of a ribosome-associated ER translocon complex involved in multi-pass membrane protein transport into the ER membrane and biogenesis. It is also involved in the regulation of calcium ion homeostasis in the ER, being also required for proper protein degradation via the ERAD (ER-associated degradation) pathway.


The actual alignment was detected with superfamily member pfam07946:

Pssm-ID: 480722  Cd Length: 323  Bit Score: 42.55  E-value: 4.80e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2032737686 3782 ARAKILQDIDRELDLVERESAKLRKKQAELDEEEKEIDaklrylEMGINRRKEALLKEREKRER 3845
Cdd:pfam07946  265 TREEEIEKIKKAAEEERAEEAQEKKEEAKKKEREEKLA------KLSPEEQRKYEEKERKKEQR 322
 
Name Accession Description Interval E-value
C2A_RIM1alpha cd04031
C2 domain first repeat contained in Rab3-interacting molecule (RIM) proteins; RIMs are ...
 4721-4855 3.42e-66

C2 domain first repeat contained in Rab3-interacting molecule (RIM) proteins; RIMs are believed to organize specialized sites of the plasma membrane called active zones. They also play a role in controlling neurotransmitter release, plasticity processes, as well as memory and learning. RIM contains an N-terminal zinc finger domain, a PDZ domain, and two C-terminal C2 domains (C2A, C2B). 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. Members here have a type-I topology and do not bind Ca2+.


Pssm-ID: 175997 [Multi-domain]  Cd Length: 125  Bit Score: 220.97  E-value: 3.42e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4721 ITGEIQLQINYDKHLGNLIIHILQARNLAPRDNNGYSDPFVKVYLLPGRgqvmvvqnaSAEYKRRTKYIQKSLNPEWNQT 4800
Cdd:cd04031      1 ITGRIQIQLWYDKVTSQLIVTVLQARDLPPRDDGSLRNPYVKVYLLPDR---------SEKSKRRTKTVKKTLNPEWNQT 71

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2032737686 4801 VIYKNISVEQLKKKTLEVTVWDYDRFSSNDFLGEVLIELSSiSQLDNTPRWYPLK 4855
Cdd:cd04031     72 FEYSNVRRETLKERTLEVTVWDYDRDGENDFLGEVVIDLAD-ALLDDEPHWYPLQ 125
PDZ_RIM-like cd06714
PDZ domain of Rab3-interacting molecule 1 (RIM), RIM2, piccolo and related domains; PDZ ...
 4520-4615 3.54e-49

PDZ domain of Rab3-interacting molecule 1 (RIM), RIM2, piccolo and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of RIM, RIM2, piccolo and related domains. RIM proteins and Gallus gallus protein piccolo (also called aczonin) are involved in neurotransmitter release at presynaptic active zones, the site of vesicle fusion. A protein complex containing RIM proteins positions synaptic vesicles containing synaptotagmin at the active zone. RIM proteins simultaneously activate docking and priming of synaptic vesicles and recruit Ca2+-channels to active zones, thereby connecting primed synaptic vesicles to Ca2+-channels. RIM binding to vesicular Rab proteins (Rab3 and Rab27 isoforms) mediates vesicle docking; RIM binding to Munc13 activates vesicle priming; RIM binding to the Ca2+-channel, both directly and indirectly via RIM-BP, recruits the Ca2+-channels. The RIM PDZ domain interacts with the C-termini of N- and P/Q-type voltage-gated Ca2+-channels. RIM1, RIM2 and piccolo also participate in regulated exocytosis through binding cAMP-GEFII (cAMP-binding protein-guanidine nucleotide exchange factor II). The piccolo PDZ domain binds cAMP-GEFII. RIM2 also plays a role in dendrite formation by melanocytes. Caenorhabditis elegans RIM (also known as unc-10) may be involved in the regulation of defecation and daumone response. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This RIM-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467198 [Multi-domain]  Cd Length: 95  Bit Score: 170.81  E-value: 3.54e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4520 FPHTRLKLLRDPKDHTVSGNGLGIRVVGGKEIPgsSGEIGAYIAKILPGGNAEQTGKLVEGMQVLEWNGIPLTGKTYEEV 4599
Cdd:cd06714      2 FLIGRIILQRDPKDGSVSGNGLGLKVVGGKMTE--SGRLGAYVTKVKPGSVADTVGHLREGDEVLEWNGISLQGKTFEEV 79

                           90
                   ....*....|....*.
gi 2032737686 4600 QSIIIQQSGEAEICVR 4615
Cdd:cd06714     80 QDIISQSKGEVELVVS 95
FYVE2_PCLO cd15776
FYVE-related domain 2 found in protein piccolo; Protein piccolo, also termed aczonin, is a ...
 919-982 2.68e-42

FYVE-related domain 2 found in protein piccolo; Protein piccolo, also termed aczonin, is a neuron-specific presynaptic active zone scaffolding protein that mainly interacts with a detergent-resistant cytoskeletal-like subcellular fraction and is involved in the organization of the interplay between neurotransmitter vesicles, the cytoskeleton, and the plasma membrane at synaptic active zones. It binds profilin, an actin-binding protein implicated in actin cytoskeletal dynamics. It also functions as a presynaptic low-affinity Ca2+ sensor and has been implicated in Ca2+ regulation of neurotransmitter release. Piccolo is a multi-domain protein containing two N-terminal FYVE zinc fingers, a polyproline tract, and a PDZ domain and two C-terminal C2 domains. This family corresponds to the second FYVE domain, which resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif.


Pssm-ID: 277315 [Multi-domain]  Cd Length: 64  Bit Score: 150.22  E-value: 2.68e-42
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2032737686  919 MSCPLCKTGLNIGSKDPPNFNTCTECKKVVCNLCGFNPMPHIAEVQEWLCLNCQTQRAMSGQLG 982
Cdd:cd15776      1 LLCPLCKTELNIGSKDPPNFNTCTECKKTVCNLCGFNPTPHLTEVKEWLCLNCQTQRAMSGQLG 64
FYVE1_PCLO cd15774
FYVE-related domain 1 found in protein piccolo; Protein piccolo, also termed aczonin, is a ...
 452-513 8.03e-42

FYVE-related domain 1 found in protein piccolo; Protein piccolo, also termed aczonin, is a neuron-specific presynaptic active zone scaffolding protein that mainly interacts with a detergent-resistant cytoskeletal-like subcellular fraction and is involved in the organization of the interplay between neurotransmitter vesicles, the cytoskeleton, and the plasma membrane at synaptic active zones. It binds profilin, an actin-binding protein implicated in actin cytoskeletal dynamics. It also functions as a presynaptic low-affinity Ca2+ sensor and has been implicated in Ca2+ regulation of neurotransmitter release. Piccolo is a multi-domain protein containing two N-terminal FYVE zinc fingers, a polyproline tract, and a PDZ domain and two C-terminal C2 domains. This family corresponds to the first FYVE domain, which resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif.


Pssm-ID: 277313 [Multi-domain]  Cd Length: 62  Bit Score: 148.64  E-value: 8.03e-42
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2032737686  452 TFCPLCTTTELLLHTPEKANYNTCTQCHTVVCSLCGFNPNPHITEISEWLCLNCQMQRTLGG 513
Cdd:cd15774      1 TICPLCKTTELLLHTPEKANYNTCTQCQTTVCSLCGFNPNPHITEKKEWLCLNCQMQRALGG 62
zf-piccolo pfam05715
Piccolo Zn-finger; This (predicted) Zinc finger is found in the bassoon and piccolo proteins. ...
 920-977 6.15e-37

Piccolo Zn-finger; This (predicted) Zinc finger is found in the bassoon and piccolo proteins. There are eight conserved cysteines, suggesting that it coordinates two zinc ligands.


Pssm-ID: 461722 [Multi-domain]  Cd Length: 60  Bit Score: 134.85  E-value: 6.15e-37
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2032737686  920 SCPLCK-TGLNIGSKDPPNFNTCTECKKVVCNLCGFNPMPHIAEVQEWLCLNCQTQRAM 977
Cdd:pfam05715    2 LCPLCKtTELNVGSKEPPNYNTCTECKSQVCNLCGFNPTPHLTEKKEWLCLNCQTQRAL 60
zf-piccolo pfam05715
Piccolo Zn-finger; This (predicted) Zinc finger is found in the bassoon and piccolo proteins. ...
 452-511 3.34e-36

Piccolo Zn-finger; This (predicted) Zinc finger is found in the bassoon and piccolo proteins. There are eight conserved cysteines, suggesting that it coordinates two zinc ligands.


Pssm-ID: 461722 [Multi-domain]  Cd Length: 60  Bit Score: 132.54  E-value: 3.34e-36
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  452 TFCPLCTTTELLLHTPEKANYNTCTQCHTVVCSLCGFNPNPHITEISEWLCLNCQMQRTL 511
Cdd:pfam05715    1 TLCPLCKTTELNVGSKEPPNYNTCTECKSQVCNLCGFNPTPHLTEKKEWLCLNCQTQRAL 60
C2 pfam00168
C2 domain;
4736-4854 1.11e-32

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 124.35  E-value: 1.11e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4736 GNLIIHILQARNLAPRDNNGYSDPFVKVYLLPGrgqvmvvqnasaEYKRRTKYIQKSLNPEWNQTVIYkniSVEQLKKKT 4815
Cdd:pfam00168    1 GRLTVTVIEAKNLPPKDGNGTSDPYVKVYLLDG------------KQKKKTKVVKNTLNPVWNETFTF---SVPDPENAV 65

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2032737686 4816 LEVTVWDYDRFSSNDFLGEVLIELSSISQLDNTPRWYPL 4854
Cdd:pfam00168   66 LEIEVYDYDRFGRDDFIGEVRIPLSELDSGEGLDGWYPL 104
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 4738-4851 8.23e-28

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.


Pssm-ID: 214577 [Multi-domain]  Cd Length: 101  Bit Score: 110.27  E-value: 8.23e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  4738 LIIHILQARNLAPRDNNGYSDPFVKVYLLPGRGQvmvvqnasaeyKRRTKYIQKSLNPEWNQTVIYkniSVEQLKKKTLE 4817
Cdd:smart00239    2 LTVKIISARNLPPKDKGGKSDPYVKVSLDGDPKE-----------KKKTKVVKNTLNPVWNETFEF---EVPPPELAELE 67

                            90       100       110
                    ....*....|....*....|....*....|....
gi 2032737686  4818 VTVWDYDRFSSNDFLGEVLIELSSISQLDNTPRW 4851
Cdd:smart00239   68 IEVYDKDRFGRDDFIGQVTIPLSDLLLGGRHEKL 101
PHA03247 PHA03247
large tegument protein UL36; Provisional
 188-736 3.91e-24

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 113.49  E-value: 3.91e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  188 QKVAPKEQGKPEEQRSPAKHPTQP-QSPKPAVQQQGPVRPTVQQTESskqqqqpggpkqvqKPGhgqpADAKQDQAKQPA 266
Cdd:PHA03247  2541 EELASDDAGDPPPPLPPAAPPAAPdRSVPPPRPAPRPSEPAVTSRAR--------------RPD----APPQSARPRAPV 2602

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  267 QPRGPQKSQPQPSePTKPIQQQTSAKPSSG------------PTKPSPQQPDSTKVTSQTAPPTKPSSQ-QPGPAKQPSQ 333
Cdd:PHA03247  2603 DDRGDPRGPAPPS-PLPPDTHAPDPPPPSPspaanepdphppPTVPPPERPRDDPAPGRVSRPRRARRLgRAAQASSPPQ 2681

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  334 QPARQGAPVK----------PSPQQTGPPKQPSQQPGPEKPSAQQAGPAKQPPQPGSGKPPPQQTGLVKQVPPQAGPTkp 403
Cdd:PHA03247  2682 RPRRRAARPTvgsltsladpPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPAR-- 2759

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  404 PSQTVGPTKPLAQQAGPTKPPGQQPGPE-KPPQQTQAGANQPTETAPKKTFCPLCTTTELLLHTPEKANYNTCTQCHTVV 482
Cdd:PHA03247  2760 PPTTAGPPAPAPPAAPAAGPPRRLTRPAvASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAP 2839

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  483 CSLCGFNPNPhiteisewlclncqmqRTLGGDLAPG----LGPGPQPLAPKQKTPIPPSAKPSPQPQPVQKKDVTPKPDP 558
Cdd:PHA03247  2840 PPPPGPPPPS----------------LPLGGSVAPGgdvrRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPD 2903

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  559 SQAadskrPPPQkkqtqlPGSPPvkskQPRAEPTDISQQTDATPKSDQVKPtqaeDKQKQPSVQKPTADSVSTSVAAEQK 638
Cdd:PHA03247  2904 QPE-----RPPQ------PQAPP----PPQPQPQPPPPPQPQPPPPPPPRP----QPPLAPTTDPAGAGEPSGAVPQPWL 2964

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  639 QDLAGPRPPTQQKVTDSPKPELAKPSQDTHPagdkPDSKPVPQVSRQKSDPKFASQPGARPDAKAQK--PIDPTQTKDDP 716
Cdd:PHA03247  2965 GALVPGRVAVPRFRVPQPAPSREAPASSTPP----LTGHSLSRVSSWASSLALHEETDPPPVSLKQTlwPPDDTEDSDAD 3040

                          570       580
                   ....*....|....*....|....*.
gi 2032737686  717 KKLPTKP------APKPDTkPAPKGP 736
Cdd:PHA03247  3041 SLFDSDSersdleALDPLP-PEPHDP 3065
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 255-664 2.37e-17

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.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 90.60  E-value: 2.37e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  255 ADAKQDQAKQPA-QPRGPQKSQPQPSePTKPIQQQTSAKPSSGPTKPSPQQPDSTKVTSQTAPPTKP-----SSQQPGPA 328
Cdd:pfam03154  162 AQQQILQTQPPVlQAQSGAASPPSPP-PPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPhtliqQTPTLHPQ 240

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  329 KQPSQQPARQGAPVKPSPQQTGPPKQPS---QQPGPEKPSAQQAGPAKQP-PQPGSGKPPPQQTGLvKQVPPQAGPTKP- 403
Cdd:pfam03154  241 RLPSPHPPLQPMTQPPPPSQVSPQPLPQpslHGQMPPMPHSLQTGPSHMQhPVPPQPFPLTPQSSQ-SQVPPGPSPAAPg 319

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  404 PSQTVGPTKPLAQQAGPTKPPGQQPGPEKPpqqtqagANQPTETAPKKTFCPLCTTTELLLHTPEKAnyntctqchtvvc 483
Cdd:pfam03154  320 QSQQRIHTPPSQSQLQSQQPPREQPLPPAP-------LSMPHIKPPPTTPIPQLPNPQSHKHPPHLS------------- 379

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  484 slcgfNPNPHiteisewlclncQMQRTLggdlapglgPGPQPLAPKQKTPI--PPSAKPSP-----QPQPVQKKDVTP-- 554
Cdd:pfam03154  380 -----GPSPF------------QMNSNL---------PPPPALKPLSSLSThhPPSAHPPPlqlmpQSQQLPPPPAQPpv 433

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  555 -KPDPSQAADSKRPPPQKKQTQLPGSPPVKSKQ-PRAEPTDISQQTDATPKSDQVKPTQAEDKQKQPSVQKPTADSVSTS 632
Cdd:pfam03154  434 lTQSQSLPPPAASHPPTSGLHQVPSQSPFPQHPfVPGGPPPITPPSGPPTSTSSAMPGIQPPSSASVSSSGPVPAAVSCP 513

                          410       420       430
                   ....*....|....*....|....*....|..
gi 2032737686  633 VAAEQKQDlagpRPPTQQKVTDSPKPELAKPS 664
Cdd:pfam03154  514 LPPVQIKE----EALDEAEEPESPPPPPRSPS 541
PTZ00121 PTZ00121
MAEBL; Provisional
 1029-1729 4.34e-15

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 83.27  E-value: 4.34e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1029 AKPKEEPGVQKEAPKLQQGRLEKTlsaDKIQQGIQKEDAKpKQGKLVKAPSADKIQHASQKEDPRiQQTKLTKTASYDRV 1108
Cdd:PTZ00121  1242 AKKAEEERNNEEIRKFEEARMAHF---ARRQAAIKAEEAR-KADELKKAEEKKKADEAKKAEEKK-KADEAKKKAEEAKK 1316

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1109 LQEVQKEDE----KLQEAKLAKTSSADKILHRVQKEDIKLQEAKLAKVPS-ADKILQGIQKEDPKLQQMKMAKALSADKI 1183
Cdd:PTZ00121  1317 ADEAKKKAEeakkKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAeAAEKKKEEAKKKADAAKKKAEEKKKADEA 1396

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1184 QLAAQREDTKLQEVKlpKAASVDKiqhgTQKDIKLQHEKIKKTSSVDKIQEEGQK-EETKLQRGKLSKTPSADKIPATAT 1262
Cdd:PTZ00121  1397 KKKAEEDKKKADELK--KAAAAKK----KADEAKKKAEEKKKADEAKKKAEEAKKaDEAKKKAEEAKKAEEAKKKAEEAK 1470

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1263 ADQKIPLSTLEEDKETVLPEKSTPHPEDKKEEITAEIKDRVAEEKAEVEAPYKGLQAKEEEDVKKEDLTTgisqvvlKAE 1342
Cdd:PTZ00121  1471 KADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAK-------KAE 1543

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1343 KAQEAEIPVQTAPLPGTDHVEAVREKIEKEDDKSDTSSSQQQKSPqglsdtgyssdgISSSLGEIPSHIPTDEKDLLKET 1422
Cdd:PTZ00121  1544 EKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKK------------AEEARIEEVMKLYEEEKKMKAEE 1611

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1423 SKKdtiSQESPPSPSDLAKLESTVLSILEAQASTLSDEKSAKSKEPSETYGEQTKDQLKTKplpvtpesyspDEEDLKAI 1502
Cdd:PTZ00121  1612 AKK---AEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKK-----------AEEDKKKA 1677

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1503 KEGEGTIAEEGKGAASSQADYKEEHEGDDMSARRQQRYDSVEDSSESENSpvprRKRRTSVGSSSSDEYKRDDSQGSGDE 1582
Cdd:PTZ00121  1678 EEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEE----NKIKAEEAKKEAEEDKKKAEEAKKDE 1753

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1583 EDfiRKQILEMSADEDASGSDDDEFIRNQLKE-ISAAESQKKEEVKSKAKGTagkhrrmaRKSSAGYDEDAGRRHSWHDD 1661
Cdd:PTZ00121  1754 EE--KKKIAHLKKEEEKKAEEIRKEKEAVIEEeLDEEDEKRRMEVDKKIKDI--------FDNFANIIEGGKEGNLVIND 1823

                          650       660       670       680       690       700
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2032737686 1662 DDETFDESPEPKYRESKSQDSEELAVSGggglRRFKTIELNSTITNKYSEVSEpQKGVLYFDEEPELE 1729
Cdd:PTZ00121  1824 SKEMEDSAIKEVADSKNMQLEEADAFEK----HKFNKNNENGEDGNKEADFNK-EKDLKEDDEEEIEE 1886
C2C_KIAA1228 cd04030
C2 domain third repeat present in uncharacterized human KIAA1228-like proteins; KIAA proteins ...
 5097-5222 6.50e-15

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.


Pssm-ID: 175996 [Multi-domain]  Cd Length: 127  Bit Score: 74.23  E-value: 6.50e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 5097 GEIKIALkkEMKTDGEQLIVEILQCRNITykFKSPDHLPDLYVKLYVvnISTQKRVIKKKTRVCRHDREPSFNETFRFSL 5176
Cdd:cd04030      3 GRIQLTI--RYSSQRQKLIVTVHKCRNLP--PCDSSDIPDPYVRLYL--LPDKSKSTRRKTSVKKDNLNPVFDETFEFPV 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2032737686 5177 SPAGHSLQILLVS--NGGKFM--KKTLIGEAYIWLDKVDLRKRIVNWHKL 5222
Cdd:cd04030     77 SLEELKRRTLDVAvkNSKSFLsrEKKLLGQVLIDLSDLDLSKGFTQWYDL 126
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 5113-5219 5.87e-14

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.


Pssm-ID: 214577 [Multi-domain]  Cd Length: 101  Bit Score: 70.59  E-value: 5.87e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  5113 QLIVEILQCRNITYKFKSpdHLPDLYVKLYVVNistqKRVIKKKTRVCRHDREPSFNETFRFSLSPAGHSLQILLVSNGG 5192
Cdd:smart00239    1 TLTVKIISARNLPPKDKG--GKSDPYVKVSLDG----DPKEKKKTKVVKNTLNPVWNETFEFEVPPPELAELEIEVYDKD 74

                            90       100
                    ....*....|....*....|....*..
gi 2032737686  5193 KFMKKTLIGEAYIWLDKVDLRKRIVNW 5219
Cdd:smart00239   75 RFGRDDFIGQVTIPLSDLLLGGRHEKL 101
C2 pfam00168
C2 domain;
5113-5222 2.33e-13

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 69.27  E-value: 2.33e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 5113 QLIVEILQCRNITYKFKSPdhLPDLYVKLYVvnistQKRVIKKKTRVCRHDREPSFNETFRFSLSPAGHSLQILLVSNGG 5192
Cdd:pfam00168    2 RLTVTVIEAKNLPPKDGNG--TSDPYVKVYL-----LDGKQKKKTKVVKNTLNPVWNETFTFSVPDPENAVLEIEVYDYD 74

                           90       100       110
                   ....*....|....*....|....*....|
gi 2032737686 5193 KFMKKTLIGEAYIWLDKVDLRKRIVNWHKL 5222
Cdd:pfam00168   75 RFGRDDFIGEVRIPLSELDSGEGLDGWYPL 104
COG5038 COG5038
Ca2+-dependent lipid-binding protein, contains C2 domain [General function prediction only];
4736-4844 3.98e-09

Ca2+-dependent lipid-binding protein, contains C2 domain [General function prediction only];


Pssm-ID: 227371 [Multi-domain]  Cd Length: 1227  Bit Score: 63.62  E-value: 3.98e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4736 GNLIIHILQARNLAPRDNNGYSDPFVKVYLlpgrgqvmvvQNASAeykRRTKYIQKSLNPEWNQTVIyknISVEQLKKKT 4815
Cdd:COG5038   1040 GYLTIMLRSGENLPSSDENGYSDPFVKLFL----------NEKSV---YKTKVVKKTLNPVWNEEFT---IEVLNRVKDV 1103

                           90       100
                   ....*....|....*....|....*....
gi 2032737686 4816 LEVTVWDYDRFSSNDFLGEVLIELSSISQ 4844
Cdd:COG5038   1104 LTINVNDWDSGEKNDLLGTAEIDLSKLEP 1132
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 182-452 5.04e-09

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 62.86  E-value: 5.04e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  182 EEAGRKQKVAPKEQGKPEEQRSPAKHPTQPQSPKPAVQQQGPV-RPTVqqtesskqqqqpggpkqvqKPghgQPADAKQD 260
Cdd:NF033839   285 KEPGNKKPSAPKPGMQPSPQPEKKEVKPEPETPKPEVKPQLEKpKPEV-------------------KP---QPEKPKPE 342

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  261 QAKQPAQPRGPQKsqPQPSEPTKPIQQQTSAKPSSGPTKPSPQQPDSTKVTSQTAPPTKPSSQQPGPAKQPsqQPARQGA 340
Cdd:NF033839   343 VKPQLETPKPEVK--PQPEKPKPEVKPQPEKPKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEKPKPEVKP--QPEKPKP 418

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  341 PVKPSPQQTGPPKQPSQQ-------PGPEKPSAQqagpakQPPQPGSGKP--PPQQTGLVKQVPPQAGPTKPPSqtvgpT 411
Cdd:NF033839   419 EVKPQPEKPKPEVKPQPEkpkpevkPQPEKPKPE------VKPQPETPKPevKPQPEKPKPEVKPQPEKPKPDN-----S 487

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 2032737686  412 KPLAQQAGPTKPPGQQPGPEKppqQTQAGANQPTETAPKKT 452
Cdd:NF033839   488 KPQADDKKPSTPNNLSKDKQP---SNQASTNEKATNKPKKS 525
PHA03247 PHA03247
large tegument protein UL36; Provisional
 516-1049 1.92e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 61.49  E-value: 1.92e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  516 APGLGPGPQPLAPKQKTPIPPSAKPSPQ--PQPVQKKDVTPKP-------DPSQAADSKRPPPQKKQTQLPGSPPVKSKQ 586
Cdd:PHA03247  2491 AAGAAPDPGGGGPPDPDAPPAPSRLAPAilPDEPVGEPVHPRMltwirglEELASDDAGDPPPPLPPAAPPAAPDRSVPP 2570

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  587 PRAEPTDISQQTDATPKSDQVKPTQAEDKqkqpSVQKPTADSVSTSVAAEQKQDLAGPRPPTQqkvtdSPKP---ELAKP 663
Cdd:PHA03247  2571 PRPAPRPSEPAVTSRARRPDAPPQSARPR----APVDDRGDPRGPAPPSPLPPDTHAPDPPPP-----SPSPaanEPDPH 2641

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  664 SQDTHPAGDKPDSKPVP------QVSRQKSDPKFASQPGARPDAKAQKP-IDPTQTKDDPKKLPTKPAPKP----DTKPA 732
Cdd:PHA03247  2642 PPPTVPPPERPRDDPAPgrvsrpRRARRLGRAAQASSPPQRPRRRAARPtVGSLTSLADPPPPPPTPEPAPhalvSATPL 2721

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  733 PKGPQAGAGPKAAPAQPAPQPQPPQktpeqprrfslnlGGITDAPKPQPTTPQETVTGKLFGFGASFFSQASNLISTAGQ 812
Cdd:PHA03247  2722 PPGPAAARQASPALPAAPAPPAVPA-------------GPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAV 2788

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  813 TGSQPSGPPPPAPAAKQPQPPAQPPAPQAAPKEAAQAQPLPKAVPVKKEAKPLTTEKSEPS-KVDGVLTKGSDLEKKPgl 891
Cdd:PHA03247  2789 ASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSlPLGGSVAPGGDVRRRP-- 2866

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  892 akdskPLAAEAKKPDGLSEP--EKASQPEMSCPLCKTGLNIGSKDPPnfntcteckkvvcnlcgfnPMPhiaevqewlcl 969
Cdd:PHA03247  2867 -----PSRSPAAKPAAPARPpvRRLARPAVSRSTESFALPPDQPERP-------------------PQP----------- 2911

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  970 ncqtqramsgqlgdmgkvpllkPGPSQPTSKPAAPPQKRPVPAVshSPQKTSTPPTPAAAKPKEEPGVQKEAPKLQQGRL 1049
Cdd:PHA03247  2912 ----------------------QAPPPPQPQPQPPPPPQPQPPP--PPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGAL 2967
PBP1 COG5180
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ...
 183-453 5.33e-08

PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification];


Pssm-ID: 444064 [Multi-domain]  Cd Length: 548  Bit Score: 59.31  E-value: 5.33e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  183 EAGRKQKVAPKEQGKPEEQRSPA-KHPTQPQSPKPAVQQQGPVRPT----VQQTESSKQQQQPGGPKQVQKPGHGQPADA 257
Cdd:COG5180    260 DAKERRRAAIGDTPAAEPPGLPVlEAGSEPQSDAPEAETARPIDVKgvasAPPATRPVRPPGGARDPGTPRPGQPTERPA 339

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  258 KQDQAKQPAQPRGPQKSQPQPSEPTKPIQQQTsAKPSSGPTKPSPQQPDSTKVTSQT------------APPTKPSSQQP 325
Cdd:COG5180    340 GVPEAASDAGQPPSAYPPAEEAVPGKPLEQGA-PRPGSSGGDGAPFQPPNGAPQPGLgrrgapgppmgaGDLVQAALDGG 418

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  326 GPAKQPSQQPARQGAPVKPSPQQTGPPKQPSQQPGPEKPSAQQAGPAKQPPQPGSGKPPPQQTGLVKQVPPQAgptkPPS 405
Cdd:COG5180    419 GRETASLGGAAGGAGQGPKADFVPGDAESVSGPAGLADQAGAAASTAMADFVAPVTDATPVDVADVLGVRPDA----ILG 494

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 2032737686  406 QTVGPTKPLAQQAGPTKPPGQqpgPEKPPqQTQAGANQPTETAPKKTF 453
Cdd:COG5180    495 GNVAPASGLDAETRIIEAEGA---PATED-FVAAELSELREAAEEKTG 538
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 247-470 6.07e-08

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 59.01  E-value: 6.07e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  247 QKPGHGQPADAKQDQAKQPAQPRGPQKSQPQPSEP-TKPIQQQTSAKPSSGPTKPSPQ--------QPDSTKVTSQTAPP 317
Cdd:NF033839   285 KEPGNKKPSAPKPGMQPSPQPEKKEVKPEPETPKPeVKPQLEKPKPEVKPQPEKPKPEvkpqletpKPEVKPQPEKPKPE 364

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  318 TKPSSQQPGPAKQPsqQPARQGAPVKPSPQQTGPPKQPSQQ-------PGPEKPSAqQAGPAKQPPQPGSGKPPPQQTGL 390
Cdd:NF033839   365 VKPQPEKPKPEVKP--QPETPKPEVKPQPEKPKPEVKPQPEkpkpevkPQPEKPKP-EVKPQPEKPKPEVKPQPEKPKPE 441

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  391 VKQVPPQAGPTKPPSQtvGPTKPLAQQAGPTKPPGQQPGPEKP------PQQTQAGANQPTETAPKKTFCPLCTTTELLL 464
Cdd:NF033839   442 VKPQPEKPKPEVKPQP--ETPKPEVKPQPEKPKPEVKPQPEKPkpdnskPQADDKKPSTPNNLSKDKQPSNQASTNEKAT 519


                   ....*.
gi 2032737686  465 HTPEKA 470
Cdd:NF033839   520 NKPKKS 525
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 1030-1748 6.42e-07

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 56.13  E-value: 6.42e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1030 KPKEEPGVQKEAPKLQQGRLEKTLSADKIQQGIQKEDAKPKQGKLVKAPSADKIQHASQKEDPRIQQTKLTKTASYDRVL 1109
Cdd:pfam02463  216 KEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEE 295

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1110 QEVQKEDEKLQEAKlaktSSADKILHRVQKEDIKLQEAKLAKVPSADKILQGIQKEDPKLQQMKMAKALSADKIQLAAQR 1189
Cdd:pfam02463  296 EELKSELLKLERRK----VDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQL 371

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1190 EDTKLQEVKLpkaASVDKIQHGTQKDIKLQHEKIKKTSSVDKIQEEGQKEETKLQRGKlsktpSADKIPATATADQKIPL 1269
Cdd:pfam02463  372 EEELLAKKKL---ESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKK-----EELEILEEEEESIELKQ 443

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1270 STLEEDKETVLPEKStphpedKKEEITAEIKDRVAEEKAEVEAPYKGLQAKEEEDVKKEDLTT---------------GI 1334
Cdd:pfam02463  444 GKLTEEKEELEKQEL------KLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQkeskarsglkvllalIK 517

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1335 SQVVLK----AEKAQEAEIPVQTAPLPGTDHVEAVREKIEKEDDKSDTSSSQQQKSPQGLSDTGYSSDGISSSLGEI--- 1407
Cdd:pfam02463  518 DGVGGRiisaHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIavl 597

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1408 PSHIPTDEKDLLKETSKKDTISQESPPSPSDLAKLESTVLSILEAQASTLSDEKSAKSKEPSETYGEQTKDQLKTKPLPV 1487
Cdd:pfam02463  598 EIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLE 677

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1488 TPESYSPDEEDLKAIKEG---EGTIAEEGKGAASSQADYKEEHEGDDMSARRQQRydsvedsseseNSPVPRRKRRTSVG 1564
Cdd:pfam02463  678 IQELQEKAESELAKEEILrrqLEIKKKEQREKEELKKLKLEAEELLADRVQEAQD-----------KINEELKLLKQKID 746

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1565 SSSSDEYKRDDSQGSGDEEDFIRKQILEMSADEDAS------GSDDDEFIRNQLKEISAAESQKKEEVKSkakgtagKHR 1638
Cdd:pfam02463  747 EEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKteklkvEEEKEEKLKAQEEELRALEEELKEEAEL-------LEE 819

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1639 RMARKSSAGYDEDAGRRHSwHDDDDETFDESPEPKYRESKSQDSEELAVSggggLRRFKTIELNSTITNKYSEVSEPQKg 1718
Cdd:pfam02463  820 EQLLIEQEEKIKEEELEEL-ALELKEEQKLEKLAEEELERLEEEITKEEL----LQELLLKEEELEEQKLKDELESKEE- 893

                          730       740       750
                   ....*....|....*....|....*....|
gi 2032737686 1719 VLYFDEEPELEMESLTDSPEDRSRGEGSSS 1748
Cdd:pfam02463  894 KEKEEKKELEEESQKLNLLEEKENEIEERI 923
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 523-737 8.20e-07

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 55.55  E-value: 8.20e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  523 PQPLAPKQKTPIPPSAKPSPQPQPVQKKdvTPKPDPSQAADSKRP-----------------PPQKKQTQL--------- 576
Cdd:NF033839   162 PQPENPEHQKPTTPAPDTKPSPQPEGKK--PSVPDINQEKEKAKLavatymskilddiqkhhLQKEKHRQIvalikelde 239

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  577 ---PGSPPVKSKQPRAEPTDISQQ--TDATPKSDQVKPTQAEDKQKQPSVQKPTA--DSVSTSVAAEQKQDLAGPRPPTQ 649
Cdd:NF033839   240 lkkQALSEIDNVNTKVEIENTVHKifADMDAVVTKFKKGLTQDTPKEPGNKKPSApkPGMQPSPQPEKKEVKPEPETPKP 319

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  650 QKvtdSPKPELAKPSQDTHPAGDKPDSKPVPQVSRQKSDPKF-ASQPGARPDAKAQKP-IDPTQTKDDPKKLPTKPAPKP 727
Cdd:NF033839   320 EV---KPQLEKPKPEVKPQPEKPKPEVKPQLETPKPEVKPQPeKPKPEVKPQPEKPKPeVKPQPETPKPEVKPQPEKPKP 396

                          250
                   ....*....|
gi 2032737686  728 DTKPAPKGPQ 737
Cdd:NF033839   397 EVKPQPEKPK 406
SP2_N cd22540
N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins ...
 173-379 1.26e-05

N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. SP2 contains the least conserved DNA-binding domain within the SP subfamily of proteins, and its DNA sequence specificity differs from the other SP proteins. It localizes primarily within subnuclear foci associated with the nuclear matrix, and can activate, or in some cases, repress expression from different promoters. The transcription factor SP2 serves as a paradigm for indirect genomic binding. It does not require its DNA-binding domain for genomic DNA binding and occupies target promoters independently of whether they contain a cognate DNA-binding motif. SP2 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP2.


Pssm-ID: 411776 [Multi-domain]  Cd Length: 511  Bit Score: 51.47  E-value: 1.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  173 LISDSDTSHeeagrkQKVAPKEQGKPEEQRSpaKHPTQPQSPKPAVQQQgpVRPTVQQTESSKQQQQPGGPKQVQKPGHG 252
Cdd:cd22540    212 LVGTQDGAT------QLQLAAAPSKPSKKIR--KKSAQAAQPAVTVAEQ--VETVLIETTADNIIQAGNNLLIVQSPGTG 281

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  253 QPAdakQDQAKQPAQPRGPQKSQPQPSEPTKPIQQQTSAKPssgptkPSPQQPdSTKVTSQTAPPTKPSSQQPGPAKQPS 332
Cdd:cd22540    282 QPA---VLQQVQVLQPKQEQQVVQIPQQALRVVQAASATLP------TVPQKP-LQNIQIQNSEPTPTQVYIKTPSGEVQ 351

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2032737686  333 QQPARQGAPVKPSPQQTGPPKQPSQQP-GPEKPSAQQAGPAKQPPQPG 379
Cdd:cd22540    352 TVLLQEAPAATATPSSSTSTVQQQVTAnNGTGTSKPNYNVRKERTLPK 399
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
 4532-4603 1.39e-05

PDZ domain; PDZ domains are found in diverse signaling proteins.


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 46.12  E-value: 1.39e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2032737686 4532 KDHTVSGNGLGIRVVGGkeipGSSGEIGAYIAKILPGGNAEQTGkLVEGMQVLEWNGIPLTGKTYEEVQSII 4603
Cdd:pfam00595    3 TLEKDGRGGLGFSLKGG----SDQGDPGIFVSEVLPGGAAEAGG-LKVGDRILSINGQDVENMTHEEAVLAL 69
Amelin smart00817
Ameloblastin precursor (Amelin); This family consists of several mammalian Ameloblastin ...
 290-378 1.90e-05

Ameloblastin precursor (Amelin); This family consists of several mammalian Ameloblastin precursor (Amelin) proteins. Matrix proteins of tooth enamel consist mainly of amelogenin but also of non-amelogenin proteins, which, although their volumetric percentage is low, have an important role in enamel mineralisation. One of the non-amelogenin proteins is ameloblastin, also known as amelin and sheathlin. Ameloblastin (AMBN) is one of the enamel sheath proteins which is though to have a role in determining the prismatic structure of growing enamel crystals.


Pssm-ID: 214832 [Multi-domain]  Cd Length: 411  Bit Score: 50.66  E-value: 1.90e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686   290 SAKPSSGPTKPSPQQPDSTKVTSQTAPPTKPSSQ--QPG--PAKQPSQQPARQGAPVKPSPQQTGPPKQPSQQPGPEKPS 365
Cdd:smart00817   74 SSFPWLRPREHETQQYEYSLPVHPPPLPSQPSLQpqQPGlkPFLQPTALPTNQATPQKNGPQPPMHLGQPPLQQAELPMI 153

                            90
                    ....*....|...
gi 2032737686   366 AQQAGPAKQPPQP 378
Cdd:smart00817  154 PPQVAPSDKPPQT 166
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
 327-409 4.51e-05

pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.


Pssm-ID: 468201 [Multi-domain]  Cd Length: 684  Bit Score: 50.01  E-value: 4.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  327 PAKQPSQQPARQgaPVKPSPQqtgpPKQPSQQPGPEKPSAQQAGPAKQPPQPGSGKPPPQQtglvkQVPPQAGPTKPPSQ 406
Cdd:NF033838   416 PAEQPQPAPAPQ--PEKPAPK----PEKPAEQPKAEKPADQQAEEDYARRSEEEYNRLTQQ-----QPPKTEKPAQPSTP 484


                   ...
gi 2032737686  407 TVG 409
Cdd:NF033838   485 KTG 487
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
 297-427 3.14e-04

polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 47.11  E-value: 3.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  297 PTKPSPQQPdSTKVTSQTAPPTKpssqQPGPAKQPSQQPAR-QGAPVKPSPQQTGPPKQPSqqpGPEKPSAQQAGPAKQp 375
Cdd:TIGR01628  380 PRMRQLPMG-SPMGGAMGQPPYY----GQGPQQQFNGQPLGwPRMSMMPTPMGPGGPLRPN---GLAPMNAVRAPSRNA- 450

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2032737686  376 pQPGSGKPPPQ----QTGLVKQVPPQAGPTKPPSQTVGPTKPLAQQAGPTKPPGQQ 427
Cdd:TIGR01628  451 -QNAAQKPPMQpvmyPPNYQSLPLSQDLPQPQSTASQGGQNKKLAQVLASATPQMQ 505
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 1333-1683 1.55e-03

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 45.29  E-value: 1.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1333 GISQVVLKAEKAQEAEI---PVQTAPLPGTDHVEAVREKIEKEDDKSDTSSSQQqkspqglSDTGYSSDGISSSLGEIPS 1409
Cdd:NF033609   538 GIDKPVVPEQPDEPGEIepiPEDSDSDPGSDSGSDSSNSDSGSDSGSDSTSDSG-------SDSASDSDSASDSDSASDS 610

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1410 HIPTDEKDLLKETSKKDTISQESPPSPSDlakLESTVLSILEAQASTLSDEKSAkSKEPSETYGEQTKDQLKTKPLPVTP 1489
Cdd:NF033609   611 DSASDSDSASDSDSASDSDSASDSDSASD---SDSDSDSDSDSDSDSDSDSDSD-SDSDSDSDSDSDSDSDSDSDSDSDS 686

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1490 ESYSPDEEDLKAIKEGEGTIAEEGKGAASSQADYKEEHEGDDmsarrqqryDSVEDSSESENSPVPRRKRRTSVGSSSSD 1569
Cdd:NF033609   687 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS---------DSDSDSDSDSDSDSDSDSDSDSDSDSDSD 757

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1570 EYKRDDSQGSGDEEDfirkqilEMSADEDA-SGSDDDEFIRNQLKEISAAESQKKEEVKSKAKGTAGKHRRMARKSSAGY 1648
Cdd:NF033609   758 SDSDSDSDSDSDSDS-------DSDSDSDSdSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 830

                          330       340       350
                   ....*....|....*....|....*....|....*
gi 2032737686 1649 DEDAGRRHSWHDDDDETFDESPEPKYRESKSQDSE 1683
Cdd:NF033609   831 DSDSDSDSDSDSDSDSDSDSDSDSDSESDSNSDSE 865
CCDC47 pfam07946
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ...
 3782-3845 4.80e-03

PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of the PAT complex, an endoplasmic reticulum (ER)-resident membrane multiprotein complex that facilitates multi-pass membrane proteins insertion into membranes. The PAT complex, formed by CCDC47 and Asterix proteins, acts as an intramembrane chaperone by directly interacting with nascent transmembrane domains (TMDs), releasing its substrates upon correct folding, and is needed for optimal biogenesis of multi-pass membrane proteins. CCDC47 is required to maintain the stability of Asterix. CCDC47 is associated with various membrane-associated processes and is component of a ribosome-associated ER translocon complex involved in multi-pass membrane protein transport into the ER membrane and biogenesis. It is also involved in the regulation of calcium ion homeostasis in the ER, being also required for proper protein degradation via the ERAD (ER-associated degradation) pathway.


Pssm-ID: 462322  Cd Length: 323  Bit Score: 42.55  E-value: 4.80e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2032737686 3782 ARAKILQDIDRELDLVERESAKLRKKQAELDEEEKEIDaklrylEMGINRRKEALLKEREKRER 3845
Cdd:pfam07946  265 TREEEIEKIKKAAEEERAEEAQEKKEEAKKKEREEKLA------KLSPEEQRKYEEKERKKEQR 322
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
 1008-1375 6.15e-03

pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.


Pssm-ID: 468201 [Multi-domain]  Cd Length: 684  Bit Score: 43.08  E-value: 6.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1008 RPVPAVSHSPQKTSTPpTPAAAKPKEEPGVQKEAPKLQQGRLEKTLSADKIQQGIQKEDAKpKQGKLVKAPSADKIQHAS 1087
Cdd:NF033838    43 GNNPTVTSSGNESQKE-HAKEVESHLEKILSEIQKSLDKRKHTQNVALNKKLSDIKTEYLY-ELNVLKEKSEAELTSKTK 120

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1088 QKEDPRIQQTK------LTKTASYDRVLQEVQK--EDEKLQEAKLAKTSSADKILHRVQKEDIKLQEAKLakvpsadKIL 1159
Cdd:NF033838   121 KELDAAFEQFKkdtlepGKKVAEATKKVEEAEKkaKDQKEEDRRNYPTNTYKTLELEIAESDVEVKKAEL-------ELV 193

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1160 QGIQKEDPKLQQMKMAKAlsadKIQlAAQREDTKLQEVKLPKAASVDKIQHGTQKDIKLQHEKIKKTSSVDKiqeegQKE 1239
Cdd:NF033838   194 KEEAKEPRDEEKIKQAKA----KVE-SKKAEATRLEKIKTDREKAEEEAKRRADAKLKEAVEKNVATSEQDK-----PKR 263

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1240 ETKlqRGKLSKTPSADK------IPATATADQKIPLSTLEEDKETVLPEKSTPHPE----DKKEE------------ITA 1297
Cdd:NF033838   264 RAK--RGVLGEPATPDKkendakSSDSSVGEETLPSPSLKPEKKVAEAEKKVEEAKkkakDQKEEdrrnyptntyktLEL 341

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1298 EIKDR-----------VAEEKAEVEAPYKGLQAKEEEDVKKEDLT--TGISQVVLKAE-----KAQE--------AEIPv 1351
Cdd:NF033838   342 EIAESdvkvkeaelelVKEEAKEPRNEEKIKQAKAKVESKKAEATrlEKIKTDRKKAEeeakrKAAEedkvkekpAEQP- 420

                          410       420       430
                   ....*....|....*....|....*....|
gi 2032737686 1352 QTAPLPGTDH------VEAVREKIEKEDDK 1375
Cdd:NF033838   421 QPAPAPQPEKpapkpeKPAEQPKAEKPADQ 450
 
Name Accession Description Interval E-value
C2A_RIM1alpha cd04031
C2 domain first repeat contained in Rab3-interacting molecule (RIM) proteins; RIMs are ...
 4721-4855 3.42e-66

C2 domain first repeat contained in Rab3-interacting molecule (RIM) proteins; RIMs are believed to organize specialized sites of the plasma membrane called active zones. They also play a role in controlling neurotransmitter release, plasticity processes, as well as memory and learning. RIM contains an N-terminal zinc finger domain, a PDZ domain, and two C-terminal C2 domains (C2A, C2B). 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. Members here have a type-I topology and do not bind Ca2+.


Pssm-ID: 175997 [Multi-domain]  Cd Length: 125  Bit Score: 220.97  E-value: 3.42e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4721 ITGEIQLQINYDKHLGNLIIHILQARNLAPRDNNGYSDPFVKVYLLPGRgqvmvvqnaSAEYKRRTKYIQKSLNPEWNQT 4800
Cdd:cd04031      1 ITGRIQIQLWYDKVTSQLIVTVLQARDLPPRDDGSLRNPYVKVYLLPDR---------SEKSKRRTKTVKKTLNPEWNQT 71

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2032737686 4801 VIYKNISVEQLKKKTLEVTVWDYDRFSSNDFLGEVLIELSSiSQLDNTPRWYPLK 4855
Cdd:cd04031     72 FEYSNVRRETLKERTLEVTVWDYDRDGENDFLGEVVIDLAD-ALLDDEPHWYPLQ 125
PDZ_RIM-like cd06714
PDZ domain of Rab3-interacting molecule 1 (RIM), RIM2, piccolo and related domains; PDZ ...
 4520-4615 3.54e-49

PDZ domain of Rab3-interacting molecule 1 (RIM), RIM2, piccolo and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of RIM, RIM2, piccolo and related domains. RIM proteins and Gallus gallus protein piccolo (also called aczonin) are involved in neurotransmitter release at presynaptic active zones, the site of vesicle fusion. A protein complex containing RIM proteins positions synaptic vesicles containing synaptotagmin at the active zone. RIM proteins simultaneously activate docking and priming of synaptic vesicles and recruit Ca2+-channels to active zones, thereby connecting primed synaptic vesicles to Ca2+-channels. RIM binding to vesicular Rab proteins (Rab3 and Rab27 isoforms) mediates vesicle docking; RIM binding to Munc13 activates vesicle priming; RIM binding to the Ca2+-channel, both directly and indirectly via RIM-BP, recruits the Ca2+-channels. The RIM PDZ domain interacts with the C-termini of N- and P/Q-type voltage-gated Ca2+-channels. RIM1, RIM2 and piccolo also participate in regulated exocytosis through binding cAMP-GEFII (cAMP-binding protein-guanidine nucleotide exchange factor II). The piccolo PDZ domain binds cAMP-GEFII. RIM2 also plays a role in dendrite formation by melanocytes. Caenorhabditis elegans RIM (also known as unc-10) may be involved in the regulation of defecation and daumone response. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This RIM-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467198 [Multi-domain]  Cd Length: 95  Bit Score: 170.81  E-value: 3.54e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4520 FPHTRLKLLRDPKDHTVSGNGLGIRVVGGKEIPgsSGEIGAYIAKILPGGNAEQTGKLVEGMQVLEWNGIPLTGKTYEEV 4599
Cdd:cd06714      2 FLIGRIILQRDPKDGSVSGNGLGLKVVGGKMTE--SGRLGAYVTKVKPGSVADTVGHLREGDEVLEWNGISLQGKTFEEV 79

                           90
                   ....*....|....*.
gi 2032737686 4600 QSIIIQQSGEAEICVR 4615
Cdd:cd06714     80 QDIISQSKGEVELVVS 95
FYVE2_PCLO cd15776
FYVE-related domain 2 found in protein piccolo; Protein piccolo, also termed aczonin, is a ...
 919-982 2.68e-42

FYVE-related domain 2 found in protein piccolo; Protein piccolo, also termed aczonin, is a neuron-specific presynaptic active zone scaffolding protein that mainly interacts with a detergent-resistant cytoskeletal-like subcellular fraction and is involved in the organization of the interplay between neurotransmitter vesicles, the cytoskeleton, and the plasma membrane at synaptic active zones. It binds profilin, an actin-binding protein implicated in actin cytoskeletal dynamics. It also functions as a presynaptic low-affinity Ca2+ sensor and has been implicated in Ca2+ regulation of neurotransmitter release. Piccolo is a multi-domain protein containing two N-terminal FYVE zinc fingers, a polyproline tract, and a PDZ domain and two C-terminal C2 domains. This family corresponds to the second FYVE domain, which resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif.


Pssm-ID: 277315 [Multi-domain]  Cd Length: 64  Bit Score: 150.22  E-value: 2.68e-42
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2032737686  919 MSCPLCKTGLNIGSKDPPNFNTCTECKKVVCNLCGFNPMPHIAEVQEWLCLNCQTQRAMSGQLG 982
Cdd:cd15776      1 LLCPLCKTELNIGSKDPPNFNTCTECKKTVCNLCGFNPTPHLTEVKEWLCLNCQTQRAMSGQLG 64
FYVE1_PCLO cd15774
FYVE-related domain 1 found in protein piccolo; Protein piccolo, also termed aczonin, is a ...
 452-513 8.03e-42

FYVE-related domain 1 found in protein piccolo; Protein piccolo, also termed aczonin, is a neuron-specific presynaptic active zone scaffolding protein that mainly interacts with a detergent-resistant cytoskeletal-like subcellular fraction and is involved in the organization of the interplay between neurotransmitter vesicles, the cytoskeleton, and the plasma membrane at synaptic active zones. It binds profilin, an actin-binding protein implicated in actin cytoskeletal dynamics. It also functions as a presynaptic low-affinity Ca2+ sensor and has been implicated in Ca2+ regulation of neurotransmitter release. Piccolo is a multi-domain protein containing two N-terminal FYVE zinc fingers, a polyproline tract, and a PDZ domain and two C-terminal C2 domains. This family corresponds to the first FYVE domain, which resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif.


Pssm-ID: 277313 [Multi-domain]  Cd Length: 62  Bit Score: 148.64  E-value: 8.03e-42
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2032737686  452 TFCPLCTTTELLLHTPEKANYNTCTQCHTVVCSLCGFNPNPHITEISEWLCLNCQMQRTLGG 513
Cdd:cd15774      1 TICPLCKTTELLLHTPEKANYNTCTQCQTTVCSLCGFNPNPHITEKKEWLCLNCQMQRALGG 62
zf-piccolo pfam05715
Piccolo Zn-finger; This (predicted) Zinc finger is found in the bassoon and piccolo proteins. ...
 920-977 6.15e-37

Piccolo Zn-finger; This (predicted) Zinc finger is found in the bassoon and piccolo proteins. There are eight conserved cysteines, suggesting that it coordinates two zinc ligands.


Pssm-ID: 461722 [Multi-domain]  Cd Length: 60  Bit Score: 134.85  E-value: 6.15e-37
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2032737686  920 SCPLCK-TGLNIGSKDPPNFNTCTECKKVVCNLCGFNPMPHIAEVQEWLCLNCQTQRAM 977
Cdd:pfam05715    2 LCPLCKtTELNVGSKEPPNYNTCTECKSQVCNLCGFNPTPHLTEKKEWLCLNCQTQRAL 60
FYVE2_BSN_PCLO cd15772
FYVE-related domain 2 found in protein bassoon and piccolo; This family includes protein ...
 920-982 1.64e-36

FYVE-related domain 2 found in protein bassoon and piccolo; This family includes protein bassoon and piccolo. Protein bassoon, also termed zinc finger protein 231, is a core component of the presynaptic cytomatrix. It is a vertebrate-specific active zone scaffolding protein that plays a key role in structural organization and functional regulation of presynaptic release sites. Bassoon may modulate synaptic transmission efficiency by binding to presynaptic P/Q-type voltage-dependent calcium channel (VDCC) complexes and modify the channel function. As one of the most highly phosphorylated synaptic proteins, bassoon can interact with the small ubiquitous adaptor protein 14-3-3 in a phosphorylation-dependent manner, which modulates its anchoring to the presynaptic cytomatrix. Protein piccolo, also termed aczonin, is a neuron-specific presynaptic active zone scaffolding protein that mainly interacts with a detergent-resistant cytoskeletal-like subcellular fraction and is involved in the organization of the interplay between neurotransmitter vesicles, the cytoskeleton, and the plasma membrane at synaptic active zones. It binds profilin, an actin-binding protein implicated in actin cytoskeletal dynamics. It also functions as a presynaptic low-affinity Ca2+ sensor and has been implicated in Ca2+ regulation of neurotransmitter release. Both bassoon and piccolo contain two N-terminal FYVE zinc fingers, a PDZ domain and two C-terminal C2 domains. Their FYVE domain resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif. This model corresponds to the second FYVE-related domain.


Pssm-ID: 277311 [Multi-domain]  Cd Length: 64  Bit Score: 133.62  E-value: 1.64e-36
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2032737686  920 SCPLCKTGLNIGSKDPPNFNTCTECKKVVCNLCGFNPMPHIAEVQEWLCLNCQTQRAMSGQLG 982
Cdd:cd15772      2 TCPLCKTELNVGSKEPPNYNTCTQCHTQVCNLCGFNPTPHLVEKKEWLCLNCQTQRLMSGGLG 64
zf-piccolo pfam05715
Piccolo Zn-finger; This (predicted) Zinc finger is found in the bassoon and piccolo proteins. ...
 452-511 3.34e-36

Piccolo Zn-finger; This (predicted) Zinc finger is found in the bassoon and piccolo proteins. There are eight conserved cysteines, suggesting that it coordinates two zinc ligands.


Pssm-ID: 461722 [Multi-domain]  Cd Length: 60  Bit Score: 132.54  E-value: 3.34e-36
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  452 TFCPLCTTTELLLHTPEKANYNTCTQCHTVVCSLCGFNPNPHITEISEWLCLNCQMQRTL 511
Cdd:pfam05715    1 TLCPLCKTTELNVGSKEPPNYNTCTECKSQVCNLCGFNPTPHLTEKKEWLCLNCQTQRAL 60
FYVE1_BSN_PCLO cd15771
FYVE-related domain 1 found in protein bassoon and piccolo; This family includes protein ...
 452-513 3.97e-34

FYVE-related domain 1 found in protein bassoon and piccolo; This family includes protein bassoon and piccolo. Protein bassoon, also termed zinc finger protein 231, is a core component of the presynaptic cytomatrix. It is a vertebrate-specific active zone scaffolding protein that plays a key role in structural organization and functional regulation of presynaptic release sites. Bassoon may modulate synaptic transmission efficiency by binding to presynaptic P/Q-type voltage-dependent calcium channel (VDCC) complexes and modify the channel function. As one of the most highly phosphorylated synaptic proteins, bassoon can interact with the small ubiquitous adaptor protein 14-3-3 in a phosphorylation-dependent manner, which modulates its anchoring to the presynaptic cytomatrix. Protein piccolo, also termed aczonin, is a neuron-specific presynaptic active zone scaffolding protein that mainly interacts with a detergent-resistant cytoskeletal-like subcellular fraction and is involved in the organization of the interplay between neurotransmitter vesicles, the cytoskeleton, and the plasma membrane at synaptic active zones. It binds profilin, an actin-binding protein implicated in actin cytoskeletal dynamics. It also functions as a presynaptic low-affinity Ca2+ sensor and has been implicated in Ca2+ regulation of neurotransmitter release. Both bassoon and piccolo contain two N-terminal FYVE zinc fingers, a PDZ domain and two C-terminal C2 domains. Their FYVE domain resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif. This model corresponds to the first FYVE-related domain.


Pssm-ID: 277310 [Multi-domain]  Cd Length: 61  Bit Score: 126.66  E-value: 3.97e-34
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2032737686  452 TFCPLCTTTELLLHTPeKANYNTCTQCHTVVCSLCGFNPNPHITEISEWLCLNCQMQRTLGG 513
Cdd:cd15771      1 TLCPLCNTTELTLHVP-KPNFNTCTQCHTTVCNQCGFNPNPHLTEVKEWLCLNCQMQRALGM 61
FYVE2_BSN cd15775
FYVE-related domain 2 found in protein bassoon; Protein bassoon, also termed zinc finger ...
 918-982 4.16e-33

FYVE-related domain 2 found in protein bassoon; Protein bassoon, also termed zinc finger protein 231, is a core component of the presynaptic cytomatrix. It is a vertebrate-specific active zone scaffolding protein that plays a key role in structural organization and functional regulation of presynaptic release sites. Bassoon may modulate synaptic transmission efficiency by binding to presynaptic P/Q-type voltage-dependent calcium channel (VDCC) complexes and modify the channel function. As one of the most highly phosphorylated synaptic proteins, bassoon can interact with the small ubiquitous adaptor protein 14-3-3 in a phosphorylation-dependent manner, which modulates its anchoring to the presynaptic cytomatrix. Bassoon contains two N-terminal FYVE zinc fingers, a PDZ domain and two C-terminal C2 domains. This family corresponds to the second FYVE domain, which resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif.


Pssm-ID: 277314 [Multi-domain]  Cd Length: 65  Bit Score: 123.87  E-value: 4.16e-33
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2032737686  918 EMSCPLCKTGLNIGSKDPPNFNTCTECKKVVCNLCGFNPMPHIAEVQEWLCLNCQTQRAMSGQLG 982
Cdd:cd15775      1 RVTCPLCKTELNVGSTEPPNYNTCTSCRTQVCNLCGFNPTPHLVEKNEWLCLNCQTQRLLEGSLG 65
C2A_SLP cd08521
C2 domain first repeat present in Synaptotagmin-like proteins; All Slp members basically share ...
 4723-4854 4.43e-33

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.


Pssm-ID: 176056 [Multi-domain]  Cd Length: 123  Bit Score: 126.22  E-value: 4.43e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4723 GEIQLQINYDKHLGNLIIHILQARNLAPRDN-NGYSDPFVKVYLLPGRgqvmvvqnaSAEYKRRTKYIQKSLNPEWNQTV 4801
Cdd:cd08521      1 GEIEFSLSYNYKTGSLEVHIKECRNLAYADEkKKRSNPYVKVYLLPDK---------SKQSKRKTSVKKNTTNPVFNETL 71

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2032737686 4802 IYKnISVEQLKKKTLEVTVWDYDRFSSNDFLGEVLIELSSISQLDNTPRWYPL 4854
Cdd:cd08521     72 KYH-ISKSQLETRTLQLSVWHHDRFGRNTFLGEVEIPLDSWDLDSQQSEWYPL 123
C2 pfam00168
C2 domain;
4736-4854 1.11e-32

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 124.35  E-value: 1.11e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4736 GNLIIHILQARNLAPRDNNGYSDPFVKVYLLPGrgqvmvvqnasaEYKRRTKYIQKSLNPEWNQTVIYkniSVEQLKKKT 4815
Cdd:pfam00168    1 GRLTVTVIEAKNLPPKDGNGTSDPYVKVYLLDG------------KQKKKTKVVKNTLNPVWNETFTF---SVPDPENAV 65

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2032737686 4816 LEVTVWDYDRFSSNDFLGEVLIELSSISQLDNTPRWYPL 4854
Cdd:pfam00168   66 LEIEVYDYDRFGRDDFIGEVRIPLSELDSGEGLDGWYPL 104
FYVE1_BSN cd15773
FYVE-related domain 1 found in protein bassoon; Protein bassoon, also termed zinc finger ...
 449-512 3.82e-31

FYVE-related domain 1 found in protein bassoon; Protein bassoon, also termed zinc finger protein 231, is a core component of the presynaptic cytomatrix. It is a vertebrate-specific active zone scaffolding protein that plays a key role in structural organization and functional regulation of presynaptic release sites. Bassoon may modulate synaptic transmission efficiency by binding to presynaptic P/Q-type voltage-dependent calcium channel (VDCC) complexes and modify the channel function. As one of the most highly phosphorylated synaptic proteins, bassoon can interact with the small ubiquitous adaptor protein 14-3-3 in a phosphorylation-dependent manner, which modulates its anchoring to the presynaptic cytomatrix. Bassoon contains two N-terminal FYVE zinc fingers, a PDZ domain and two C-terminal C2 domains. This family corresponds to the first FYVE domain, which resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif.


Pssm-ID: 277312 [Multi-domain]  Cd Length: 64  Bit Score: 118.26  E-value: 3.82e-31
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2032737686  449 PKKTFCPLCTTTELLlHTPEKANYNTCTQCHTVVCSLCGFNPNPHITEISEWLCLNCQMQRTLG 512
Cdd:cd15773      1 PSSTLCPICNTTELT-SFPSQPNFNTCTQCHNKVCNQCGFNPNPHLTEVKEWLCLNCQMQRALG 63
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 4738-4854 2.05e-29

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.


Pssm-ID: 175973 [Multi-domain]  Cd Length: 102  Bit Score: 114.86  E-value: 2.05e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4738 LIIHILQARNLAPRDNNGYSDPFVKVYLLPGRgqvmvvqnasaeyKRRTKYIQKSLNPEWNQTViykNISVEQLKKKTLE 4817
Cdd:cd00030      1 LRVTVIEARNLPAKDLNGKSDPYVKVSLGGKQ-------------KFKTKVVKNTLNPVWNETF---EFPVLDPESDTLT 64

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2032737686 4818 VTVWDYDRFSSNDFLGEVLIELSSI-SQLDNTPRWYPL 4854
Cdd:cd00030     65 VEVWDKDRFSKDDFLGEVEIPLSELlDSGKEGELWLPL 102
C2B_SLP_1-2-3-4 cd04020
C2 domain second repeat present in Synaptotagmin-like proteins 1-4; All Slp members basically ...
 4710-4841 3.93e-29

C2 domain second repeat present in Synaptotagmin-like proteins 1-4; 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. 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.


Pssm-ID: 175987 [Multi-domain]  Cd Length: 162  Bit Score: 116.27  E-value: 3.93e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4710 PTETTKSASHPITGEIQlqinydkhlgnliIHILQARNLAPRDNNGYSDPFVKVYLLPGRgqvmvvqnaSAEYKRRTKYI 4789
Cdd:cd04020     14 ESEGALKSKKPSTGELH-------------VWVKEAKNLPALKSGGTSDSFVKCYLLPDK---------SKKSKQKTPVV 71

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2032737686 4790 QKSLNPEWNQTVIYKNISVEQLKKKTLEVTVWDYDRFSSNDFLGEVLIELSS 4841
Cdd:cd04020     72 KKSVNPVWNHTFVYDGVSPEDLSQACLELTVWDHDKLSSNDFLGGVRLGLGT 123
C2_PKC_alpha_gamma cd04026
C2 domain in Protein Kinase C (PKC) alpha and gamma; A single C2 domain is found in PKC alpha ...
 4723-4859 6.57e-29

C2 domain in Protein Kinase C (PKC) alpha and gamma; A single C2 domain is found in PKC alpha and gamma. The PKC family of serine/threonine kinases regulates apoptosis, proliferation, migration, motility, chemo-resistance, and differentiation. There are 3 groups: group 1(alpha, betaI, beta II, gamma) which require phospholipids and calcium, group 2 (delta, epsilon, theta, eta) which do not require calcium for activation, and group 3 (xi, iota/lambda) which are atypical and can be activated in the absence of diacylglycerol and calcium. 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. Members here have a type-I topology.


Pssm-ID: 175992 [Multi-domain]  Cd Length: 131  Bit Score: 114.67  E-value: 6.57e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4723 GEIQLQINYDKhlGNLIIHILQARNLAPRDNNGYSDPFVKVYLLPgrgqvmvvqNASAEYKRRTKYIQKSLNPEWNQTVI 4802
Cdd:cd04026      2 GRIYLKISVKD--NKLTVEVREAKNLIPMDPNGLSDPYVKLKLIP---------DPKNETKQKTKTIKKTLNPVWNETFT 70

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2032737686 4803 YkNISvEQLKKKTLEVTVWDYDRFSSNDFLGEVLIELSSI--SQLDNtprWYPLKEQSE 4859
Cdd:cd04026     71 F-DLK-PADKDRRLSIEVWDWDRTTRNDFMGSLSFGVSELikMPVDG---WYKLLNQEE 124
C2B_Rabphilin_Doc2 cd08384
C2 domain second repeat present in Rabphilin and Double C2 domain; Rabphilin is found neurons ...
 4725-4841 3.35e-28

C2 domain second repeat present in Rabphilin and Double C2 domain; Rabphilin is found neurons and in neuroendrocrine cells, while Doc2 is found not only in the brain but in tissues, including mast cells, chromaffin cells, and osteoblasts. Rabphilin and Doc2s share highly homologous tandem C2 domains, although their N-terminal structures are completely different: rabphilin contains an N-terminal Rab-binding domain (RBD),7 whereas Doc2 contains an N-terminal Munc13-1-interacting domain (MID). 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.


Pssm-ID: 176030 [Multi-domain]  Cd Length: 133  Bit Score: 112.44  E-value: 3.35e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4725 IQLQINYDKHLGNLIIHILQARNLAPRDNNGYSDPFVKVYLLPgrgqvmvvqNASAEYKRRTKYIQKSLNPEWNQTVIYK 4804
Cdd:cd08384      2 ILVSLMYNTQRRGLIVGIIRCVNLAAMDANGYSDPFVKLYLKP---------DAGKKSKHKTQVKKKTLNPEFNEEFFYD 72

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2032737686 4805 nISVEQLKKKTLEVTVWDYDRFSSNDFLGEVLIELSS 4841
Cdd:cd08384     73 -IKHSDLAKKTLEITVWDKDIGKSNDYIGGLQLGINA 108
C2B_PI3K_class_II cd08381
C2 domain second repeat present in class II phosphatidylinositol 3-kinases (PI3Ks); There are ...
 4722-4855 3.56e-28

C2 domain second repeat present in class II phosphatidylinositol 3-kinases (PI3Ks); There are 3 classes of PI3Ks based on structure, regulation, and specificity. All classes contain a N-terminal C2 domain, a PIK domain, and a kinase catalytic domain. Unlike class I and class III, class II PI3Ks have additionally a PX domain and a C-terminal C2 domain containing a nuclear localization signal both of which bind phospholipids though in a slightly different fashion. PI3Ks (AKA phosphatidylinositol (PtdIns) 3-kinases) regulate cell processes such as cell growth, differentiation, proliferation, and motility. PI3Ks work on phosphorylation of phosphatidylinositol, phosphatidylinositide (4)P (PtdIns (4)P),2 or PtdIns(4,5)P2. Specifically they phosphorylate the D3 hydroxyl group of phosphoinositol lipids on the inositol ring. 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.


Pssm-ID: 176027 [Multi-domain]  Cd Length: 122  Bit Score: 112.00  E-value: 3.56e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4722 TGEIQLQINYDKhlGNLIIHILQARNLAPRDNNgYSDPFVKVYLLPgrgqvmvvqNASAEYKRRTKYIQKSLNPEWNQTV 4801
Cdd:cd08381      1 GGQVKLSISYKN--GTLFVMVMHAKNLPLLDGS-DPDPYVKTYLLP---------DPQKTTKRKTKVVRKTRNPTFNEML 68

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2032737686 4802 IYKNISVEQLKKKTLEVTVWDYDRFSSNDFLGEVLIELSSISQLDNTPRWYPLK 4855
Cdd:cd08381     69 VYDGLPVEDLQQRVLQVSVWSHDSLVENEFLGGVCIPLKKLDLSQETEKWYPLG 122
C2A_SLP-1_2 cd08393
C2 domain first repeat present in Synaptotagmin-like proteins 1 and 2; All Slp members ...
 4723-4855 4.30e-28

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.


Pssm-ID: 176039 [Multi-domain]  Cd Length: 125  Bit Score: 111.76  E-value: 4.30e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4723 GEIQLQINYDKHLGNLIIHILQARNLAPRD-NNGYSDPFVKVYLLPGRgqvmvvqnaSAEYKRRTKYIQKSLNPEWNQTV 4801
Cdd:cd08393      2 GSVQFALDYDPKLRELHVHVIQCQDLAAADpKKQRSDPYVKTYLLPDK---------SNRGKRKTSVKKKTLNPVFNETL 72

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2032737686 4802 IYKnISVEQLKKKTLEVTVWDYDRFSSNDFLGEVLIELSSISQLDNTPRWYPLK 4855
Cdd:cd08393     73 RYK-VEREELPTRVLNLSVWHRDSLGRNSFLGEVEVDLGSWDWSNTQPTWYPLQ 125
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 4738-4851 8.23e-28

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.


Pssm-ID: 214577 [Multi-domain]  Cd Length: 101  Bit Score: 110.27  E-value: 8.23e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  4738 LIIHILQARNLAPRDNNGYSDPFVKVYLLPGRGQvmvvqnasaeyKRRTKYIQKSLNPEWNQTVIYkniSVEQLKKKTLE 4817
Cdd:smart00239    2 LTVKIISARNLPPKDKGGKSDPYVKVSLDGDPKE-----------KKKTKVVKNTLNPVWNETFEF---EVPPPELAELE 67

                            90       100       110
                    ....*....|....*....|....*....|....
gi 2032737686  4818 VTVWDYDRFSSNDFLGEVLIELSSISQLDNTPRW 4851
Cdd:smart00239   68 IEVYDKDRFGRDDFIGQVTIPLSDLLLGGRHEKL 101
C2A_Synaptotagmin-7 cd08386
C2A domain first repeat present in Synaptotagmin 7; Synaptotagmin is a membrane-trafficking ...
 4723-4855 1.18e-27

C2A domain first repeat present in Synaptotagmin 7; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Synaptotagmin 7, a member of class 2 synaptotagmins, is located in presynaptic plasma membranes in neurons, dense-core vesicles in endocrine cells, and lysosomes in fibroblasts. It has been shown to play a role in regulation of Ca2+-dependent lysosomal exocytosis in fibroblasts and may also function as a vesicular Ca2+-sensor. It is distinguished from the other synaptotagmins by having over 12 splice forms. 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.


Pssm-ID: 176032 [Multi-domain]  Cd Length: 125  Bit Score: 110.50  E-value: 1.18e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4723 GEIQLQINYDKHLGNLIIHILQARNLAPRDNNGYSDPFVKVYLLPGRGQvmvvqnasaeyKRRTKYIQKSLNPEWNQTVI 4802
Cdd:cd08386      3 GRIQFSVSYDFQESTLTLKILKAVELPAKDFSGTSDPFVKIYLLPDKKH-----------KLETKVKRKNLNPHWNETFL 71

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2032737686 4803 YKNISVEQLKKKTLEVTVWDYDRFSSNDFLGEVLIELSSISQLDNTPRWYPLK 4855
Cdd:cd08386     72 FEGFPYEKLQQRVLYLQVLDYDRFSRNDPIGEVSLPLNKVDLTEEQTFWKDLK 124
C2A_Rabphilin_Doc2 cd04035
C2 domain first repeat present in Rabphilin and Double C2 domain; Rabphilin is found neurons ...
 4723-4840 1.62e-27

C2 domain first repeat present in Rabphilin and Double C2 domain; Rabphilin is found neurons and in neuroendrocrine cells, while Doc2 is found not only in the brain but in tissues, including mast cells, chromaffin cells, and osteoblasts. Rabphilin and Doc2s share highly homologous tandem C2 domains, although their N-terminal structures are completely different: rabphilin contains an N-terminal Rab-binding domain (RBD),7 whereas Doc2 contains an N-terminal Munc13-1-interacting domain (MID). 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.


Pssm-ID: 176000 [Multi-domain]  Cd Length: 123  Bit Score: 110.06  E-value: 1.62e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4723 GEIQLQINYDKHLGNLIIHILQARNLAPRDNNGYSDPFVKVYLLPGrgqvmvvqnASAEYKRRTKYIQKSLNPEWNQTVI 4802
Cdd:cd04035      2 GTLEFTLLYDPANSALHCTIIRAKGLKAMDANGLSDPYVKLNLLPG---------ASKATKLRTKTVHKTRNPEFNETLT 72

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2032737686 4803 YKNISVEQLKKKTLEVTVWDYDRFsSNDFLGEVLIELS 4840
Cdd:cd04035     73 YYGITEEDIQRKTLRLLVLDEDRF-GNDFLGETRIPLK 109
FYVE_BSN_PCLO cd15751
FYVE-related domain found in protein bassoon and piccolo; This family includes protein bassoon ...
 921-977 8.33e-27

FYVE-related domain found in protein bassoon and piccolo; This family includes protein bassoon and piccolo. Protein bassoon, also termed zinc finger protein 231, is a core component of the presynaptic cytomatrix. It is a vertebrate-specific active zone scaffolding protein that plays a key role in structural organization and functional regulation of presynaptic release sites. Bassoon may modulate synaptic transmission efficiency by binding to presynaptic P/Q-type voltage-dependent calcium channel (VDCC) complexes and modify the channel function. As one of the most highly phosphorylated synaptic proteins, bassoon can interact with the small ubiquitous adaptor protein 14-3-3 in a phosphorylation-dependent manner, which modulates its anchoring to the presynaptic cytomatrix. Protein piccolo, also termed aczonin, is a neuron-specific presynaptic active zone scaffolding protein that mainly interacts with a detergent-resistant cytoskeletal-like subcellular fraction and is involved in the organization of the interplay between neurotransmitter vesicles, the cytoskeleton, and the plasma membrane at synaptic active zones. It binds profilin, an actin-binding protein implicated in actin cytoskeletal dynamics. It also functions as a presynaptic low-affinity Ca2+ sensor and has been implicated in Ca2+ regulation of neurotransmitter release. Both bassoon and piccolo contain two N-terminal FYVE zinc fingers, a PDZ domain and two C-terminal C2 domains. Their FYVE domain resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif.


Pssm-ID: 277290 [Multi-domain]  Cd Length: 62  Bit Score: 106.00  E-value: 8.33e-27
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2032737686  921 CPLCK-TGLNIGSKDPPNFNTCTECKKVVCNLCGFNPMPHIAEVQEWLCLNCQTQRAM 977
Cdd:cd15751      3 CPLCGtSELPLGSKSPPNYNTCTDCKNRVCNQCGFNSTPPVTKVKEWLCLNCQKKRAL 60
C2A_Synaptotagmin-1-5-6-9-10 cd08385
C2A domain first repeat present in Synaptotagmins 1, 5, 6, 9, and 10; Synaptotagmin is a ...
 4723-4851 1.08e-26

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.


Pssm-ID: 176031 [Multi-domain]  Cd Length: 124  Bit Score: 107.74  E-value: 1.08e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4723 GEIQLQINYDKHLGNLIIHILQARNLAPRDNNGYSDPFVKVYLLPGRGQvmvvqnasaeyKRRTKYIQKSLNPEWNQTVI 4802
Cdd:cd08385      3 GKLQFSLDYDFQSNQLTVGIIQAADLPAMDMGGTSDPYVKVYLLPDKKK-----------KFETKVHRKTLNPVFNETFT 71

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2032737686 4803 YKnISVEQLKKKTLEVTVWDYDRFSSNDFLGEVLIELSSISQLDNTPRW 4851
Cdd:cd08385     72 FK-VPYSELGNKTLVFSVYDFDRFSKHDLIGEVRVPLLTVDLGHVTEEW 119
FYVE1_PCLO cd15774
FYVE-related domain 1 found in protein piccolo; Protein piccolo, also termed aczonin, is a ...
 921-979 5.58e-26

FYVE-related domain 1 found in protein piccolo; Protein piccolo, also termed aczonin, is a neuron-specific presynaptic active zone scaffolding protein that mainly interacts with a detergent-resistant cytoskeletal-like subcellular fraction and is involved in the organization of the interplay between neurotransmitter vesicles, the cytoskeleton, and the plasma membrane at synaptic active zones. It binds profilin, an actin-binding protein implicated in actin cytoskeletal dynamics. It also functions as a presynaptic low-affinity Ca2+ sensor and has been implicated in Ca2+ regulation of neurotransmitter release. Piccolo is a multi-domain protein containing two N-terminal FYVE zinc fingers, a polyproline tract, and a PDZ domain and two C-terminal C2 domains. This family corresponds to the first FYVE domain, which resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif.


Pssm-ID: 277313 [Multi-domain]  Cd Length: 62  Bit Score: 103.57  E-value: 5.58e-26
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  921 CPLCK-TGLNIGSKDPPNFNTCTECKKVVCNLCGFNPMPHIAEVQEWLCLNCQTQRAMSG 979
Cdd:cd15774      3 CPLCKtTELLLHTPEKANYNTCTQCQTTVCSLCGFNPNPHITEKKEWLCLNCQMQRALGG 62
FYVE2_BSN cd15775
FYVE-related domain 2 found in protein bassoon; Protein bassoon, also termed zinc finger ...
 451-516 1.47e-25

FYVE-related domain 2 found in protein bassoon; Protein bassoon, also termed zinc finger protein 231, is a core component of the presynaptic cytomatrix. It is a vertebrate-specific active zone scaffolding protein that plays a key role in structural organization and functional regulation of presynaptic release sites. Bassoon may modulate synaptic transmission efficiency by binding to presynaptic P/Q-type voltage-dependent calcium channel (VDCC) complexes and modify the channel function. As one of the most highly phosphorylated synaptic proteins, bassoon can interact with the small ubiquitous adaptor protein 14-3-3 in a phosphorylation-dependent manner, which modulates its anchoring to the presynaptic cytomatrix. Bassoon contains two N-terminal FYVE zinc fingers, a PDZ domain and two C-terminal C2 domains. This family corresponds to the second FYVE domain, which resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif.


Pssm-ID: 277314 [Multi-domain]  Cd Length: 65  Bit Score: 102.30  E-value: 1.47e-25
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2032737686  451 KTFCPLCTTtELLLHTPEKANYNTCTQCHTVVCSLCGFNPNPHITEISEWLCLNCQMQRTLGGDLA 516
Cdd:cd15775      1 RVTCPLCKT-ELNVGSTEPPNYNTCTSCRTQVCNLCGFNPTPHLVEKNEWLCLNCQTQRLLEGSLG 65
FYVE1_BSN_PCLO cd15771
FYVE-related domain 1 found in protein bassoon and piccolo; This family includes protein ...
 921-979 2.32e-25

FYVE-related domain 1 found in protein bassoon and piccolo; This family includes protein bassoon and piccolo. Protein bassoon, also termed zinc finger protein 231, is a core component of the presynaptic cytomatrix. It is a vertebrate-specific active zone scaffolding protein that plays a key role in structural organization and functional regulation of presynaptic release sites. Bassoon may modulate synaptic transmission efficiency by binding to presynaptic P/Q-type voltage-dependent calcium channel (VDCC) complexes and modify the channel function. As one of the most highly phosphorylated synaptic proteins, bassoon can interact with the small ubiquitous adaptor protein 14-3-3 in a phosphorylation-dependent manner, which modulates its anchoring to the presynaptic cytomatrix. Protein piccolo, also termed aczonin, is a neuron-specific presynaptic active zone scaffolding protein that mainly interacts with a detergent-resistant cytoskeletal-like subcellular fraction and is involved in the organization of the interplay between neurotransmitter vesicles, the cytoskeleton, and the plasma membrane at synaptic active zones. It binds profilin, an actin-binding protein implicated in actin cytoskeletal dynamics. It also functions as a presynaptic low-affinity Ca2+ sensor and has been implicated in Ca2+ regulation of neurotransmitter release. Both bassoon and piccolo contain two N-terminal FYVE zinc fingers, a PDZ domain and two C-terminal C2 domains. Their FYVE domain resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif. This model corresponds to the first FYVE-related domain.


Pssm-ID: 277310 [Multi-domain]  Cd Length: 61  Bit Score: 101.62  E-value: 2.32e-25
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2032737686  921 CPLCKTGLNIGSKDPPNFNTCTECKKVVCNLCGFNPMPHIAEVQEWLCLNCQTQRAMSG 979
Cdd:cd15771      3 CPLCNTTELTLHVPKPNFNTCTQCHTTVCNQCGFNPNPHLTEVKEWLCLNCQMQRALGM 61
FYVE2_BSN_PCLO cd15772
FYVE-related domain 2 found in protein bassoon and piccolo; This family includes protein ...
 454-515 3.06e-25

FYVE-related domain 2 found in protein bassoon and piccolo; This family includes protein bassoon and piccolo. Protein bassoon, also termed zinc finger protein 231, is a core component of the presynaptic cytomatrix. It is a vertebrate-specific active zone scaffolding protein that plays a key role in structural organization and functional regulation of presynaptic release sites. Bassoon may modulate synaptic transmission efficiency by binding to presynaptic P/Q-type voltage-dependent calcium channel (VDCC) complexes and modify the channel function. As one of the most highly phosphorylated synaptic proteins, bassoon can interact with the small ubiquitous adaptor protein 14-3-3 in a phosphorylation-dependent manner, which modulates its anchoring to the presynaptic cytomatrix. Protein piccolo, also termed aczonin, is a neuron-specific presynaptic active zone scaffolding protein that mainly interacts with a detergent-resistant cytoskeletal-like subcellular fraction and is involved in the organization of the interplay between neurotransmitter vesicles, the cytoskeleton, and the plasma membrane at synaptic active zones. It binds profilin, an actin-binding protein implicated in actin cytoskeletal dynamics. It also functions as a presynaptic low-affinity Ca2+ sensor and has been implicated in Ca2+ regulation of neurotransmitter release. Both bassoon and piccolo contain two N-terminal FYVE zinc fingers, a PDZ domain and two C-terminal C2 domains. Their FYVE domain resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif. This model corresponds to the second FYVE-related domain.


Pssm-ID: 277311 [Multi-domain]  Cd Length: 64  Bit Score: 101.65  E-value: 3.06e-25
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2032737686  454 CPLCTTtELLLHTPEKANYNTCTQCHTVVCSLCGFNPNPHITEISEWLCLNCQMQRTLGGDL 515
Cdd:cd15772      3 CPLCKT-ELNVGSKEPPNYNTCTQCHTQVCNLCGFNPTPHLVEKKEWLCLNCQTQRLMSGGL 63
C2A_SLP-4_5 cd04029
C2 domain first repeat present in Synaptotagmin-like proteins 4 and 5; All Slp members ...
 4722-4854 9.39e-25

C2 domain first repeat present in Synaptotagmin-like proteins 4 and 5; 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. SHD of Slp (except for the Slp4-SHD) function as a specific Rab27A/B-binding domain. In addition to Slp, rabphilin, Noc2, and Munc13-4 also function as Rab27-binding proteins. It has been demonstrated that Slp4/granuphilin promotes dense-core vesicle exocytosis. The C2A domain of Slp4 is Ca2+ dependent. 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.


Pssm-ID: 175995 [Multi-domain]  Cd Length: 125  Bit Score: 102.52  E-value: 9.39e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4722 TGEIQLQINYDKHLGNLIIHILQARNLAPRDNNGY-SDPFVKVYLLPGRgqvmvvqnaSAEYKRRTKYIQKSLNPEWNQT 4800
Cdd:cd04029      1 SGEILFSLSYDYKTQSLNVHVKECRNLAYGDEAKKrSNPYVKTYLLPDK---------SRQSKRKTSIKRNTTNPVYNET 71

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2032737686 4801 VIYKnISVEQLKKKTLEVTVWDYDRFSSNDFLGEVLIELSSiSQLDN-TPRWYPL 4854
Cdd:cd04029     72 LKYS-ISHSQLETRTLQLSVWHYDRFGRNTFLGEVEIPLDS-WNFDSqHEECLPL 124
C2C_KIAA1228 cd04030
C2 domain third repeat present in uncharacterized human KIAA1228-like proteins; KIAA proteins ...
 4722-4855 9.58e-25

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.


Pssm-ID: 175996 [Multi-domain]  Cd Length: 127  Bit Score: 102.35  E-value: 9.58e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4722 TGEIQLQINYDKHLGNLIIHILQARNLAPRDNNGYSDPFVKVYLLPGRgqvmvvqnaSAEYKRRTKYIQKSLNPEWNQTV 4801
Cdd:cd04030      2 LGRIQLTIRYSSQRQKLIVTVHKCRNLPPCDSSDIPDPYVRLYLLPDK---------SKSTRRKTSVKKDNLNPVFDETF 72

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2032737686 4802 IYkNISVEQLKKKTLEVTVWDYDRFSS--NDFLGEVLIELSSISQLDNTPRWYPLK 4855
Cdd:cd04030     73 EF-PVSLEELKRRTLDVAVKNSKSFLSreKKLLGQVLIDLSDLDLSKGFTQWYDLT 127
FYVE1_BSN cd15773
FYVE-related domain 1 found in protein bassoon; Protein bassoon, also termed zinc finger ...
 921-977 2.04e-24

FYVE-related domain 1 found in protein bassoon; Protein bassoon, also termed zinc finger protein 231, is a core component of the presynaptic cytomatrix. It is a vertebrate-specific active zone scaffolding protein that plays a key role in structural organization and functional regulation of presynaptic release sites. Bassoon may modulate synaptic transmission efficiency by binding to presynaptic P/Q-type voltage-dependent calcium channel (VDCC) complexes and modify the channel function. As one of the most highly phosphorylated synaptic proteins, bassoon can interact with the small ubiquitous adaptor protein 14-3-3 in a phosphorylation-dependent manner, which modulates its anchoring to the presynaptic cytomatrix. Bassoon contains two N-terminal FYVE zinc fingers, a PDZ domain and two C-terminal C2 domains. This family corresponds to the first FYVE domain, which resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif.


Pssm-ID: 277312 [Multi-domain]  Cd Length: 64  Bit Score: 99.39  E-value: 2.04e-24
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2032737686  921 CPLCKTGLNIGSKDPPNFNTCTECKKVVCNLCGFNPMPHIAEVQEWLCLNCQTQRAM 977
Cdd:cd15773      6 CPICNTTELTSFPSQPNFNTCTQCHNKVCNQCGFNPNPHLTEVKEWLCLNCQMQRAL 62
C2A_Synaptotagmin-8 cd08387
C2A domain first repeat present in Synaptotagmin 8; Synaptotagmin is a membrane-trafficking ...
 4722-4855 3.36e-24

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.


Pssm-ID: 176033 [Multi-domain]  Cd Length: 124  Bit Score: 100.94  E-value: 3.36e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4722 TGEIQLQINYDKHLGNLIIHILQARNLAPRDNNGYSDPFVKVYLLPGRGQVmvvqnasaeykRRTKYIQKSLNPEWNQTV 4801
Cdd:cd08387      2 RGELHFSLEYDKDMGILNVKLIQARNLQPRDFSGTADPYCKVRLLPDRSNT-----------KQSKIHKKTLNPEFDESF 70

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2032737686 4802 IYKnISVEQLKKKTLEVTVWDYDRFSSNDFLGEVLIELSSISQLDNTPRWYPLK 4855
Cdd:cd08387     71 VFE-VPPQELPKRTLEVLLYDFDQFSRDECIGVVELPLAEVDLSEKLDLWRKIQ 123
PHA03247 PHA03247
large tegument protein UL36; Provisional
 188-736 3.91e-24

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 113.49  E-value: 3.91e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  188 QKVAPKEQGKPEEQRSPAKHPTQP-QSPKPAVQQQGPVRPTVQQTESskqqqqpggpkqvqKPGhgqpADAKQDQAKQPA 266
Cdd:PHA03247  2541 EELASDDAGDPPPPLPPAAPPAAPdRSVPPPRPAPRPSEPAVTSRAR--------------RPD----APPQSARPRAPV 2602

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  267 QPRGPQKSQPQPSePTKPIQQQTSAKPSSG------------PTKPSPQQPDSTKVTSQTAPPTKPSSQ-QPGPAKQPSQ 333
Cdd:PHA03247  2603 DDRGDPRGPAPPS-PLPPDTHAPDPPPPSPspaanepdphppPTVPPPERPRDDPAPGRVSRPRRARRLgRAAQASSPPQ 2681

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  334 QPARQGAPVK----------PSPQQTGPPKQPSQQPGPEKPSAQQAGPAKQPPQPGSGKPPPQQTGLVKQVPPQAGPTkp 403
Cdd:PHA03247  2682 RPRRRAARPTvgsltsladpPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPAR-- 2759

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  404 PSQTVGPTKPLAQQAGPTKPPGQQPGPE-KPPQQTQAGANQPTETAPKKTFCPLCTTTELLLHTPEKANYNTCTQCHTVV 482
Cdd:PHA03247  2760 PPTTAGPPAPAPPAAPAAGPPRRLTRPAvASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAP 2839

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  483 CSLCGFNPNPhiteisewlclncqmqRTLGGDLAPG----LGPGPQPLAPKQKTPIPPSAKPSPQPQPVQKKDVTPKPDP 558
Cdd:PHA03247  2840 PPPPGPPPPS----------------LPLGGSVAPGgdvrRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPD 2903

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  559 SQAadskrPPPQkkqtqlPGSPPvkskQPRAEPTDISQQTDATPKSDQVKPtqaeDKQKQPSVQKPTADSVSTSVAAEQK 638
Cdd:PHA03247  2904 QPE-----RPPQ------PQAPP----PPQPQPQPPPPPQPQPPPPPPPRP----QPPLAPTTDPAGAGEPSGAVPQPWL 2964

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  639 QDLAGPRPPTQQKVTDSPKPELAKPSQDTHPagdkPDSKPVPQVSRQKSDPKFASQPGARPDAKAQK--PIDPTQTKDDP 716
Cdd:PHA03247  2965 GALVPGRVAVPRFRVPQPAPSREAPASSTPP----LTGHSLSRVSSWASSLALHEETDPPPVSLKQTlwPPDDTEDSDAD 3040

                          570       580
                   ....*....|....*....|....*.
gi 2032737686  717 KKLPTKP------APKPDTkPAPKGP 736
Cdd:PHA03247  3041 SLFDSDSersdleALDPLP-PEPHDP 3065
FYVE_BSN_PCLO cd15751
FYVE-related domain found in protein bassoon and piccolo; This family includes protein bassoon ...
 454-512 4.80e-23

FYVE-related domain found in protein bassoon and piccolo; This family includes protein bassoon and piccolo. Protein bassoon, also termed zinc finger protein 231, is a core component of the presynaptic cytomatrix. It is a vertebrate-specific active zone scaffolding protein that plays a key role in structural organization and functional regulation of presynaptic release sites. Bassoon may modulate synaptic transmission efficiency by binding to presynaptic P/Q-type voltage-dependent calcium channel (VDCC) complexes and modify the channel function. As one of the most highly phosphorylated synaptic proteins, bassoon can interact with the small ubiquitous adaptor protein 14-3-3 in a phosphorylation-dependent manner, which modulates its anchoring to the presynaptic cytomatrix. Protein piccolo, also termed aczonin, is a neuron-specific presynaptic active zone scaffolding protein that mainly interacts with a detergent-resistant cytoskeletal-like subcellular fraction and is involved in the organization of the interplay between neurotransmitter vesicles, the cytoskeleton, and the plasma membrane at synaptic active zones. It binds profilin, an actin-binding protein implicated in actin cytoskeletal dynamics. It also functions as a presynaptic low-affinity Ca2+ sensor and has been implicated in Ca2+ regulation of neurotransmitter release. Both bassoon and piccolo contain two N-terminal FYVE zinc fingers, a PDZ domain and two C-terminal C2 domains. Their FYVE domain resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif.


Pssm-ID: 277290 [Multi-domain]  Cd Length: 62  Bit Score: 95.21  E-value: 4.80e-23
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2032737686  454 CPLCTTTELLLHTPEKANYNTCTQCHTVVCSLCGFNPNPHITEISEWLCLNCQMQRTLG 512
Cdd:cd15751      3 CPLCGTSELPLGSKSPPNYNTCTDCKNRVCNQCGFNSTPPVTKVKEWLCLNCQKKRALG 61
FYVE2_PCLO cd15776
FYVE-related domain 2 found in protein piccolo; Protein piccolo, also termed aczonin, is a ...
 454-515 4.83e-23

FYVE-related domain 2 found in protein piccolo; Protein piccolo, also termed aczonin, is a neuron-specific presynaptic active zone scaffolding protein that mainly interacts with a detergent-resistant cytoskeletal-like subcellular fraction and is involved in the organization of the interplay between neurotransmitter vesicles, the cytoskeleton, and the plasma membrane at synaptic active zones. It binds profilin, an actin-binding protein implicated in actin cytoskeletal dynamics. It also functions as a presynaptic low-affinity Ca2+ sensor and has been implicated in Ca2+ regulation of neurotransmitter release. Piccolo is a multi-domain protein containing two N-terminal FYVE zinc fingers, a polyproline tract, and a PDZ domain and two C-terminal C2 domains. This family corresponds to the second FYVE domain, which resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif.


Pssm-ID: 277315 [Multi-domain]  Cd Length: 64  Bit Score: 95.13  E-value: 4.83e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2032737686  454 CPLCTTtELLLHTPEKANYNTCTQCHTVVCSLCGFNPNPHITEISEWLCLNCQMQRTLGGDL 515
Cdd:cd15776      3 CPLCKT-ELNIGSKDPPNFNTCTECKKTVCNLCGFNPTPHLTEVKEWLCLNCQTQRAMSGQL 63
C2B_Synaptotagmin cd00276
C2 domain second repeat present in Synaptotagmin; Synaptotagmin is a membrane-trafficking ...
 4723-4854 6.83e-23

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.


Pssm-ID: 175975 [Multi-domain]  Cd Length: 134  Bit Score: 97.27  E-value: 6.83e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4723 GEIQLQINYDKHLGNLIIHILQARNLAPRDNNGYSDPFVKVYLLPGRGQVmvvqnasaeYKRRTKYIQKSLNPEWNQTVI 4802
Cdd:cd00276      1 GELLLSLSYLPTAERLTVVVLKARNLPPSDGKGLSDPYVKVSLLQGGKKL---------KKKKTSVKKGTLNPVFNEAFS 71

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2032737686 4803 YkNISVEQLKKKTLEVTVWDYDRFSSNDFLGEVLIELSSIS-------QLDNTPR-----WYPL 4854
Cdd:cd00276     72 F-DVPAEQLEEVSLVITVVDKDSVGRNEVIGQVVLGPDSGGeelehwnEMLASPRkpiarWHKL 134
C2B_Synaptotagmin-7 cd08405
C2 domain second repeat present in Synaptotagmin 7; Synaptotagmin is a membrane-trafficking ...
 4723-4855 6.12e-22

C2 domain second repeat present in Synaptotagmin 7; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Synaptotagmin 7, a member of class 2 synaptotagmins, is located in presynaptic plasma membranes in neurons, dense-core vesicles in endocrine cells, and lysosomes in fibroblasts. It has been shown to play a role in regulation of Ca2+-dependent lysosomal exocytosis in fibroblasts and may also function as a vesicular Ca2+-sensor. It is distinguished from the other synaptotagmins by having over 12 splice forms. 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.


Pssm-ID: 176050 [Multi-domain]  Cd Length: 136  Bit Score: 94.79  E-value: 6.12e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4723 GEIQLQINYDKHLGNLIIHILQARNLAPRDNNGYSDPFVKVYLLPGRGQVmvvqnasaeYKRRTKYIQKSLNPEWNQTVI 4802
Cdd:cd08405      2 GELLLSLCYNPTANRITVNIIKARNLKAMDINGTSDPYVKVWLMYKDKRV---------EKKKTVIKKRTLNPVFNESFI 72

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2032737686 4803 YkNISVEQLKKKTLEVTVWDYDRFSSNDFLGEVLI-------ELSSISQLDNTPR-----WYPLK 4855
Cdd:cd08405     73 F-NIPLERLRETTLIITVMDKDRLSRNDLIGKIYLgwksgglELKHWKDMLSKPRqpvaqWHRLK 136
C2B_Munc13-like cd04009
C2 domain second repeat in Munc13 (mammalian uncoordinated)-like proteins; C2-like domains are ...
 4723-4848 1.28e-20

C2 domain second repeat in Munc13 (mammalian uncoordinated)-like proteins; C2-like domains are thought to be involved in phospholipid binding in a Ca2+ independent manner in both Unc13 and Munc13. Caenorabditis elegans Unc13 has a central domain with sequence similarity to PKC, which includes C1 and C2-related domains. Unc13 binds phorbol esters and DAG with high affinity in a phospholipid manner. Mutations in Unc13 results in abnormal neuronal connections and impairment in cholinergic neurotransmission in the nematode. Munc13 is the mammalian homolog which are expressed in the brain. There are 3 isoforms (Munc13-1, -2, -3) and are thought to play a role in neurotransmitter release and are hypothesized to be high-affinity receptors for phorbol esters. Unc13 and Munc13 contain both C1 and C2 domains. There are two C2 related domains present, one central and one at the carboxyl end. Munc13-1 contains a third C2-like domain. Munc13 interacts with syntaxin, synaptobrevin, and synaptotagmin suggesting a role for these as scaffolding 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 third C2 repeat, C2C, and has a type-II topology.


Pssm-ID: 175976 [Multi-domain]  Cd Length: 133  Bit Score: 90.76  E-value: 1.28e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4723 GEIQLQINYDKHLGNLIIHILQARNLAPRDNNGYSDPFVKVYLLPGRGQVMVVqnasaeyKRRTKYIQKSLNPEWNQTvI 4802
Cdd:cd04009      3 GVLTVKAYYRASEQSLRVEILNARNLLPLDSNGSSDPFVKVELLPRHLFPDVP-------TPKTQVKKKTLFPLFDES-F 74

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 2032737686 4803 YKNISVEQLKKK--TLEVTVWDYDRFSSNDFLGEVLIELSSISQLDNT 4848
Cdd:cd04009     75 EFNVPPEQCSVEgaLLLFTVKDYDLLGSNDFEGEAFLPLNDIPGVEDT 122
C2B_Synaptotagmin-1 cd08402
C2 domain second repeat present in Synaptotagmin 1; Synaptotagmin is a membrane-trafficking ...
 4723-4855 1.59e-20

C2 domain second repeat present in Synaptotagmin 1; 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 the 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. It, like synaptotagmin-2, has an N-glycosylated N-terminus. Synaptotagmin 4, a member of class 4 synaptotagmins, is located in the brain. It functions are unknown. It, like synaptotagmin-11, has an Asp to Ser substitution in its C2A domain. 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.


Pssm-ID: 176047 [Multi-domain]  Cd Length: 136  Bit Score: 90.54  E-value: 1.59e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4723 GEIQLQINYDKHLGNLIIHILQARNLAPRDNNGYSDPFVKVYLLPGRGQVMvvqnasaeyKRRTKYIQKSLNPEWNQTVI 4802
Cdd:cd08402      2 GDICFSLRYVPTAGKLTVVILEAKNLKKMDVGGLSDPYVKIHLMQNGKRLK---------KKKTTIKKRTLNPYYNESFS 72

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2032737686 4803 YKnISVEQLKKKTLEVTVWDYDRFSSNDFLGEVLI-------ELSSISQLDNTPR-----WYPLK 4855
Cdd:cd08402     73 FE-VPFEQIQKVHLIVTVLDYDRIGKNDPIGKVVLgcnatgaELRHWSDMLASPRrpiaqWHTLQ 136
C2D_Tricalbin-like cd04040
C2 domain fourth repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are ...
 4738-4857 2.37e-19

C2 domain fourth repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are present in Tricalbin, a yeast homolog of Synaptotagmin, which is involved in membrane trafficking and sorting. 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 fifth C2 repeat, C2E, and has a type-II topology.


Pssm-ID: 176005 [Multi-domain]  Cd Length: 115  Bit Score: 86.47  E-value: 2.37e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4738 LIIHILQARNLAPRDNNGYSDPFVKVYLlpgrgqvmvvqNASAEYKrrTKYIQKSLNPEWNQTViykNISVEQLKKKTLE 4817
Cdd:cd04040      1 LTVDVISAENLPSADRNGKSDPFVKFYL-----------NGEKVFK--TKTIKKTLNPVWNESF---EVPVPSRVRAVLK 64

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 2032737686 4818 VTVWDYDRFSSNDFLGEVLIELSSISQLDNTPRWYPLKEQ 4857
Cdd:cd04040     65 VEVYDWDRGGKDDLLGSAYIDLSDLEPEETTELTLPLDGQ 104
C2A_Synaptotagmin-like cd04024
C2 domain first repeat present in Synaptotagmin-like proteins; Synaptotagmin is a ...
 4736-4866 6.25e-19

C2 domain first repeat present in Synaptotagmin-like proteins; 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.


Pssm-ID: 175990 [Multi-domain]  Cd Length: 128  Bit Score: 85.94  E-value: 6.25e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4736 GNLIIHILQARNLAPRD--NNGYSDPFVKVYLlpgrgqvmvvqnasAEYKRRTKYIQKSLNPEWNqtvIYKNISVEQLKK 4813
Cdd:cd04024      1 GVLRVHVVEAKDLAAKDrsGKGKSDPYAILSV--------------GAQRFKTQTIPNTLNPKWN---YWCEFPIFSAQN 63

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2032737686 4814 KTLEVTVWDYDRFSSNDFLGEVLIELSSI---SQLDNTPRWYPLKEQSENIDHGKS 4866
Cdd:cd04024     64 QLLKLILWDKDRFAGKDYLGEFDIALEEVfadGKTGQSDKWITLKSTRPGKTSVVS 119
C2A_Synaptotagmin-15-17 cd08390
C2A domain first repeat present in Synaptotagmins 15 and 17; Synaptotagmin is a ...
 4723-4840 6.25e-19

C2A domain first repeat present in Synaptotagmins 15 and 17; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. It is thought to be involved in the trafficking and exocytosis of secretory vesicles in non-neuronal tissues and is Ca2+ independent. Human synaptotagmin 15 has 2 alternatively spliced forms that encode proteins with different C-termini. The larger, SYT15a, contains a N-terminal TM region, a putative fatty-acylation site, and 2 tandem C terminal C2 domains. The smaller, SYT15b, lacks the C-terminal portion of the second C2 domain. Unlike most other synaptotagmins it is nearly absent in the brain and rather is found in the heart, lungs, skeletal muscle, and testis. Synaptotagmin 17 is located in the brain, kidney, and prostate and is thought to be a peripheral membrane protein. 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.


Pssm-ID: 176036 [Multi-domain]  Cd Length: 123  Bit Score: 85.77  E-value: 6.25e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4723 GEIQLQINYDKHLGNLIIHILQARNLAPRD-NNGYSDPFVKVYLLPGRGQVmvvqnasaeykRRTKYIQKSLNPEWNQTV 4801
Cdd:cd08390      1 GRLWFSVQYDLEEEQLTVSLIKARNLPPRTkDVAHCDPFVKVCLLPDERRS-----------LQSKVKRKTQNPNFDETF 69

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2032737686 4802 IYKnISVEQLKKKTLEVTVWDYDRFSSNDFLGEVLIELS 4840
Cdd:cd08390     70 VFQ-VSFKELQRRTLRLSVYDVDRFSRHCIIGHVLFPLK 107
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 321-716 1.16e-18

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 94.67  E-value: 1.16e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  321 SSQQPGPAKQPSQQPARQGAPVKPSPQQTGPPKQPSQQPGPEKPSAQQAGPAKQPPQPGSGKPPPQQTGLVKQVPPQAGP 400
Cdd:PRK07764   383 RRLGVAGGAGAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAP 462

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  401 TKPPSQTVGPTKPLAQQAGPTKPPGQQPGPEkPPQQTQAGANQPT--------------ETAPKKTFcplcTTTELLLHT 466
Cdd:PRK07764   463 SAQPAPAPAAAPEPTAAPAPAPPAAPAPAAA-PAAPAAPAAPAGAddaatlrerwpeilAAVPKRSR----KTWAILLPE 537

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  467 PEKANY--NTCTQCHTVVCSLCGFNpNPHITE-----ISEWLCLNCQMQRTLGGDlaPGLGPGPQPLAPKQKTPIPPSAK 539
Cdd:PRK07764   538 ATVLGVrgDTLVLGFSTGGLARRFA-SPGNAEvlvtaLAEELGGDWQVEAVVGPA--PGAAGGEGPPAPASSGPPEEAAR 614

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  540 PSPQPQPVQkkdvTPKPDPSQAADSKRPPPQKKQTQLPGSPPVKSKQPRAEPTDISQQ-----TDATPKSDQVKPTQAED 614
Cdd:PRK07764   615 PAAPAAPAA----PAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGwpakaGGAAPAAPPPAPAPAAP 690

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  615 KQKQPSVQKPTADSVSTSVAAEQKQDLAGPRPPTQQ------KVTDSPKPELAKPSQDTHPAGDKPDSKPVPQVSRQKSD 688
Cdd:PRK07764   691 AAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQgasapsPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAP 770

                          410       420
                   ....*....|....*....|....*...
gi 2032737686  689 PkfASQPGARPDAKAQKPIDPTQTKDDP 716
Cdd:PRK07764   771 A--AAPPPSPPSEEEEMAEDDAPSMDDE 796
PHA03247 PHA03247
large tegument protein UL36; Provisional
 278-745 5.28e-18

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 93.08  E-value: 5.28e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  278 PSEPTKPIQQQTSAKPSSGPTKPSPQQPDSTKVTSQTAPPTKPSSQQPGPAKQPSQQPARQGAPvKPSPQQTGPPKQPSQ 357
Cdd:PHA03247  2551 PPPPLPPAAPPAAPDRSVPPPRPAPRPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPP-SPLPPDTHAPDPPPP 2629

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  358 QPGPEKPSAQQAGPAKQPPQPGSGKPP-PQQTGLVKQVPPQAGPTKPPSQTVGPTKPLAQQA-GP----TKPPGQQPGPE 431
Cdd:PHA03247  2630 SPSPAANEPDPHPPPTVPPPERPRDDPaPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTvGSltslADPPPPPPTPE 2709

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  432 KPPQQTQAGANQPTETAPKKTFCPlctttelllhtpekanyntctqchtvvcslcgfnpnphiteisewlclncqmqrtl 511
Cdd:PHA03247  2710 PAPHALVSATPLPPGPAAARQASP-------------------------------------------------------- 2733

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  512 ggdlAPGLGPGPQPLAPKQKTPIPPSAKPSPqPQPVQKKDVTPKPDPSQAADSKRPPPQKKQTQLPGSPPVKSKQPRAEP 591
Cdd:PHA03247  2734 ----ALPAAPAPPAVPAGPATPGGPARPARP-PTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPP 2808

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  592 TDISQQTDATPKSDQVKPTQAEDKQKQPSVQKPTADSVSTSVAAEQKQDLAGP---RPPTQQKVtdspkpelAKPSQDTH 668
Cdd:PHA03247  2809 AAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDvrrRPPSRSPA--------AKPAAPAR 2880

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2032737686  669 PagdKPDSKPVPQVSRQksdpkfasqpgarPDAKAQKPidptqtkDDPKKLPTKPAPKPDTKPAPKGPQAGAGPKAA 745
Cdd:PHA03247  2881 P---PVRRLARPAVSRS-------------TESFALPP-------DQPERPPQPQAPPPPQPQPQPPPPPQPQPPPP 2934
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 255-664 2.37e-17

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.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 90.60  E-value: 2.37e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  255 ADAKQDQAKQPA-QPRGPQKSQPQPSePTKPIQQQTSAKPSSGPTKPSPQQPDSTKVTSQTAPPTKP-----SSQQPGPA 328
Cdd:pfam03154  162 AQQQILQTQPPVlQAQSGAASPPSPP-PPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPhtliqQTPTLHPQ 240

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  329 KQPSQQPARQGAPVKPSPQQTGPPKQPS---QQPGPEKPSAQQAGPAKQP-PQPGSGKPPPQQTGLvKQVPPQAGPTKP- 403
Cdd:pfam03154  241 RLPSPHPPLQPMTQPPPPSQVSPQPLPQpslHGQMPPMPHSLQTGPSHMQhPVPPQPFPLTPQSSQ-SQVPPGPSPAAPg 319

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  404 PSQTVGPTKPLAQQAGPTKPPGQQPGPEKPpqqtqagANQPTETAPKKTFCPLCTTTELLLHTPEKAnyntctqchtvvc 483
Cdd:pfam03154  320 QSQQRIHTPPSQSQLQSQQPPREQPLPPAP-------LSMPHIKPPPTTPIPQLPNPQSHKHPPHLS------------- 379

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  484 slcgfNPNPHiteisewlclncQMQRTLggdlapglgPGPQPLAPKQKTPI--PPSAKPSP-----QPQPVQKKDVTP-- 554
Cdd:pfam03154  380 -----GPSPF------------QMNSNL---------PPPPALKPLSSLSThhPPSAHPPPlqlmpQSQQLPPPPAQPpv 433

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  555 -KPDPSQAADSKRPPPQKKQTQLPGSPPVKSKQ-PRAEPTDISQQTDATPKSDQVKPTQAEDKQKQPSVQKPTADSVSTS 632
Cdd:pfam03154  434 lTQSQSLPPPAASHPPTSGLHQVPSQSPFPQHPfVPGGPPPITPPSGPPTSTSSAMPGIQPPSSASVSSSGPVPAAVSCP 513

                          410       420       430
                   ....*....|....*....|....*....|..
gi 2032737686  633 VAAEQKQDlagpRPPTQQKVTDSPKPELAKPS 664
Cdd:pfam03154  514 LPPVQIKE----EALDEAEEPESPPPPPRSPS 541
C2D_Ferlin cd04017
C2 domain fourth repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and ...
 4740-4855 1.10e-16

C2 domain fourth repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and other proteins, such as Synaptotagmins, are implicated in facilitating the fusion process when cell membranes fuse together. There are six known human Ferlins: Dysferlin (Fer1L1), Otoferlin (Fer1L2), Myoferlin (Fer1L3), Fer1L4, Fer1L5, and Fer1L6. Defects in these genes can lead to a wide range of diseases including muscular dystrophy (dysferlin), deafness (otoferlin), and infertility (fer-1, fertilization factor-1). Structurally they have 6 tandem C2 domains, designated as (C2A-C2F) and a single C-terminal transmembrane domain, though there is a new study that disputes this and claims that there are actually 7 tandem C2 domains with another C2 domain inserted between C2D and C2E. In a subset of them (Dysferlin, Myoferlin, and Fer1) there is an additional conserved domain called DysF. 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 fourth C2 repeat, C2D, and has a type-II topology.


Pssm-ID: 175984 [Multi-domain]  Cd Length: 135  Bit Score: 79.51  E-value: 1.10e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4740 IHILQARNLAPRDNNGYSDPFVKVYLLpgrgqvmvvqNASAEykrrTKYIQKSLNPEWNQTVIYKNISVEQLKKKTLE-- 4817
Cdd:cd04017      5 AYIYQARDLLAADKSGLSDPFARVSFL----------NQSQE----TEVIKETLSPTWDQTLIFDEVELYGSPEEIAQnp 70

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2032737686 4818 ----VTVWDYDRFSSNDFLGEVLI--ELSSISQLDNTP--RWYPLK 4855
Cdd:cd04017     71 plvvVELFDQDSVGKDEFLGRSVAkpLVKLDLEEDFPPklQWFPIY 116
C2A_Synaptotagmin-4-11 cd08388
C2A domain first repeat present in Synaptotagmins 4 and 11; Synaptotagmin is a ...
 4723-4842 2.61e-16

C2A domain first repeat present in Synaptotagmins 4 and 11; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Synaptotagmins 4 and 11, class 4 synaptotagmins, are located in the brain. Their functions are unknown. They are distinguished from the other synaptotagmins by having and Asp to Ser substitution in their C2A 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.


Pssm-ID: 176034 [Multi-domain]  Cd Length: 128  Bit Score: 78.55  E-value: 2.61e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4723 GEIQLQINYDKHLGNLIIHILQARNLAPRD-NNGYSDPFVKVYLLPGRgqvmvvqnasaEYKRRTKYIQKSLNPEWNQTV 4801
Cdd:cd08388      3 GTLFFSLRYNSEKKALLVNIIECRDLPAMDeQSGTSDPYVKLQLLPEK-----------EHKVKTRVLRKTRNPVYDETF 71

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 2032737686 4802 IYKNISVEQLKKKTLEVTVWDYDRFSSNDFLGEVLIELSSI 4842
Cdd:cd08388     72 TFYGIPYNQLQDLSLHFAVLSFDRYSRDDVIGEVVCPLAGA 112
C2C_MCTP_PRT cd08377
C2 domain third repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); ...
 4736-4858 4.13e-16

C2 domain third repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); MCTPs are involved in Ca2+ signaling at the membrane. The cds in this family contain multiple C2 domains as well as a C-terminal PRT domain. It is one of four protein classes that are anchored to membranes via a transmembrane region; the others being synaptotagmins, extended synaptotagmins, and ferlins. MCTPs are the only membrane-bound C2 domain proteins that contain two functional TMRs. MCTPs are unique in that they bind Ca2+ but not phospholipids. 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.


Pssm-ID: 176023 [Multi-domain]  Cd Length: 119  Bit Score: 77.34  E-value: 4.13e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4736 GNLIIHILQARNLAPRDNNGYSDPFVkvyllpgrgqVMVVQNAsaeyKRRTKYIQKSLNPEWNQTVIY--KNI-SVeqlk 4812
Cdd:cd08377      1 GFLQVKVIRASGLAAADIGGKSDPFC----------VLELVNA----RLQTHTIYKTLNPEWNKIFTFpiKDIhDV---- 62

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2032737686 4813 kktLEVTVWDYDRFSSNDFLGEVLIELSSISqlDNTPRWYPLKEQS 4858
Cdd:cd08377     63 ---LEVTVYDEDKDKKPEFLGKVAIPLLSIK--NGERKWYALKDKK 103
PHA03247 PHA03247
large tegument protein UL36; Provisional
 62-455 4.63e-16

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 86.92  E-value: 4.63e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686   62 RAQGLPRGNLAGAEPP---PMQRHPeldtsrhPRQPGKPPDPGPPGLSKSRTVDVLKTEQRAPGRSPSTLSLRESKSRTd 138
Cdd:PHA03247  2599 RAPVDDRGDPRGPAPPsplPPDTHA-------PDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRL- 2670

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  139 fKEDQKPSMMPSFLSEANPLSAVTSVVNKFNPfdlisdSDTSHEEAGRKQKVAPKEQGKPEEQRSPAKHPTQPQSPKPAV 218
Cdd:PHA03247  2671 -GRAAQASSPPQRPRRRAARPTVGSLTSLADP------PPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPA 2743

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  219 QQQGPVRP-TVQQTESSKQQQQPGGPKQVQKPGHGQPADAKQDQAKQPAQPRGPQKSQPQPSEPTKPIQQQTSAKP-SSG 296
Cdd:PHA03247  2744 VPAGPATPgGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPpAAS 2823

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  297 PTKPSPQQPDSTKVTSQTAPPTKPSSQQPGPAKQPSQQPARQGAPVKPSPQQTGPPKQPSQ---QPGPEKPSAQQAGPak 373
Cdd:PHA03247  2824 PAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRrlaRPAVSRSTESFALP-- 2901

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  374 qPPQPGSGKPP--PQQTGLVKQVPPQAGPTKPPSQTVGPTKPLAQQAGPTKPPGQQPGPEKPpqqtQAGANQPTETAPKK 451
Cdd:PHA03247  2902 -PDQPERPPQPqaPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQP----WLGALVPGRVAVPR 2976


                   ....
gi 2032737686  452 TFCP 455
Cdd:PHA03247  2977 FRVP 2980
C2A_MCTP_PRT_plant cd04022
C2 domain first repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); ...
 4738-4858 6.07e-16

C2 domain first repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); plant subset; MCTPs are involved in Ca2+ signaling at the membrane. Plant-MCTPs are composed of a variable N-terminal sequence, four C2 domains, two transmembrane regions (TMRs), and a short C-terminal sequence. It is one of four protein classes that are anchored to membranes via a transmembrane region; the others being synaptotagmins, extended synaptotagmins, and ferlins. MCTPs are the only membrane-bound C2 domain proteins that contain two functional TMRs. MCTPs are unique in that they bind Ca2+ but not phospholipids. 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-II topology.


Pssm-ID: 175989 [Multi-domain]  Cd Length: 127  Bit Score: 77.38  E-value: 6.07e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4738 LIIHILQARNLAPRDNNGYSDPFVKVYLLpgrGQvmvvqnasaeyKRRTKYIQKSLNPEWNQTVIYKNISVEQLKKKTLE 4817
Cdd:cd04022      2 LVVEVVDAQDLMPKDGQGSSSAYVELDFD---GQ-----------KKRTRTKPKDLNPVWNEKLVFNVSDPSRLSNLVLE 67

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 2032737686 4818 VTVWDYDRFS-SNDFLGEVLIELSSI-SQLDNTPRWYPLKEQS 4858
Cdd:cd04022     68 VYVYNDRRSGrRRSFLGRVRISGTSFvPPSEAVVQRYPLEKRG 110
PHA03247 PHA03247
large tegument protein UL36; Provisional
 72-622 7.16e-16

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 86.15  E-value: 7.16e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686   72 AGAEPPPM---QRHPELDTSRHPRQPGKPPDPGPPGlSKSRTVDV--LKTEQRAPG--RSPSTLSLRESKSRTDFKEDQK 144
Cdd:PHA03247  2548 AGDPPPPLppaAPPAAPDRSVPPPRPAPRPSEPAVT-SRARRPDAppQSARPRAPVddRGDPRGPAPPSPLPPDTHAPDP 2626

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  145 PSMMPSFLSEANPLSAVTSVVNKFNPFDLISDSDTSHEEAGRKQKVAPKEQGKPEEQRSPAKHPT------------QPQ 212
Cdd:PHA03247  2627 PPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTvgsltsladpppPPP 2706

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  213 SPKPAVQQQGPVRPTVQQTESSKQQQQPGGPKQVQKPGHGQPA-DAKQDQAKQPAQPRGPQKSQPqPSEPTKPIQQQTSA 291
Cdd:PHA03247  2707 TPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPAtPGGPARPARPPTTAGPPAPAP-PAAPAAGPPRRLTR 2785

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  292 KPSSGPTKPSPQQPDSTKVTSQTAPPTKPSSQQPgpakqPSQQPArQGAPVKPSPQQTGPPKQPSQQPGPEKPsaqqaGP 371
Cdd:PHA03247  2786 PAVASLSESRESLPSPWDPADPPAAVLAPAAALP-----PAASPA-GPLPPPTSAQPTAPPPPPGPPPPSLPL-----GG 2854

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  372 AKQPPQPGSGKPPPQQTglvkqVPPQAGPTKPPSQTVG------PTKPLAQ---QAGPTKPPGQQPGPEKPPQQTQAGAN 442
Cdd:PHA03247  2855 SVAPGGDVRRRPPSRSP-----AAKPAAPARPPVRRLArpavsrSTESFALppdQPERPPQPQAPPPPQPQPQPPPPPQP 2929

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  443 QPTETAPKKTFCPLCTTTElllhtPEKANYNTctqchtvvcslcGFNPNPhiteiseWLclncqmqrtlgGDLAPGLGPG 522
Cdd:PHA03247  2930 QPPPPPPPRPQPPLAPTTD-----PAGAGEPS------------GAVPQP-------WL-----------GALVPGRVAV 2974

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  523 PQPLAPKQKTPIPPSAKPSPQPQPVQKKDVT-----------PKPDPSQAADSKRPPPQKKQTQLPGSPPVKSKQPRAEP 591
Cdd:PHA03247  2975 PRFRVPQPAPSREAPASSTPPLTGHSLSRVSswasslalheeTDPPPVSLKQTLWPPDDTEDSDADSLFDSDSERSDLEA 3054

                          570       580       590
                   ....*....|....*....|....*....|..
gi 2032737686  592 TDISQQTDATPKSDQVKP-TQAEDKQKQPSVQ 622
Cdd:PHA03247  3055 LDPLPPEPHDPFAHEPDPaTPEAGARESPSSQ 3086
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 188-679 1.33e-15

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 85.14  E-value: 1.33e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  188 QKVAPKEQGKPEEQRSPAKHPTQPQSPKPAVQQQGPVRPTVQQTESSKQQQQPGGPKQVQKPGHGQPADAKQDQAKQPAQ 267
Cdd:PRK10263   361 QPVPGPQTGEPVIAPAPEGYPQQSQYAQPAVQYNEPLQQPVQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQ 440

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  268 PRGPQKSQPQPSEPT---KPIQQQTSAKPSSGPTKPSPQQPDSTKVTSQTAPptKPSSQQPGPAKQP-------SQQPAR 337
Cdd:PRK10263   441 PVAGNAWQAEEQQSTfapQSTYQTEQTYQQPAAQEPLYQQPQPVEQQPVVEP--EPVVEETKPARPPlyyfeevEEKRAR 518

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  338 QGAPVKPSPQqtgPPKQPSQQPGPEKPSAQQAGPAKQPPQPGSGKPPPQQTGlVKQVPPQAG-------PTKPPSQTVGP 410
Cdd:PRK10263   519 EREQLAAWYQ---PIPEPVKEPEPIKSSLKAPSVAAVPPVEAAAAVSPLASG-VKKATLATGaaatvaaPVFSLANSGGP 594

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  411 TKPLAQQAGPTKP-PGQQPGPEK----------PPQQTQAGANQPTETAPKKTFCPLCTTTELLLHTPEKANYNTCTQCH 479
Cdd:PRK10263   595 RPQVKEGIGPQLPrPKRIRVPTRrelasygiklPSQRAAEEKAREAQRNQYDSGDQYNDDEIDAMQQDELARQFAQTQQQ 674

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  480 TVVCSLCgfNPNPHITEISEWLC--------LNCQMQRTLGGDLApglGPGPQPLAPKQKTPIPPSAKPSPQpQPVQKKD 551
Cdd:PRK10263   675 RYGEQYQ--HDVPVNAEDADAAAeaelarqfAQTQQQRYSGEQPA---GANPFSLDDFEFSPMKALLDDGPH-EPLFTPI 748

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  552 VTPKPDPSQAAdskRPPPQKKQTQLPGSPPVKSKQPraeptdisQQTDATPKSDQVKPTQAEDKQKQPSVQKPTADSVST 631
Cdd:PRK10263   749 VEPVQQPQQPV---APQQQYQQPQQPVAPQPQYQQP--------QQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQY 817

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2032737686  632 svaaEQKQDLAGPRPPTQQkvtdsPKPELAKPSQDT--HPAGDKP-DSKPV 679
Cdd:PRK10263   818 ----QQPQQPVAPQPQYQQ-----PQQPVAPQPQDTllHPLLMRNgDSRPL 859
C2B_RasGAP cd08675
C2 domain second repeat of Ras GTPase activating proteins (GAPs); RasGAPs suppress Ras ...
 4738-4863 2.24e-15

C2 domain second repeat of Ras GTPase activating proteins (GAPs); RasGAPs suppress Ras function by enhancing the GTPase activity of Ras proteins resulting in the inactive GDP-bound form of Ras. In this way it can control cellular proliferation and differentiation. The proteins here all contain two tandem C2 domains, a Ras-GAP domain, and a pleckstrin homology (PH)-like 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. Members here have a type-I topology.


Pssm-ID: 176057 [Multi-domain]  Cd Length: 137  Bit Score: 75.87  E-value: 2.24e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4738 LIIHILQARNLAPRdNNGYSDPFVKVYLLPGRGQVMvvqnasaeykRRTKYIQKSLNPEWNQTVIY------------KN 4805
Cdd:cd08675      1 LSVRVLECRDLALK-SNGTCDPFARVTLNYSSKTDT----------KRTKVKKKTNNPRFDEAFYFeltigfsyekksFK 69

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2032737686 4806 ISVEQLKKKTLEVTVWDYDRFSSNDFLGEVLIELSSISQLDNTPRWYPLKEQSENIDH 4863
Cdd:cd08675     70 VEEEDLEKSELRVELWHASMVSGDDFLGEVRIPLQGLQQAGSHQAWYFLQPREAPGTR 127
PDZ_canonical cd00136
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs ...
 4537-4615 3.20e-15

canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain. PDZ domains usually bind to short specific peptide sequences located at the C-terminal end of their partner proteins known as PDZ binding motifs. These domains can also interact with internal peptide motifs and certain lipids, and can take part in a head-to-tail oligomerization with other PDZ domains. The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467153 [Multi-domain]  Cd Length: 81  Bit Score: 73.73  E-value: 3.20e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2032737686 4537 SGNGLGIRVVGGKEIPGssgeiGAYIAKILPGGNAEQTGKLVEGMQVLEWNGIPLTGKTYEEVQSIIIQQSGEAEICVR 4615
Cdd:cd00136      8 PGGGLGFSIRGGKDGGG-----GIFVSRVEPGGPAARDGRLRVGDRILEVNGVSLEGLTHEEAVELLKSAGGEVTLTVR 81
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 255-733 3.88e-15

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.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 83.28  E-value: 3.88e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  255 ADAKQDQAKQPAQPRGPQKSQPQPSEPTKPIQQQTSAkPSSGPTkpspqqPDSTKVTSQTAPPTKPSSQQPGPAKQPS-- 332
Cdd:pfam03154  158 SDSSAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQA-ATAGPT------PSAPSVPPQGSPATSQPPNQTQSTAAPHtl 230

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  333 -QQPARQGAPVKPSPQqtgPPKQPSQQPGPEKPSAQQAGPAKQPPQPGSGKPPPQQTG---LVKQVPPQAGPTKPP-SQT 407
Cdd:pfam03154  231 iQQTPTLHPQRLPSPH---PPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGpshMQHPVPPQPFPLTPQsSQS 307

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  408 VGPTKPLAQQAGPTKPPGQQPGPEKPPQQTQAGANQPTETAPKktfcplctttelllhtpekanyntctqchtvvcslcg 487
Cdd:pfam03154  308 QVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPL------------------------------------- 350

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  488 fnPNPHITeisewlclncqmqrtlggdlapglgpgpqplaPKQKTPIPPSAKPSPQPQPVQkkdvTPKPDPSQAADSKRP 567
Cdd:pfam03154  351 --SMPHIK--------------------------------PPPTTPIPQLPNPQSHKHPPH----LSGPSPFQMNSNLPP 392

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  568 PPQKKqtqlPGSPPVKSKQPRAEPTDISqqtdATPKSDQVKPTQAedkqkQPSV--QKPTADSVSTSVAAEQKQDLAGPR 645
Cdd:pfam03154  393 PPALK----PLSSLSTHHPPSAHPPPLQ----LMPQSQQLPPPPA-----QPPVltQSQSLPPPAASHPPTSGLHQVPSQ 459

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  646 PPTQQK--VTDSPKPELAKPSQDTHPAGDKPDSKPVPQVSRQKSDPKFASQPGARPDAK-AQKPIDPTQTKDDPKKLPTK 722
Cdd:pfam03154  460 SPFPQHpfVPGGPPPITPPSGPPTSTSSAMPGIQPPSSASVSSSGPVPAAVSCPLPPVQiKEEALDEAEEPESPPPPPRS 539

                          490
                   ....*....|.
gi 2032737686  723 PAPKPDTKPAP 733
Cdd:pfam03154  540 PSPEPTVVNTP 550
PTZ00121 PTZ00121
MAEBL; Provisional
 1029-1729 4.34e-15

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 83.27  E-value: 4.34e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1029 AKPKEEPGVQKEAPKLQQGRLEKTlsaDKIQQGIQKEDAKpKQGKLVKAPSADKIQHASQKEDPRiQQTKLTKTASYDRV 1108
Cdd:PTZ00121  1242 AKKAEEERNNEEIRKFEEARMAHF---ARRQAAIKAEEAR-KADELKKAEEKKKADEAKKAEEKK-KADEAKKKAEEAKK 1316

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1109 LQEVQKEDE----KLQEAKLAKTSSADKILHRVQKEDIKLQEAKLAKVPS-ADKILQGIQKEDPKLQQMKMAKALSADKI 1183
Cdd:PTZ00121  1317 ADEAKKKAEeakkKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAeAAEKKKEEAKKKADAAKKKAEEKKKADEA 1396

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1184 QLAAQREDTKLQEVKlpKAASVDKiqhgTQKDIKLQHEKIKKTSSVDKIQEEGQK-EETKLQRGKLSKTPSADKIPATAT 1262
Cdd:PTZ00121  1397 KKKAEEDKKKADELK--KAAAAKK----KADEAKKKAEEKKKADEAKKKAEEAKKaDEAKKKAEEAKKAEEAKKKAEEAK 1470

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1263 ADQKIPLSTLEEDKETVLPEKSTPHPEDKKEEITAEIKDRVAEEKAEVEAPYKGLQAKEEEDVKKEDLTTgisqvvlKAE 1342
Cdd:PTZ00121  1471 KADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAK-------KAE 1543

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1343 KAQEAEIPVQTAPLPGTDHVEAVREKIEKEDDKSDTSSSQQQKSPqglsdtgyssdgISSSLGEIPSHIPTDEKDLLKET 1422
Cdd:PTZ00121  1544 EKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKK------------AEEARIEEVMKLYEEEKKMKAEE 1611

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1423 SKKdtiSQESPPSPSDLAKLESTVLSILEAQASTLSDEKSAKSKEPSETYGEQTKDQLKTKplpvtpesyspDEEDLKAI 1502
Cdd:PTZ00121  1612 AKK---AEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKK-----------AEEDKKKA 1677

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1503 KEGEGTIAEEGKGAASSQADYKEEHEGDDMSARRQQRYDSVEDSSESENSpvprRKRRTSVGSSSSDEYKRDDSQGSGDE 1582
Cdd:PTZ00121  1678 EEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEE----NKIKAEEAKKEAEEDKKKAEEAKKDE 1753

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1583 EDfiRKQILEMSADEDASGSDDDEFIRNQLKE-ISAAESQKKEEVKSKAKGTagkhrrmaRKSSAGYDEDAGRRHSWHDD 1661
Cdd:PTZ00121  1754 EE--KKKIAHLKKEEEKKAEEIRKEKEAVIEEeLDEEDEKRRMEVDKKIKDI--------FDNFANIIEGGKEGNLVIND 1823

                          650       660       670       680       690       700
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2032737686 1662 DDETFDESPEPKYRESKSQDSEELAVSGggglRRFKTIELNSTITNKYSEVSEpQKGVLYFDEEPELE 1729
Cdd:PTZ00121  1824 SKEMEDSAIKEVADSKNMQLEEADAFEK----HKFNKNNENGEDGNKEADFNK-EKDLKEDDEEEIEE 1886
C2B_RasA1_RasA4 cd04025
C2 domain second repeat present in RasA1 and RasA4; RasA1 and RasA4 are GAP1s (GTPase ...
 4741-4854 4.60e-15

C2 domain second repeat present in RasA1 and RasA4; RasA1 and RasA4 are GAP1s (GTPase activating protein 1s ), Ras-specific GAP members, which suppresses Ras function by enhancing the GTPase activity of Ras proteins resulting in the inactive GDP-bound form of Ras. In this way it can control cellular proliferation and differentiation. Both proteins contain two C2 domains, a Ras-GAP domain, a plextrin homology (PH)-like domain, and a Bruton's Tyrosine Kinase (BTK) zinc binding 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. This cd contains the second C2 repeat, C2B, and has a type-I topology.


Pssm-ID: 175991 [Multi-domain]  Cd Length: 123  Bit Score: 74.83  E-value: 4.60e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4741 HILQARNLAPRDNNGYSDPFVKVYLlpgRGQVmvvqnasaeykRRTKYIQKSLNPEWNQTVIYKnisVEQLKKKTLEVTV 4820
Cdd:cd04025      5 HVLEARDLAPKDRNGTSDPFVRVFY---NGQT-----------LETSVVKKSCYPRWNEVFEFE---LMEGADSPLSVEV 67

                           90       100       110
                   ....*....|....*....|....*....|....
gi 2032737686 4821 WDYDRFSSNDFLGEVLIELSSISQLDNTPRWYPL 4854
Cdd:cd04025     68 WDWDLVSKNDFLGKVVFSIQTLQQAKQEEGWFRL 101
C2A_C2C_Synaptotagmin_like cd08391
C2 domain first and third repeat in Synaptotagmin-like proteins; Synaptotagmin is a ...
 4736-4867 5.22e-15

C2 domain first and third repeat in Synaptotagmin-like proteins; 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 either the first or third repeat in Synaptotagmin-like proteins with a type-I topology.


Pssm-ID: 176037 [Multi-domain]  Cd Length: 121  Bit Score: 74.25  E-value: 5.22e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4736 GNLIIHILQARNLAPRDNN------GYSDPFVKVyllpgrgQVmvvqnasAEYKRRTKYIQKSLNPEWNQTviYKNIsVE 4809
Cdd:cd08391      1 GVLRIHVIEAQDLVAKDKFvgglvkGKSDPYVIV-------RV-------GAQTFKSKVIKENLNPKWNEV--YEAV-VD 63

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2032737686 4810 QLKKKTLEVTVWDYDRfSSNDFLGEVLIELSSISQLDNTPRWYPLkeqsENIDHGKSH 4867
Cdd:cd08391     64 EVPGQELEIELFDEDP-DKDDFLGRLSIDLGSVEKKGFIDEWLPL----EDVKSGRLH 116
C2E_Ferlin cd04037
C2 domain fifth repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and ...
 4740-4839 5.91e-15

C2 domain fifth repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and other proteins, such as Synaptotagmins, are implicated in facilitating the fusion process when cell membranes fuse together. There are six known human Ferlins: Dysferlin (Fer1L1), Otoferlin (Fer1L2), Myoferlin (Fer1L3), Fer1L4, Fer1L5, and Fer1L6. Defects in these genes can lead to a wide range of diseases including muscular dystrophy (dysferlin), deafness (otoferlin), and infertility (fer-1, fertilization factor-1). Structurally they have 6 tandem C2 domains, designated as (C2A-C2F) and a single C-terminal transmembrane domain, though there is a new study that disputes this and claims that there are actually 7 tandem C2 domains with another C2 domain inserted between C2D and C2E. In a subset of them (Dysferlin, Myoferlin, and Fer1) there is an additional conserved domain called DysF. 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 fifth C2 repeat, C2E, and has a type-II topology.


Pssm-ID: 176002 [Multi-domain]  Cd Length: 124  Bit Score: 74.51  E-value: 5.91e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4740 IHILQARNLAPRDNNGYSDPFVKvyllpgrgqvmvVQNASAEYKRRTKYIQKSLNPEWNQTVIyknISVEQLKKKTLEVT 4819
Cdd:cd04037      4 VYVVRARNLQPKDPNGKSDPYLK------------IKLGKKKINDRDNYIPNTLNPVFGKMFE---LEATLPGNSILKIS 68

                           90       100
                   ....*....|....*....|
gi 2032737686 4820 VWDYDRFSSNDFLGEVLIEL 4839
Cdd:cd04037     69 VMDYDLLGSDDLIGETVIDL 88
C2C_KIAA1228 cd04030
C2 domain third repeat present in uncharacterized human KIAA1228-like proteins; KIAA proteins ...
 5097-5222 6.50e-15

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.


Pssm-ID: 175996 [Multi-domain]  Cd Length: 127  Bit Score: 74.23  E-value: 6.50e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 5097 GEIKIALkkEMKTDGEQLIVEILQCRNITykFKSPDHLPDLYVKLYVvnISTQKRVIKKKTRVCRHDREPSFNETFRFSL 5176
Cdd:cd04030      3 GRIQLTI--RYSSQRQKLIVTVHKCRNLP--PCDSSDIPDPYVRLYL--LPDKSKSTRRKTSVKKDNLNPVFDETFEFPV 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2032737686 5177 SPAGHSLQILLVS--NGGKFM--KKTLIGEAYIWLDKVDLRKRIVNWHKL 5222
Cdd:cd04030     77 SLEELKRRTLDVAvkNSKSFLsrEKKLLGQVLIDLSDLDLSKGFTQWYDL 126
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 169-601 1.23e-14

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.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 81.74  E-value: 1.23e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  169 NPFDLISDSDTSHEEAgrkqkvapKEQGKPEEQRSPAKHPTQPQSPKPAVQQQGPVRPTVQQTESSKQQQQPGGPKQVQK 248
Cdd:pfam03154  150 SPQDNESDSDSSAQQQ--------ILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQT 221

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  249 PGHGQPADAKQdQAKQPAQPRGPQKSQPQPSEPTKPIQQQTSAKPSSGPTKPSPQQPDSTKVtsQTAPPTKPSSQQPGPA 328
Cdd:pfam03154  222 QSTAAPHTLIQ-QTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSL--QTGPSHMQHPVPPQPF 298

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  329 KQPSQQPARQGaPVKPSPQQTGPPKQPSQQPGPEKPSAQQAGPAKQP--PQPGSG---KPPPqqTGLVKQVP-PQAgpTK 402
Cdd:pfam03154  299 PLTPQSSQSQV-PPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPlpPAPLSMphiKPPP--TTPIPQLPnPQS--HK 373

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  403 PPSQTVGPTkPLAQQAGPTKPPG---------QQPGPEKPPQQTQAGANQPTETAPKKTfcPLCTTTELllHTPEKANYN 473
Cdd:pfam03154  374 HPPHLSGPS-PFQMNSNLPPPPAlkplsslstHHPPSAHPPPLQLMPQSQQLPPPPAQP--PVLTQSQS--LPPPAASHP 448

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  474 TCTQCHTVVcSLCGFNPNPHITEISEwlclncqmqrtlggDLAPGLGPgPQPLAPKQKTPIPPSAKPSPQPQPVQKKDVT 553
Cdd:pfam03154  449 PTSGLHQVP-SQSPFPQHPFVPGGPP--------------PITPPSGP-PTSTSSAMPGIQPPSSASVSSSGPVPAAVSC 512

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*...
gi 2032737686  554 PKPdpsqAADSKRPPPQkkQTQLPGSPPVKSKQPRAEPTDISQQTDAT 601
Cdd:pfam03154  513 PLP----PVQIKEEALD--EAEEPESPPPPPRSPSPEPTVVNTPSHAS 554
C2A_Munc13-like cd08676
C2 domain first repeat in Munc13 (mammalian uncoordinated)-like proteins; C2-like domains are ...
 4738-4854 1.28e-14

C2 domain first repeat in Munc13 (mammalian uncoordinated)-like proteins; C2-like domains are thought to be involved in phospholipid binding in a Ca2+ independent manner in both Unc13 and Munc13. Caenorabditis elegans Unc13 has a central domain with sequence similarity to PKC, which includes C1 and C2-related domains. Unc13 binds phorbol esters and DAG with high affinity in a phospholipid manner. Mutations in Unc13 results in abnormal neuronal connections and impairment in cholinergic neurotransmission in the nematode. Munc13 is the mammalian homolog which are expressed in the brain. There are 3 isoforms (Munc13-1, -2, -3) and are thought to play a role in neurotransmitter release and are hypothesized to be high-affinity receptors for phorbol esters. Unc13 and Munc13 contain both C1 and C2 domains. There are two C2 related domains present, one central and one at the carboxyl end. Munc13-1 contains a third C2-like domain. Munc13 interacts with syntaxin, synaptobrevin, and synaptotagmin suggesting a role for these as scaffolding 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 second C2 repeat, C2B, and has a type-II topology.


Pssm-ID: 176058 [Multi-domain]  Cd Length: 153  Bit Score: 74.33  E-value: 1.28e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4738 LIIHILQARNLAPRDNNGYSDPFVKVYLLPG---------------RGQVMVVQNASAEYKRRTKYIQKSLNPEWNQTVI 4802
Cdd:cd08676     30 LKVTVIEAKGLLAKDVNGFSDPYCMLGIVPAsrernsekskkrkshRKKAVLKDTVPAKSIKVTEVKPQTLNPVWNETFR 109

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2032737686 4803 YKnisVEQLKKKTLEVTVWDYDrfssNDFLGEVLIELSSISQlDNTPRWYPL 4854
Cdd:cd08676    110 FE---VEDVSNDQLHLDIWDHD----DDFLGCVNIPLKDLPS-CGLDSWFKL 153
C2A_MCTP_PRT cd04042
C2 domain first repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); ...
 4738-4863 1.85e-14

C2 domain first repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); MCTPs are involved in Ca2+ signaling at the membrane. MCTP is composed of a variable N-terminal sequence, three C2 domains, two transmembrane regions (TMRs), and a short C-terminal sequence. It is one of four protein classes that are anchored to membranes via a transmembrane region; the others being synaptotagmins, extended synaptotagmins, and ferlins. MCTPs are the only membrane-bound C2 domain proteins that contain two functional TMRs. MCTPs are unique in that they bind Ca2+ but not phospholipids. 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-II topology.


Pssm-ID: 176007 [Multi-domain]  Cd Length: 121  Bit Score: 72.69  E-value: 1.85e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4738 LIIHILQARNLAPRDNNGYSDPFVKVYLlpgrGQVMVvqnasaeYKRRTkyIQKSLNPEWNQTVIyknISVEQLKKKtLE 4817
Cdd:cd04042      2 LDIHLKEGRNLAARDRGGTSDPYVKFKY----GGKTV-------YKSKT--IYKNLNPVWDEKFT---LPIEDVTQP-LY 64

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2032737686 4818 VTVWDYDRFSSNDFLGEVLIELSSISQldNTPRWYPLKEQSENIDH 4863
Cdd:cd04042     65 IKVFDYDRGLTDDFMGSAFVDLSTLEL--NKPTEVKLKLEDPNSDE 108
C2B_RIM1alpha cd04028
C2 domain second repeat contained in Rab3-interacting molecule (RIM) proteins; RIMs are ...
 5093-5227 2.74e-14

C2 domain second repeat contained in Rab3-interacting molecule (RIM) proteins; RIMs are believed to organize specialized sites of the plasma membrane called active zones. They also play a role in controlling neurotransmitter release, plasticity processes, as well as memory and learning. RIM contains an N-terminal zinc finger domain, a PDZ domain, and two C-terminal C2 domains (C2A, C2B). 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. Members here have a type-I topology and do not bind Ca2+.


Pssm-ID: 175994 [Multi-domain]  Cd Length: 146  Bit Score: 73.19  E-value: 2.74e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 5093 TQVMGEIKIALkkeMKTDGeQLIVEILQCRNITYKFKSpDHLPDLYVKLYVVniSTQKRVIKKKTRVCRHDREPSFNETF 5172
Cdd:cd04028     14 SPSMGDIQLGL---YDKKG-QLEVEVIRARGLVQKPGS-KVLPAPYVKVYLL--EGKKCIAKKKTKIARKTLDPLYQQQL 86

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2032737686 5173 RFSLSPAGHSLQILLVSNGGKFMKKTLIGEAYIWLDKVDLRKRIVNWHKLLVSST 5227
Cdd:cd04028     87 VFDVSPTGKTLQVIVWGDYGRMDKKVFMGVAQILLDDLDLSNLVIGWYKLFPTSS 141
C2A_SLP-3 cd08392
C2 domain first repeat present in Synaptotagmin-like protein 3; All Slp members basically ...
 4722-4855 3.35e-14

C2 domain first repeat present in Synaptotagmin-like protein 3; 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. SHD of Slp (except for the Slp4-SHD) function as a specific Rab27A/B-binding domain. In addition to Slp, rabphilin, Noc2, and Munc13-4 also function as Rab27-binding proteins. Little is known about the expression or localization of Slp3. The C2A domain of Slp3 is Ca2+ dependent. It has been demonstrated that Slp3 promotes dense-core vesicle exocytosis. 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.


Pssm-ID: 176038 [Multi-domain]  Cd Length: 128  Bit Score: 72.55  E-value: 3.35e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4722 TGEIQLQINYDKHLGNLIIHILQARNLAPRDNNGYS-DPFVKVYLLPGRgqvmvvqnaSAEYKRRTKYIQKSLNPEWNQT 4800
Cdd:cd08392      1 TGEIEFALHYNFRTSCLEITIKACRNLAYGDEKKKKcHPYVKVCLLPDK---------SHNSKRKTAVKKGTVNPVFNET 71

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2032737686 4801 VIYKnISVEQLKKKTLEVTVWDYDRFSSNDFLGEVLIELSSISQLDNTP---RWYPLK 4855
Cdd:cd08392     72 LKYV-VEADLLSSRQLQVSVWHSRTLKRRVFLGEVLIPLADWDFEDTDSqrfLWYPLN 128
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 5113-5219 5.87e-14

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.


Pssm-ID: 214577 [Multi-domain]  Cd Length: 101  Bit Score: 70.59  E-value: 5.87e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  5113 QLIVEILQCRNITYKFKSpdHLPDLYVKLYVVNistqKRVIKKKTRVCRHDREPSFNETFRFSLSPAGHSLQILLVSNGG 5192
Cdd:smart00239    1 TLTVKIISARNLPPKDKG--GKSDPYVKVSLDG----DPKEKKKTKVVKNTLNPVWNETFEFEVPPPELAELEIEVYDKD 74

                            90       100
                    ....*....|....*....|....*..
gi 2032737686  5193 KFMKKTLIGEAYIWLDKVDLRKRIVNW 5219
Cdd:smart00239   75 RFGRDDFIGQVTIPLSDLLLGGRHEKL 101
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 249-439 8.47e-14

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 78.49  E-value: 8.47e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  249 PGHGQPADAKQDQAKQPAQPRGPqksqPQPSEPTKPIQQQTSAKPSSGPTKPSPQQPDSTKVTSQTAPPTKPSSQQPGPA 328
Cdd:PRK07764   596 GGEGPPAPASSGPPEEAARPAAP----AAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPA 671

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  329 KQPSQQPARQG---APVKPSPQQTGPPKQPSQQPGPEKPSAQQAGPAKQPPQPGSGKPPPQQTGlVKQVPPqagPTKPPS 405
Cdd:PRK07764   672 KAGGAAPAAPPpapAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAA-DDPVPL---PPEPDD 747

                          170       180       190
                   ....*....|....*....|....*....|....
gi 2032737686  406 QTVGPTKPLAQQAGPTKPPGQQPGPEKPPQQTQA 439
Cdd:PRK07764   748 PPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSE 781
C2B_Synaptotagmin cd00276
C2 domain second repeat present in Synaptotagmin; Synaptotagmin is a membrane-trafficking ...
 5112-5222 1.16e-13

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.


Pssm-ID: 175975 [Multi-domain]  Cd Length: 134  Bit Score: 71.08  E-value: 1.16e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 5112 EQLIVEILQCRNItyKFKSPDHLPDLYVKLYVVNisTQKRVIKKKTRVCRHDREPSFNETFRFSLSP---AGHSLQILLV 5188
Cdd:cd00276     14 ERLTVVVLKARNL--PPSDGKGLSDPYVKVSLLQ--GGKKLKKKKTSVKKGTLNPVFNEAFSFDVPAeqlEEVSLVITVV 89

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2032737686 5189 SNgGKFMKKTLIGEAYI-----------WLDKVD-LRKRIVNWHKL 5222
Cdd:cd00276     90 DK-DSVGRNEVIGQVVLgpdsggeelehWNEMLAsPRKPIARWHKL 134
C2B_Synaptotagmin-4 cd08404
C2 domain second repeat present in Synaptotagmin 4; Synaptotagmin is a membrane-trafficking ...
 4723-4843 1.42e-13

C2 domain second repeat present in Synaptotagmin 4; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Synaptotagmin 4, a member of class 4 synaptotagmins, is located in the brain. It functions are unknown. It, like synaptotagmin-11, has an Asp to Ser substitution in its C2A domain. 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.


Pssm-ID: 176049 [Multi-domain]  Cd Length: 136  Bit Score: 70.92  E-value: 1.42e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4723 GEIQLQINYDKHLGNLIIHILQARNLAPRDNNGYSDPFVKVYLLPGRGQVMvvqnasaeyKRRTKYIQKSLNPEWNQTVI 4802
Cdd:cd08404      2 GELLLSLCYQPTTNRLTVVVLKARHLPKMDVSGLADPYVKVNLYYGKKRIS---------KKKTHVKKCTLNPVFNESFV 72

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 2032737686 4803 YkNISVEQLKKKTLEVTVWDYDRFSSNDFLGEVLIELSSIS 4843
Cdd:cd08404     73 F-DIPSEELEDISVEFLVLDSDRVTKNEVIGRLVLGPKASG 112
C2B_MCTP_PRT_plant cd08378
C2 domain second repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); ...
 4761-4854 1.60e-13

C2 domain second repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); plant subset; MCTPs are involved in Ca2+ signaling at the membrane. Plant-MCTPs are composed of a variable N-terminal sequence, four C2 domains, two transmembrane regions (TMRs), and a short C-terminal sequence. It is one of four protein classes that are anchored to membranes via a transmembrane region; the others being synaptotagmins, extended synaptotagmins, and ferlins. MCTPs are the only membrane-bound C2 domain proteins that contain two functional TMRs. MCTPs are unique in that they bind Ca2+ but not phospholipids. 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-II topology.


Pssm-ID: 176024 [Multi-domain]  Cd Length: 121  Bit Score: 70.03  E-value: 1.60e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4761 VKVYLLPGRGQVMVVQNASAEYKRRTKYIQKSLNPEWNQTVIyknISVEQLKKKTLEVTVWDYDrFSSNDFLGEVLIELS 4840
Cdd:cd08378      7 VKARGLPANSNDPVVEVKLGNYKGSTKAIERTSNPEWNQVFA---FSKDRLQGSTLEVSVWDKD-KAKDDFLGGVCFDLS 82

                           90       100
                   ....*....|....*....|.
gi 2032737686 4841 SI-------SQLdnTPRWYPL 4854
Cdd:cd08378     83 EVptrvppdSPL--APQWYRL 101
C2B_RIM1alpha cd04028
C2 domain second repeat contained in Rab3-interacting molecule (RIM) proteins; RIMs are ...
 4720-4854 1.77e-13

C2 domain second repeat contained in Rab3-interacting molecule (RIM) proteins; RIMs are believed to organize specialized sites of the plasma membrane called active zones. They also play a role in controlling neurotransmitter release, plasticity processes, as well as memory and learning. RIM contains an N-terminal zinc finger domain, a PDZ domain, and two C-terminal C2 domains (C2A, C2B). 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. Members here have a type-I topology and do not bind Ca2+.


Pssm-ID: 175994 [Multi-domain]  Cd Length: 146  Bit Score: 70.88  E-value: 1.77e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4720 PITGEIQLQINYDKhlGNLIIHILQARNLAPRDNNGY-SDPFVKVYLLPGRGQVMvvqnasaeyKRRTKYIQKSLNPEWN 4798
Cdd:cd04028     15 PSMGDIQLGLYDKK--GQLEVEVIRARGLVQKPGSKVlPAPYVKVYLLEGKKCIA---------KKKTKIARKTLDPLYQ 83

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2032737686 4799 QTVIYKnisvEQLKKKTLEVTVW-DYDRFSSNDFLGEVLIELSSISQLDNTPRWYPL 4854
Cdd:cd04028     84 QQLVFD----VSPTGKTLQVIVWgDYGRMDKKVFMGVAQILLDDLDLSNLVIGWYKL 136
C2 pfam00168
C2 domain;
5113-5222 2.33e-13

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 69.27  E-value: 2.33e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 5113 QLIVEILQCRNITYKFKSPdhLPDLYVKLYVvnistQKRVIKKKTRVCRHDREPSFNETFRFSLSPAGHSLQILLVSNGG 5192
Cdd:pfam00168    2 RLTVTVIEAKNLPPKDGNG--TSDPYVKVYL-----LDGKQKKKTKVVKNTLNPVWNETFTFSVPDPENAVLEIEVYDYD 74

                           90       100       110
                   ....*....|....*....|....*....|
gi 2032737686 5193 KFMKKTLIGEAYIWLDKVDLRKRIVNWHKL 5222
Cdd:pfam00168   75 RFGRDDFIGEVRIPLSELDSGEGLDGWYPL 104
C2B_Synaptotagmin-3-5-6-9-10 cd08403
C2 domain second repeat present in Synaptotagmins 3, 5, 6, 9, and 10; Synaptotagmin is a ...
 4723-4854 5.48e-13

C2 domain second repeat present in Synaptotagmins 3, 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 3, a member of class 3 synaptotagmins, is located in the brain and localized to the active zone and plasma membrane. It functions as a Ca2+ sensor for fast exocytosis. It, along with synaptotagmins 5,6, and 10, has disulfide bonds at its N-terminus. 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 second C2 repeat, C2B, and has a type-I topology.


Pssm-ID: 176048 [Multi-domain]  Cd Length: 134  Bit Score: 69.07  E-value: 5.48e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4723 GEIQLQINYDKHLGNLIIHILQARNLAPRDNNGYSDPFVKVYLL-PGRgqvmvvqnasaEYKRRTKYIQKS-LNPEWNQT 4800
Cdd:cd08403      1 GELMFSLCYLPTAGRLTLTIIKARNLKAMDITGFSDPYVKVSLMcEGR-----------RLKKKKTSVKKNtLNPTYNEA 69

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2032737686 4801 VIYkNISVEQLKKKTLEVTVWDYDRFSSNDFLGEVLIELSSISQ--------LDN----TPRWYPL 4854
Cdd:cd08403     70 LVF-DVPPENVDNVSLIIAVVDYDRVGHNELIGVCRVGPNADGQgrehwnemLANprkpIAQWHQL 134
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 255-736 5.52e-13

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.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 76.34  E-value: 5.52e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  255 ADAKQDQAKQPAQPRGPQKSQPQPSEpTKPIQQQTSAKP--------SSGPTKPSPQQPDSTkvtsqtappTKPSSQQPG 326
Cdd:pfam03154   97 ATAKKSKTQEISRPNSPSEGEGESSD-GRSVNDEGSSDPkdidqdnrSTSPSIPSPQDNESD---------SDSSAQQQI 166

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  327 PAKQPSQQPARQGAPVKPSPQQTGPPKQPSQQPGPEKPSAqqagpakqppqpgsgkpPPQQTGLVKQVPPQAGPTKPPSQ 406
Cdd:pfam03154  167 LQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSV-----------------PPQGSPATSQPPNQTQSTAAPHT 229

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  407 TVGPTKPLAQQAGPTKPPGQQPGPEKPPqqtqaganqPTETAPKKTFCPLctttellLHTPekanyntctqchtvvcslc 486
Cdd:pfam03154  230 LIQQTPTLHPQRLPSPHPPLQPMTQPPP---------PSQVSPQPLPQPS-------LHGQ------------------- 274

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  487 gFNPNPHITEISEWLCLNCQMQRTLGGDLAPGLG---PGPQPLAPKQKTPIPPSAKPSPQPQPVQKKDVTPKPDPSQAAD 563
Cdd:pfam03154  275 -MPPMPHSLQTGPSHMQHPVPPQPFPLTPQSSQSqvpPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSMP 353

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  564 SKRPPPQKKQTQLPGSPPVKSKQPRAEPTDISQQTDATPKSdQVKPTQAEDKQKQPSVQKPTADSVStsvaaeQKQDLag 643
Cdd:pfam03154  354 HIKPPPTTPIPQLPNPQSHKHPPHLSGPSPFQMNSNLPPPP-ALKPLSSLSTHHPPSAHPPPLQLMP------QSQQL-- 424

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  644 PRPPTQqkvtdspKPELAKPSQDTHPAGDKPDSKPVPQVSRQKSDPKFASQPGARPDAKAQKPIDPTQTKDDPKKLPTKP 723
Cdd:pfam03154  425 PPPPAQ-------PPVLTQSQSLPPPAASHPPTSGLHQVPSQSPFPQHPFVPGGPPPITPPSGPPTSTSSAMPGIQPPSS 497

                          490
                   ....*....|...
gi 2032737686  724 APKPDTKPAPKGP 736
Cdd:pfam03154  498 ASVSSSGPVPAAV 510
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 259-737 5.98e-13

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 75.82  E-value: 5.98e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  259 QDQAKQPAQPRGPQKSQPQPSE-----PTKPIQQQTSAKPSSGPTKPSPQQPDSTKVTSQTAPPTKPSSQQPGPAKQPSQ 333
Cdd:pfam09606   63 PQGGQGNGGMGGGQQGMPDPINalqnlAGQGTRPQMMGPMGPGPGGPMGQQMGGPGTASNLLASLGRPQMPMGGAGFPSQ 142

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  334 QPARQGApvKPSPQQTGPPKQPSQQPGPEKPsaQQAGPAKQPPQPGSGKPPPQQtglvkQVPPQAGPtkpPSQTVGPTKP 413
Cdd:pfam09606  143 MSRVGRM--QPGGQAGGMMQPSSGQPGSGTP--NQMGPNGGPGQGQAGGMNGGQ-----QGPMGGQM---PPQMGVPGMP 210

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  414 LAQQAGPTKPPGQQPGPEKPPQQTQAGANQ-PTETAPkktfcplctttelllhtpekanyntctqchtvvcslcgfnPNP 492
Cdd:pfam09606  211 GPADAGAQMGQQAQANGGMNPQQMGGAPNQvAMQQQQ----------------------------------------PQQ 250

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  493 HITEISEWLCLNcQMQRTLGGD--LAPGLGPGpQPLAPKQKTPIPPSAKPSPQPQPVQKKDVTPKpdPSQAADSKRPPPQ 570
Cdd:pfam09606  251 QGQQSQLGMGIN-QMQQMPQGVggGAGQGGPG-QPMGPPGQQPGAMPNVMSIGDQNNYQQQQTRQ--QQQQQGGNHPAAH 326

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  571 KKQTQLPGSPpvkSKQPRAEPTDISQQTDATPKSDqvkPTQAEDKQKQPSVQKPTADSVSTSVAAEQKQDLAGPRPPTQQ 650
Cdd:pfam09606  327 QQQMNQSVGQ---GGQVVALGGLNHLETWNPGNFG---GLGANPMQRGQPGMMSSPSPVPGQQVRQVTPNQFMRQSPQPS 400

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  651 KVtdSPKPELAKPSQdTHPAGDKPDSKPVPQVSRQKSdpkfaSQPGARPDAKAQKPIDPTQTkddpkklptkpaPKPDTK 730
Cdd:pfam09606  401 VP--SPQGPGSQPPQ-SHPGGMIPSPALIPSPSPQMS-----QQPAQQRTIGQDSPGGSLNT------------PGQSAV 460


                   ....*..
gi 2032737686  731 PAPKGPQ 737
Cdd:pfam09606  461 NSPLNPQ 467
PDZ1_GgSTXBP4-like cd06692
PDZ1 domain of Gallus gallus uncharacterized syntaxin-binding protein 4 (STXBP4) isoform X1, ...
 4539-4616 8.21e-13

PDZ1 domain of Gallus gallus uncharacterized syntaxin-binding protein 4 (STXBP4) isoform X1, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of Gallus gallus uncharacterized syntaxin-binding protein 4 (STXBP4) isoform X1, and related domains. Gallus gallus STXBP4 isoform X1 contains 2 PDZ domains (PDZ1 and PDZ2). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This STXBP4-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467179 [Multi-domain]  Cd Length: 88  Bit Score: 66.86  E-value: 8.21e-13
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2032737686 4539 NGLGIRVVGGKEiPGSSGEIGAYIAKILPGGNAEQTGKLVEGMQVLEWNGIPLTGKTYEEVQSIIIQQSgeAEICVRL 4616
Cdd:cd06692      8 KGLGIKIIGGYR-ENTGEEFGIFIKRILPGGLAATDGRLKEGDLILEVNGESLQGVTNERAVSILRSAS--ASNHMSL 82
C2A_fungal cd04041
C2 domain first repeat; fungal group; C2 domains were first identified in Protein Kinase C ...
 4736-4858 8.94e-13

C2 domain first repeat; fungal group; C2 domains were first identified in Protein Kinase C (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.


Pssm-ID: 176006 [Multi-domain]  Cd Length: 111  Bit Score: 67.67  E-value: 8.94e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4736 GNLIIHILQARNLAPRDNN-GYSDPFVKVYLlpgrgqvmvvqNASAEYKRRTKYIQKSLNPEWNQTVIYKNISVEQLKKK 4814
Cdd:cd04041      1 GVLVVTIHRATDLPKADFGtGSSDPYVTASF-----------AKFGKPLYSTRIIRKDLNPVWEETWFVLVTPDEVKAGE 69

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2032737686 4815 TLEVTVWDYDRFSSNDFLGEVLIELSSISQldnTPRWYPLKEQS 4858
Cdd:cd04041     70 RLSCRLWDSDRFTADDRLGRVEIDLKELIE---DRNWMGRREDG 110
C2A_SLP cd08521
C2 domain first repeat present in Synaptotagmin-like proteins; All Slp members basically share ...
 5097-5222 9.78e-13

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.


Pssm-ID: 176056 [Multi-domain]  Cd Length: 123  Bit Score: 68.05  E-value: 9.78e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 5097 GEIKIALKKEMKTDGeqLIVEILQCRNITYKfKSPDHLPDLYVKLYVV-NISTQKrviKKKTRVCRHDREPSFNETFRFS 5175
Cdd:cd08521      1 GEIEFSLSYNYKTGS--LEVHIKECRNLAYA-DEKKKRSNPYVKVYLLpDKSKQS---KRKTSVKKNTTNPVFNETLKYH 74

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2032737686 5176 LSPAGHSLQILLVS--NGGKFMKKTLIGEAYIWLDKVDLRKRIVNWHKL 5222
Cdd:cd08521     75 ISKSQLETRTLQLSvwHHDRFGRNTFLGEVEIPLDSWDLDSQQSEWYPL 123
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 5114-5222 1.00e-12

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.


Pssm-ID: 175973 [Multi-domain]  Cd Length: 102  Bit Score: 67.09  E-value: 1.00e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 5114 LIVEILQCRNITYKFKSpdHLPDLYVKLYVVNistqkrVIKKKTRVCRHDREPSFNETFRFSLSPAGHSLQILLVSNGGK 5193
Cdd:cd00030      1 LRVTVIEARNLPAKDLN--GKSDPYVKVSLGG------KQKFKTKVVKNTLNPVWNETFEFPVLDPESDTLTVEVWDKDR 72

                           90       100       110
                   ....*....|....*....|....*....|
gi 2032737686 5194 FMKKTLIGEAYIWLDKV-DLRKRIVNWHKL 5222
Cdd:cd00030     73 FSKDDFLGEVEIPLSELlDSGKEGELWLPL 102
Glutenin_hmw pfam03157
High molecular weight glutenin subunit; Members of this family include high molecular weight ...
 195-440 1.04e-12

High molecular weight glutenin subunit; Members of this family include high molecular weight subunits of glutenin. This group of gluten proteins is thought to be largely responsible for the elastic properties of gluten, and hence, doughs. Indeed, glutenin high molecular weight subunits are classified as elastomeric proteins, because the glutenin network can withstand significant deformations without breaking, and return to the original conformation when the stress is removed. Elastomeric proteins differ considerably in amino acid sequence, but they are all polymers whose subunits consist of elastomeric domains, composed of repeated motifs, and non-elastic domains that mediate cross-linking between the subunits. The elastomeric domain motifs are all rich in glycine residues in addition to other hydrophobic residues. High molecular weight glutenin subunits have an extensive central elastomeric domain, flanked by two terminal non-elastic domains that form disulphide cross-links. The central elastomeric domain is characterized by the following three repeated motifs: PGQGQQ, GYYPTS[P/L]QQ, GQQ. It possesses overlapping beta-turns within and between the repeated motifs, and assumes a regular helical secondary structure with a diameter of approx. 1.9 nm and a pitch of approx. 1.5 nm.


Pssm-ID: 367362 [Multi-domain]  Cd Length: 786  Bit Score: 74.98  E-value: 1.04e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  195 QGKPEEQRSPAKHPTQPQSPK-------PAVQQQGPVRPTVQQTESSKQQQQPGGPKQVQKPGHGQpadakqdQAKQPAQ 267
Cdd:pfam03157  271 QWQQSGQGQQGYYPTSLQQPGqgqsgyyPTSQQQAGQLQQEQQLGQEQQDQQPGQGRQGQQPGQGQ-------QGQQPAQ 343

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  268 PRGPQKSQP--QPSEPTKPIQQQTSAKPSSGPTKPSPQQPDSTKVTSQT---------APPTKPSSQQPGPAKQPSQQPA 336
Cdd:pfam03157  344 GQQPGQGQPgyYPTSPQQPGQGQPGYYPTSQQQPQQGQQPEQGQQGQQQgqgqqgqqpGQGQQPGQGQPGYYPTSPQQSG 423

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  337 rQGAP--VKPSPQQTGPPKQPSQ--QPGPEKPS----------AQQAGPAKQPPQPGSGKP-----PPQQTGLVKQVPP- 396
Cdd:pfam03157  424 -QGQPgyYPTSPQQSGQGQQPGQgqQPGQEQPGqgqqpgqgqqGQQPGQPEQGQQPGQGQPgyyptSPQQSGQGQQLGQw 502

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2032737686  397 -QAGPTKPPSQTVGPTKPLAQQAG--PTKP----PGQQPGPEKPPQQTQAG 440
Cdd:pfam03157  503 qQQGQGQPGYYPTSPLQPGQGQPGyyPTSPqqpgQGQQLGQLQQPTQGQQG 553
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 199-444 1.26e-12

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 74.69  E-value: 1.26e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  199 EEQ-RSPAKHPTQPQSPKPAVQQQGPVrPTVQQTESSKQQQQPGGPKQVQKpgHGQPADAKQDQAKQPAQPRGPQKSQPQ 277
Cdd:pfam09770   97 EEQvRFNRQQPAARAAQSSAQPPASSL-PQYQYASQQSQQPSKPVRTGYEK--YKEPEPIPDLQVDASLWGVAPKKAAAP 173

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  278 PSEPtkpiqqQTSAKPSSGPtkpspqqPDSTKVTS-------QTAPPTKPSSQQPG-PAKQPSQQPARQGAPVKPSPQQT 349
Cdd:pfam09770  174 APAP------QPAAQPASLP-------APSRKMMSleeveaaMRAQAKKPAQQPAPaPAQPPAAPPAQQAQQQQQFPPQI 240

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  350 GPPKQPSQQPGPEKPSAQQAGPAK--QPPQPGSGKPPPQQTglvkQVPPQAGPTKPPSQTVGPTK--------PLAQQAG 419
Cdd:pfam09770  241 QQQQQPQQQPQQPQQHPGQGHPVTilQRPQSPQPDPAQPSI----QPQAQQFHQQPPPVPVQPTQilqnpnrlSAARVGY 316

                          250       260
                   ....*....|....*....|....*.
gi 2032737686  420 PTKP-PGQQPGPEKPPQQTQAGANQP 444
Cdd:pfam09770  317 PQNPqPGVQPAPAHQAHRQQGSFGRQ 342
C2_Intersectin cd08375
C2 domain present in Intersectin; A single instance of the C2 domain is located C terminally ...
 4736-4850 1.59e-12

C2 domain present in Intersectin; A single instance of the C2 domain is located C terminally in the intersectin protein. Intersectin functions as a scaffolding protein, providing a link between the actin cytoskeleton and the components of endocytosis and plays a role in signal transduction. In addition to C2, intersectin contains several additional domains including: Eps15 homology domains, SH3 domains, a RhoGEF domain, and a PH 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. The members here have topology I.


Pssm-ID: 176021 [Multi-domain]  Cd Length: 136  Bit Score: 67.79  E-value: 1.59e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4736 GNLIIHILQARNLAPRDNNGYSDPFVKVYLlpgrgqvmvvqnASAEYKrrTKYIQKSLNPEWNQTVIYkniSVEQLKKKT 4815
Cdd:cd08375     15 GRLMVVIVEGRDLKPCNSNGKSDPYCEVSM------------GSQEHK--TKVVSDTLNPKWNSSMQF---FVKDLEQDV 77

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2032737686 4816 LEVTVWDYDRFSSNDFLGEVLIELSSISQLDNTPR 4850
Cdd:cd08375     78 LCITVFDRDFFSPDDFLGRTEIRVADILKETKESK 112
PHA03247 PHA03247
large tegument protein UL36; Provisional
 61-420 2.10e-12

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 74.59  E-value: 2.10e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686   61 SRAQGLPRGNLAGAEPPPMQRH-PELDTSRHPRQPGkppdpgppglSKSRTvdvlkTEQRAPGRSPSTLSLRES-KSRTD 138
Cdd:PHA03247  2633 PAANEPDPHPPPTVPPPERPRDdPAPGRVSRPRRAR----------RLGRA-----AQASSPPQRPRRRAARPTvGSLTS 2697

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  139 FKE----DQKPSMMPSFLSEANPLSAVTSVVNKFNPFDLISDSD--------TSHEEAGRKQKVAPKEQGKPEEQRSPAK 206
Cdd:PHA03247  2698 LADppppPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPpavpagpaTPGGPARPARPPTTAGPPAPAPPAAPAA 2777

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  207 HPtQPQSPKPAVQQQGPVRPTVQQTESSKQQQQPGGPKQVQKPGHGQPAD----------AKQDQAKQPAQP-------- 268
Cdd:PHA03247  2778 GP-PRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGplppptsaqpTAPPPPPGPPPPslplggsv 2856

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  269 --------RGPQKSQP-QPSEPTKPIQQQTSAKPSSGPTKPSPQQPDstkvtSQTAPPTKPSSQQPGPAKQPSQQPARQG 339
Cdd:PHA03247  2857 apggdvrrRPPSRSPAaKPAAPARPPVRRLARPAVSRSTESFALPPD-----QPERPPQPQAPPPPQPQPQPPPPPQPQP 2931

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  340 APvkPSPQQTGPPKQPSQQPGPekpsaqQAGPAKQPPQPGSGKPPPQQTGLVKQVPPQAGPTKPPSQTvgPTKPLAQQAG 419
Cdd:PHA03247  2932 PP--PPPPRPQPPLAPTTDPAG------AGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPAS--STPPLTGHSL 3001


                   .
gi 2032737686  420 P 420
Cdd:PHA03247  3002 S 3002
PHA03378 PHA03378
EBNA-3B; Provisional
 200-445 4.48e-12

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 73.18  E-value: 4.48e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  200 EQRSPAKHPTQPQSPKPA-----VQQQGPVRPTVQQTESSKQQQQPGGPKQVQKPGHGQPAdAKQDQAKQPAQPRgpQKS 274
Cdd:PHA03378   549 ESDEPASTEPVHDQLLPApglgpLQIQPLTSPTTSQLASSAPSYAQTPWPVPHPSQTPEPP-TTQSHIPETSAPR--QWP 625

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  275 QPQPSEPTKPIQQQTSakPSSGPTKPSPQQPDSTKVTSQTAPPTKPSSQ--QPGPAKQPSQQPaRQGAP--VKPSPQQTG 350
Cdd:PHA03378   626 MPLRPIPMRPLRMQPI--TFNVLVFPTPHQPPQVEITPYKPTWTQIGHIpyQPSPTGANTMLP-IQWAPgtMQPPPRAPT 702

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  351 PPKQPSQQPGPEKPSAQQAGPAK---------QPPQPGSGKPPPQQTGLVKQVPPQAGPTK--PPSQTVGPTKPLAQQAG 419
Cdd:PHA03378   703 PMRPPAAPPGRAQRPAAATGRARppaaapgraRPPAAAPGRARPPAAAPGRARPPAAAPGRarPPAAAPGAPTPQPPPQA 782

                          250       260       270
                   ....*....|....*....|....*....|...
gi 2032737686  420 PTKP-------PGQQPGPEKPPQQTQAGANQPT 445
Cdd:PHA03378   783 PPAPqqrprgaPTPQPPPQAGPTSMQLMPRAAP 815
Glutenin_hmw pfam03157
High molecular weight glutenin subunit; Members of this family include high molecular weight ...
 182-443 5.70e-12

High molecular weight glutenin subunit; Members of this family include high molecular weight subunits of glutenin. This group of gluten proteins is thought to be largely responsible for the elastic properties of gluten, and hence, doughs. Indeed, glutenin high molecular weight subunits are classified as elastomeric proteins, because the glutenin network can withstand significant deformations without breaking, and return to the original conformation when the stress is removed. Elastomeric proteins differ considerably in amino acid sequence, but they are all polymers whose subunits consist of elastomeric domains, composed of repeated motifs, and non-elastic domains that mediate cross-linking between the subunits. The elastomeric domain motifs are all rich in glycine residues in addition to other hydrophobic residues. High molecular weight glutenin subunits have an extensive central elastomeric domain, flanked by two terminal non-elastic domains that form disulphide cross-links. The central elastomeric domain is characterized by the following three repeated motifs: PGQGQQ, GYYPTS[P/L]QQ, GQQ. It possesses overlapping beta-turns within and between the repeated motifs, and assumes a regular helical secondary structure with a diameter of approx. 1.9 nm and a pitch of approx. 1.5 nm.


Pssm-ID: 367362 [Multi-domain]  Cd Length: 786  Bit Score: 72.67  E-value: 5.70e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  182 EEAGRKQKVAPKEQGKPEEQRSPAKHPTQPQspKPAVQQQGPVRPTVQQTesskqqQQPGGPKQVQKPGHGQPADAKQ-- 259
Cdd:pfam03157  390 QQQGQGQQGQQPGQGQQPGQGQPGYYPTSPQ--QSGQGQPGYYPTSPQQS------GQGQQPGQGQQPGQEQPGQGQQpg 461

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  260 -----DQAKQPAQPRGPQKSQP--------QPSEPTKPIQQQTSAKPSSGPTKPSPQQPDSTKVTSQTAPPTKP-SSQQP 325
Cdd:pfam03157  462 qgqqgQQPGQPEQGQQPGQGQPgyyptspqQSGQGQQLGQWQQQGQGQPGYYPTSPLQPGQGQPGYYPTSPQQPgQGQQL 541

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  326 GPAKQPSQQPARQGAPVKPSPQQTGPPKQPSQQPGPEKpsAQQAGPAKQP--PQPGSGKPPPQQTGLVKQVP--PQAGPT 401
Cdd:pfam03157  542 GQLQQPTQGQQGQQSGQGQQGQQPGQGQQGQQPGQGQQ--GQQPGQGQQPgqGQPGYYPTSPQQSGQGQQPGqwQQPGQG 619

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 2032737686  402 KPPSQTVGPTKPLAQQAGPTKPPGQQPGP-EKPPQQTQAGANQ 443
Cdd:pfam03157  620 QPGYYPTSSLQLGQGQQGYYPTSPQQPGQgQQPGQWQQSGQGQ 662
PTZ00121 PTZ00121
MAEBL; Provisional
 1029-1741 6.05e-12

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 72.87  E-value: 6.05e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1029 AKPKEEPGVQKEAPKLQQGRleKTLSADKIQQGIQKEDAKpKQGKLVKAPSADKIQHASQKEDPRiqQTKLTKTASYDRV 1108
Cdd:PTZ00121  1151 AKRVEIARKAEDARKAEEAR--KAEDAKKAEAARKAEEVR-KAEELRKAEDARKAEAARKAEEER--KAEEARKAEDAKK 1225

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1109 LQEVQKEDEKLQEAKLAKtsSADKIlhRVQKEDIKLQEAKLAKVPSAdkilQGIQKEDPKLQQMKMAKALSADKIQLAAQ 1188
Cdd:PTZ00121  1226 AEAVKKAEEAKKDAEEAK--KAEEE--RNNEEIRKFEEARMAHFARR----QAAIKAEEARKADELKKAEEKKKADEAKK 1297

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1189 REDTKLQEVKLPKAASVDKIQHGTQK--DIKLQHEKIKKTSSVDKIQEEGQKEETKLQRGKLSKTPSADKIPATATADQK 1266
Cdd:PTZ00121  1298 AEEKKKADEAKKKAEEAKKADEAKKKaeEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAK 1377

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1267 IPLSTLEEDKETV--LPEKSTPHPEDKKEeiTAEIKDRVAEEKAEVEAPYKGLQAKEEEDVKKedlttgisqvvlKAEKA 1344
Cdd:PTZ00121  1378 KKADAAKKKAEEKkkADEAKKKAEEDKKK--ADELKKAAAAKKKADEAKKKAEEKKKADEAKK------------KAEEA 1443

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1345 QEAEIPVQTAplPGTDHVEAVREKIEkEDDKSDTSSSQqqkspqglsdtgyssdgissslgeipshipTDEKDLLKETSK 1424
Cdd:PTZ00121  1444 KKADEAKKKA--EEAKKAEEAKKKAE-EAKKADEAKKK------------------------------AEEAKKADEAKK 1490

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1425 KdtiSQESPPSPSDLAKLESTVLSILEAQAStlsdEKSAKSKEPSETYGEQTKDQLKTKPLPVTPESYSPDEEDLKA--- 1501
Cdd:PTZ00121  1491 K---AEEAKKKADEAKKAAEAKKKADEAKKA----EEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAeek 1563

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1502 IKEGEGTIAEEGKGAASSQAD-------------YKEEHEGDDMSARRQQRYDSVEDSSESENSPVPRRKRRTSVGSSSS 1568
Cdd:PTZ00121  1564 KKAEEAKKAEEDKNMALRKAEeakkaeearieevMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEA 1643

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1569 DEYKRDDSQGSGDEEDFIRKQILEMSADEDASgsdddefirnqlkeiSAAESQKKEEVKSKAKGTAGKHRRMARKSS--- 1645
Cdd:PTZ00121  1644 EEKKKAEELKKAEEENKIKAAEEAKKAEEDKK---------------KAEEAKKAEEDEKKAAEALKKEAEEAKKAEelk 1708

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1646 AGYDEDAGRRHSWHDDDDETFDESPEPKYR-ESKSQDSEELAVSGGgglRRFKTIELNSTITNKYSEVSEPQKGVL---- 1720
Cdd:PTZ00121  1709 KKEAEEKKKAEELKKAEEENKIKAEEAKKEaEEDKKKAEEAKKDEE---EKKKIAHLKKEEEKKAEEIRKEKEAVIeeel 1785

                          730       740
                   ....*....|....*....|..
gi 2032737686 1721 -YFDEEPELEMESLTDSPEDRS 1741
Cdd:PTZ00121  1786 dEEDEKRRMEVDKKIKDIFDNF 1807
C2_ArfGAP cd04038
C2 domain present in Arf GTPase Activating Proteins (GAP); ArfGAP is a GTPase activating ...
 4735-4846 9.89e-12

C2 domain present in Arf GTPase Activating Proteins (GAP); ArfGAP is a GTPase activating protein which regulates the ADP ribosylation factor Arf, a member of the Ras superfamily of GTP-binding proteins. The GTP-bound form of Arf is involved in Golgi morphology and is involved in recruiting coat proteins. ArfGAP is responsible for the GDP-bound form of Arf which is necessary for uncoating the membrane and allowing the Golgi to fuse with an acceptor compartment. These proteins contain an N-terminal ArfGAP domain containing the characteristic zinc finger motif (Cys-x2-Cys-x(16,17)-x2-Cys) and C-terminal C2 domain. C2 domains were first identified in Protein Kinase C (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.


Pssm-ID: 176003 [Multi-domain]  Cd Length: 145  Bit Score: 65.81  E-value: 9.89e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4735 LGNLIIHILQARNLAPRDNNGySDPFVKVYLlpgrgqvmvvqnasAEYKRRTKYIQKSLNPEWNQTViykNISVEQLKKk 4814
Cdd:cd04038      1 LGLLKVRVVRGTNLAVRDFTS-SDPYVVLTL--------------GNQKVKTRVIKKNLNPVWNEEL---TLSVPNPMA- 61

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2032737686 4815 TLEVTVWDYDRFSSNDFLGEVLIELS---SISQLD 4846
Cdd:cd04038     62 PLKLEVFDKDTFSKDDSMGEAEIDLEplvEAAKLD 96
C2B_Synaptotagmin-17 cd08410
C2 domain second repeat present in Synaptotagmin 17; Synaptotagmin is a membrane-trafficking ...
 4723-4837 1.50e-11

C2 domain second repeat present in Synaptotagmin 17; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Synaptotagmin 17 is located in the brain, kidney, and prostate and is thought to be a peripheral membrane protein. 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.


Pssm-ID: 176055 [Multi-domain]  Cd Length: 135  Bit Score: 64.91  E-value: 1.50e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4723 GEIQLQINYDKHLGNLIIHILQARNLAPRDNNGYSDPFVKVYLLPGRGQVMVvqnasaeykRRTKYIQKSLNPEWNQTVI 4802
Cdd:cd08410      1 GELLLSLNYLPSAGRLNVDIIRAKQLLQTDMSQGSDPFVKIQLVHGLKLIKT---------KKTSCMRGTIDPFYNESFS 71

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2032737686 4803 YKnISVEQLKKKTLEVTVWDYDRFSSNDFLGEVLI 4837
Cdd:cd08410     72 FK-VPQEELENVSLVFTVYGHNVKSSNDFIGRIVI 105
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 265-737 2.46e-11

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 70.88  E-value: 2.46e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  265 PAQPRGPqkSQPQPSEPTKPIQQQTSAKPSSGPTKPSP---QQPDSTKVTSQTAPPTKPSS---QQPGPAKQPSQQPARQ 338
Cdd:PRK10263   336 PVEPVTQ--TPPVASVDVPPAQPTVAWQPVPGPQTGEPviaPAPEGYPQQSQYAQPAVQYNeplQQPVQPQQPYYAPAAE 413

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  339 GAPVKP--SPQQTGPPKQPSQQPGPEKPSAQQAGPAKQP-----PQPGSGKPPPQQTGLVKQVPPQAGPTKPPSQTVGPt 411
Cdd:PRK10263   414 QPAQQPyyAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQqstfaPQSTYQTEQTYQQPAAQEPLYQQPQPVEQQPVVEP- 492

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  412 KPLAQQAGPTKPP---GQQPGPEKPPQQTQAGANQPTETAPKKTFCPLCTTTELLlhtpekanyntctqchtVVCSLCGF 488
Cdd:PRK10263   493 EPVVEETKPARPPlyyFEEVEEKRAREREQLAAWYQPIPEPVKEPEPIKSSLKAP-----------------SVAAVPPV 555

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  489 NPNPHITEISEWLCLNCQMQRTLGGDLAPGL----GPGPQPLAPKQKTPIPPSAKPSPQPQPVQKKDVTPKPDPSQAADS 564
Cdd:PRK10263   556 EAAAAVSPLASGVKKATLATGAAATVAAPVFslanSGGPRPQVKEGIGPQLPRPKRIRVPTRRELASYGIKLPSQRAAEE 635

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  565 KRPPPQKKQTQlpgsppvKSKQPRAEPTDISQQTD-----ATPKSDQVKPTQAEDKQKQPSVQKPTADS-VSTSVAAEQK 638
Cdd:PRK10263   636 KAREAQRNQYD-------SGDQYNDDEIDAMQQDElarqfAQTQQQRYGEQYQHDVPVNAEDADAAAEAeLARQFAQTQQ 708

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  639 QDLAGPRP--------------PTQQKVTDSPKPELAKPsqdthpaGDKPDSKPVPQVSRQKSDPKfASQPGARPDAKAQ 704
Cdd:PRK10263   709 QRYSGEQPaganpfslddfefsPMKALLDDGPHEPLFTP-------IVEPVQQPQQPVAPQQQYQQ-PQQPVAPQPQYQQ 780

                          490       500       510
                   ....*....|....*....|....*....|....*
gi 2032737686  705 --KPIDPTQTKDDPKKlPTKPAPKPDTKPAPKGPQ 737
Cdd:PRK10263   781 pqQPVAPQPQYQQPQQ-PVAPQPQYQQPQQPVAPQ 814
C2B_MCTP_PRT cd08376
C2 domain second repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); ...
 4740-4856 2.77e-11

C2 domain second repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); MCTPs are involved in Ca2+ signaling at the membrane. MCTP is composed of a variable N-terminal sequence, three C2 domains, two transmembrane regions (TMRs), and a short C-terminal sequence. It is one of four protein classes that are anchored to membranes via a transmembrane region; the others being synaptotagmins, extended synaptotagmins, and ferlins. MCTPs are the only membrane-bound C2 domain proteins that contain two functional TMRs. MCTPs are unique in that they bind Ca2+ but not phospholipids. 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-II topology.


Pssm-ID: 176022 [Multi-domain]  Cd Length: 116  Bit Score: 63.43  E-value: 2.77e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4740 IHILQARNLAPRDNNGYSDPFVKVYLlpgRGQvmvvqnasaeyKRRTKYIQKSLNPEWnqtviyknisVEQL-------K 4812
Cdd:cd08376      4 IVLVEGKNLPPMDDNGLSDPYVKFRL---GNE-----------KYKSKVCSKTLNPQW----------LEQFdlhlfddQ 59

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2032737686 4813 KKTLEVTVWDYDRFSSNDFLGEVLIELSSISQLDNTPRWYPLKE 4856
Cdd:cd08376     60 SQILEIEVWDKDTGKKDEFIGRCEIDLSALPREQTHSLELELED 103
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 247-580 5.92e-11

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 69.27  E-value: 5.92e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  247 QKPGHGQPADAKQDQAKQPAQPRGPQKSQPQPSEP---------TKPIQQQTSAKPSSGPTKPSPQQPDSTKVT----SQ 313
Cdd:pfam09606   75 GQQGMPDPINALQNLAGQGTRPQMMGPMGPGPGGPmgqqmggpgTASNLLASLGRPQMPMGGAGFPSQMSRVGRmqpgGQ 154

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  314 TAPPTKPSSQQPGPAKQ----PSQQPArQGAPVKPSPQQTGPP--KQPSQ-----QPGPEKPSAQ---QAGPAKQ-PPQP 378
Cdd:pfam09606  155 AGGMMQPSSGQPGSGTPnqmgPNGGPG-QGQAGGMNGGQQGPMggQMPPQmgvpgMPGPADAGAQmgqQAQANGGmNPQQ 233

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  379 GSGKP--------PPQQTGLVKQVPPQAGPTKPPSQTVGPTKPLAQQAGPTKPPGQQPGPEKP----------------P 434
Cdd:pfam09606  234 MGGAPnqvamqqqQPQQQGQQSQLGMGINQMQQMPQGVGGGAGQGGPGQPMGPPGQQPGAMPNvmsigdqnnyqqqqtrQ 313

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  435 QQTQAGANQPtETAPKKTFCPLCTTTElLLHTPEKANYNTCTQCHTVvcslcGFNPNPHITEISEWLCLNCQMQRTLGGD 514
Cdd:pfam09606  314 QQQQQGGNHP-AAHQQQMNQSVGQGGQ-VVALGGLNHLETWNPGNFG-----GLGANPMQRGQPGMMSSPSPVPGQQVRQ 386

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  515 LAP--GLGPGPQPLAPKQKTP--IPPSAkPSPQPQPVQKKDVTPKPDPSQAADSKRPPPQkkqtQLPGSP 580
Cdd:pfam09606  387 VTPnqFMRQSPQPSVPSPQGPgsQPPQS-HPGGMIPSPALIPSPSPQMSQQPAQQRTIGQ----DSPGGS 451
C2B_PI3K_class_II cd08381
C2 domain second repeat present in class II phosphatidylinositol 3-kinases (PI3Ks); There are ...
 5135-5222 5.95e-11

C2 domain second repeat present in class II phosphatidylinositol 3-kinases (PI3Ks); There are 3 classes of PI3Ks based on structure, regulation, and specificity. All classes contain a N-terminal C2 domain, a PIK domain, and a kinase catalytic domain. Unlike class I and class III, class II PI3Ks have additionally a PX domain and a C-terminal C2 domain containing a nuclear localization signal both of which bind phospholipids though in a slightly different fashion. PI3Ks (AKA phosphatidylinositol (PtdIns) 3-kinases) regulate cell processes such as cell growth, differentiation, proliferation, and motility. PI3Ks work on phosphorylation of phosphatidylinositol, phosphatidylinositide (4)P (PtdIns (4)P),2 or PtdIns(4,5)P2. Specifically they phosphorylate the D3 hydroxyl group of phosphoinositol lipids on the inositol ring. 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.


Pssm-ID: 176027 [Multi-domain]  Cd Length: 122  Bit Score: 62.70  E-value: 5.95e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 5135 PDLYVKLYVvnISTQKRVIKKKTRVCRHDREPSFNETFRFSLSPA----GHSLQiLLVSNGGKFMKKTLIGEAYIWLDKV 5210
Cdd:cd08381     33 PDPYVKTYL--LPDPQKTTKRKTKVVRKTRNPTFNEMLVYDGLPVedlqQRVLQ-VSVWSHDSLVENEFLGGVCIPLKKL 109

                           90
                   ....*....|..
gi 2032737686 5211 DLRKRIVNWHKL 5222
Cdd:cd08381    110 DLSQETEKWYPL 121
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 246-706 9.04e-11

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 68.95  E-value: 9.04e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  246 VQKPGHGQPADAKQDQAKQPAQPRGPQKSQPQPSEPTKPIQQQTSAKPSSGPTKPSP-QQPDSTKVTSQTapptkpssQQ 324
Cdd:PTZ00449   489 IKKSKKKLAPIEEEDSDKHDEPPEGPEASGLPPKAPGDKEGEEGEHEDSKESDEPKEgGKPGETKEGEVG--------KK 560

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  325 PGPAKQ--PSQQPARQGAPvkPSPQQTGPPKQPSQQPGPEKP-SAQQAGPAKQPPQPGSGKPPpqqtglvkQVPPQAGPT 401
Cdd:PTZ00449   561 PGPAKEhkPSKIPTLSKKP--EFPKDPKHPKDPEEPKKPKRPrSAQRPTRPKSPKLPELLDIP--------KSPKRPESP 630

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  402 KPPSQTVGPTKPLAqqagPTKPPGQQ-PGPEKPPQqtqaganqptetAPKKTFCPlcTTTELLLHTPEKANYNTCTQCHT 480
Cdd:PTZ00449   631 KSPKRPPPPQRPSS----PERPEGPKiIKSPKPPK------------SPKPPFDP--KFKEKFYDDYLDAAAKSKETKTT 692

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  481 VVCSlcgfnpNPHITEISEWLCLNCQMQRTLGGDLAPGLGPGPQPLAPKQKTPIPPSAKPSPQPQPVQKKDV----TP-- 554
Cdd:PTZ00449   693 VVLD------ESFESILKETLPETPGTPFTTPRPLPPKLPRDEEFPFEPIGDPDAEQPDDIEFFTPPEEERTffheTPad 766

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  555 KPDPSQAADSKRPPPQKKQTqlpGSPPVKSKQPRAePTDISQQTDAT----PK----SDQVKPTQAEDKQKQPSVQKPTA 626
Cdd:PTZ00449   767 TPLPDILAEEFKEEDIHAET---GEPDEAMKRPDS-PSEHEDKPPGDhpslPKkrhrLDGLALSTTDLESDAGRIAKDAS 842

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  627 DSVSTSVAAEQKQDLAGPR------PPTQQKVTDSPKPElaKPSQDTHPagdkPDSKPVPQVSRQKSDPKFASQPGARPD 700
Cdd:PTZ00449   843 GKIVKLKRSKSFDDLTTVEeaeemgAEARKIVVDDDGTE--ADDEDTHP----PEEKHKSEVRRRRPPKKPSKPKKPSKP 916


                   ....*.
gi 2032737686  701 AKAQKP 706
Cdd:PTZ00449   917 KKPKKP 922
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 177-406 9.64e-11

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 68.52  E-value: 9.64e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  177 SDTSHEEAGR--KQKVAPKEQGKPEeQRSPAKHPTQPQSPKPAVQQQGPVR------------PTVQQ-------TESSK 235
Cdd:pfam09770   92 SDAIEEEQVRfnRQQPAARAAQSSA-QPPASSLPQYQYASQQSQQPSKPVRtgyekykepepiPDLQVdaslwgvAPKKA 170

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  236 QQQQPGGPKQVQKPGHGQPAD----------AKQDQAKQPAQPRGPQ-KSQPQPSEPTKPIQQQTSAKPSSGPTKPSPQQ 304
Cdd:pfam09770  171 AAPAPAPQPAAQPASLPAPSRkmmsleeveaAMRAQAKKPAQQPAPApAQPPAAPPAQQAQQQQQFPPQIQQQQQPQQQP 250

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  305 PDSTKVTSQTAPPT---KPSSQQPGPAkQPSQQPARQGAPVKPSPQqtgpPKQPSQQ-PGPEKPSAQQAGPAKQPPQPGS 380
Cdd:pfam09770  251 QQPQQHPGQGHPVTilqRPQSPQPDPA-QPSIQPQAQQFHQQPPPV----PVQPTQIlQNPNRLSAARVGYPQNPQPGVQ 325

                          250       260
                   ....*....|....*....|....*.
gi 2032737686  381 GKPPPQQTGLVKQVPPQAGPTKPPSQ 406
Cdd:pfam09770  326 PAPAHQAHRQQGSFGRQAPIITHPQQ 351
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 184-387 1.51e-10

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 68.09  E-value: 1.51e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  184 AGRKQKVAPKEQGKPEEQRSPAkHPTQPQSPKPAVQQQGPVRPTVQQTESSKQqqqpggpkqvQKPGHGQPADAKQDQAK 263
Cdd:PRK07764   595 AGGEGPPAPASSGPPEEAARPA-APAAPAAPAAPAPAGAAAAPAEASAAPAPG----------VAAPEHHPKHVAVPDAS 663

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  264 QPAQPRGPQKSQPQPSEPTKPIQQQtsakPSSGPTKPSPQQPDstkvtsQTAPPTKPSSQQPGPAKQPSQQPARQGAPVK 343
Cdd:PRK07764   664 DGGDGWPAKAGGAAPAAPPPAPAPA----APAAPAGAAPAQPA------PAPAATPPAGQADDPAAQPPQAAQGASAPSP 733

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 2032737686  344 PSPQQTGPPKQPSQQPGPEKP--SAQQAGPAKQPPQPGSGKPPPQQ 387
Cdd:PRK07764   734 AADDPVPLPPEPDDPPDPAGApaQPPPPPAPAPAAAPAAAPPPSPP 779
C2B_Munc13 cd04027
C2 domain second repeat in Munc13 (mammalian uncoordinated) proteins; C2-like domains are ...
 4738-4859 3.60e-10

C2 domain second repeat in Munc13 (mammalian uncoordinated) proteins; C2-like domains are thought to be involved in phospholipid binding in a Ca2+ independent manner in both Unc13 and Munc13. Caenorabditis elegans Unc13 has a central domain with sequence similarity to PKC, which includes C1 and C2-related domains. Unc13 binds phorbol esters and DAG with high affinity in a phospholipid manner. Mutations in Unc13 results in abnormal neuronal connections and impairment in cholinergic neurotransmission in the nematode. Munc13 is the mammalian homolog which are expressed in the brain. There are 3 isoforms (Munc13-1, -2, -3) and are thought to play a role in neurotransmitter release and are hypothesized to be high-affinity receptors for phorbol esters. Unc13 and Munc13 contain both C1 and C2 domains. There are two C2 related domains present, one central and one at the carboxyl end. Munc13-1 contains a third C2-like domain. Munc13 interacts with syntaxin, synaptobrevin, and synaptotagmin suggesting a role for these as scaffolding 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 second C2 repeat, C2B, and has a type-II topology.


Pssm-ID: 175993 [Multi-domain]  Cd Length: 127  Bit Score: 60.66  E-value: 3.60e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4738 LIIHILQARNLAPRDNNGYSDPFVKVyllpgrgQVmvvqnasAEYKRRTKYIQKSLNPEWNQTVIYK-NISVEQLKkktl 4816
Cdd:cd04027      3 ISITVVCAQGLIAKDKTGTSDPYVTV-------QV-------GKTKKRTKTIPQNLNPVWNEKFHFEcHNSSDRIK---- 64

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2032737686 4817 eVTVWDYD---------RFS--SNDFLGEVLIELSSIS-QLDntpRWYPLKEQSE 4859
Cdd:cd04027     65 -VRVWDEDddiksrlkqKFTreSDDFLGQTIIEVRTLSgEMD---VWYNLEKRTD 115
C2_KIAA0528-like cd08688
C2 domain found in the Human KIAA0528 cDNA clone; The members of this CD are named after the ...
 4740-4854 4.00e-10

C2 domain found in the Human KIAA0528 cDNA clone; The members of this CD are named after the Human KIAA0528 cDNA clone. All members here contain a single C2 repeat. No other information on this protein is currently known. 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.


Pssm-ID: 176070 [Multi-domain]  Cd Length: 110  Bit Score: 60.01  E-value: 4.00e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4740 IHILQARNLAPRD-NNGYSDPFVKVYLlpgrgqvmvvqnASAEYKrrTKYIQKSLNPEWNQTVIYKNISVEQLKKKTLEV 4818
Cdd:cd08688      3 VRVVAARDLPVMDrSSDLTDAFVEVKF------------GSTTYK--TDVVKKSLNPVWNSEWFRFEVDDEELQDEPLQI 68

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2032737686 4819 TVWDYDRFSSNDFLGEVLIELSSISQLDNTPR---WYPL 4854
Cdd:cd08688     69 RVMDHDTYSANDAIGKVYIDLNPLLLKDSVSQisgWFPI 107
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
 322-436 6.57e-10

Proline-rich protein; This family includes several eukaryotic proline-rich proteins.


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 61.21  E-value: 6.57e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  322 SQQPGPAKQPSQQPARQGAPVKPSPqqtGPPKQPSQQPGPEKPsaqQAGPAKQPPQPGSGKP--PPQQTGLVKQVPPQAG 399
Cdd:pfam15240   46 PQGPPPGGFPPQPPASDDPPGPPPP---GGPQQPPPQGGKQKP---QGPPPQGGPRPPPGKPqgPPPQGGNQQQGPPPPG 119

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2032737686  400 -PTKPPSQTVG-PTKPLAQQAGPTKPPGQQPGPEKPPQQ 436
Cdd:pfam15240  120 kPQGPPPQGGGpPPQGGNQQGPPPPPPGNPQGPPQRPPQ 158
Glutenin_hmw pfam03157
High molecular weight glutenin subunit; Members of this family include high molecular weight ...
 247-696 1.18e-09

High molecular weight glutenin subunit; Members of this family include high molecular weight subunits of glutenin. This group of gluten proteins is thought to be largely responsible for the elastic properties of gluten, and hence, doughs. Indeed, glutenin high molecular weight subunits are classified as elastomeric proteins, because the glutenin network can withstand significant deformations without breaking, and return to the original conformation when the stress is removed. Elastomeric proteins differ considerably in amino acid sequence, but they are all polymers whose subunits consist of elastomeric domains, composed of repeated motifs, and non-elastic domains that mediate cross-linking between the subunits. The elastomeric domain motifs are all rich in glycine residues in addition to other hydrophobic residues. High molecular weight glutenin subunits have an extensive central elastomeric domain, flanked by two terminal non-elastic domains that form disulphide cross-links. The central elastomeric domain is characterized by the following three repeated motifs: PGQGQQ, GYYPTS[P/L]QQ, GQQ. It possesses overlapping beta-turns within and between the repeated motifs, and assumes a regular helical secondary structure with a diameter of approx. 1.9 nm and a pitch of approx. 1.5 nm.


Pssm-ID: 367362 [Multi-domain]  Cd Length: 786  Bit Score: 64.97  E-value: 1.18e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  247 QKPGHGQpadaKQDQAKQPAQPRGPQksqpQPSEPTKPIQQQTSAKPSSGPTKPSPQQPDSTKVTSQTAPPTKPSSQQPG 326
Cdd:pfam03157  129 QRPGQGQ----QPGQGQQWYYPTSPQ----QPGQWQQPGQGQQGYYPTSPQQSGQRQQPGQGQQLRQGQQGQQSGQGQPG 200

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  327 PAKQPSQQP------ARQGAPVKPSP----QQTGPPKQPSQ-QPGPEKPSAQQAGPAKQPPQPGSGKPPPQ-------QT 388
Cdd:pfam03157  201 YYPTSSQQPgqlqqtGQGQQGQQPERgqqgQQPGQGQQPGQgQQGQQPGQPQQLGQGQQGYYPISPQQPRQwqqsgqgQQ 280

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  389 GLVKQVPPQAG-------PTKPPSQTVGPTKPLAQQAGPTKPPGQQPGPEKPPQQTQ----AGANQPTETAPKKTfcplc 457
Cdd:pfam03157  281 GYYPTSLQQPGqgqsgyyPTSQQQAGQLQQEQQLGQEQQDQQPGQGRQGQQPGQGQQgqqpAQGQQPGQGQPGYY----- 355

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  458 TTTELLLHTPEKANYNTCTQCHTVvcslcgfNPNPHITEISEWLCLNCQMQRTlGGDLAPGLG-PGPQPLAPKQKTPIPP 536
Cdd:pfam03157  356 PTSPQQPGQGQPGYYPTSQQQPQQ-------GQQPEQGQQGQQQGQGQQGQQP-GQGQQPGQGqPGYYPTSPQQSGQGQP 427

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  537 SAKPSPQPQPVQKKDVTPKPDPSQAA-DSKRPPPQKKQTQLPGSPPVKSK----QPRAEPTDISQQTDATPKSDQVKPTQ 611
Cdd:pfam03157  428 GYYPTSPQQSGQGQQPGQGQQPGQEQpGQGQQPGQGQQGQQPGQPEQGQQpgqgQPGYYPTSPQQSGQGQQLGQWQQQGQ 507

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  612 AEDKQKQPSVQKPTADSVSTSVAAEQKQDLAGPRPPTQQKVTDSPKPELAKPSQDTHPAGDKPDSKpvPQVSRQKSDPKF 691
Cdd:pfam03157  508 GQPGYYPTSPLQPGQGQPGYYPTSPQQPGQGQQLGQLQQPTQGQQGQQSGQGQQGQQPGQGQQGQQ--PGQGQQGQQPGQ 585


                   ....*
gi 2032737686  692 ASQPG 696
Cdd:pfam03157  586 GQQPG 590
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
 516-736 1.29e-09

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 64.56  E-value: 1.29e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  516 APGLGPGPQPLAPKQKTPIPPSakPSPQPQPVQKKDVTPKP-DPSQAADSKRPP----PQKKQTQLPGSPPVKSKQPRAE 590
Cdd:PLN03209   332 ESDAADGPKPVPTKPVTPEAPS--PPIEEEPPQPKAVVPRPlSPYTAYEDLKPPtspiPTPPSSSPASSKSVDAVAKPAE 409

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  591 PtDISQQTDATPKSDQVKPTQAEDKQ-------------KQPSVQKPTADSVSTSVAAEQKQDLAGPRPPTQQKVTDSPK 657
Cdd:PLN03209   410 P-DVVPSPGSASNVPEVEPAQVEAKKtrplspyaryedlKPPTSPSPTAPTGVSPSVSSTSSVPAVPDTAPATAATDAAA 488

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  658 PELAKP---SQDTHPAGDKPDSKPVPQVSRQKSDPKFASQ-PGARPDAKAQKPIDPTQTKdDPKKLPTKPAP-----KPD 728
Cdd:PLN03209   489 PPPANMrplSPYAVYDDLKPPTSPSPAAPVGKVAPSSTNEvVKVGNSAPPTALADEQHHA-QPKPRPLSPYTmyedlKPP 567


                   ....*...
gi 2032737686  729 TKPAPKGP 736
Cdd:PLN03209   568 TSPTPSPV 575
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 187-682 1.53e-09

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 64.71  E-value: 1.53e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  187 KQKVAP-------KEQGKPEEQRSPAKHPTQPQSPKPAVQQQGPVRPTVQQTESSKQQQQPGGPKQvQKPGhgqPADAKQ 259
Cdd:PTZ00449   493 KKKLAPieeedsdKHDEPPEGPEASGLPPKAPGDKEGEEGEHEDSKESDEPKEGGKPGETKEGEVG-KKPG---PAKEHK 568

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  260 DQ-----AKQPAQPRGPqKSQPQPSEPTKPIQQQTSAKPSSgptKPSPQQPDSTKVTSQTAPPTKPSSqqpgPAKQPSqq 334
Cdd:PTZ00449   569 PSkiptlSKKPEFPKDP-KHPKDPEEPKKPKRPRSAQRPTR---PKSPKLPELLDIPKSPKRPESPKS----PKRPPP-- 638

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  335 PARQGAPVKP-SPQQTGPPKQPSQQPGPEKPSAQQAGPAKQPPQPGSGKPPPQQTGLVKQVPPQAGPTKPPSQTVGPTKP 413
Cdd:PTZ00449   639 PQRPSSPERPeGPKIIKSPKPPKSPKPPFDPKFKEKFYDDYLDAAAKSKETKTTVVLDESFESILKETLPETPGTPFTTP 718

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  414 laqQAGPTKPPGQQPGPEKPPQQTQAganqpTETAPKKTFCPLCTTTELLLHTPEKanyntctqchtvvcslcgfNPNPH 493
Cdd:PTZ00449   719 ---RPLPPKLPRDEEFPFEPIGDPDA-----EQPDDIEFFTPPEEERTFFHETPAD-------------------TPLPD 771

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  494 IT--EISEwlclncqmqRTLGGDLAPGLGPGPQPLAPKQKTPIPPSAKPSpQPQPVQKKDVTPKPDPSQAADSKRpppqk 571
Cdd:PTZ00449   772 ILaeEFKE---------EDIHAETGEPDEAMKRPDSPSEHEDKPPGDHPS-LPKKRHRLDGLALSTTDLESDAGR----- 836

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  572 kQTQLPGSPPVKSKQPRA--EPTDISQQTDATPKSDQV----KPTQAEDKQKQPSVQKptadsvstsvaaeQKQDLAGPR 645
Cdd:PTZ00449   837 -IAKDASGKIVKLKRSKSfdDLTTVEEAEEMGAEARKIvvddDGTEADDEDTHPPEEK-------------HKSEVRRRR 902

                          490       500       510
                   ....*....|....*....|....*....|....*..
gi 2032737686  646 PPtqQKVTDSPKPelAKPSQDThpagdKPDSKPVPQV 682
Cdd:PTZ00449   903 PP--KKPSKPKKP--SKPKKPK-----KPDSAFIPSI 930
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 255-680 1.59e-09

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 64.81  E-value: 1.59e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  255 ADAKQDQAKQPAqPRGPQKSQPQPSEPTKPIQQQ---------TSAKPSSGPTKPSPQQPDSTkvtsqTAPPTKPSSQQP 325
Cdd:PHA03307    51 AAVTVVAGAAAC-DRFEPPTGPPPGPGTEAPANEsrstptwslSTLAPASPAREGSPTPPGPS-----SPDPPPPTPPPA 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  326 GPAkqpsqqparqgapvkPSPQQTGPPKQPSQQPGPEKPSAQQAGPAKQPPQPGSGKPPPQQTGLVKQVPPQAGPTKPPs 405
Cdd:PHA03307   125 SPP---------------PSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSS- 188

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  406 qtVGPTKPLAQQAGPTKPPGQQPGPEkppqqTQAGANQPTETAPKKTFCPLCTTTELLLHTPEKAnyntCTQCHTVVCSL 485
Cdd:PHA03307   189 --PPAEPPPSTPPAAASPRPPRRSSP-----ISASASSPAPAPGRSAADDAGASSSDSSSSESSG----CGWGPENECPL 257

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  486 CGFNPNPHITEI---SEWLCLNCQMQRTLGGDLAPGLGPGPQPLAPKQKTPIPP--------------SAKPSPQPQPVQ 548
Cdd:PHA03307   258 PRPAPITLPTRIweaSGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSprasssssssressSSSTSSSSESSR 337

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  549 KKDVTPKPDPSQAADSKRPPPqkkqtQLPGSPPVKSKQPRAEPtdisqQTDATPKSDqvkptqaedkqkqPSVQKPTADS 628
Cdd:PHA03307   338 GAAVSPGPSPSRSPSPSRPPP-----PADPSSPRKRPRPSRAP-----SSPAASAGR-------------PTRRRARAAV 394

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2032737686  629 VSTSVAAEQKQDLAGPRPPTQQKVTDSPKPELAKPSQDTHPAGDK-PDSKPVP 680
Cdd:PHA03307   395 AGRARRRDATGRFPAGRPRPSPLDAGAASGAFYARYPLLTPSGEPwPGSPPPP 447
C2_Kibra cd08680
C2 domain found in Human protein Kibra; Kibra is thought to be a regulator of the Salvador ...
 4725-4854 2.21e-09

C2 domain found in Human protein Kibra; Kibra is thought to be a regulator of the Salvador (Sav)/Warts (Wts)/Hippo (Hpo) (SWH) signaling network, which limits tissue growth by inhibiting cell proliferation and promoting apoptosis. The core of the pathway consists of a MST and LATS family kinase cascade that ultimately phosphorylates and inactivates the YAP/Yorkie (Yki) transcription coactivator. The FERM domain proteins Merlin (Mer) and Expanded (Ex) are part of the upstream regulation controlling pathway mechanism. Kibra colocalizes and associates with Mer and Ex and is thought to transduce an extracellular signal via the SWH network. The apical scaffold machinery that contains Hpo, Wts, and Ex recruits Yki to the apical membrane facilitating its inhibitory phosphorlyation by Wts. Since Kibra associates with Ex and is apically located it is hypothesized that KIBRA is part of the scaffold, helps in the Hpo/Wts complex, and helps recruit Yki for inactivation that promotes SWH pathway activity. Kibra contains two amino-terminal WW domains, an internal C2-like domain, and a carboxy-terminal glutamic acid-rich stretch. 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.


Pssm-ID: 176062  Cd Length: 124  Bit Score: 58.40  E-value: 2.21e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4725 IQLQINYDKHLGNLIIHILQARNLA---PRDNngySDPFVKVYLLPGrgqvmvVQNASAEYkrRTKYIQKSLNPEWNqTV 4801
Cdd:cd08680      3 VQIGLRYDSGDSSLVISVEQLRNLSalsIPEN---SKVYVRVALLPC------SSSTSCLF--RTKALEDQDKPVFN-EV 70

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2032737686 4802 IYKNISVEQLKKKTLEVTVWDYDRFSSNDFLGEVLIELSSISQLDN-TPRWYPL 4854
Cdd:cd08680     71 FRVPISSTKLYQKTLQVDVCSVGPDQQEECLGGAQISLADFESSEEmSTKWYNL 124
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 189-425 2.37e-09

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 64.24  E-value: 2.37e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  189 KVAPKEQGKPEEQRSPAKHPTQPQSPKPAVQQQGPVRPtvqqtesskqqqqpggpkqvqkPGHGQPADAKQDQAKQPAQP 268
Cdd:PRK07764   593 GAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPA----------------------GAAAAPAEASAAPAPGVAAP 650

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  269 RGPQKSQPQPsEPTKPIQQQTSAKPSSGPTKPSPQQPDSTKVTSQTAPPtkpSSQQPGPAKQPSQQPARQGAPVKPSPQQ 348
Cdd:PRK07764   651 EHHPKHVAVP-DASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAP---AQPAPAPAATPPAGQADDPAAQPPQAAQ 726

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  349 TGPPKQPS---QQPGPEKPSAQQAGPAKQPPQPGSGKPPPqqtglvkqvPPQAGPTKPPSQTVGPTKPLAQQAGPTKPPG 425
Cdd:PRK07764   727 GASAPSPAaddPVPLPPEPDDPPDPAGAPAQPPPPPAPAP---------AAAPAAAPPPSPPSEEEEMAEDDAPSMDDED 797
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
 1295-1584 2.72e-09

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 64.30  E-value: 2.72e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1295 ITAEIKDRVAEEKAEVEAPYKGLQAKEEEDVKKEDLttgisQVVLKA----EKAQEAEIPV-QTAPLPGTDHVEAVREKI 1369
Cdd:PTZ00108  1099 LTKEKVEKLNAELEKKEKELEKLKNTTPKDMWLEDL-----DKFEEAleeqEEVEEKEIAKeQRLKSKTKGKASKLRKPK 1173

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1370 EKEDDKSDtsssqqqkspqgLSDTGYSSDGISSSLGeiPSHIPTDEKDLLKETS-KKDTISQESPPSPSDLAKLESTVLS 1448
Cdd:PTZ00108  1174 LKKKEKKK------------KKSSADKSKKASVVGN--SKRVDSDEKRKLDDKPdNKKSNSSGSDQEDDEEQKTKPKKSS 1239

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1449 ILEAQASTLSDEKSAKSKEPSETYGEQTKDQLKTKPLPVTPESYSPDE-------EDLKAIKEGEGTIAEEGKGAASSQA 1521
Cdd:PTZ00108  1240 VKRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPpskrpdgESNGGSKPSSPTKKKVKKRLEGSLA 1319

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2032737686 1522 DYKEEHEGDDMSARRQQRYDSVEDSSESENSPVPRRKRRTSVGSSS-SDEYKRDDSQGSGDEED 1584
Cdd:PTZ00108  1320 ALKKKKKSEKKTARKKKSKTRVKQASASQSSRLLRRPRKKKSDSSSeDDDDSEVDDSEDEDDED 1383
PDZ3_PDZD2-PDZ1_hPro-IL-16-like cd06759
PDZ domain 3 of PDZ domain containing 2 (PDZD2), PDZ domain 1 of human pro-interleukin-16 ...
 4538-4598 3.09e-09

PDZ domain 3 of PDZ domain containing 2 (PDZD2), PDZ domain 1 of human pro-interleukin-16 (isoform 1, 1332 AA), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of PDZD2, also known as KIAA0300, PIN-1, activated in prostate cancer (AIPC) and PDZ domain-containing protein 3 (PDZK3). PDZD2 has seven PDZ domains. PDZD2 is expressed at exceptionally high levels in the pancreas and certain cancer tissues, such as prostate cancer. It promotes the proliferation of insulinoma cells and is upregulated during prostate tumorigenesis. In osteosarcoma (OS), the microRNA miR-363 acts as a tumor suppressor by inhibiting PDZD2. This family also includes the first PDZ domain (PDZ1) of human pro-interleukin-16 (isoform 1, also known as nPro-Il-16; 1332 amino-acid protein). Precursor IL-16 is cleaved to produce pro-IL-16 and mature IL-16 (derived from the C-terminal 121 AA). Pro-IL-16 functions as a regulator of T cell growth; mature IL-16 is a CD4 ligand that induces chemotaxis and CD25 expression in CD4+ T cells. IL-16 bioactivity has been closely associated with the progression of several different cancers. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PDZD2-like family PDZ3 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467240 [Multi-domain]  Cd Length: 87  Bit Score: 56.90  E-value: 3.09e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2032737686 4538 GNGLGIRVVGGKEIPgsSGEIGAYIAKILPGGNAEQTGKLVEGMQVLEWNGIPLTGKTYEE 4598
Cdd:cd06759     11 GKGLGFSIVGGRDSP--RGPMGIYVKTIFPGGAAAEDGRLKEGDEILEVNGESLQGLTHQE 69
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 249-648 3.27e-09

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 63.47  E-value: 3.27e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  249 PGHGQPADAKQDQAKQPAQPRGPQKSQPQPSEPtkpiQQQTSAKPSSGPTKPSPQQPDSTKvtSQTAPPTKPSSQQPGPA 328
Cdd:PRK07764   408 AAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPA----PPSPAGNAPAGGAPSPPPAAAPSA--QPAPAPAAAPEPTAAPA 481

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  329 KQPSQQPARQGAPVKPSPQQTGPPKQPSQQPG---PE----------------KPSAQQAGPAKQPPQPGSGKPP----- 384
Cdd:PRK07764   482 PAPPAAPAPAAAPAAPAAPAAPAGADDAATLRerwPEilaavpkrsrktwailLPEATVLGVRGDTLVLGFSTGGlarrf 561

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  385 -------------PQQTGLVKQVPPQAGPTKPPSQTVGPTKPLAQQAGPTKP-PGQQPGPEKPPQQTQAGANQPTETAPK 450
Cdd:PRK07764   562 aspgnaevlvtalAEELGGDWQVEAVVGPAPGAAGGEGPPAPASSGPPEEAArPAAPAAPAAPAAPAPAGAAAAPAEASA 641

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  451 KTFCPLCTTTELLLHTPEKANyntctqchtvvcslcgfnpnphiteisewlclncqmqrTLGGDLAPGLGPGPQPLAPKQ 530
Cdd:PRK07764   642 APAPGVAAPEHHPKHVAVPDA--------------------------------------SDGGDGWPAKAGGAAPAAPPP 683

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  531 KTPIPPSAKPSPQPQPVQKKDVTPKPDPSQAADSKRPPPQKKQTQLPGSPPVKSKQPRA-EPTDISQQTDATPKSDQVKP 609
Cdd:PRK07764   684 APAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPpEPDDPPDPAGAPAQPPPPPA 763

                          410       420       430
                   ....*....|....*....|....*....|....*....
gi 2032737686  610 TQAEDKQKQPSVQKPTADSVSTSVAAEQKQDLAGPRPPT 648
Cdd:PRK07764   764 PAPAAAPAAAPPPSPPSEEEEMAEDDAPSMDDEDRRDAE 802
PDZ2-PTPN13_FRMPD2-like cd06792
PDZ domain 2 of tyrosine kinase PTPN13, FERM and PDZ domain-containing protein 2 (FRMPD2), and ...
 4539-4609 3.40e-09

PDZ domain 2 of tyrosine kinase PTPN13, FERM and PDZ domain-containing protein 2 (FRMPD2), and similar domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of human PTPN13, and related domains. PTPN13, also known as Fas-associated protein-tyrosine phosphatase 1 (FAP-1), protein-tyrosine phosphatase 1E (PTP-E1), and protein-tyrosine phosphatase (PTPL1), negatively regulates FAS-mediated apoptosis and NGFR-mediated pro-apoptotic signaling, and may also regulate phosphoinositide 3-kinase (PI3K) signaling. It contains 5 PDZ domains; interaction partners of its second PDZ domain (PDZ2) include the Fas receptor (TNFRSF6) and thyroid receptor-interacting protein 6 (TRIP6). The second PDZ (PDZ2) domain, but not PDZ1 or PDZ3, of FRMPD2 binds to GluN2A and GluN2B, two subunits of N-methyl-d-aspartic acid (NMDA) receptors. Other binding partners of the FRMPDZ2 PDZ2 domain include NOD2, and catenin family members, delta catenin (CTNND2), armadillo repeat gene deleted in velo-cardio-facial syndrome (ARVCF) and p0071 (also known as plakophilin 4; PKP4). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PTPN13-like family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467254 [Multi-domain]  Cd Length: 87  Bit Score: 56.84  E-value: 3.40e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2032737686 4539 NGLGIRVVGGKEIPGSSGeiGAYIAKILPGGNAEQTGKLVEGMQVLEWNGIPLTGKTYEEVQSiIIQQSGE 4609
Cdd:cd06792     12 GSLGISVTGGINTSVRHG--GIYVKSLVPGGAAEQDGRIQKGDRLLEVNGVSLEGVTHKQAVE-CLKNAGQ 79
C2A_Synaptotagmin-14_16 cd08389
C2A domain first repeat present in Synaptotagmins 14 and 16; Synaptotagmin 14 and 16 are ...
 4723-4855 3.56e-09

C2A domain first repeat present in Synaptotagmins 14 and 16; Synaptotagmin 14 and 16 are membrane-trafficking proteins in specific tissues outside the brain. Both of these contain C-terminal tandem C2 repeats, but only Synaptotagmin 14 has an N-terminal transmembrane domain and a putative fatty-acylation site. 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 and this is indeed the case here. 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.


Pssm-ID: 176035 [Multi-domain]  Cd Length: 124  Bit Score: 57.64  E-value: 3.56e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4723 GEIQLQINYDKHLGNLIIHILQARNLAPRDNNGYSDPFVKVYLLPGRGQvmvvqnasaeyKRRTKyIQKSLNPEWNQTVI 4802
Cdd:cd08389      3 GDLDVAFEYDPSARKLTVTVIRAQDIPTKDRGGASSWQVHLVLLPSKKQ-----------RAKTK-VQRGPNPVFNETFT 70

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2032737686 4803 YKNISVEQLKKKTLEVTVWDYDRFSSNDFLGEVLIELSSISQLDNTPRWYPLK 4855
Cdd:cd08389     71 FSRVEPEELNNMALRFRLYGVERMRKERLIGEKVVPLSQLNLEGETTVWLTLE 123
COG5038 COG5038
Ca2+-dependent lipid-binding protein, contains C2 domain [General function prediction only];
4736-4844 3.98e-09

Ca2+-dependent lipid-binding protein, contains C2 domain [General function prediction only];


Pssm-ID: 227371 [Multi-domain]  Cd Length: 1227  Bit Score: 63.62  E-value: 3.98e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4736 GNLIIHILQARNLAPRDNNGYSDPFVKVYLlpgrgqvmvvQNASAeykRRTKYIQKSLNPEWNQTVIyknISVEQLKKKT 4815
Cdd:COG5038   1040 GYLTIMLRSGENLPSSDENGYSDPFVKLFL----------NEKSV---YKTKVVKKTLNPVWNEEFT---IEVLNRVKDV 1103

                           90       100
                   ....*....|....*....|....*....
gi 2032737686 4816 LEVTVWDYDRFSSNDFLGEVLIELSSISQ 4844
Cdd:COG5038   1104 LTINVNDWDSGEKNDLLGTAEIDLSKLEP 1132
PDZ2_PDZD2-like cd06758
PDZ domain 2 of PDZ domain containing 2 (PDZD2), and related domains; PDZ (PSD-95 ...
 4532-4603 4.50e-09

PDZ domain 2 of PDZ domain containing 2 (PDZD2), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of PDZD2, also known as KIAA0300, PIN-1, activated in prostate cancer (AIPC) and PDZ domain-containing protein 3 (PDZK3). PDZD2 has seven PDZ domains, and is expressed at exceptionally high levels in the pancreas and certain cancer tissues such as prostate cancer. It promotes the proliferation of insulinoma cells and is upregulated during prostate tumorigenesis. In osteosarcoma (OS), the microRNA miR-363 acts as a tumor suppressor by inhibiting PDZD2. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PDZD2-like family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467239 [Multi-domain]  Cd Length: 88  Bit Score: 56.21  E-value: 4.50e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2032737686 4532 KDHTVSGN-GLGIRVVGGKeipGSS-GEIGAYIAKILPGGNAEQTGKLVEGMQVLEWNGIPLTGKTYEEVQSII 4603
Cdd:cd06758      4 KMHLLKEKgGLGIQITGGK---GSKrGDIGIFVAGVEEGGSADRDGRLKKGDELLMINGQSLIGLSHQEAVAIL 74
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 182-452 5.04e-09

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 62.86  E-value: 5.04e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  182 EEAGRKQKVAPKEQGKPEEQRSPAKHPTQPQSPKPAVQQQGPV-RPTVqqtesskqqqqpggpkqvqKPghgQPADAKQD 260
Cdd:NF033839   285 KEPGNKKPSAPKPGMQPSPQPEKKEVKPEPETPKPEVKPQLEKpKPEV-------------------KP---QPEKPKPE 342

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  261 QAKQPAQPRGPQKsqPQPSEPTKPIQQQTSAKPSSGPTKPSPQQPDSTKVTSQTAPPTKPSSQQPGPAKQPsqQPARQGA 340
Cdd:NF033839   343 VKPQLETPKPEVK--PQPEKPKPEVKPQPEKPKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEKPKPEVKP--QPEKPKP 418

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  341 PVKPSPQQTGPPKQPSQQ-------PGPEKPSAQqagpakQPPQPGSGKP--PPQQTGLVKQVPPQAGPTKPPSqtvgpT 411
Cdd:NF033839   419 EVKPQPEKPKPEVKPQPEkpkpevkPQPEKPKPE------VKPQPETPKPevKPQPEKPKPEVKPQPEKPKPDN-----S 487

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 2032737686  412 KPLAQQAGPTKPPGQQPGPEKppqQTQAGANQPTETAPKKT 452
Cdd:NF033839   488 KPQADDKKPSTPNNLSKDKQP---SNQASTNEKATNKPKKS 525
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
 261-435 6.97e-09

Proline-rich protein; This family includes several eukaryotic proline-rich proteins.


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 58.13  E-value: 6.97e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  261 QAKQPAQPRGPQKSQPQPSE-PTKPIQQQTSAKPSSGPTKPSPQQPDstkvtsqtapptKPSSQQPGPAKQPSQQPARQG 339
Cdd:pfam15240   25 QEDSPSLISEEEGQSQQGGQgPQGPPPGGFPPQPPASDDPPGPPPPG------------GPQQPPPQGGKQKPQGPPPQG 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  340 APVKPSPQQTGPPKQPSQQPgpekpsaqqagpaKQPPQPGSGKPPPQQTGlvkQVPPQAGPTKPPsqtvgPTKPLAQQAG 419
Cdd:pfam15240   93 GPRPPPGKPQGPPPQGGNQQ-------------QGPPPPGKPQGPPPQGG---GPPPQGGNQQGP-----PPPPPGNPQG 151

                          170
                   ....*....|....*.
gi 2032737686  420 PTKPPGQQPGPEKPPQ 435
Cdd:pfam15240  152 PPQRPPQPGNPQGPPQ 167
PHA03247 PHA03247
large tegument protein UL36; Provisional
 290-1029 7.09e-09

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 63.03  E-value: 7.09e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  290 SAKPSSGPTKPSPQQPDSTKVTSQTAPPTKPSsQQPGPAKQPSQQPARQGAPVKPSPQQTGPPkqPSQQPGPEKPSAQQA 369
Cdd:PHA03247  2491 AAGAAPDPGGGGPPDPDAPPAPSRLAPAILPD-EPVGEPVHPRMLTWIRGLEELASDDAGDPP--PPLPPAAPPAAPDRS 2567

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  370 GPakqPPQPGSGKPPPQQTGLVKQ--VPPQAGPTKPPsqtVGPTKPLAQQAGPTKPPGQQPGPEKPPQQTQAGANQPTET 447
Cdd:PHA03247  2568 VP---PPRPAPRPSEPAVTSRARRpdAPPQSARPRAP---VDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPH 2641

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  448 APKKTFCPlctttelllHTPEKAnyntctqchtvvcslcgfnPNPHITEISEwlclNCQMQRTLGGDLAPGLGPGPqPLA 527
Cdd:PHA03247  2642 PPPTVPPP---------ERPRDD-------------------PAPGRVSRPR----RARRLGRAAQASSPPQRPRR-RAA 2688

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  528 PKQKTPIPPSAKPSPQPQPvqkkdvtPKPDPSQAADSKRPPPQKKQTQLPGSPPVKSKQPRAEPTdisqqTDATPKSDQV 607
Cdd:PHA03247  2689 RPTVGSLTSLADPPPPPPT-------PEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPA-----GPATPGGPAR 2756

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  608 KPTQAedkqkqpsvqkptadSVSTSVAAEQKQDLAGPRPPTqqkvtdSPKPELAKPSQDTHPAGDKPDSKPVPQVSrqkS 687
Cdd:PHA03247  2757 PARPP---------------TTAGPPAPAPPAAPAAGPPRR------LTRPAVASLSESRESLPSPWDPADPPAAV---L 2812

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  688 DPKFASQPGARPDAKAQKPIDPTQTKDDPKKLPTKPAPKPDTKPAPKGPqagagpkaapaqpapqpqppqktpeQPRRfs 767
Cdd:PHA03247  2813 APAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGD-------------------------VRRR-- 2865

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  768 lnlgGITDAPKPQPTTPQETvtgklfgfgasffsQASNLISTAGQTGSQPSGPPPPAPAAKQPQPPAQPPAPQAAPKEAA 847
Cdd:PHA03247  2866 ----PPSRSPAAKPAAPARP--------------PVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPP 2927

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  848 QAQPLPKAVPVKKEAKPLTTEKSEPSKVDGVLTKGSDLEKKPGLAKDSKPLAAEAKKPDGLSEPEKASQPEMSCPLCKT- 926
Cdd:PHA03247  2928 QPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLSRVSSw 3007

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  927 ----GLNIGSKDPPnfntcTECKKVVcnlcgfnpmphiaevqeWLCLNCQTQRAMSGQLGDMGKVPL--LKPGPSQPTSK 1000
Cdd:PHA03247  3008 asslALHEETDPPP-----VSLKQTL-----------------WPPDDTEDSDADSLFDSDSERSDLeaLDPLPPEPHDP 3065

                          730       740
                   ....*....|....*....|....*....
gi 2032737686 1001 PAAPPQKRPVPAVSHSPQKTSTPPTPAAA 1029
Cdd:PHA03247  3066 FAHEPDPATPEAGARESPSSQFGPPPLSA 3094
C2_fungal_Inn1p-like cd08681
C2 domain found in fungal Ingression 1 (Inn1) proteins; Saccharomyces cerevisiae Inn1 ...
 4736-4860 7.27e-09

C2 domain found in fungal Ingression 1 (Inn1) proteins; Saccharomyces cerevisiae Inn1 associates with the contractile actomyosin ring at the end of mitosis and is needed for cytokinesis. The C2 domain of Inn1, located at the N-terminus, is required for ingression of the plasma membrane. The C-terminus is relatively unstructured and contains eight PXXP motifs that are thought to mediate interaction of Inn1 with other proteins with SH3 domains in the cytokinesis proteins Hof1 (an F-BAR protein) and Cyk3 (whose overexpression can restore primary septum formation in Inn1Delta cells) as well as recruiting Inn1 to the bud-neck by binding to Cyk3. Inn1 and Cyk3 appear to cooperate in activating chitin synthase Chs2 for primary septum formation, which allows coordination of actomyosin ring contraction with ingression of the cleavage furrow. It is thought that the C2 domain of Inn1 helps to preserve the link between the actomyosin ring and the plasma membrane, contributing both to membrane ingression, as well as to stability of the contracting ring. Additionally, Inn1 might induce curvature of the plasma membrane adjacent to the contracting ring, thereby promoting ingression of the membrane. It has been shown that the C2 domain of human synaptotagmin induces curvature in target membranes and thereby contributes to fusion of these membranes with synaptic vesicles. 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 synaptotagmin1. 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.


Pssm-ID: 176063 [Multi-domain]  Cd Length: 118  Bit Score: 56.87  E-value: 7.27e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4736 GNLIIHILQARNLAPRDNNGYSDPFVKVYLlpgrgqvmvvqnasAEYKRRTKYIQKS-LNPEWNQTVIYkNISVEqlKKK 4814
Cdd:cd08681      1 GTLVVVVLKARNLPNKRKLDKQDPYCVLRI--------------GGVTKKTKTDFRGgQHPEWDEELRF-EITED--KKP 63

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2032737686 4815 TLEVTVWDyDRFSSNDFLGEVLIELSSISQLDNTPRWYPLKEQSEN 4860
Cdd:cd08681     64 ILKVAVFD-DDKRKPDLIGDTEVDLSPALKEGEFDDWYELTLKGRY 108
C2_NEDD4_NEDD4L cd04033
C2 domain present in the Human neural precursor cell-expressed, developmentally down-regulated ...
 4738-4868 8.49e-09

C2 domain present in the Human neural precursor cell-expressed, developmentally down-regulated 4 (NEDD4) and NEDD4-like (NEDD4L/NEDD42); Nedd4 and Nedd4-2 are two of the nine members of the Human Nedd4 family. All vertebrates appear to have both Nedd4 and Nedd4-2 genes. They are thought to participate in the regulation of epithelial Na+ channel (ENaC) activity. They also have identical specificity for ubiquitin conjugating enzymes (E2). Nedd4 and Nedd4-2 are composed of a C2 domain, 2-4 WW domains, and a ubiquitin ligase Hect domain. Their WW domains can bind PPxY (PY) or LPSY motifs, and in vitro studies suggest that WW3 and WW4 of both proteins bind PY motifs in the key substrates, with WW3 generally exhibiting higher affinity. Most Nedd4 family members, especially Nedd4-2, also have multiple splice variants, which might play different roles in regulating their substrates. 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.


Pssm-ID: 175999 [Multi-domain]  Cd Length: 133  Bit Score: 56.98  E-value: 8.49e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4738 LIIHILQARNLAPRDNNGYSDPFVKVYLLPGR--GQVMVVQnasaeykrrTKYIQKSLNPEWNQTVIYKnisVEQLKKKt 4815
Cdd:cd04033      2 LRVKVLAGIDLAKKDIFGASDPYVKISLYDPDgnGEIDSVQ---------TKTIKKTLNPKWNEEFFFR---VNPREHR- 68

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2032737686 4816 LEVTVWDYDRFSSNDFLGEVLIELSS--ISQLDN----TPRWYPLKEQSEnidhgKSHS 4868
Cdd:cd04033     69 LLFEVFDENRLTRDDFLGQVEVPLNNlpTETPGNerryTFKDYLLRPRSS-----KSRV 122
C2B_Synaptotagmin-12 cd08406
C2 domain second repeat present in Synaptotagmin 12; Synaptotagmin is a membrane-trafficking ...
 4723-4855 1.03e-08

C2 domain second repeat present in Synaptotagmin 12; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Synaptotagmin 12, a member of class 6 synaptotagmins, is located in the brain. It functions are unknown. It, like synaptotagmins 8 and 13, do not have any consensus Ca2+ binding sites. 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.


Pssm-ID: 176051 [Multi-domain]  Cd Length: 136  Bit Score: 56.72  E-value: 1.03e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4723 GEIQLQINYDKHLGNLIIHILQARNLAPRDNNGYSDPFVKVYLLpgrgqvmvvQNASAEYKRRTKYIQKSLNPEWNQTVI 4802
Cdd:cd08406      2 GEILLSLSYLPTAERLTVVVVKARNLVWDNGKTTADPFVKVYLL---------QDGRKISKKKTSVKRDDTNPIFNEAMI 72

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2032737686 4803 YkNISVEQLKKKTLEVTVWDYDRFSSNDFLGEVLI-------ELSSISQLDNTPR-----WYPLK 4855
Cdd:cd08406     73 F-SVPAIVLQDLSLRVTVAESTEDGKTPNVGHVIIgpaasgmGLSHWNQMLASLRkpvamWHPLR 136
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
184-434 1.07e-08

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 61.79  E-value: 1.07e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  184 AGRKQKVAPKEQGKPEeQRSPAKHPTQPQSPKPAVQQQGPVRPTVQqteSSKQQQQPGGPKQVQKPGHGQPADAKQDQAK 263
Cdd:PRK07003   369 GGGVPARVAGAVPAPG-ARAAAAVGASAVPAVTAVTGAAGAALAPK---AAAAAAATRAEAPPAAPAPPATADRGDDAAD 444

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  264 QPA--QPRGPQKSQPQPSEPTKPIQQQTSAKPSSGPTKPSPqqPDSTKvtsQTAPPTKPSSQQPGPAKQPSQQPARQGAP 341
Cdd:PRK07003   445 GDApvPAKANARASADSRCDERDAQPPADSGSASAPASDAP--PDAAF---EPAPRAAAPSAATPAAVPDARAPAAASRE 519

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  342 VKPSPQQTGPPKQPSQQPGPEKPSAQ------------------------QAGPAKQPPQPGSGKPPPQQTGLVKQVPPQ 397
Cdd:PRK07003   520 DAPAAAAPPAPEARPPTPAAAAPAARaggaaaaldvlrnagmrvssdrgaRAAAAAKPAAAPAAAPKPAAPRVAVQVPTP 599

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 2032737686  398 AGPTKPPSQTVGPTKPLAQQAGPTKPPgqQPGPEKPP 434
Cdd:PRK07003   600 RARAATGDAPPNGAARAEQAAESRGAP--PPWEDIPP 634
C2_Munc13_fungal cd04043
C2 domain in Munc13 (mammalian uncoordinated) proteins; fungal group; C2-like domains are ...
 4740-4841 1.25e-08

C2 domain in Munc13 (mammalian uncoordinated) proteins; fungal group; C2-like domains are thought to be involved in phospholipid binding in a Ca2+ independent manner in both Unc13 and Munc13. Caenorabditis elegans Unc13 has a central domain with sequence similarity to PKC, which includes C1 and C2-related domains. Unc13 binds phorbol esters and DAG with high affinity in a phospholipid manner. Mutations in Unc13 results in abnormal neuronal connections and impairment in cholinergic neurotransmission in the nematode. Munc13 is the mammalian homolog which are expressed in the brain. There are 3 isoforms (Munc13-1, -2, -3) and are thought to play a role in neurotransmitter release and are hypothesized to be high-affinity receptors for phorbol esters. Unc13 and Munc13 contain both C1 and C2 domains. There are two C2 related domains present, one central and one at the carboxyl end. Munc13-1 contains a third C2-like domain. Munc13 interacts with syntaxin, synaptobrevin, and synaptotagmin suggesting a role for these as scaffolding 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 second C2 repeat, C2B, and has a type-II topology.


Pssm-ID: 176008 [Multi-domain]  Cd Length: 126  Bit Score: 56.50  E-value: 1.25e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4740 IHILQARNLAPRDNNGYSDPFVkvyllpgrgqVMVVQNASAEYKrRTKYIQKSLNPEWNQTViykNISVEQLKKKTLEVT 4819
Cdd:cd04043      5 IRIVRAENLKADSSNGLSDPYV----------TLVDTNGKRRIA-KTRTIYDTLNPRWDEEF---ELEVPAGEPLWISAT 70

                           90       100
                   ....*....|....*....|..
gi 2032737686 4820 VWDYDRFSSNDFLGEVLIELSS 4841
Cdd:cd04043     71 VWDRSFVGKHDLCGRASLKLDP 92
PDZ7_MUPP1-PD6_PATJ-like cd06671
PDZ domain 7 of multi-PDZ-domain protein 1 (MUPP1), PDZ domain 6 of PATJ (protein-associated ...
 4521-4603 1.27e-08

PDZ domain 7 of multi-PDZ-domain protein 1 (MUPP1), PDZ domain 6 of PATJ (protein-associated tight junction) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 7 of MUPP1 and PDZ domain 6 of PATJ, and related domains. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, 9, and 13; consequently, MUPP1 PDZ7 and 8 align with PATJ PDZ6 and 7; and MUPP1 PDZ domains 10-12 align with PATJ PDZ domains 8-10. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like family PDZ7 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467159 [Multi-domain]  Cd Length: 96  Bit Score: 55.40  E-value: 1.27e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4521 PHTRLKLLRDPkdhtvsGNGLGIRVVGGKEI---PGSSGEI-GAYIAKILPGGNAEQTGKLVEGMQVLEWNGIPLTGKTY 4596
Cdd:cd06671      1 PPRRVELWREP------GKSLGISIVGGRVMgsrLSNGEEIrGIFIKHVLEDSPAGRNGTLKTGDRILEVNGVDLRNATH 74


                   ....*..
gi 2032737686 4597 EEVQSII 4603
Cdd:cd06671     75 EEAVEAI 81
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 192-430 1.48e-08

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 61.56  E-value: 1.48e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  192 PKEQGKPEEQRSPAKHPTQPQ--------SPKPAVQQQGPVRPTVQQTESSKQQQQPGGPKQVQKP--GHGQPADAKQDQ 261
Cdd:pfam09606  231 PQQMGGAPNQVAMQQQQPQQQgqqsqlgmGINQMQQMPQGVGGGAGQGGPGQPMGPPGQQPGAMPNvmSIGDQNNYQQQQ 310

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  262 AKQPAQPRGPQKSQPQPSEPTKPIQQQTSAKPSSGPTKPSPQQPdsTKVTSQTAPPtkpsSQQPGPAKQPSQQPARQGAP 341
Cdd:pfam09606  311 TRQQQQQQGGNHPAAHQQQMNQSVGQGGQVVALGGLNHLETWNP--GNFGGLGANP----MQRGQPGMMSSPSPVPGQQV 384

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  342 vkpspQQTGPPKQPSQQPGPEKPSAQqaGPAKQPPQPGSGKPPPqQTGLVKQVPPQAGPTKPPSQTVGPTKPlaqqAGPT 421
Cdd:pfam09606  385 -----RQVTPNQFMRQSPQPSVPSPQ--GPGSQPPQSHPGGMIP-SPALIPSPSPQMSQQPAQQRTIGQDSP----GGSL 452


                   ....*....
gi 2032737686  422 KPPGQQPGP 430
Cdd:pfam09606  453 NTPGQSAVN 461
C2_PKC_alpha_gamma cd04026
C2 domain in Protein Kinase C (PKC) alpha and gamma; A single C2 domain is found in PKC alpha ...
 5097-5179 1.52e-08

C2 domain in Protein Kinase C (PKC) alpha and gamma; A single C2 domain is found in PKC alpha and gamma. The PKC family of serine/threonine kinases regulates apoptosis, proliferation, migration, motility, chemo-resistance, and differentiation. There are 3 groups: group 1(alpha, betaI, beta II, gamma) which require phospholipids and calcium, group 2 (delta, epsilon, theta, eta) which do not require calcium for activation, and group 3 (xi, iota/lambda) which are atypical and can be activated in the absence of diacylglycerol and calcium. 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. Members here have a type-I topology.


Pssm-ID: 175992 [Multi-domain]  Cd Length: 131  Bit Score: 56.12  E-value: 1.52e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 5097 GEIKIalkkEMKTDGEQLIVEILQCRNITYKfkSPDHLPDLYVKLYVvnISTQKRVIKKKTRVCRHDREPSFNETFRFSL 5176
Cdd:cd04026      2 GRIYL----KISVKDNKLTVEVREAKNLIPM--DPNGLSDPYVKLKL--IPDPKNETKQKTKTIKKTLNPVWNETFTFDL 73


                   ...
gi 2032737686 5177 SPA 5179
Cdd:cd04026     74 KPA 76
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
 251-386 1.85e-08

Proline-rich protein; This family includes several eukaryotic proline-rich proteins.


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 56.97  E-value: 1.85e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  251 HGQPADAKQDQAKQPAQPRGPQKSQPQPSEPTKPIQQQTSAKPSSGPTKPSPQQPDSTKVTSQTAPPTKPSSQQPGPAKQ 330
Cdd:pfam15240   39 SQQGGQGPQGPPPGGFPPQPPASDDPPGPPPPGGPQQPPPQGGKQKPQGPPPQGGPRPPPGKPQGPPPQGGNQQQGPPPP 118

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2032737686  331 PSQQparqgapvKPSPQQTGPPKQPSQQPGPEKPSA-QQAGPAKQPPQPGSGKPPPQ 386
Cdd:pfam15240  119 GKPQ--------GPPPQGGGPPPQGGNQQGPPPPPPgNPQGPPQRPPQPGNPQGPPQ 167
PHA03247 PHA03247
large tegument protein UL36; Provisional
 516-1049 1.92e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 61.49  E-value: 1.92e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  516 APGLGPGPQPLAPKQKTPIPPSAKPSPQ--PQPVQKKDVTPKP-------DPSQAADSKRPPPQKKQTQLPGSPPVKSKQ 586
Cdd:PHA03247  2491 AAGAAPDPGGGGPPDPDAPPAPSRLAPAilPDEPVGEPVHPRMltwirglEELASDDAGDPPPPLPPAAPPAAPDRSVPP 2570

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  587 PRAEPTDISQQTDATPKSDQVKPTQAEDKqkqpSVQKPTADSVSTSVAAEQKQDLAGPRPPTQqkvtdSPKP---ELAKP 663
Cdd:PHA03247  2571 PRPAPRPSEPAVTSRARRPDAPPQSARPR----APVDDRGDPRGPAPPSPLPPDTHAPDPPPP-----SPSPaanEPDPH 2641

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  664 SQDTHPAGDKPDSKPVP------QVSRQKSDPKFASQPGARPDAKAQKP-IDPTQTKDDPKKLPTKPAPKP----DTKPA 732
Cdd:PHA03247  2642 PPPTVPPPERPRDDPAPgrvsrpRRARRLGRAAQASSPPQRPRRRAARPtVGSLTSLADPPPPPPTPEPAPhalvSATPL 2721

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  733 PKGPQAGAGPKAAPAQPAPQPQPPQktpeqprrfslnlGGITDAPKPQPTTPQETVTGKLFGFGASFFSQASNLISTAGQ 812
Cdd:PHA03247  2722 PPGPAAARQASPALPAAPAPPAVPA-------------GPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAV 2788

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  813 TGSQPSGPPPPAPAAKQPQPPAQPPAPQAAPKEAAQAQPLPKAVPVKKEAKPLTTEKSEPS-KVDGVLTKGSDLEKKPgl 891
Cdd:PHA03247  2789 ASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSlPLGGSVAPGGDVRRRP-- 2866

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  892 akdskPLAAEAKKPDGLSEP--EKASQPEMSCPLCKTGLNIGSKDPPnfntcteckkvvcnlcgfnPMPhiaevqewlcl 969
Cdd:PHA03247  2867 -----PSRSPAAKPAAPARPpvRRLARPAVSRSTESFALPPDQPERP-------------------PQP----------- 2911

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  970 ncqtqramsgqlgdmgkvpllkPGPSQPTSKPAAPPQKRPVPAVshSPQKTSTPPTPAAAKPKEEPGVQKEAPKLQQGRL 1049
Cdd:PHA03247  2912 ----------------------QAPPPPQPQPQPPPPPQPQPPP--PPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGAL 2967
PTZ00121 PTZ00121
MAEBL; Provisional
 1018-1807 2.07e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 61.31  E-value: 2.07e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1018 QKTSTPPTPAAAKPKEEPGVQKEAPKLQQGRleKTLSADKIQQGIQKEDAKPKQGKLvKAPSADKIQHASQKEDPRiqQT 1097
Cdd:PTZ00121  1104 KKTETGKAEEARKAEEAKKKAEDARKAEEAR--KAEDARKAEEARKAEDAKRVEIAR-KAEDARKAEEARKAEDAK--KA 1178

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1098 KLTKTASYDRVLQEVQKEDE--KLQEAKlaKTSSADKILHRVQKEDIKLQEAkLAKVPSADKILQGIQKEDPKLQQMKMA 1175
Cdd:PTZ00121  1179 EAARKAEEVRKAEELRKAEDarKAEAAR--KAEEERKAEEARKAEDAKKAEA-VKKAEEAKKDAEEAKKAEEERNNEEIR 1255

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1176 KALSADKIQLAAQREDTKLQEVKlpKAASVDKIQHGTQKDIKLQHEKIKKTSSVDKIQEEGQK-EETKLQRGKLSKTPSA 1254
Cdd:PTZ00121  1256 KFEEARMAHFARRQAAIKAEEAR--KADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKaDEAKKKAEEAKKKADA 1333

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1255 DKIPATAtADQKIPLSTLEEDKETVLPEKSTPHPE-DKKEEITAEIKDRVAEEKAEVEAPYKGLQAKEEEDVKKEDLTTG 1333
Cdd:PTZ00121  1334 AKKKAEE-AKKAAEAAKAEAEAAADEAEAAEEKAEaAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKK 1412

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1334 ISQVVLKAEKAQEAEIPVQTAplpgTDHVEAVREKIEKEDDKSDTSSSQQQKSPQGLSDTGYSSDGISSSlgeipshipT 1413
Cdd:PTZ00121  1413 AAAAKKKADEAKKKAEEKKKA----DEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKK---------A 1479

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1414 DEKDLLKETSKKdtiSQESPPSPSDLAKLESTVLSILEAQAStlsdEKSAKSKEPSETYGEQTKDQLKTKPLPVTPESYS 1493
Cdd:PTZ00121  1480 EEAKKADEAKKK---AEEAKKKADEAKKAAEAKKKADEAKKA----EEAKKADEAKKAEEAKKADEAKKAEEKKKADELK 1552

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1494 PDEEDLKA---IKEGEGTIAEEGKGAASSQAD-------------YKEEHEGDDMSARRQQRYDSVEDSSESENSPVPRR 1557
Cdd:PTZ00121  1553 KAEELKKAeekKKAEEAKKAEEDKNMALRKAEeakkaeearieevMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEK 1632

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1558 KRRTSVGSSSSDEYKRDDSQGSGDEEDFIRKQILEMSADEDASgsdddefirnqlkeiSAAESQKKEEVKSKAKGTAGKH 1637
Cdd:PTZ00121  1633 KKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKK---------------KAEEAKKAEEDEKKAAEALKKE 1697

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1638 RRMARKSS---AGYDEDAGRRHSWHDDDDETFDESPEPKYR-ESKSQDSEELAVSGGgglRRFKTIELNSTITNKYSEVS 1713
Cdd:PTZ00121  1698 AEEAKKAEelkKKEAEEKKKAEELKKAEEENKIKAEEAKKEaEEDKKKAEEAKKDEE---EKKKIAHLKKEEEKKAEEIR 1774

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1714 EPQKGVLY-----FDEEPELEMESLTDSPEDRSR------GEGSSSLHAS--SFTPGTSPTSVSSLDEDSDSSPSHKKLG 1780
Cdd:PTZ00121  1775 KEKEAVIEeeldeEDEKRRMEVDKKIKDIFDNFAniieggKEGNLVINDSkeMEDSAIKEVADSKNMQLEEADAFEKHKF 1854

                          810       820
                   ....*....|....*....|....*....
gi 2032737686 1781 GESKQQRKARHRTHGPLLPT--IEDSSEE 1807
Cdd:PTZ00121  1855 NKNNENGEDGNKEADFNKEKdlKEDDEEE 1883
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 191-444 2.12e-08

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 61.16  E-value: 2.12e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  191 APKEQGKPEEQRSPAKHPTQPQSPKPAVQQQGPVRPTVQQTESSKQQQQPGGPKQVQKPGHGQPADAKQDQAKQPAQPRG 270
Cdd:PRK07764   391 AGAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAP 470

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  271 PQKSQPQPSEPTKPIQQQTSAKPSSGPTKPSPQQPDSTKVTSQTAPP--------------------------------- 317
Cdd:PRK07764   471 AAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAPAGADDAATLRERWPeilaavpkrsrktwaillpeatvlgvrgdtlvl 550

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  318 --TKPSSQQ----------------------------PGPAKQPSQQPARQGAPVKPSPQQTGPPKQPSQ--QPGPEKPS 365
Cdd:PRK07764   551 gfSTGGLARrfaspgnaevlvtalaeelggdwqveavVGPAPGAAGGEGPPAPASSGPPEEAARPAAPAApaAPAAPAPA 630

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2032737686  366 AQQAGPAKQPPQPGSGKPPPQQTGLVKQVPPQAGPTKPPSQTVGPTKPLAQQAGPTKPPGQQPGPEKPPQQTQAGANQP 444
Cdd:PRK07764   631 GAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATP 709
C2A_SLP-4_5 cd04029
C2 domain first repeat present in Synaptotagmin-like proteins 4 and 5; All Slp members ...
 5097-5222 2.21e-08

C2 domain first repeat present in Synaptotagmin-like proteins 4 and 5; 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. SHD of Slp (except for the Slp4-SHD) function as a specific Rab27A/B-binding domain. In addition to Slp, rabphilin, Noc2, and Munc13-4 also function as Rab27-binding proteins. It has been demonstrated that Slp4/granuphilin promotes dense-core vesicle exocytosis. The C2A domain of Slp4 is Ca2+ dependent. 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.


Pssm-ID: 175995 [Multi-domain]  Cd Length: 125  Bit Score: 55.52  E-value: 2.21e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 5097 GEIKIALKKEMKTDGeqLIVEILQCRNITYKFKSpDHLPDLYVKLYVvnISTQKRVIKKKTRVCRHDREPSFNETFRFSL 5176
Cdd:cd04029      2 GEILFSLSYDYKTQS--LNVHVKECRNLAYGDEA-KKRSNPYVKTYL--LPDKSRQSKRKTSIKRNTTNPVYNETLKYSI 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2032737686 5177 SP---AGHSLQiLLVSNGGKFMKKTLIGEAYIWLDKVDLRKRIVNWHKL 5222
Cdd:cd04029     77 SHsqlETRTLQ-LSVWHYDRFGRNTFLGEVEIPLDSWNFDSQHEECLPL 124
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
183-413 2.23e-08

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 61.02  E-value: 2.23e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  183 EAGRKQKVAPKEQGKPEEQRSPAKHPTQPQSPKPAVQQQGPVRPTVQQTESSKQQQQPGGPKQVQKPGHGQPADAKQDQA 262
Cdd:PRK07003   392 GASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPPATADRGDDAADGDAPVPAKANARASADSRCDERDAQPP 471

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  263 KQPAQPRGPQKSQPqPSEPTKPIQQQTSAKPSSGPTKPSPQQPDSTKVTSQTAPPTKPSSQQPGPAKQPSQQPARQG--- 339
Cdd:PRK07003   472 ADSGSASAPASDAP-PDAAFEPAPRAAAPSAATPAAVPDARAPAAASREDAPAAAAPPAPEARPPTPAAAAPAARAGgaa 550

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  340 --------APVKPSPQQT----GPPKQPSQQPGPEKPSAQQagPAKQPPQPGSGKPPPQQTglvkqvPPQAGPTKPPSQT 407
Cdd:PRK07003   551 aaldvlrnAGMRVSSDRGaraaAAAKPAAAPAAAPKPAAPR--VAVQVPTPRARAATGDAP------PNGAARAEQAAES 622


                   ....*.
gi 2032737686  408 VGPTKP 413
Cdd:PRK07003   623 RGAPPP 628
PHA03378 PHA03378
EBNA-3B; Provisional
 192-402 2.43e-08

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 60.85  E-value: 2.43e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  192 PKEQGKPEEQRSPAK--HPTQPQSPKPAVQQQGPVRPTVQQT-ESSKQQQQPGGPKQVQKPGH--GQPADAKQDQAKQPA 266
Cdd:PHA03378   609 PTTQSHIPETSAPRQwpMPLRPIPMRPLRMQPITFNVLVFPTpHQPPQVEITPYKPTWTQIGHipYQPSPTGANTMLPIQ 688

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  267 QprGPQKSQPQPSEPTKpiqqqtsAKPSSGPtkPSPQQPDSTKVTSQTAPPTKPSSQQPgPAKQPSQQPARQGAPVKPSP 346
Cdd:PHA03378   689 W--APGTMQPPPRAPTP-------MRPPAAP--PGRAQRPAAATGRARPPAAAPGRARP-PAAAPGRARPPAAAPGRARP 756

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2032737686  347 QQTGPPKQPSQQPGPEKPSAQ---QAGPA-KQPPQPGSGKPPPQQTG------LVKQVPPQAGPTK 402
Cdd:PHA03378   757 PAAAPGRARPPAAAPGAPTPQpppQAPPApQQRPRGAPTPQPPPQAGptsmqlMPRAAPGQQGPTK 822
dnaA PRK14086
chromosomal replication initiator protein DnaA;
204-453 2.47e-08

chromosomal replication initiator protein DnaA;


Pssm-ID: 237605 [Multi-domain]  Cd Length: 617  Bit Score: 60.61  E-value: 2.47e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  204 PAKHPTQPQSPkPAVQQQGPVRPTVQQTESskqqqqpggpkqvqkPGHGQPADakqdQAKQPAQPRGPQKSQPQPSEPtk 283
Cdd:PRK14086    90 PSAGEPAPPPP-HARRTSEPELPRPGRRPY---------------EGYGGPRA----DDRPPGLPRQDQLPTARPAYP-- 147

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  284 piQQQTSAKPSSGPTKPSPQQPDSTKVT-SQTAPPTKPSSQQPGPakQPSQQPARQGAPvkpspqQTGPPKQPSQQPGPE 362
Cdd:PRK14086   148 --AYQQRPEPGAWPRAADDYGWQQQRLGfPPRAPYASPASYAPEQ--ERDREPYDAGRP------EYDQRRRDYDHPRPD 217

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  363 KPSAQQAGPAKQPPQPGSGKPPpqqtglvKQVPPQAGPTKPPSQTVGPTKPlaqqagptKPPGQQPGPEKPPQQTQAGAN 442
Cdd:PRK14086   218 WDRPRRDRTDRPEPPPGAGHVH-------RGGPGPPERDDAPVVPIRPSAP--------GPLAAQPAPAPGPGEPTARLN 282

                          250
                   ....*....|.
gi 2032737686  443 qptetaPKKTF 453
Cdd:PRK14086   283 ------PKYTF 287
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
288-452 4.43e-08

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 59.79  E-value: 4.43e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  288 QTSAKPSSGPTKPSPQQPdstkvtsqtAPPTKPSSQQPGPAKQPSQQPARQgapvkPSPQQTGPPKQPSQqpgpekpsAQ 367
Cdd:PRK14971   358 QLAQLTQKGDDASGGRGP---------KQHIKPVFTQPAAAPQPSAAAAAS-----PSPSQSSAAAQPSA--------PQ 415

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  368 QAGPAKQPPQPGSGKPPPQqtglVKQVPPQAGPTKPPSQTVGPTKPLAqqagPTKPPGQQPGPEKPPQQTQAGANQPTET 447
Cdd:PRK14971   416 SATQPAGTPPTVSVDPPAA----VPVNPPSTAPQAVRPAQFKEEKKIP----VSKVSSLGPSTLRPIQEKAEQATGNIKE 487


                   ....*
gi 2032737686  448 APKKT 452
Cdd:PRK14971   488 APTGT 492
PBP1 COG5180
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ...
 183-453 5.33e-08

PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification];


Pssm-ID: 444064 [Multi-domain]  Cd Length: 548  Bit Score: 59.31  E-value: 5.33e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  183 EAGRKQKVAPKEQGKPEEQRSPA-KHPTQPQSPKPAVQQQGPVRPT----VQQTESSKQQQQPGGPKQVQKPGHGQPADA 257
Cdd:COG5180    260 DAKERRRAAIGDTPAAEPPGLPVlEAGSEPQSDAPEAETARPIDVKgvasAPPATRPVRPPGGARDPGTPRPGQPTERPA 339

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  258 KQDQAKQPAQPRGPQKSQPQPSEPTKPIQQQTsAKPSSGPTKPSPQQPDSTKVTSQT------------APPTKPSSQQP 325
Cdd:COG5180    340 GVPEAASDAGQPPSAYPPAEEAVPGKPLEQGA-PRPGSSGGDGAPFQPPNGAPQPGLgrrgapgppmgaGDLVQAALDGG 418

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  326 GPAKQPSQQPARQGAPVKPSPQQTGPPKQPSQQPGPEKPSAQQAGPAKQPPQPGSGKPPPQQTGLVKQVPPQAgptkPPS 405
Cdd:COG5180    419 GRETASLGGAAGGAGQGPKADFVPGDAESVSGPAGLADQAGAAASTAMADFVAPVTDATPVDVADVLGVRPDA----ILG 494

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 2032737686  406 QTVGPTKPLAQQAGPTKPPGQqpgPEKPPqQTQAGANQPTETAPKKTF 453
Cdd:COG5180    495 GNVAPASGLDAETRIIEAEGA---PATED-FVAAELSELREAAEEKTG 538
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 247-470 6.07e-08

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 59.01  E-value: 6.07e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  247 QKPGHGQPADAKQDQAKQPAQPRGPQKSQPQPSEP-TKPIQQQTSAKPSSGPTKPSPQ--------QPDSTKVTSQTAPP 317
Cdd:NF033839   285 KEPGNKKPSAPKPGMQPSPQPEKKEVKPEPETPKPeVKPQLEKPKPEVKPQPEKPKPEvkpqletpKPEVKPQPEKPKPE 364

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  318 TKPSSQQPGPAKQPsqQPARQGAPVKPSPQQTGPPKQPSQQ-------PGPEKPSAqQAGPAKQPPQPGSGKPPPQQTGL 390
Cdd:NF033839   365 VKPQPEKPKPEVKP--QPETPKPEVKPQPEKPKPEVKPQPEkpkpevkPQPEKPKP-EVKPQPEKPKPEVKPQPEKPKPE 441

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  391 VKQVPPQAGPTKPPSQtvGPTKPLAQQAGPTKPPGQQPGPEKP------PQQTQAGANQPTETAPKKTFCPLCTTTELLL 464
Cdd:NF033839   442 VKPQPEKPKPEVKPQP--ETPKPEVKPQPEKPKPEVKPQPEKPkpdnskPQADDKKPSTPNNLSKDKQPSNQASTNEKAT 519


                   ....*.
gi 2032737686  465 HTPEKA 470
Cdd:NF033839   520 NKPKKS 525
C2_cPLA2 cd04036
C2 domain present in cytosolic PhosphoLipase A2 (cPLA2); A single copy of the C2 domain is ...
 4737-4843 6.12e-08

C2 domain present in cytosolic PhosphoLipase A2 (cPLA2); A single copy of the C2 domain is present in cPLA2 which releases arachidonic acid from membranes initiating the biosynthesis of potent inflammatory mediators such as prostaglandins, leukotrienes, and platelet-activating factor. 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. Members of this cd have a type-II topology.


Pssm-ID: 176001 [Multi-domain]  Cd Length: 119  Bit Score: 54.19  E-value: 6.12e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4737 NLIIHILQARNLAPRDNNGYSDPFVKVYLlPgrgqvmvvqNASAEyKRRTKYIQKSLNPEWNQTVIY------KNIsveq 4810
Cdd:cd04036      1 LLTVRVLRATNITKGDLLSTPDCYVELWL-P---------TASDE-KKRTKTIKNSINPVWNETFEFriqsqvKNV---- 65

                           90       100       110
                   ....*....|....*....|....*....|...
gi 2032737686 4811 lkkktLEVTVWDYDRFSSnDFLGEVLIELSSIS 4843
Cdd:cd04036     66 -----LELTVMDEDYVMD-DHLGTVLFDVSKLK 92
C2_Rab11-FIP_classI cd08682
C2 domain found in Rab11-family interacting proteins (FIP) class I; Rab GTPases recruit ...
 4742-4855 6.68e-08

C2 domain found in Rab11-family interacting proteins (FIP) class I; Rab GTPases recruit various effector proteins to organelles and vesicles. Rab11-family interacting proteins (FIPs) are involved in mediating the role of Rab11. FIPs can be divided into three classes: class I FIPs (Rip11a, Rip11b, RCP, and FIP2) which contain a C2 domain after N-terminus of the protein, class II FIPs (FIP3 and FIP4) which contain two EF-hands and a proline rich region, and class III FIPs (FIP1) which exhibits no homology to known protein domains. All FIP proteins contain a highly conserved, 20-amino acid motif at the C-terminus of the protein, known as Rab11/25 binding domain (RBD). Class I FIPs are thought to bind to endocytic membranes via their C2 domain, which interacts directly with phospholipids. Class II FIPs do not have any membrane binding domains leaving much to speculate about the mechanism involving FIP3 and FIP4 interactions with endocytic membranes. The members in this CD are class I FIPs. The exact function of the Rab11 and FIP interaction is unknown, but there is speculation that it involves the role of forming a targeting complex that recruits a group of proteins involved in membrane transport to organelles. 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.


Pssm-ID: 176064 [Multi-domain]  Cd Length: 126  Bit Score: 54.38  E-value: 6.68e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4742 ILQARNLAPRDNNGYSDPFVkvyllpgrgqvmVVQNASAEYkrRTKYIQKSLNPEWNQTVIYK--NISVEQLKKKTLEVT 4819
Cdd:cd08682      5 VLQARGLLCKGKSGTNDAYV------------IIQLGKEKY--STSVKEKTTSPVWKEECSFElpGLLSGNGNRATLQLT 70

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2032737686 4820 VWDYDRFSSNDFLGEVLIELSSISQLDNTPR--WYPLK 4855
Cdd:cd08682     71 VMHRNLLGLDKFLGQVSIPLNDLDEDKGRRRtrWFKLE 108
C2A_Copine cd04048
C2 domain first repeat in Copine; There are 2 copies of the C2 domain present in copine, a ...
 4742-4842 8.36e-08

C2 domain first repeat in Copine; There are 2 copies of the C2 domain present in copine, a protein involved in membrane trafficking, protein-protein interactions, and perhaps even cell division and growth. 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.


Pssm-ID: 176013 [Multi-domain]  Cd Length: 120  Bit Score: 53.73  E-value: 8.36e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4742 ILQARNLAPRDNNGYSDPFVKVYllpgrgqvmVVQNASAEYKR--RTKYIQKSLNPEWNQTVI--YkNISVEQlkkkTLE 4817
Cdd:cd04048      6 SISCRNLLDKDVLSKSDPFVVVY---------VKTGGSGQWVEigRTEVIKNNLNPDFVTTFTvdY-YFEEVQ----KLR 71

                           90       100
                   ....*....|....*....|....*....
gi 2032737686 4818 VTVWDYD----RFSSNDFLGEVLIELSSI 4842
Cdd:cd04048     72 FEVYDVDskskDLSDHDFLGEAECTLGEI 100
PDZ3_MAGI-1_3-like cd06733
PDZ domain 3 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ...
 4539-4615 1.14e-07

PDZ domain 3 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of MAGI1, 2, 3 (MAGI is also known as Membrane-associated guanylate kinase, WW and PDZ domain-containing protein) and related domains. MAGI proteins have been implicated in the control of cell migration and invasion through altering the activity of phosphatase and tensin homolog (PTEN) and modulating Akt signaling. Four MAGI proteins have been identified (MAGI1-3 and MAGIX). MAGI1-3 have 6 PDZ domains and bind to the C-terminus of PTEN via their PDZ2 domain. MAGIX has a single PDZ domain that is related to MAGI1-3 PDZ domain 5. Other binding partners for MAGI1 include JAM4, C-terminal tail of high risk HPV-18 E6, megalin, TRAF6, Kir4.1 (basolateral K+ channel subunit), and cadherin 23; for MAGI2, include DASM1, dendrin, axin, beta- and delta-catenin, neuroligin, hyperpolarization-activated cation channels, beta1-adrenergic receptors, NMDA receptor, and TARPs; and for MAGI3 includes LPA2. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MAGI family PDZ3 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as beta-strands A, -B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467215 [Multi-domain]  Cd Length: 85  Bit Score: 52.23  E-value: 1.14e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2032737686 4539 NGLGIRVVGGKEiPGSSGEIGAyiakILPGGNAEQTGKLVEGMQVLEWNGIPLTGKTYEEVQSIIIQ--QSGEAEICVR 4615
Cdd:cd06733     11 TGFGFRILGGTE-EGSQVSIGA----IVPGGAADLDGRLRTGDELLSVDGVNVVGASHHKVVDLMGNaaRNGQVNLTVR 84
C2B_Copine cd04047
C2 domain second repeat in Copine; There are 2 copies of the C2 domain present in copine, a ...
 4743-4835 1.34e-07

C2 domain second repeat in Copine; There are 2 copies of the C2 domain present in copine, a protein involved in membrane trafficking, protein-protein interactions, and perhaps even cell division and growth. 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.


Pssm-ID: 176012 [Multi-domain]  Cd Length: 110  Bit Score: 52.95  E-value: 1.34e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4743 LQARNLAPRDNNGYSDPFVKVYLLPGRGQ-VMVvqnasaeykRRTKYIQKSLNPEWNQTviykNISVEQL----KKKTLE 4817
Cdd:cd04047      7 FSGKKLDKKDFFGKSDPFLEISRQSEDGTwVLV---------YRTEVIKNTLNPVWKPF----TIPLQKLcngdYDRPIK 73

                           90
                   ....*....|....*...
gi 2032737686 4818 VTVWDYDRFSSNDFLGEV 4835
Cdd:cd04047     74 IEVYDYDSSGKHDLIGEF 91
PDZ_Lin-7-like cd06796
PDZ domain of protein Lin-7 and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), ...
 4540-4615 1.53e-07

PDZ domain of protein Lin-7 and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Lin-7 (also known as LIN-7 or LIN7), and related domains. Lin-7 targets and organize protein complexes to epithelial and synaptic plasma membranes. There are three mammalian Lin-7 homologs: Lin-7A (protein lin-7 homolog A, also known as mammalian lin-seven protein 1 (MALS-1), vertebrate lin-7 homolog 1 (Veli-1), tax interaction protein 33); Lin-7B (also known as MALS-2, Veli-2); and Lin-7C (also known as MALS-3, Veli-3). Lin-7 is involved in localization of the Let-23 growth factor receptor to the basolateral membrane of epithelial cells, in tight junction localization of insulin receptor substrate p53 (IRSp53), in retaining gamma-aminobutyric (GABA) transporter (BGT-1) at the basolateral surface of epithelial cells, and in regulating recruitment of neurotransmitter receptors to the postsynaptic density (PSD). The Lin7 PDZ domain binds Let-23, BGT and beta-catenin, and NMDA (N-methyl-D-aspartate) receptor NR2B. Lin-7 also binds to the PDZ binding motif located in the C-terminal tail of Rhotekin, an effector protein for small GTPase Rho. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Lin-7-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467258 [Multi-domain]  Cd Length: 86  Bit Score: 52.05  E-value: 1.53e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2032737686 4540 GLGIRVVGGKEipgSSGEIgaYIAKILPGGNAEQTGKLVEGMQVLEWNGIPLTGKTYEEVQSIIIQQSGEAEICVR 4615
Cdd:cd06796     13 GLGFNVMGGKE---QNSPI--YISRIIPGGVADRHGGLKRGDQLLSVNGVSVEGEHHEKAVELLKAAQGSVKLVVR 83
PDZ2_Par3-like cd23058
PDZ domain 2 of partitioning defective 3 (Par3), and related domains; PDZ (PSD-95 ...
 4539-4602 1.63e-07

PDZ domain 2 of partitioning defective 3 (Par3), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of Par3 (or PAR3 or Par-3, also known as Atypical PKC isotype-specific-interacting protein, ASIP, Drosophila Bazooka) and related domains. Par3 is a scaffold protein involved in organizing cell polarity across animals. Par3 binds numerous molecules both for its recruitment to one pole of the cell and for downstream contributions to polarized cell function. It regulates cell polarity by targeting the Par complex proteins Par6 and atypical protein kinase C (aPKC) to specific cortical sites. Physical interactions between Par3 and the Par complex include Par3 PDZ domain 1 binding to the Par6 PDZ domain, Par3 PDZ domain 1 and PDZ domain 3 binding the Par6's PDZ-binding motif, and an interaction with an undefined region of aPKC that requires both Par3 PDZ2 and PDZ3. The PDZ domains of Par3 have also been implicated as potential phosphoinositide signaling integrators, since its second PDZ domain binds to phosphoinositides, and the third PDZ interacts with phosphoinositide phosphatase PTEN. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Par3 family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467271 [Multi-domain]  Cd Length: 93  Bit Score: 52.26  E-value: 1.63e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2032737686 4539 NGLGIRVVGGKEIPGSSGEIgaYIAKILPGGNAEQTGKLVEGMQVLEWNGIPLTGKTYEEVQSI 4602
Cdd:cd23058     15 EGLGFSITSRDNPTGGSGPI--YIKNILPKGAAIQDGRLKAGDRLLEVNGVDVTGKTQEEVVSL 76
PDZ1_FRMPD2-like cd23071
PDZ domain 1 of FERM and PDZ domain-containing protein 2 (FRMPD2), and related domains; PDZ ...
 4524-4614 1.80e-07

PDZ domain 1 of FERM and PDZ domain-containing protein 2 (FRMPD2), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of FRMPD2 (also known as PDZ domain-containing protein 4, and related domains. FRMPD2 is localized in the basolateral membranes of polarized epithelial cells and is associated with tight junction formation and immune response; it contains 3 PDZ domains. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PTPN13 family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467284 [Multi-domain]  Cd Length: 92  Bit Score: 52.11  E-value: 1.80e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4524 RLKLLRDPKdhtvsgNGLGIRVVGGKEIpgSSGEIGAYIAKILPGGNAEQTGKLVEGMQVLEWNGIPLTGKTYEEVQSII 4603
Cdd:cd23071      4 CVTLKRDPK------RGFGFVIVGGENT--GKLDLGIFIASIIPGGPAEKDGRIKPGGRLISLNNISLEGVTFNTAVKIL 75

                           90
                   ....*....|.
gi 2032737686 4604 IQQSGEAEICV 4614
Cdd:cd23071     76 QNSPDEVELII 86
PDZ_MPP-like cd06726
PDZ domain of membrane palmitoylated proteins (MPPs), and related domains; PDZ (PSD-95 ...
 4540-4608 2.00e-07

PDZ domain of membrane palmitoylated proteins (MPPs), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MPP1-7 (also known as MAGUK p55 subfamily members 1-7), and related domains. MPPs comprise a subfamily of a larger group of multidomain proteins, namely, membrane-associated guanylate kinases (MAGUKs). MPPs form diverse protein complexes at the cell membranes, which are involved in a wide range of cellular processes, including establishing proper cell structure, polarity and cell adhesion. MPPs have only one PDZ domain. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MPP1-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467208 [Multi-domain]  Cd Length: 80  Bit Score: 51.50  E-value: 2.00e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2032737686 4540 GLGIRVVGGKEIpgssgeigayIAKILPGGNAEQTGKLVEGMQVLEWNGIPLTGKTYEEVQSIIIQQSG 4608
Cdd:cd06726     14 GATIKMEEDSVI----------VARILHGGMAHRSGLLHVGDEILEINGIPVSGKTVDELQKLLSSLSG 72
C2B_Synaptotagmin-7 cd08405
C2 domain second repeat present in Synaptotagmin 7; Synaptotagmin is a membrane-trafficking ...
 5114-5222 2.11e-07

C2 domain second repeat present in Synaptotagmin 7; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Synaptotagmin 7, a member of class 2 synaptotagmins, is located in presynaptic plasma membranes in neurons, dense-core vesicles in endocrine cells, and lysosomes in fibroblasts. It has been shown to play a role in regulation of Ca2+-dependent lysosomal exocytosis in fibroblasts and may also function as a vesicular Ca2+-sensor. It is distinguished from the other synaptotagmins by having over 12 splice forms. 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.


Pssm-ID: 176050 [Multi-domain]  Cd Length: 136  Bit Score: 53.19  E-value: 2.11e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 5114 LIVEILQCRNItyKFKSPDHLPDLYVKLYVvnISTQKRVIKKKTRVCRHDREPSFNETFRFSLsPAgHSLQ----ILLVS 5189
Cdd:cd08405     17 ITVNIIKARNL--KAMDINGTSDPYVKVWL--MYKDKRVEKKKTVIKKRTLNPVFNESFIFNI-PL-ERLRettlIITVM 90

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 2032737686 5190 NGGKFMKKTLIGEAYI-----------WLDKV-DLRKRIVNWHKL 5222
Cdd:cd08405     91 DKDRLSRNDLIGKIYLgwksgglelkhWKDMLsKPRQPVAQWHRL 135
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 251-453 2.58e-07

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 57.79  E-value: 2.58e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  251 HGQPADAKQDQ-------AKQPAQPRGPQKSQPQPS------------EPTKPIQQQTSAKPSSGPTkpspQQPDSTKVT 311
Cdd:PRK10263   682 HDVPVNAEDADaaaeaelARQFAQTQQQRYSGEQPAganpfslddfefSPMKALLDDGPHEPLFTPI----VEPVQQPQQ 757

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  312 SQTAPPTKPSSQQPGPAKQPSQQParqgapvkpspQQTGPPKQPSQQPGPEKPSAQQAGPAKQPPQPGSGKPPPQQTglV 391
Cdd:PRK10263   758 PVAPQQQYQQPQQPVAPQPQYQQP-----------QQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQP--V 824

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2032737686  392 KQVPPQAGPTKPPSQTVGPT--KPLAQQAGPTKPPGQqpgPEKPPQQTQAGANQPTETAPKKTF 453
Cdd:PRK10263   825 APQPQYQQPQQPVAPQPQDTllHPLLMRNGDSRPLHK---PTTPLPSLDLLTPPPSEVEPVDTF 885
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
268-400 2.71e-07

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 57.09  E-value: 2.71e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  268 PRGPQKS-QPQPSEPTKPIQQQTSAKPSsgptkpspQQPDSTKVTSQtaPPTKPSSQQPGPAkqPSQQPARQGAPVKPSP 346
Cdd:PRK14971   372 GRGPKQHiKPVFTQPAAAPQPSAAAAAS--------PSPSQSSAAAQ--PSAPQSATQPAGT--PPTVSVDPPAAVPVNP 439

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2032737686  347 QQTGPPKQPSQQPGPEKPSAQQAGPAKQPPQPGSGKPPPQQ-TGLVKQVPPQAGP 400
Cdd:PRK14971   440 PSTAPQAVRPAQFKEEKKIPVSKVSSLGPSTLRPIQEKAEQaTGNIKEAPTGTQK 494
C2A_Synaptotagmin-15-17 cd08390
C2A domain first repeat present in Synaptotagmins 15 and 17; Synaptotagmin is a ...
 5106-5222 3.22e-07

C2A domain first repeat present in Synaptotagmins 15 and 17; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. It is thought to be involved in the trafficking and exocytosis of secretory vesicles in non-neuronal tissues and is Ca2+ independent. Human synaptotagmin 15 has 2 alternatively spliced forms that encode proteins with different C-termini. The larger, SYT15a, contains a N-terminal TM region, a putative fatty-acylation site, and 2 tandem C terminal C2 domains. The smaller, SYT15b, lacks the C-terminal portion of the second C2 domain. Unlike most other synaptotagmins it is nearly absent in the brain and rather is found in the heart, lungs, skeletal muscle, and testis. Synaptotagmin 17 is located in the brain, kidney, and prostate and is thought to be a peripheral membrane protein. 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.


Pssm-ID: 176036 [Multi-domain]  Cd Length: 123  Bit Score: 52.26  E-value: 3.22e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 5106 EMKTDGEQLIVEILQCRNITYKFKSPDHlPDLYVKLYVvnISTQKRVikKKTRVCRHDREPSFNETFRFSLSPA---GHS 5182
Cdd:cd08390      8 QYDLEEEQLTVSLIKARNLPPRTKDVAH-CDPFVKVCL--LPDERRS--LQSKVKRKTQNPNFDETFVFQVSFKelqRRT 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 2032737686 5183 LQILLVSNgGKFMKKTLIGEAYIWLDKVDLRKRIVNWHKL 5222
Cdd:cd08390     83 LRLSVYDV-DRFSRHCIIGHVLFPLKDLDLVKGGVVWRDL 121
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 292-434 3.80e-07

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 56.65  E-value: 3.80e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  292 KPSSGPTKPSPqqpdstkvtSQTAPPTKPSSQQPGPAKQPSQQPARQGAPVKPSPQQTGPPKQPSQQPGPEKPSAQQAGP 371
Cdd:PRK14951   365 KPAAAAEAAAP---------AEKKTPARPEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVAAPAAAAPA 435

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2032737686  372 AKQPPQPGSGKPPPQQTglvkqvPPQAGPTKPPSQTVGPTKPLAQQAGPtkPPGQQPGPEKPP 434
Cdd:PRK14951   436 AAPAAAPAAVALAPAPP------AQAAPETVAIPVRVAPEPAVASAAPA--PAAAPAAARLTP 490
PHA03378 PHA03378
EBNA-3B; Provisional
 182-675 3.81e-07

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 57.00  E-value: 3.81e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  182 EEAGRKQKVAPKEQGKPeeqrspakhptQPQSPKPAVQQQgpvRPTVQQTESSKQQQQPGGPKQVQKPGHGqPADAKQDQ 261
Cdd:PHA03378   427 EEEHRKKKAARTEQPRA-----------TPHSQAPTVVLH---RPPTQPLEGPTGPLSVQAPLEPWQPLPH-PQVTPVIL 491

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  262 AKQPAQPRGPQKSQPQPSEPTKPIQQQtsaKPSSGPTKPSPQQPDSTK-----------VTSQTAPPTKPSSQQPGPAKQ 330
Cdd:PHA03378   492 HQPPAQGVQAHGSMLDLLEKDDEDMEQ---RVMATLLPPSPPQPRAGRrapcvytedldIESDEPASTEPVHDQLLPAPG 568

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  331 PSQ---QP-----ARQGAPVKPSPQQTGPPK-QPSQQPGPekPSAQQAGPAKQPPqpgsgkpppqqtglvKQVPPQAGPT 401
Cdd:PHA03378   569 LGPlqiQPltsptTSQLASSAPSYAQTPWPVpHPSQTPEP--PTTQSHIPETSAP---------------RQWPMPLRPI 631

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  402 kppsqtvgPTKPLAQQAGPTKPPGQqPGPEKPPQqTQAGANQPTETAPKKtfcplctttelLLHTPEKANYNTCtqchtv 481
Cdd:PHA03378   632 --------PMRPLRMQPITFNVLVF-PTPHQPPQ-VEITPYKPTWTQIGH-----------IPYQPSPTGANTM------ 684

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  482 vcslcgfnpnphiteisewlclncqmqrtlggdLAPGLGPGPQPLAPKQKTPI-PPSAKPSPQPQPVQKKDVTPKP---- 556
Cdd:PHA03378   685 ---------------------------------LPIQWAPGTMQPPPRAPTPMrPPAAPPGRAQRPAAATGRARPPaaap 731

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  557 ---DPSQAADSKRPPPQKKQT--QLPGSPPVKSKQPRAEP-TDISQQTDATPKSDQVKPTQAEDKQKQPSVqKPTADSVS 630
Cdd:PHA03378   732 graRPPAAAPGRARPPAAAPGraRPPAAAPGRARPPAAAPgAPTPQPPPQAPPAPQQRPRGAPTPQPPPQA-GPTSMQLM 810

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*..
gi 2032737686  631 TSVAAEQKQDLAGPRPPTQQKVTDSPKPELAKPS--QDTHPAGDKPD 675
Cdd:PHA03378   811 PRAAPGQQGPTKQILRQLLTGGVKRGRPSLKKPAalERQAAAGPTPS 857
PDZ1_MUPP1-like cd06689
PDZ domain 1 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ...
 4537-4614 4.06e-07

PDZ domain 1 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of MUPP1 and PATJ, and related domains. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, 9, and 13; consequently, MUPP1 PDZ7 and 8 align with PATJ PDZ6 and 7; and MUPP1 PDZ domains 10-12 align with PATJ PDZ domains 8-10. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467176 [Multi-domain]  Cd Length: 102  Bit Score: 51.09  E-value: 4.06e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2032737686 4537 SGNGLGIRVVGGKEipGSSGEIGAYIAKILPGGNAEQTGKLVEGMQVLEWNGIPL-TGKTYEEVQSIIIQQSGEAEICV 4614
Cdd:cd06689     24 ESGGLGFSVVGLKS--ENRGELGIFVQEIQPGSVAARDGRLKENDQILAINGQPLdQSISHQQAIAILQQAKGSVELVV 100
motB PRK05996
MotB family protein;
147-375 4.54e-07

MotB family protein;


Pssm-ID: 235665 [Multi-domain]  Cd Length: 423  Bit Score: 55.86  E-value: 4.54e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  147 MMPSFL-----SEANPLSAvTSVVNKFNPFDLiSDSDTSheEAGRKqKVAPKEQGKPEEQRSPAKhPTQPQSPKPAVQQQ 221
Cdd:PRK05996    43 MMAFFLvmwliNAANEETK-AAVASYFNPIKL-TDRKPS--EKGLK-DPVDGAEGEQKPGKSKFE-EDQRVEGSSAVTGD 116

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  222 GPVRPTVQQTESSKQQ----QQPGGPKQVQKPGHGQPADAKQD-QAKQPAQPRGPQKSQP--QPSEP---TKPIQQQTSA 291
Cdd:PRK05996   117 DTTRTSGDQTNYSEADlfrnPYAVLAEIAQEVGQQANVSAKGDgGAAQSGPATGADGGEAyrDPFDPdfwSKQVEVTTAG 196

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  292 KPSS-GPTKPSPQQPDSTKVTSQTAPPTKPSsqqpgPAKQPsQQPARQGAPVK--PSPQQTGPPKQPSQQPGPEKPSAQQ 368
Cdd:PRK05996   197 DLLPpGQAREQAQGAKSATAAPATVPQAAPL-----PQAQP-KKAATEEELIAdaKKAATGEPAANAAKAAKPEPMPDDQ 270


                   ....*..
gi 2032737686  369 AGPAKQP 375
Cdd:PRK05996   271 QKEAEQL 277
PDZ1_PTPN13_FRMPD2-like cd06694
PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13),FERM and PDZ ...
 4523-4609 5.37e-07

PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13),FERM and PDZ domain-containing protein 2 (FRMPD2), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of PTPN13 [also known as Fas-associated protein-tyrosine phosphatase 1 (FAP-1), protein-tyrosine phosphatase 1E (PTP-E1), and protein-tyrosine phosphatase (PTPL1)], FRMPD2 (also known as PDZ domain-containing protein 4; PDZ domain-containing protein 5C), and related domains. PTPN13 regulates negative apoptotic signaling and mediates phosphoinositide 3-kinase (PI3K) signaling. PTPN13 has five PDZ domains. Proteins known to interact with PTPN13 PDZ domains include: PLEKHA1 and PLEKHA2 via PTPN13-PDZ domain 1, Fas receptor and thyroid receptor-interacting protein 6 via PTPN13-PDZ domain 2, nerve growth factor receptor and protein kinase N2 via PTPN13-PDZ domain 3, PDZ and LIM domain 4 (PDLIM4) via PTPN13-PDZ domains 2 and 4, and brain calpain-2 via PTPN13-PDZ domains 3, 4 and 5. Calpain-2-mediated PTPN13 fragments may be involved in abnormal tau aggregation and increased risk for Alzheimer's disease. FRMPD2 is localized in the basolateral membranes of polarized epithelial cells and is associated with tight junction formation and immune response; it contains 3 PDZ domains. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PTPN13 family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467180 [Multi-domain]  Cd Length: 92  Bit Score: 50.47  E-value: 5.37e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4523 TRLKLLRDPKdhtvsgNGLGIRVVGGkEIPGSSgEIGAYIAKILPGGNAEQTGKLVEGMQVLEWNGIPLTGKTYEEVQSi 4602
Cdd:cd06694      3 VIVTLKKDPQ------KGLGFTIVGG-ENSGSL-DLGIFVKSIIPGGPADKDGRIKPGDRIIAINGQSLEGKTHHAAVE- 73


                   ....*..
gi 2032737686 4603 IIQQSGE 4609
Cdd:cd06694     74 IIQNAPD 80
PDZ3_Dlg1-2-4-like cd06795
PDZ domain 3 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg) ...
 4538-4598 5.43e-07

PDZ domain 3 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of Drosophila Dlg1, human Dlg1, 2, and 4 and related domains. Dlg1 (also known as synapse-associated protein Dlg197; SAP-97), Dlg2 (also known as channel-associated protein of synapse-110; postsynaptic density protein 93, PSD-93), Dlg4 (also known as postsynaptic density protein 95, PSD-95; synapse-associated protein 90, SAP-90) each have 3 PDZ domains and belong to the membrane-associated guanylate kinase family. Dlg1 regulates antigen receptor signaling and cell polarity in lymphocytes, B-cell proliferation and antibody production, and TGFalpha bioavailability; its PDZ3 domain binds pro-TGFalpha, and its PDZ2 domain binds the TACE metalloprotease responsible for cleaving pro-TGFalpha to a soluble form. Dlg2 is involved in N-methyl-D-aspartate (NMDA) receptor signaling, regulating surface expression of NMDA receptors in dorsal horn neurons of the spinal cord; it interacts with NMDA receptor subunits and with Shaker-type K+ channel subunits to cluster into a channel complex. The Dlg4 PDZ1 domain binds NMDA receptors, and its PDZ2 domain binds neuronal nitric oxide synthase (nNOS), forming a complex in neurons. The Drosophila Scribble complex (Scribble, Dlg, and lethal giant larvae) plays a role in apico-basal cell polarity, and in other forms of polarity, including regulation of the actin cytoskeleton, cell signaling and vesicular trafficking, and in tumor development; postsynaptic targeting of Drosophila DLG requires interactions mediated by the first two PDZ domains. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Dlg-like family PDZ3 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467257 [Multi-domain]  Cd Length: 91  Bit Score: 50.43  E-value: 5.43e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2032737686 4538 GNGLGIRVVGGKEipgssGEiGAYIAKILPGGNAEQTGKLVEGMQVLEWNGIPLTGKTYEE 4598
Cdd:cd06795     11 STGLGFNIVGGED-----GE-GIFISFILAGGPADLSGELRRGDQILSVNGVDLRNATHEQ 65
C2B_Synaptotagmin-15 cd08409
C2 domain second repeat present in Synaptotagmin 15; Synaptotagmin is a membrane-trafficking ...
 4722-4854 5.65e-07

C2 domain second repeat present in Synaptotagmin 15; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. It is thought to be involved in the trafficking and exocytosis of secretory vesicles in non-neuronal tissues and is Ca2+ independent. Human synaptotagmin 15 has 2 alternatively spliced forms that encode proteins with different C-termini. The larger, SYT15a, contains a N-terminal TM region, a putative fatty-acylation site, and 2 tandem C terminal C2 domains. The smaller, SYT15b, lacks the C-terminal portion of the second C2 domain. Unlike most other synaptotagmins it is nearly absent in the brain and rather is found in the heart, lungs, skeletal muscle, and testis. 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.


Pssm-ID: 176054 [Multi-domain]  Cd Length: 137  Bit Score: 51.95  E-value: 5.65e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4722 TGEIQLQINYDKHLGNLIIHILQARNLAPRDNNGySDPFVKVYLLPGRGQVMvvqnasaeyKRRTKYIQKSLNPEWNQTV 4801
Cdd:cd08409      1 LGDIQISLTYNPTLNRLTVVVLRARGLRQLDHAH-TSVYVKVSLMIHNKVVK---------TKKTEVVDGAASPSFNESF 70

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2032737686 4802 IYKnISVEQLKKKTLEVTVWDYDRFSSNDFLGEVLI---------ELSSISQLDNTP-----RWYPL 4854
Cdd:cd08409     71 SFK-VTSRQLDTASLSLSVMQSGGVRKSKLLGRVVLgpfmyargkELEHWNDMLSKPkelikRWHAL 136
PTZ00121 PTZ00121
MAEBL; Provisional
 1087-2019 5.77e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 56.69  E-value: 5.77e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1087 SQKEDPRIQQTKLTKTASYDRVLQEVQkEDEKLQEAKLAKTSSADKILHRVQkEDIKLQEAKLAKvpSADKILQGIQKED 1166
Cdd:PTZ00121  1075 SYKDFDFDAKEDNRADEATEEAFGKAE-EAKKTETGKAEEARKAEEAKKKAE-DARKAEEARKAE--DARKAEEARKAED 1150

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1167 PKLQQMKMaKALSADKIQLAAQREDTKLQE-----VKLPKAASVDKIQHGTQKDIKLQHEKIKKTSSVDKIQEEGQKEET 1241
Cdd:PTZ00121  1151 AKRVEIAR-KAEDARKAEEARKAEDAKKAEaarkaEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAV 1229

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1242 KlqrgklsKTPSADKIPATATADQKIPLSTLEEDKEtvlpEKSTPHPEDKKEEITAEIKdRVAEEKAEVEAPYKGLQAKE 1321
Cdd:PTZ00121  1230 K-------KAEEAKKDAEEAKKAEEERNNEEIRKFE----EARMAHFARRQAAIKAEEA-RKADELKKAEEKKKADEAKK 1297

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1322 EEDVKKEDlttgisQVVLKAEKAQEAEipvqtaplpgtdhveAVREKIEKEDDKSDTSssqqqkspqglsdtgyssdgis 1401
Cdd:PTZ00121  1298 AEEKKKAD------EAKKKAEEAKKAD---------------EAKKKAEEAKKKADAA---------------------- 1334

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1402 sslgeipshiptdeKDLLKETSKKDTISQESPPSPSDLAKLESTvlsilEAQASTLSDEKSAKSKEPSETYGEQTK--DQ 1479
Cdd:PTZ00121  1335 --------------KKKAEEAKKAAEAAKAEAEAAADEAEAAEE-----KAEAAEKKKEEAKKKADAAKKKAEEKKkaDE 1395

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1480 LKTKPlpvtpesyspdEEDLKAIKEGEGTiAEEGKGAASSQADYKEEHEGDDMSARRQQRYDSVEDSSESENSPVPRRKR 1559
Cdd:PTZ00121  1396 AKKKA-----------EEDKKKADELKKA-AAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAK 1463

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1560 RTSVGSSSSDEYKRDDSQGSGDEEdfirkqiLEMSADEDASGSDDdefIRNQLKEISAAESQKKEEVKSKA----KGTAG 1635
Cdd:PTZ00121  1464 KKAEEAKKADEAKKKAEEAKKADE-------AKKKAEEAKKKADE---AKKAAEAKKKADEAKKAEEAKKAdeakKAEEA 1533

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1636 KHRRMARKSSAGYDEDAGRRHswhddddETFDESPEPKYRESKSQDSEElavsgggglrrfKTIELNSTITNKYSEVSEP 1715
Cdd:PTZ00121  1534 KKADEAKKAEEKKKADELKKA-------EELKKAEEKKKAEEAKKAEED------------KNMALRKAEEAKKAEEARI 1594

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1716 QKGVLYFDEEPELEMESLTDSPEDRSRGEgssslhassftpgtsptsvssldedsdsspshkklggeskQQRKARHrthg 1795
Cdd:PTZ00121  1595 EEVMKLYEEEKKMKAEEAKKAEEAKIKAE----------------------------------------ELKKAEE---- 1630

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1796 pllptiedsseeeelreeeELLKEQEKQRELEQQQRKSSSKKSKKDKDELRAQRRRERPKtppsnlspiEDASPTEELRQ 1875
Cdd:PTZ00121  1631 -------------------EKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAE---------EDKKKAEEAKK 1682

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1876 AaemEELHRSSCSEYSPSIESEPEGFEISPEKIIEVQKVYKLPTAVSLYSPTDEQPtglpKEESQKTLKSAEEVYEEMMH 1955
Cdd:PTZ00121  1683 A---EEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEA----KKEAEEDKKKAEEAKKDEEE 1755

                          890       900       910       920       930       940
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2032737686 1956 KSKSFQMSNEKDEVFEKESLYGGMLIEDYIYEsliEDTYNGTIDTSLVMRQDESSEYIQQRGKE 2019
Cdd:PTZ00121  1756 KKKIAHLKKEEEKKAEEIRKEKEAVIEEELDE---EDEKRRMEVDKKIKDIFDNFANIIEGGKE 1816
PHA03418 PHA03418
hypothetical E4 protein; Provisional
 297-435 6.36e-07

hypothetical E4 protein; Provisional


Pssm-ID: 177646 [Multi-domain]  Cd Length: 230  Bit Score: 53.97  E-value: 6.36e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  297 PTKPSPQQPdstkvTSQTAPPTKPSSQ-QPGPAKQPSQQPARQGAPV---KPSPQQTGPPKQPSQQP-GPEKPSAQQAGP 371
Cdd:PHA03418    34 PLLPAPHHP-----NPQEDPDKNPSPPpDPPLTPRPPAQPNGHNKPPvtkQPGGEGTEEDHQAPLAAdADDDPRPGKRSK 108

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2032737686  372 AKQP-PQPGSGKPPPQQTGLvKQVPPQAGPTKPPSQTVGPTKPLAQQAGPTKPP---------GQQPGPEKPPQ 435
Cdd:PHA03418   109 ADEHgPAPGRAALAPFKLDL-DQDPLHGDPDPPPGATGGQGEEPPEGGEESQPPlgegegaveGHPPPLPPAPE 181
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 1030-1748 6.42e-07

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 56.13  E-value: 6.42e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1030 KPKEEPGVQKEAPKLQQGRLEKTLSADKIQQGIQKEDAKPKQGKLVKAPSADKIQHASQKEDPRIQQTKLTKTASYDRVL 1109
Cdd:pfam02463  216 KEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEE 295

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1110 QEVQKEDEKLQEAKlaktSSADKILHRVQKEDIKLQEAKLAKVPSADKILQGIQKEDPKLQQMKMAKALSADKIQLAAQR 1189
Cdd:pfam02463  296 EELKSELLKLERRK----VDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQL 371

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1190 EDTKLQEVKLpkaASVDKIQHGTQKDIKLQHEKIKKTSSVDKIQEEGQKEETKLQRGKlsktpSADKIPATATADQKIPL 1269
Cdd:pfam02463  372 EEELLAKKKL---ESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKK-----EELEILEEEEESIELKQ 443

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1270 STLEEDKETVLPEKStphpedKKEEITAEIKDRVAEEKAEVEAPYKGLQAKEEEDVKKEDLTT---------------GI 1334
Cdd:pfam02463  444 GKLTEEKEELEKQEL------KLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQkeskarsglkvllalIK 517

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1335 SQVVLK----AEKAQEAEIPVQTAPLPGTDHVEAVREKIEKEDDKSDTSSSQQQKSPQGLSDTGYSSDGISSSLGEI--- 1407
Cdd:pfam02463  518 DGVGGRiisaHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIavl 597

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1408 PSHIPTDEKDLLKETSKKDTISQESPPSPSDLAKLESTVLSILEAQASTLSDEKSAKSKEPSETYGEQTKDQLKTKPLPV 1487
Cdd:pfam02463  598 EIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLE 677

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1488 TPESYSPDEEDLKAIKEG---EGTIAEEGKGAASSQADYKEEHEGDDMSARRQQRydsvedsseseNSPVPRRKRRTSVG 1564
Cdd:pfam02463  678 IQELQEKAESELAKEEILrrqLEIKKKEQREKEELKKLKLEAEELLADRVQEAQD-----------KINEELKLLKQKID 746

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1565 SSSSDEYKRDDSQGSGDEEDFIRKQILEMSADEDAS------GSDDDEFIRNQLKEISAAESQKKEEVKSkakgtagKHR 1638
Cdd:pfam02463  747 EEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKteklkvEEEKEEKLKAQEEELRALEEELKEEAEL-------LEE 819

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1639 RMARKSSAGYDEDAGRRHSwHDDDDETFDESPEPKYRESKSQDSEELAVSggggLRRFKTIELNSTITNKYSEVSEPQKg 1718
Cdd:pfam02463  820 EQLLIEQEEKIKEEELEEL-ALELKEEQKLEKLAEEELERLEEEITKEEL----LQELLLKEEELEEQKLKDELESKEE- 893

                          730       740       750
                   ....*....|....*....|....*....|
gi 2032737686 1719 VLYFDEEPELEMESLTDSPEDRSRGEGSSS 1748
Cdd:pfam02463  894 KEKEEKKELEEESQKLNLLEEKENEIEERI 923
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 180-451 7.43e-07

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 55.95  E-value: 7.43e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  180 SHEEAGRKQKVAPKEQGKPEEQRSPAKHPtqpqSPKPAVQQQGPVRPTVQQTESSKQQQQPGGPKqVQKPGHGQPADAKQ 259
Cdd:PHA03307    76 GTEAPANESRSTPTWSLSTLAPASPAREG----SPTPPGPSSPDPPPPTPPPASPPPSPAPDLSE-MLRPVGSPGPPPAA 150

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  260 DQAKQPAQPRGPQKSQPQPSEPTKPIQ--QQTSAKPSSGP-----------TKPSPQQPDSTKVTSQTAPPTKP------ 320
Cdd:PHA03307   151 SPPAAGASPAAVASDAASSRQAALPLSspEETARAPSSPPaepppstppaaASPRPPRRSSPISASASSPAPAPgrsaad 230

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  321 ----------SSQQ-----------PGPAKQPSQQPARQGAPVKPSPQQTGPPKQPSQQPGPEKpsaqqaGPAKQPPQPG 379
Cdd:PHA03307   231 dagasssdssSSESsgcgwgpenecPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRER------SPSPSPSSPG 304

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  380 SGKPPPQQTGLVKQVPPQ--------AGPTKPPSQTVGPTKPLAQQAGPTKPPGQQPGPekPPQQTQAGANQPTETAPKK 451
Cdd:PHA03307   305 SGPAPSSPRASSSSSSSRessssstsSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPS--SPRKRPRPSRAPSSPAASA 382
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 523-737 8.20e-07

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 55.55  E-value: 8.20e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  523 PQPLAPKQKTPIPPSAKPSPQPQPVQKKdvTPKPDPSQAADSKRP-----------------PPQKKQTQL--------- 576
Cdd:NF033839   162 PQPENPEHQKPTTPAPDTKPSPQPEGKK--PSVPDINQEKEKAKLavatymskilddiqkhhLQKEKHRQIvalikelde 239

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  577 ---PGSPPVKSKQPRAEPTDISQQ--TDATPKSDQVKPTQAEDKQKQPSVQKPTA--DSVSTSVAAEQKQDLAGPRPPTQ 649
Cdd:NF033839   240 lkkQALSEIDNVNTKVEIENTVHKifADMDAVVTKFKKGLTQDTPKEPGNKKPSApkPGMQPSPQPEKKEVKPEPETPKP 319

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  650 QKvtdSPKPELAKPSQDTHPAGDKPDSKPVPQVSRQKSDPKF-ASQPGARPDAKAQKP-IDPTQTKDDPKKLPTKPAPKP 727
Cdd:NF033839   320 EV---KPQLEKPKPEVKPQPEKPKPEVKPQLETPKPEVKPQPeKPKPEVKPQPEKPKPeVKPQPETPKPEVKPQPEKPKP 396

                          250
                   ....*....|
gi 2032737686  728 DTKPAPKGPQ 737
Cdd:NF033839   397 EVKPQPEKPK 406
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 188-368 9.69e-07

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 55.40  E-value: 9.69e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  188 QKVAPKEQGKPEEQRSPAKHP-TQPQSPKPAVQQQGPVRPTVQQtesskqqqqpgGPKQVQKPGHGQPADAKQDQAKQPA 266
Cdd:pfam09606  303 QNNYQQQQTRQQQQQQGGNHPaAHQQQMNQSVGQGGQVVALGGL-----------NHLETWNPGNFGGLGANPMQRGQPG 371

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  267 QPRGPQksqPQPSEPTKPIQQQTSAKPSSGPTKPSPQQPDSTKVTSQTAPPTKPSSQQPGPAKQPSQQPARQGAPVKPSP 346
Cdd:pfam09606  372 MMSSPS---PVPGQQVRQVTPNQFMRQSPQPSVPSPQGPGSQPPQSHPGGMIPSPALIPSPSPQMSQQPAQQRTIGQDSP 448

                          170       180
                   ....*....|....*....|..
gi 2032737686  347 qqTGPPKQPSQQPGPEKPSAQQ 368
Cdd:pfam09606  449 --GGSLNTPGQSAVNSPLNPQE 468
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 47-439 1.19e-06

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 55.56  E-value: 1.19e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686   47 QLSEEERRQIAAVMSRAQGLPRGNLAGAEPPPMQRHPELDTSRHPRQPGKPPDPGPPGLSKSRtvdvlktEQRAPGRSPs 126
Cdd:PHA03307    42 QLVSDSAELAAVTVVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREG-------SPTPPGPSS- 113

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  127 tlslresksrtdfkEDQKPSMMPSFLSEANPlsavtsvvnkfnPFDLISDSDTSHEEAGRKQKVAPKEQGKPEEQRSPAK 206
Cdd:PHA03307   114 --------------PDPPPPTPPPASPPPSP------------APDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAA 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  207 HPTQPQSPKPAVQQQ-------GPVRPTVQQTESSKQQQQPGGPKQVQKPGHGQPADAKQDQAKQPAQPRGPQKSQPQPS 279
Cdd:PHA03307   168 SSRQAALPLSSPEETarapsspPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGC 247

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  280 EpTKPIQQQTSAKPSSGPTKPSPQQPDSTKVTSQTAPPTKPSSqqPGPAKQPSQQPARQGAPVKPSPQQTGPPKQPSQQP 359
Cdd:PHA03307   248 G-WGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSS--SPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRES 324

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  360 GPEKPSAQQAGPAKQPPQPGsgkPPPQqtglvkqvpPQAGPTKPPSQTVGPTKPLAQQAGPTKPPGQQPGPEKPPQQTQA 439
Cdd:PHA03307   325 SSSSTSSSSESSRGAAVSPG---PSPS---------RSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRARA 392
C2A_SLP-3 cd08392
C2 domain first repeat present in Synaptotagmin-like protein 3; All Slp members basically ...
 5096-5222 1.19e-06

C2 domain first repeat present in Synaptotagmin-like protein 3; 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. SHD of Slp (except for the Slp4-SHD) function as a specific Rab27A/B-binding domain. In addition to Slp, rabphilin, Noc2, and Munc13-4 also function as Rab27-binding proteins. Little is known about the expression or localization of Slp3. The C2A domain of Slp3 is Ca2+ dependent. It has been demonstrated that Slp3 promotes dense-core vesicle exocytosis. 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.


Pssm-ID: 176038 [Multi-domain]  Cd Length: 128  Bit Score: 50.60  E-value: 1.19e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 5096 MGEIKIALKKEMKTdgEQLIVEILQCRNITY-KFKSPDHLPdlYVKLYVvnISTQKRVIKKKTRVCRHDREPSFNETFRF 5174
Cdd:cd08392      1 TGEIEFALHYNFRT--SCLEITIKACRNLAYgDEKKKKCHP--YVKVCL--LPDKSHNSKRKTAVKKGTVNPVFNETLKY 74

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2032737686 5175 SLSPAGHSLQILLVS--NGGKFMKKTLIGEAYIWLDKVDLRKRIV---NWHKL 5222
Cdd:cd08392     75 VVEADLLSSRQLQVSvwHSRTLKRRVFLGEVLIPLADWDFEDTDSqrfLWYPL 127
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
247-444 1.30e-06

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 54.88  E-value: 1.30e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  247 QKPGHGQPADAKQDQAKQPAQPRG------PQKSQPQPSEPTKPIQQQTSAKPSSGPTKPSPQqPDSTKVTSQTAPPTKP 320
Cdd:PRK12323   367 QSGGGAGPATAAAAPVAQPAPAAAapaaaaPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPA-PEALAAARQASARGPG 445

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  321 SSQQPGPAkqPSQQPARQGAPVKPSPQqtGPPKQPSQQPGPEKPSAQQAgPAKQPPQPGSGKPP-PQQTGLVKQVPPQAG 399
Cdd:PRK12323   446 GAPAPAPA--PAAAPAAAARPAAAGPR--PVAAAAAAAPARAAPAAAPA-PADDDPPPWEELPPeFASPAPAQPDAAPAG 520

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 2032737686  400 PTKPPSQTVGPTKPLAQQAGPTKPPGQQPGPEKPPQQTQAGANQP 444
Cdd:PRK12323   521 WVAESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRP 565
PHA03377 PHA03377
EBNA-3C; Provisional
 186-453 1.64e-06

EBNA-3C; Provisional


Pssm-ID: 177614 [Multi-domain]  Cd Length: 1000  Bit Score: 55.06  E-value: 1.64e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  186 RKQKVAPKEQGKPEEQRSPAkhpTQPQSPKPAVQQQGPVRPTVQQtesskqqqqpggpkqvqkpGHGQPADAKQDQAKQP 265
Cdd:PHA03377   654 RAGRDGSGIQQEPSSRRQPA---TQSTPPRPSWLPSVFVLPSVDA-------------------GRAQPSEESHLSSMSP 711

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  266 AQPRGpQKSQPQPSEPTKPIQqqTSAKPSSGPtKPSPQQPDSTKVTSQTAPPTKPSSQQPGPAKQP---SQQPARQGAPV 342
Cdd:PHA03377   712 TQPIS-HEEQPRYEDPDDPLD--LSLHPDQAP-PPSHQAPYSGHEEPQAQQAPYPGYWEPRPPQAPylgYQEPQAQGVQV 787

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  343 KPSPQQTGPPKQPSQQPGPEKPSAQQA-----GPAKQPPQPGSGKPPPQQTGL-------VKQVPPQAGPTKPPS--QTV 408
Cdd:PHA03377   788 SSYPGYAGPWGLRAQHPRYRHSWAYWSqypghGHPQGPWAPRPPHLPPQWDGSaghgqdqVSQFPHLQSETGPPRlqLSQ 867

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2032737686  409 GPTKPLAQ--------------QAGPTKP-PGQQPGPEKPPQQTQA-GANQPTETAPKKTF 453
Cdd:PHA03377   868 VPQLPYSQtlvsssapswsspqPRAPIRPiPTRFPPPPMPLQDSMAvGCDSSGTACPSMPF 928
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
198-417 1.75e-06

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 54.50  E-value: 1.75e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  198 PEEQRSPAKHPTQPQSPKPAVQQQGPVRPTVQqtesskqqqQPGGPKQVQKPGHGQPADAKQDQAKQPAQPRGPQKSQPQ 277
Cdd:PRK12323   381 PVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAA---------AAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPA 451

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  278 PSEPTKPIqqqtsakPSSGPTKPSPQQPDSTkvtsqTAPPTKPSSQQPGPAKQPSQQPARQGAPVK---PSPQQTGP--- 351
Cdd:PRK12323   452 PAPAAAPA-------AAARPAAAGPRPVAAA-----AAAAPARAAPAAAPAPADDDPPPWEELPPEfasPAPAQPDAapa 519

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2032737686  352 --PKQPSQQPGPEKPSAQQAGPAKQPPQPGSGKPPPQQTGLVKQVPPQAGPTKPPSQTVG---------PTKPLAQQ 417
Cdd:PRK12323   520 gwVAESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRASASGLPDMFDGdwpalaarlPVRGLAQQ 596
C2_PSD cd04039
C2 domain present in Phosphatidylserine decarboxylase (PSD); PSD is involved in the ...
 4736-4849 1.78e-06

C2 domain present in Phosphatidylserine decarboxylase (PSD); PSD is involved in the biosynthesis of aminophospholipid by converting phosphatidylserine (PtdSer) to phosphatidylethanolamine (PtdEtn). There is a single C2 domain present and it is thought to confer PtdSer binding motif that is common to PKC and synaptotagmin. 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.


Pssm-ID: 176004 [Multi-domain]  Cd Length: 108  Bit Score: 49.56  E-value: 1.78e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4736 GNLIIHILQARNLAPRDN---NGYS-DPFV------KVYllpgrgqvmvvqnasaeykrRTKYIQKSLNPEWNQTVIYKN 4805
Cdd:cd04039      1 GVVFMEIKSITDLPPLKNmtrTGFDmDPFViisfgrRVF--------------------RTSWRRHTLNPVFNERLAFEV 60

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2032737686 4806 ISVEqlKKKTLEVTVWDYDRFSSNDFLGEVLIELSSISQLDNTP 4849
Cdd:cd04039     61 YPHE--KNFDIQFKVLDKDKFSFNDYVATGSLSVQELLNAAPQP 102
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 183-448 1.92e-06

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 54.61  E-value: 1.92e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  183 EAGRKQKVAPKEQGKPEEQRSPAKHPTQPQ----SPKPAVQQQGPVRPTVQQTESSKQQQQPGGPKQVQKPGHGQPADAK 258
Cdd:PRK07764   371 ERGLLARLERLERRLGVAGGAGAPAAAAPSaaaaAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPA 450

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  259 QDQAKQPAQPRGPQKSQPQPSEPTKPIQQQTSAKPSSGPTKPSPQQPDST------------------------------ 308
Cdd:PRK07764   451 GGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPaapagaddaatlrerwpeilaavpkrsrkt 530

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  309 ----------------------------------------------------KVTSQTAPPTKPSSQQPGPAKQPSQQPA 336
Cdd:PRK07764   531 waillpeatvlgvrgdtlvlgfstgglarrfaspgnaevlvtalaeelggdwQVEAVVGPAPGAAGGEGPPAPASSGPPE 610

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  337 RQGAPVKPS-PQQTGPPKQPSQQPGPEKPSAQQAGPAKQPPQPGSGKPPPQQTGLVKQVPPQAGPTKPPSQTVGPTK--P 413
Cdd:PRK07764   611 EAARPAAPAaPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPaaP 690

                          330       340       350
                   ....*....|....*....|....*....|....*
gi 2032737686  414 LAQQAGPTKPPGQQPGPEKPPQQTQAGANQPTETA 448
Cdd:PRK07764   691 AAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAA 725
C2_PLC_like cd00275
C2 domain present in Phosphoinositide-specific phospholipases C (PLC); PLCs are involved in ...
 4737-4844 1.99e-06

C2 domain present in Phosphoinositide-specific phospholipases C (PLC); PLCs are involved in the hydrolysis of phosphatidylinositol-4,5-bisphosphate (PIP2) to d-myo-inositol-1,4,5-trisphosphate (1,4,5-IP3) and sn-1,2-diacylglycerol (DAG). 1,4,5-IP3 and DAG are second messengers in eukaryotic signal transduction cascades. PLC is composed of a N-terminal PH domain followed by a series of EF hands, a catalytic TIM barrel and a C-terminal C2 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. Members here have a type-II topology.


Pssm-ID: 175974 [Multi-domain]  Cd Length: 128  Bit Score: 50.23  E-value: 1.99e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4737 NLIIHILQARNL--APRDNNGYSDPFVKVYllpgrgqvMVVQNASAEYKRRTKYIQK-SLNPEWNQT----VIYKNISVe 4809
Cdd:cd00275      3 TLTIKIISGQQLpkPKGDKGSIVDPYVEVE--------IHGLPADDSAKFKTKVVKNnGFNPVWNETfefdVTVPELAF- 73

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2032737686 4810 qlkkktLEVTVWDYDRFsSNDFLGEVLIELSSISQ 4844
Cdd:cd00275     74 ------LRFVVYDEDSG-DDDFLGQACLPLDSLRQ 101
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 170-446 2.00e-06

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 54.79  E-value: 2.00e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  170 PFDLISDSDTSHEEAGRKQKVAPKEQGKPEEQRSPAKHPTQPQSPKPAVQQQ-------GPVRPTVQQTESSKQQQQPGG 242
Cdd:PHA03307   131 APDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETarapsspPAEPPPSTPPAAASPRPPRRS 210

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  243 PKQVQKPGHGQPADAKQDQAKQPAQPRGPQKSQPQPSEpTKPIQQQTSAKPSSGPTKPSPQQPDSTKVTSQTAPPTKPSS 322
Cdd:PHA03307   211 SPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCG-WGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSS 289

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  323 qqPGPAKQPSQQPARQGAPVKPSPQQTGPPKQPSQQPGPEKPSAQQAGPAKQPPQPGsgkPPPQQTGLVKQVPPQAGPTK 402
Cdd:PHA03307   290 --SPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPG---PSPSRSPSPSRPPPPADPSS 364

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 2032737686  403 PPSQTVGPTKPLAQQAGPTKPPGQQPGPEKPPQQTQAGANQPTE 446
Cdd:PHA03307   365 PRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATGRFP 408
C2B_RasA3 cd04010
C2 domain second repeat present in RAS p21 protein activator 3 (RasA3); RasA3 are members of ...
 4738-4880 2.01e-06

C2 domain second repeat present in RAS p21 protein activator 3 (RasA3); RasA3 are members of GTPase activating protein 1 (GAP1), a Ras-specific GAP, which suppresses Ras function by enhancing the GTPase activity of Ras proteins resulting in the inactive GDP-bound form of Ras. In this way it can control cellular proliferation and differentiation. RasA3 contains an N-terminal C2 domain, a Ras-GAP domain, a plextrin homology (PH)-like domain, and a Bruton's Tyrosine Kinase (BTK) zinc binding 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. This cd contains the second C2 repeat, C2B, and has a type-I topology.


Pssm-ID: 175977 [Multi-domain]  Cd Length: 148  Bit Score: 50.47  E-value: 2.01e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4738 LIIHILQARNLAPrdNNGYSDPFVKVYLL-PGRGQVMvvqnasaeykRRTKYIQKSLNPEWNQTVI------------YK 4804
Cdd:cd04010      2 LSVRVIECSDLAL--KNGTCDPYASVTLIySNKKQDT----------KRTKVKKKTNNPQFDEAFYfdvtidsspekkQF 69

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2032737686 4805 NISVEQLKKKTLEVTVWDYDRFSSNDFLGEVLIELSSISQLDNTPR-WYPLKEQSEnidhgkSHSEKSSQQSPKPSV 4880
Cdd:cd04010     70 EMPEEDAEKLELRVDLWHASMGGGDVFLGEVRIPLRGLDLQAGSHQaWYFLQPREE------KSTPPGTRSSKDNSL 140
PDZ2_MUPP1-like cd06667
PDZ domain 2 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ...
 4538-4608 2.03e-06

PDZ domain 2 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) and similar domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of MUPP1 and PATJ, and related domains. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, 9, and 13; consequently, MUPP1 PDZ7 and 8 align with PATJ PDZ6 and 7; and MUPP1 PDZ domains 10-12 align with PATJ PDZ domains 8-10. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F


Pssm-ID: 467155 [Multi-domain]  Cd Length: 80  Bit Score: 48.43  E-value: 2.03e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2032737686 4538 GNGLGIRVVGGKeipgSSGEIgayIAKILPGGNAEQTGKLVEGMQVLEWNGIPLTGKTYEEVQSiIIQQSG 4608
Cdd:cd06667      9 GSGLGFGIVGGK----STGVV---VKTILPGGVADRDGRLRSGDHILQIGDTNLRGMGSEQVAQ-VLRQCG 71
PHA03247 PHA03247
large tegument protein UL36; Provisional
 202-439 2.07e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 54.94  E-value: 2.07e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  202 RSPAKHPTQPqsPKPAVQQQGpvRPTVQQTESSKQQQQPGGPKQVQKPGHGQPADakQDQAKQPAQPRGPQKSQPQPSEP 281
Cdd:PHA03247  2869 RSPAAKPAAP--ARPPVRRLA--RPAVSRSTESFALPPDQPERPPQPQAPPPPQP--QPQPPPPPQPQPPPPPPPRPQPP 2942

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  282 TKPiQQQTSAKPSSGPTKPSPQQ----PDSTKVTSQTAPPTKPSSQQPGPAKQPSQQPARQGAPVKPSP----QQTGPP- 352
Cdd:PHA03247  2943 LAP-TTDPAGAGEPSGAVPQPWLgalvPGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLSRVSSWASSlalhEETDPPp 3021

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  353 ---KQPSQQPGPEKPSAQQAGPAKQPPQPGSGKPPPQqtglvkqvPPQagPTKPPSQtvgPTKPLAQQAGPTKPPGQQPG 429
Cdd:PHA03247  3022 vslKQTLWPPDDTEDSDADSLFDSDSERSDLEALDPL--------PPE--PHDPFAH---EPDPATPEAGARESPSSQFG 3088

                          250
                   ....*....|
gi 2032737686  430 PekPPQQTQA 439
Cdd:PHA03247  3089 P--PPLSANA 3096
PDZ12_MUPP1-like cd06675
PDZ domain 12 of multi-PDZ-domain protein 1 (MUPP1), PDZ domain 10 of protein-associated tight ...
 4527-4614 2.44e-06

PDZ domain 12 of multi-PDZ-domain protein 1 (MUPP1), PDZ domain 10 of protein-associated tight junction (PATJ, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 12 of MUPP1, PDZ domain 10 of PATJ, and related domains. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, 9, and 13; consequently, MUPP1 PDZ7 and 8 align with PATJ PDZ6 and 7; and MUPP1 PDZ domains 10-12 align with PATJ PDZ domains 8-10. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like PDZ12 family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F


Pssm-ID: 467163 [Multi-domain]  Cd Length: 86  Bit Score: 48.51  E-value: 2.44e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4527 LLRDPKDhtvsgnGLGIRVVGGKeipGSS-GEIGAYIAKILPGGNAEQTGKLVEGMQVLEWNGIPLTGKTYEEVQSIIIQ 4605
Cdd:cd06675      5 IKRGPQD------SLGISIAGGV---GSPlGDVPVFIAMIQPNGVAAQTGKLKVGDRIVSINGQSTDGLTHSEAVNLLKN 75


                   ....*....
gi 2032737686 4606 QSGEAEICV 4614
Cdd:cd06675     76 ASGTIILQV 84
PDZ4_Scribble-like cd06701
PDZ domain 4 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 4538-4599 2.69e-06

PDZ domain 4 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 4 of Drosophila Scribble (also known as LAP4), human Scribble homolog (also known as hScrib, LAP4, CriB1, ScrB1 and Vartul), and related domains. They belong to the LAP family, which describes proteins that contain either one or four PDZ domains and 16 LRRs (leucine-rich repeats) and function in controlling cell shape, size and subcellular protein localization. In Drosophila, the Scribble complex, comprising Scribble, discs large, and lethal giant larvae, plays a role in apico-basal cell polarity, in other forms of polarity, including regulation of the actin cytoskeleton, cell signaling and vesicular trafficking, and in tumor development. Mammalian Scribble is important in many aspects of cancer development. Scribble and its homologs can be downregulated or overexpressed in cancer; they have a role in cancer beyond their function in loss of cell polarity. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Scribble-like family PDZ4 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467185 [Multi-domain]  Cd Length: 98  Bit Score: 48.76  E-value: 2.69e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2032737686 4538 GNGLGIRVVGGkeIPGSSG------EIGAYIAKILPGGNAEQTGKLVEGMQVLEWNGIPLTGKTYEEV 4599
Cdd:cd06701     14 GEKLGISIRGG--AKGHAGnpldptDEGIFISKINPDGAAARDGRLKVGQRILEVNGQSLLGATHQEA 79
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
254-429 2.69e-06

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 54.11  E-value: 2.69e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  254 PADAKQDQAKQPAQPRGPQKSQPQPsEPTKPIQQQTSAKPssGPTKPSPQQPDSTKVtSQTAPPTKPSSQQPGPAKQP-- 331
Cdd:PRK12323   406 PAAAPAAAAAARAVAAAPARRSPAP-EALAAARQASARGP--GGAPAPAPAPAAAPA-AAARPAAAGPRPVAAAAAAApa 481

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  332 SQQPARQGAPV--KPSPQQTGPPKQPSqqPGPEKPSAQQAGPAKQP-PQPGSGKPPPQQTGLVKQVPPQAGPTK--PPSQ 406
Cdd:PRK12323   482 RAAPAAAPAPAddDPPPWEELPPEFAS--PAPAQPDAAPAGWVAESiPDPATADPDDAFETLAPAPAAAPAPRAaaATEP 559

                          170       180
                   ....*....|....*....|....
gi 2032737686  407 TVGPTKPLAQQAG-PTKPPGQQPG 429
Cdd:PRK12323   560 VVAPRPPRASASGlPDMFDGDWPA 583
PDZ_SYNJ2BP-like cd06709
PDZ domain of synaptojanin-2-binding protein (SYNJ2BP), and related domains; PDZ (PSD-95 ...
 4538-4599 2.74e-06

PDZ domain of synaptojanin-2-binding protein (SYNJ2BP), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of SYNJ2BP, and related domains. SYNJ2BP (also known as mitochondrial outer membrane protein 25, OMP25) regulates endocytosis of activin type 2 receptor kinases through the Ral/RALBP1-dependent pathway and may be involved in suppression of activin-induced signal transduction. Binding partners of the SYNJ2BP PDZ domain include activin type II receptors (ActR-II), and SYNJ2. SYNJ2BP interacts with the PDZ binding motif of the Notch Delta-like ligand 1 (DLL1) and DLL4, promoting Delta-Notch signaling, and inhibiting sprouting angiogenesis. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This SYNJ2BP-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467193 [Multi-domain]  Cd Length: 86  Bit Score: 48.44  E-value: 2.74e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2032737686 4538 GNGLGIRVVGGKEIPGSSGEIGAYIAKILPGGNAEQTGKLVEGMQVLEWNGIPLTGKTYEEV 4599
Cdd:cd06709      9 PSGLGFNIVGGTDQPYIPNDSGIYVAKIKEDGAAAIDGRLQEGDKILEINGQSLENLTHQDA 70
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 167-316 2.91e-06

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 54.32  E-value: 2.91e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  167 KFNPFDLISDsDTSHEEAgRKQKVAPKEQgkPEEQRSPAKHPTQPQSPKPAVQQ-QGPVRPTVQQTESSKQQQQPGGPKQ 245
Cdd:PRK10263   728 EFSPMKALLD-DGPHEPL-FTPIVEPVQQ--PQQPVAPQQQYQQPQQPVAPQPQyQQPQQPVAPQPQYQQPQQPVAPQPQ 803

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  246 VQKPghgQPADAKQDQAKQPAQPRGPQKSQPQPSEPTKPIQQQT----------SAKPSSGPTKPSPQQPDSTKVTSQTA 315
Cdd:PRK10263   804 YQQP---QQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQDTllhpllmrngDSRPLHKPTTPLPSLDLLTPPPSEVE 880


                   .
gi 2032737686  316 P 316
Cdd:PRK10263   881 P 881
PHA03269 PHA03269
envelope glycoprotein C; Provisional
 285-430 3.17e-06

envelope glycoprotein C; Provisional


Pssm-ID: 165527 [Multi-domain]  Cd Length: 566  Bit Score: 53.58  E-value: 3.17e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  285 IQQQTSAKPSSGPTkPSPQQPDSTKVTSQTAPPTKPSSQQPGPAKQPSQQPARqgapvKPSPQQtGPPKQPSQQPGPEKP 364
Cdd:PHA03269    15 INLIIANLNTNIPI-PELHTSAATQKPDPAPAPHQAASRAPDPAVAPTSAASR-----KPDLAQ-APTPAASEKFDPAPA 87

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  365 SAQQAG----PAKQPPQPGSGKPPPqqtglvkQVPPQAGPTKPPSQTVGPTKPLAQQAGPTKPPGQQPGP 430
Cdd:PHA03269    88 PHQAASrapdPAVAPQLAAAPKPDA-------AEAFTSAAQAHEAPADAGTSAASKKPDPAAHTQHSPPP 150
Androgen_recep pfam02166
Androgen receptor;
300-424 3.18e-06

Androgen receptor;


Pssm-ID: 426632 [Multi-domain]  Cd Length: 501  Bit Score: 53.39  E-value: 3.18e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  300 PSPQQPDSTkvtSQTAPPTKPSSQQPGPAKQPSQQPARQgapvKPSPQQTGPPKQPSQQPGPEKPSAQQAGPA------- 372
Cdd:pfam02166   32 PGPRHPEAA---GGAAPPGARLQHQQQQQQQVPQQPQQQ----ESSPRQPQASVQPQQAGDDGSPPAHNRGPAgylaled 104

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2032737686  373 KQPPQPGSGKPPPQQTglvkqvpPQAGPTKPPSQTVGPTKPLAQQAGPTKPP 424
Cdd:pfam02166  105 DEQPQPSQAQPAAECC-------PENGCVPEPGAAAAAGKGLPQQAVAPAAP 149
PDZ_MPP3-MPP4-MPP7-like cd06799
PDZ domain of membrane palmitoylated proteins 3 (MPP3), MPP4, and MPP7, and related domains; ...
 4543-4608 3.33e-06

PDZ domain of membrane palmitoylated proteins 3 (MPP3), MPP4, and MPP7, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MPP3, MPP4, and MPP7, and related domains. MPP3 (also known as MAGUK p55 subfamily member 3, erythrocyte membrane protein p55, or EMP55), MPP4 (also known as MAGUK p55 subfamily member 4 or Discs large homolog 6), and MPP7 (also known as MAGUK p55 subfamily member 7) are membrane-associated guanylate kinase (MAGUK)-like proteins. MPP3 is part of a cell adhesion protein complex including tumor suppressor CADM1 and actin-binding protein 4.1B. Participation in the Crumbs cell polarity complex has also been demonstrated for MPP7 in epithelial cells, and for MPP3 and MPP4 in the retina. MPP4 is needed for proper localization of plasma membrane calcium ATPases and maintenance of calcium homeostasis at the rod photoreceptor synaptic terminals. Binding partners of the MPP3 PDZ domain include nectin-3, serotonin 5-hydroxytryptamine, 5-HT(2C) receptor, and a cell adhesion protein, TSLC1 (tumor suppressor in lung cancer 1); fragments of MPP4 having the PDZ domain bind CRB (PDZ-SH3-GUK) and GABA transporter GAT1 (PDZ-SH3). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MPP1-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467260 [Multi-domain]  Cd Length: 81  Bit Score: 48.01  E-value: 3.33e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2032737686 4543 IRVVGGKEIPGS-------SGEIgaYIAKILPGGNAEQTGKLVEGMQVLEWNGIPLTGKTYEEVQSIIIQQSG 4608
Cdd:cd06799      3 VRLVKNNEPLGAtikrdekTGAI--VVARIMRGGAADRSGLIHVGDELREVNGISVEGKDPEEVIQILANSQG 73
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
 321-450 3.39e-06

Proline-rich protein; This family includes several eukaryotic proline-rich proteins.


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 50.42  E-value: 3.39e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  321 SSQQPGPAKQPSQQPARQGAPVKPSPQQTGPPKQPSQQPGPEKPSAQQAGPAkqPPQPGSGKPPPQQTGLVKQV--PPQA 398
Cdd:pfam15240   15 SAQSSSEDVSQEDSPSLISEEEGQSQQGGQGPQGPPPGGFPPQPPASDDPPG--PPPPGGPQQPPPQGGKQKPQgpPPQG 92

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2032737686  399 GPTKPPSQTVGPTKPLA-QQAGPTKPPGQQPGPEKPPQQTQAGANQPTETAPK 450
Cdd:pfam15240   93 GPRPPPGKPQGPPPQGGnQQQGPPPPGKPQGPPPQGGGPPPQGGNQQGPPPPP 145
PDZ2_Dlg1-2-4-like cd06724
PDZ domain 2 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg) ...
 4525-4614 3.82e-06

PDZ domain 2 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of Drosophila Dlg1, human Dlg1,2, and 4 and related domains. Dlg1 (also known as synapse-associated protein Dlg197 or SAP-97), Dlg2 (also known as channel-associated protein of synapse-110, postsynaptic density protein 93, or PSD-93), Dlg4 (also known as postsynaptic density protein 95, PSD-95, synapse-associated protein 90, or SAP-90) each have 3 PDZ domains and belong to the membrane-associated guanylate kinase family. Dlg1 regulates antigen receptor signaling and cell polarity in lymphocytes, B-cell proliferation and antibody production, and TGFalpha bioavailability; its PDZ3 domain binds pro-TGFalpha, and its PDZ2 domain binds the TACE metalloprotease responsible for cleaving pro-TGFalpha to a soluble form. Dlg2 is involved in N-methyl-D-aspartate (NMDA) receptor signaling. It regulates surface expression of NMDA receptors in dorsal horn neurons of the spinal cord, and it also interacts with NMDA receptor subunits and with Shaker-type K+ channel subunits to cluster into a channel complex. Dlg4 PDZ1 domain binds NMDA receptors, and its PDZ2 domain binds neuronal nitric oxide synthase (nNOS), forming a complex in neurons. The Drosophila Scribble complex (Scribble, Dlg, and lethal giant larvae) plays a role in apico-basal cell polarity, and in other forms of polarity, including regulation of the actin cytoskeleton, cell signaling and vesicular trafficking, and in tumor development. Postsynaptic targeting of Drosophila DLG requires interactions mediated by the first two PDZ domains. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Dlg-like family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467207 [Multi-domain]  Cd Length: 85  Bit Score: 48.03  E-value: 3.82e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4525 LKLLRDPKdhtvsgnGLGIRVVGGK---EIPGSSGeigAYIAKILPGGNAEQTGKLVEGMQVLEWNGIPLTGKTYEEVQS 4601
Cdd:cd06724      2 IKLVKGPK-------GLGFSIAGGVgnqHIPGDNG---IYVTKIIEGGAAQKDGRLQVGDKLLAVNDVSLEEVTHEEAVA 71

                           90
                   ....*....|...
gi 2032737686 4602 IIIQQSGEAEICV 4614
Cdd:cd06724     72 ALKNTSDVVYLKV 84
PHA03379 PHA03379
EBNA-3A; Provisional
 196-633 3.93e-06

EBNA-3A; Provisional


Pssm-ID: 223066 [Multi-domain]  Cd Length: 935  Bit Score: 53.52  E-value: 3.93e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  196 GKPEEQRSPAKHPTQPQS--PKPAVQQQgpvRPTVQQtesSKQQQQPGGPKQVQKPGhgqpadakqdqakqPAQPRGPqk 273
Cdd:PHA03379   396 KLTERAREALEKASEPTYgtPRPPVEKP---RPEVPQ---SLETATSHGSAQVPEPP--------------PVHDLEP-- 453

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  274 sqpqpseptKPIQQQTSAKPssGPTKPSPQQPdstkvtsqtAPPTKPSSQQPGPAKQPSQQPARQGAPVKP--SPQQTGP 351
Cdd:PHA03379   454 ---------GPLHDQHSMAP--CPVAQLPPGP---------LQDLEPGDQLPGVVQDGRPACAPVPAPAGPivRPWEASL 513

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  352 PKQPSQQPGPEKPSAQQAGPAKQP----PQPGSGKPP------PQQTGLVKQV-----PPQAGPTKPPSQTVGPTKPLAQ 416
Cdd:PHA03379   514 SQVPGVAFAPVMPQPMPVEPVPVPtvalERPVCPAPPliamqgPGETSGIVRVrerwrPAPWTPNPPRSPSQMSVRDRLA 593

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  417 QAGPTKPPGQQPGPEKPPQQTQAGANQPTETapkktfcPLCTTTELLLHTPEKANYNTCTQCHTVVCSLCGFNpNPHITE 496
Cdd:PHA03379   594 RLRAEAQPYQASVEVQPPQLTQVSPQQPMEY-------PLEPEQQMFPGSPFSQVADVMRAGGVPAMQPQYFD-LPLQQP 665

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  497 ISEWLCLncQMQRTLGGDLAPGLGPGPQPLAPKQKTPIPPSAKPS---PQpQPVQKKDVTPKPDPSQAADSKRPPPQKKQ 573
Cdd:PHA03379   666 ISQGAPL--APLRASMGPVPPVPATQPQYFDIPLTEPINQGASAAhflPQ-QPMEGPLVPERWMFQGATLSQSVRPGVAQ 742

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2032737686  574 TQ---LPGSPPVKSKQPRA----EP---------TDISQQTDATPKSDQVkPTQAEDKQKQPSVQKPTADSVSTSV 633
Cdd:PHA03379   743 SQyfdLPLTQPINHGAPAAhflhQPpmegpwvpeQWMFQGAPPSQGTDVV-QHQLDALGYVLHVLNHPGVPVSPAV 817
C2B_Synaptotagmin-14_16 cd08408
C2 domain second repeat present in Synaptotagmins 14 and 16; Synaptotagmin 14 and 16 are ...
 5114-5223 4.14e-06

C2 domain second repeat present in Synaptotagmins 14 and 16; Synaptotagmin 14 and 16 are membrane-trafficking proteins in specific tissues outside the brain. Both of these contain C-terminal tandem C2 repeats, but only Synaptotagmin 14 has an N-terminal transmembrane domain and a putative fatty-acylation site. 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 and this is indeed the case here. 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.


Pssm-ID: 176053 [Multi-domain]  Cd Length: 138  Bit Score: 49.29  E-value: 4.14e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 5114 LIVEILQCRNitYKFKSPDHLPDLYVKLYVVNiSTQKRVIKKKTRVCRHDREPSFNETFRFSLSPAGHSLQILLVS--NG 5191
Cdd:cd08408     17 LSVEVIKGSN--FKNLAMNKAPDTYVKLTLLN-SDGQEISKSKTSIRRGQPDPEFKETFVFQVALFQLSEVTLMFSvyNK 93

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 2032737686 5192 GKFMKKTLIG------------EAYIWLDKVDLR-KRIVNWHKLL 5223
Cdd:cd08408     94 RKMKRKEMIGwfslglnssgeeEEEHWNEMKESKgQQVCRWHTLL 138
PHA03378 PHA03378
EBNA-3B; Provisional
 323-736 4.17e-06

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 53.53  E-value: 4.17e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  323 QQPGPAKQPSQQPARQGapvkPSPQQTGPPKQPsqQPGPEKPSAQQAGPAKQPPQPGsgkppPQQTGLVKQVPPQAGPTK 402
Cdd:PHA03378   433 KKAARTEQPRATPHSQA----PTVVLHRPPTQP--LEGPTGPLSVQAPLEPWQPLPH-----PQVTPVILHQPPAQGVQA 501

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  403 PPS-------------QTV-------GPTKPLAQQAGP----------------TKPPGQQPGPEKPPQQTQAGANQPTE 446
Cdd:PHA03378   502 HGSmldllekddedmeQRVmatllppSPPQPRAGRRAPcvytedldiesdepasTEPVHDQLLPAPGLGPLQIQPLTSPT 581

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  447 TAPKKTFCPLCTTTELLLHTPEKANYNTCTQCHTvvcslcgfnpnPHITEISEW-LCLNCQMQRTLGGDLAPGLGPG-PQ 524
Cdd:PHA03378   582 TSQLASSAPSYAQTPWPVPHPSQTPEPPTTQSHI-----------PETSAPRQWpMPLRPIPMRPLRMQPITFNVLVfPT 650

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  525 PLAPKQKTPIPPsakpspQPQPVQKKDVTPKPDPSQAADSKRPPPQKKQTQLPGSPPVKSKQPRAEPTDISQQTDATPKS 604
Cdd:PHA03378   651 PHQPPQVEITPY------KPTWTQIGHIPYQPSPTGANTMLPIQWAPGTMQPPPRAPTPMRPPAAPPGRAQRPAAATGRA 724

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  605 --DQVKPTQAEDKQKQPSVQKPTAdsvSTSVAAEQKQDLAGPRPPTQqkvtdsPKPELAKPSQdthpagdKPDSKPVPQv 682
Cdd:PHA03378   725 rpPAAAPGRARPPAAAPGRARPPA---AAPGRARPPAAAPGRARPPA------AAPGAPTPQP-------PPQAPPAPQ- 787

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2032737686  683 SRQKSDPKFASQPGARPDAKAQKPIDPTQTKDDPKKLPTKPAPKPDTK--PAPKGP 736
Cdd:PHA03378   788 QRPRGAPTPQPPPQAGPTSMQLMPRAAPGQQGPTKQILRQLLTGGVKRgrPSLKKP 843
C2A_Synaptotagmin-1-5-6-9-10 cd08385
C2A domain first repeat present in Synaptotagmins 1, 5, 6, 9, and 10; Synaptotagmin is a ...
 5112-5223 4.93e-06

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.


Pssm-ID: 176031 [Multi-domain]  Cd Length: 124  Bit Score: 48.80  E-value: 4.93e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 5112 EQLIVEILQCRNitykfkspdhLP--------DLYVKLYVVNIStqkrviKKK--TRVCRHDREPSFNETFRFSLSPAGH 5181
Cdd:cd08385     16 NQLTVGIIQAAD----------LPamdmggtsDPYVKVYLLPDK------KKKfeTKVHRKTLNPVFNETFTFKVPYSEL 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2032737686 5182 SLQILLVS--NGGKFMKKTLIGEAYIWLDKVDLRKRIVNWHKLL 5223
Cdd:cd08385     80 GNKTLVFSvyDFDRFSKHDLIGEVRVPLLTVDLGHVTEEWRDLE 123
PHA03377 PHA03377
EBNA-3C; Provisional
 202-729 5.00e-06

EBNA-3C; Provisional


Pssm-ID: 177614 [Multi-domain]  Cd Length: 1000  Bit Score: 53.13  E-value: 5.00e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  202 RSPAKHPTQPQSPKPAVQqqgPVRPTVQQTESSKQQQQPGGPKQVQ-----------KPGHGQPADAKQDQAKQPaqprg 270
Cdd:PHA03377   410 RVPWRKPRTLPWPTPKTH---PVKRTLVKTSGRSDEAEQAQSTPERpgpsdqpsvpvEPAHLTPVEHTTVILHQP----- 481

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  271 PQKSQPQPSEPTKP-------------------IQQQTSAKPSS--GPTKPSPQQPDSTKVTSQTAPPTKPSSQQPGPAK 329
Cdd:PHA03377   482 PQSPPTVAIKPAPPpsrrrrgacvvydddiievIDVETTEEEESvtQPAKPHRKVQDGFQRSGRRQKRATPPKVSPSDRG 561

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  330 QPSQQPARQGAPVKPSPQQTGPPKQPSQQPGPEKPSAQQAGPAKQPPQPGSGKPPPQQTGLVKQVPPQAGPTKPPSQTVG 409
Cdd:PHA03377   562 PPKASPPVMAPPSTGPRVMATPSTGPRDMAPPSTGPRQQAKCKDGPPASGPHEKQPPSSAPRDMAPSVVRMFLRERLLEQ 641

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  410 PTKPLAQQAGPTKPPGQQPGPEKPPQQTQAGANQPTetapkkTFCPLCTTTELLLHTPEKANYNTCTQCHtvVCSLCGFN 489
Cdd:PHA03377   642 STGPKPKSFWEMRAGRDGSGIQQEPSSRRQPATQST------PPRPSWLPSVFVLPSVDAGRAQPSEESH--LSSMSPTQ 713

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  490 PNPHiteiSEWLCLNcQMQRTLGGDLAPGLGPGPQPLAPKQKTPIPPsAKPSPQPQPVQkkdvtPKPDPSQAADSKRPPP 569
Cdd:PHA03377   714 PISH----EEQPRYE-DPDDPLDLSLHPDQAPPPSHQAPYSGHEEPQ-AQQAPYPGYWE-----PRPPQAPYLGYQEPQA 782

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  570 QKKQ-TQLPGSP---PVKSKQPRAEPTdisqqTDATPKSDQVKPTQAEDKQKQPSVqKPTADSvstsvAAEQKQDLAGPR 645
Cdd:PHA03377   783 QGVQvSSYPGYAgpwGLRAQHPRYRHS-----WAYWSQYPGHGHPQGPWAPRPPHL-PPQWDG-----SAGHGQDQVSQF 851

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  646 PPTQQKvTDSPKPELAKPSQDTHPagDKPDSKPVPQVSrqksdpkfASQPGArpdakaqkPIDPTqtkddPKKLPTKPAP 725
Cdd:PHA03377   852 PHLQSE-TGPPRLQLSQVPQLPYS--QTLVSSSAPSWS--------SPQPRA--------PIRPI-----PTRFPPPPMP 907


                   ....
gi 2032737686  726 KPDT 729
Cdd:PHA03377   908 LQDS 911
PDZ3_PTPN13_FRMPD2-like cd06695
PDZ domain 3 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), FERM and PDZ ...
 4537-4603 5.18e-06

PDZ domain 3 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), FERM and PDZ domain-containing protein 2 (FRMPD2), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of PTPN13 [also known as Fas-associated protein-tyrosine phosphatase 1 (FAP-1), protein-tyrosine phosphatase 1E (PTP-E1), and protein-tyrosine phosphatase (PTPL1)], FRMPD2 (also known as PDZ domain-containing protein 4; PDZ domain-containing protein 5C), and related domains. PTPN13 regulates negative apoptotic signaling and mediates phosphoinositide 3-kinase (PI3K) signaling. PTPN13 has five PDZ domains. Proteins known to interact with PTPN13 PDZ domains include: PLEKHA1 and PLEKHA2 via PTPN13-PDZ domain 1, Fas receptor and thyroid receptor-interacting protein 6 via PTPN13-PDZ domain 2, nerve growth factor receptor and protein kinase N2 via PTPN13-PDZ domain 3, PDZ and LIM domain 4 (PDLIM4) via PTPN13-PDZ domains 2 and 4, and brain calpain-2 via PTPN13-PDZ domains 3, 4 and 5. Calpain-2-mediated PTPN13 fragments may be involved in abnormal tau aggregation and increased risk for Alzheimer's disease. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). FRMPD2 is localized in the basolateral membranes of polarized epithelial cells and is associated with tight junction formation and immune response; it contains 3 PDZ domains). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PTPN13 family PDZ3 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467181 [Multi-domain]  Cd Length: 90  Bit Score: 47.64  E-value: 5.18e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2032737686 4537 SGNGLGIRVVGGK-EIPGSSGEIGAYIAKILPGGNAEQTGKLVEGMQVLEWNGIPLTGKTYEEVQSII 4603
Cdd:cd06695      9 GSSGLGFSFLGGEnNSPEDPFSGLVRIKKLFPGQPAAESGLIQEGDVILAVNGEPLKGLSYQEVLSLL 76
PHA03418 PHA03418
hypothetical E4 protein; Provisional
 294-439 5.51e-06

hypothetical E4 protein; Provisional


Pssm-ID: 177646 [Multi-domain]  Cd Length: 230  Bit Score: 50.89  E-value: 5.51e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  294 SSGPTKPSPQQ-PDSTKVTSQTAPPTKPSSQQPGPAKQP--SQQPARQG------APVKPSPQQTGPPKQPSQQPGPEK- 363
Cdd:PHA03418    36 LPAPHHPNPQEdPDKNPSPPPDPPLTPRPPAQPNGHNKPpvTKQPGGEGteedhqAPLAADADDDPRPGKRSKADEHGPa 115

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  364 PSAQQAGPAK----QPPQPGSGKPPPQQTGLVKQVPPQAGPTKPPsqtvgptkPLAQQAGPTK--PPGQQPGPEKPPQQT 437
Cdd:PHA03418   116 PGRAALAPFKldldQDPLHGDPDPPPGATGGQGEEPPEGGEESQP--------PLGEGEGAVEghPPPLPPAPEPKPHNG 187


                   ..
gi 2032737686  438 QA 439
Cdd:PHA03418   188 DA 189
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
 333-449 6.28e-06

Proline-rich protein; This family includes several eukaryotic proline-rich proteins.


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 49.65  E-value: 6.28e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  333 QQPARQGAPVKPSPQQTGPPKQPSQQPGPEKPSaQQAGPAKQPPQPGSGK---PPPQQTGLVKQVPPQAGPTKPPSQTVG 409
Cdd:pfam15240   36 EGQSQQGGQGPQGPPPGGFPPQPPASDDPPGPP-PPGGPQQPPPQGGKQKpqgPPPQGGPRPPPGKPQGPPPQGGNQQQG 114

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2032737686  410 PTKPLAQQAGP--TKPPGQQPGPEKPPQQTQAGANQPTETAP 449
Cdd:pfam15240  115 PPPPGKPQGPPpqGGGPPPQGGNQQGPPPPPPGNPQGPPQRP 156
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
 271-431 6.44e-06

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 52.56  E-value: 6.44e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  271 PQKSQPQPSEPTKPIQQQTSAKPSSGPTKPSPQQpdstkvtsqtAPPTKPSSQQPGPAKQPSQQPARQGAPVKPSPQQTG 350
Cdd:PRK07994   361 PAAPLPEPEVPPQSAAPAASAQATAAPTAAVAPP----------QAPAVPPPPASAPQQAPAVPLPETTSQLLAARQQLQ 430

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  351 PPKQPSQQPGPEKPSAQQAGPAKQPPQPGSGKPPPQQTGLVKQVPPQAGPTKPPSQTVGPTKPLAQQAGPTKPPGQQPGP 430
Cdd:PRK07994   431 RAQGATKAKKSEPAAASRARPVNSALERLASVRPAPSALEKAPAKKEAYRWKATNPVEVKKEPVATPKALKKALEHEKTP 510


                   .
gi 2032737686  431 E 431
Cdd:PRK07994   511 E 511
PDZ13_MUPP1-like cd06676
PDZ domain 13 of multi-PDZ-domain protein 1 (MUPP1) and related domains; PDZ (PSD-95 ...
 4540-4614 6.64e-06

PDZ domain 13 of multi-PDZ-domain protein 1 (MUPP1) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 13 of MUPP1. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, PDZ9, and PDZ13. This MuPP1-like PDZ13 domain is therefore absent from PATJ. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like family PDZ13 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467164 [Multi-domain]  Cd Length: 83  Bit Score: 47.34  E-value: 6.64e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2032737686 4540 GLGIRVVGGKEIPgsSGEIGAYIAKILPGGNAEQTGKLVEGMQVLEWNGIPLTGKTYEEVQSIIIQQSGEAEICV 4614
Cdd:cd06676     10 GLGFSIVGGFGSP--HGDLPIYVKTVFEKGAAAEDGRLKRGDQILAVNGESLEGVTHEEAVNILKKTKGTVTLTV 82
PHA03418 PHA03418
hypothetical E4 protein; Provisional
 249-404 7.32e-06

hypothetical E4 protein; Provisional


Pssm-ID: 177646 [Multi-domain]  Cd Length: 230  Bit Score: 50.51  E-value: 7.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  249 PGHGQPADAKQDQAKQPAQPRGPQKSQPQPSEPTKPIQQQTSAKPSSGPTKPSPQQPDStkvTSQTAPPTKPSSQQPGPA 328
Cdd:PHA03418    39 PHHPNPQEDPDKNPSPPPDPPLTPRPPAQPNGHNKPPVTKQPGGEGTEEDHQAPLAADA---DDDPRPGKRSKADEHGPA 115

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2032737686  329 kqpsqqPAR-QGAPVKPSPQQTGPpkqpsqQPGPEKPSAQQAGPAKQPPQPG--SGKPPPQQTGLVKQVPPQAGPTKPP 404
Cdd:PHA03418   116 ------PGRaALAPFKLDLDQDPL------HGDPDPPPGATGGQGEEPPEGGeeSQPPLGEGEGAVEGHPPPLPPAPEP 182
PDZ2_LNX1_2-like cd06678
PDZ domain 2 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ ...
 4534-4609 7.54e-06

PDZ domain 2 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of LNX1 (also known as PDZ domain-containing RING finger protein 2, PDZRN2) and LNX2 (also known as PDZ domain-containing RING finger protein 1, PDZRN1), and related domains. LNX1 and LNX2 are Ring (Really Interesting New Gene) finger and PDZ domain-containing E3 ubiquitin ligases that bind to the cell fate determinant protein NUMB and mediate its ubiquitination. LNX1 can ubiquitinate a number of other ligands including PPFIA1, KLHL11, KIF7 and ERC2. LNX1 and LNX2 each have four PDZ domains. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This LNX family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467166 [Multi-domain]  Cd Length: 82  Bit Score: 46.86  E-value: 7.54e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2032737686 4534 HTVSGNGLGIRVVGGKEIPGssgeigAYIAKILPGGNAEQTGKLVEGMQVLEWNGIPLTGKTYEEVQSiIIQQSGE 4609
Cdd:cd06678      6 NKRDGEQLGIKLVRKKDEPG------VFILDLLEGGLAARDGRLKSDDRVLAINGQDLRHGTPEQAAQ-IIQASGE 74
PDZ2_DLG5-like cd06765
PDZ domain 2 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density ...
 4543-4603 8.10e-06

PDZ domain 2 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of Drosophila and mammalian Dlg5, and related domains. Dlg5 is a scaffold protein with multiple conserved functions that are independent of each other in regulating growth, cell polarity, and cell adhesion. It has a coiled-coil domain, 4 PDZ domains and a MAGUK domain (an SH3 domain next to a non-catalytically active guanylate kinase domain). Deregulation of Dlg5 has been implicated in the malignancy of several cancer types. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Dlg5-like family PSZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467246 [Multi-domain]  Cd Length: 77  Bit Score: 46.96  E-value: 8.10e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2032737686 4543 IRVVGGKEiPGSSGEIGAYIAKILPGGNAEQTGKLVEGMQVLEWNGIPLTGKTYEEVQSII 4603
Cdd:cd06765      2 INLSGQKD-SGISLENGVFISRIVPGSPAAKEGSLTVGDRIIAINGIALDNKSLSECEALL 61
PDZ4_PDZD2-PDZ2_hPro-IL-16-like cd06760
PDZ domain 4 of PDZ domain containing 2 (PDZD2), PDZ domain 2 of human pro-interleukin-16 ...
 4534-4615 8.97e-06

PDZ domain 4 of PDZ domain containing 2 (PDZD2), PDZ domain 2 of human pro-interleukin-16 (isoform 1, 1332 AA), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 4 of PDZD2, also known as KIAA0300, PIN-1, activated in prostate cancer (AIPC) and PDZ domain-containing protein 3 (PDZK3). PDZD2 has seven PDZ domains. PDZD2 is expressed at exceptionally high levels in the pancreas and certain cancer tissues, such as prostate cancer. It promotes the proliferation of insulinoma cells and is upregulated during prostate tumorigenesis. In osteosarcoma (OS), the microRNA miR-363 acts as a tumor suppressor by inhibiting PDZD2. This family also includes the second PDZ domain (PDZ2) of human pro-interleukin-16 (isoform 1, also known as nPro-Il-16; 1332 amino-acid protein). Precursor IL-16 is cleaved to produce pro-IL-16 and mature IL-16 (derived from the C-terminal 121 AA). Pro-IL-16 functions as a regulator of T cell growth; mature IL-16 is a CD4 ligand that induces chemotaxis and CD25 expression in CD4+ T cells. IL-16 bioactivity has been closely associated with the progression of several different cancers PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PDZD2-like family PDZ4 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467241 [Multi-domain]  Cd Length: 90  Bit Score: 46.88  E-value: 8.97e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4534 HTVSGNGLGIRVVGgkeIPGSSGEIGAYIAKILPGGNAEQTGKLVEGMQVLEWNGIPLTGKTYEEVQSIIIQ-QSGEAEI 4612
Cdd:cd06760     10 NKEPGVGLGIGLCC---LPLENDIPGIFIHHLSPGSVAHMDGRLRRGDQILEINGTSLRNVTLNEAYAILSQcKPGPVTL 86


                   ...
gi 2032737686 4613 CVR 4615
Cdd:cd06760     87 IIS 89
PDZ2_Scribble-like cd06703
PDZ domain 2 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 4526-4614 9.42e-06

PDZ domain 2 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of Drosophila Scribble (also known as LAP4), human Scribble homolog (also known as hScrib, LAP4, CriB1, ScrB1 and Vartul), and related domains. They belong to the LAP family, which describes proteins that contain either one or four PDZ domains and 16 LRRs (leucine-rich repeats) and function in controlling cell shape, size and subcellular protein localization. In Drosophila, the Scribble complex, comprising Scribble, discs large, and lethal giant larvae, plays a role in apico-basal cell polarity, in other forms of polarity, including regulation of the actin cytoskeleton, cell signaling and vesicular trafficking, and in tumor development. Mammalian Scribble is important in many aspects of cancer development. Scribble and its homologs can be downregulated or overexpressed in cancer; they have a role in cancer beyond their function in loss of cell polarity. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Scribble-like family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467187 [Multi-domain]  Cd Length: 92  Bit Score: 46.87  E-value: 9.42e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4526 KLLRDpkdhtvsGNGLGIRVVGGKE-IPGSSGEIGAYIAKILPGGNAEQTGKLVEGMQVLEWNGIPLTGKTYEEVQSIII 4604
Cdd:cd06703      6 TLIRD-------GKGLGFSIAGGKGsTPFRDGDEGIFISRITEGGAADRDGKLQVGDRVLSINGVDVTEARHDQAVALLT 78

                           90
                   ....*....|
gi 2032737686 4605 QQSGEAEICV 4614
Cdd:cd06703     79 SSSPTITLVV 88
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 269-710 9.61e-06

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 52.23  E-value: 9.61e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  269 RGPQKSQPQPSEPTKPIQ--QQTSAKPSSGPTKPSPQQPDSTKVTSQTAPPTKPS---SQQPGPAKQPSQQPARQGAPVK 343
Cdd:pfam05109  423 KAPESTTTSPTLNTTGFAapNTTTGLPSSTHVPTNLTAPASTGPTVSTADVTSPTpagTTSGASPVTPSPSPRDNGTESK 502

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  344 -------------PSPQQTGP-PKQPSQQPGPEKPSAQQAGP--AKQPPQPGSGKPPPQQTglvkqvPPQAGPTKPpsqT 407
Cdd:pfam05109  503 apdmtsptsavttPTPNATSPtPAVTTPTPNATSPTLGKTSPtsAVTTPTPNATSPTPAVT------TPTPNATIP---T 573

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  408 VGPTKPLAQQAGPTKPPGQQPGPEKPPQqtqagANQPTETAPKKTFCPLCTTtelllhTPEKANYNTCTQCHTVV-CSLC 486
Cdd:pfam05109  574 LGKTSPTSAVTTPTPNATSPTVGETSPQ-----ANTTNHTLGGTSSTPVVTS------PPKNATSAVTTGQHNITsSSTS 642

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  487 GFNPNPhiTEISEWLCLNCQMQRTlggdlapglgpgpqplapkQKTPIPPSAKPSPQPQPVQkkdVTPKPDPSQAADSKR 566
Cdd:pfam05109  643 SMSLRP--SSISETLSPSTSDNST-------------------SHMPLLTSAHPTGGENITQ---VTPASTSTHHVSTSS 698

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  567 PPPQKKQTQLPGSPPVKSKQPRAEPTDIsqqTDATPKSDQVKPtqaedkqKQPSVQKPTADSVSTSvaAEQKQDLAGPRP 646
Cdd:pfam05109  699 PAPRPGTTSQASGPGNSSTSTKPGEVNV---TKGTPPKNATSP-------QAPSGQKTAVPTVTST--GGKANSTTGGKH 766

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2032737686  647 PTQQKVTDSPKPELAKPSQDTHPAGDKPDSKPVPQVSRQKSDPKFASQPGARPDAKAQKPIDPT 710
Cdd:pfam05109  767 TTGHGARTSTEPTTDYGGDSTTPRTRYNATTYLPPSTSSKLRPRWTFTSPPVTTAQATVPVPPT 830
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 263-872 1.03e-05

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.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 52.46  E-value: 1.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  263 KQPAQPRG---PQKSQPQPSEPTKPiqqqTSAKPSSGPTKPSPQQPDSTKVTSQTAPPTKPSSQQPGPAKQPSQQPARQG 339
Cdd:pfam03154   23 KQTASPDGrasPTNEDLRSSGRNSP----SAASTSSNDSKAESMKKSSKKIKEEAPSPLKSAKRQREKGASDTEEPERAT 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  340 APvKPSPQQTGPPKQPSQQPGPEKPSA-----------------QQAGPAKQPPQ--PGSGKPPPQQTGLVKQVPPQAGP 400
Cdd:pfam03154   99 AK-KSKTQEISRPNSPSEGEGESSDGRsvndegssdpkdidqdnRSTSPSIPSPQdnESDSDSSAQQQILQTQPPVLQAQ 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  401 TKPPSQTVGPTKPLAQQAGPTKPPGQQPGPEKPPQQTQAGANQPTETAPKKTFCPLCTTtellLHTPEKanyntctqcht 480
Cdd:pfam03154  178 SGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPT----LHPQRL----------- 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  481 vvcslcgfnPNPHiteisewlclncqmqrtlggdlaPGLGPGPQPlapkqktPIPPSAKPSPQPQPVQKKDVTPKPDPSQ 560
Cdd:pfam03154  243 ---------PSPH-----------------------PPLQPMTQP-------PPPSQVSPQPLPQPSLHGQMPPMPHSLQ 283

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  561 AADSKRPPPQKKQtqlPGSPPVKSKQPRAEPTDISQQTDATPKSDQVKPTQAEDKQKQPSVQKPTADSvstsvaaeqkqD 640
Cdd:pfam03154  284 TGPSHMQHPVPPQ---PFPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPA-----------P 349

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  641 LAGPR---PPTqqkvtdSPKPELAKPSQDTHPAgdkpdskpvpqvsrQKSDPKFASQPGARPDAKAQKPIDPTQTKDDPK 717
Cdd:pfam03154  350 LSMPHikpPPT------TPIPQLPNPQSHKHPP--------------HLSGPSPFQMNSNLPPPPALKPLSSLSTHHPPS 409

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  718 KLPTKPAPKPDTKPAPKGPQAGAGPKAAPAQPAPQPQPPqktpeqprrfslNLGGITDAPkPQPTTPQEtvtgklfgfga 797
Cdd:pfam03154  410 AHPPPLQLMPQSQQLPPPPAQPPVLTQSQSLPPPAASHP------------PTSGLHQVP-SQSPFPQH----------- 465

                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2032737686  798 SFFSQASNLISTagqtgsqPSGPPPPAPAAKQPQPPAQPPAPQAAPKEAAQAQPLPKAVPVKKEAKPLTTEKSEP 872
Cdd:pfam03154  466 PFVPGGPPPITP-------PSGPPTSTSSAMPGIQPPSSASVSSSGPVPAAVSCPLPPVQIKEEALDEAEEPESP 533
PRK10927 PRK10927
cell division protein FtsN;
131-386 1.07e-05

cell division protein FtsN;


Pssm-ID: 236797 [Multi-domain]  Cd Length: 319  Bit Score: 51.22  E-value: 1.07e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  131 RESKSRTDFKEDQKPSMMPSFLSEAnplSAVtsVVNKFNPFDLISDSDTSHEEAGRKQKVA-------PKEQG---KPEE 200
Cdd:PRK10927    16 RRKKSTSRKKQRNLPAVSPAMVAIA---AAV--LVTFIGGLYFITHHKKEESETLQSQKVTgnglppkPEERWryiKELE 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  201 QRSPA-KHPTQPQS------PKPAVQQQGPVRPTVQQTESSKQQQQPGGPKQVQKPGHGQPADAKQDQAKQPAQprgPQK 273
Cdd:PRK10927    91 SRQPGvRAPTEPSAggevktPEQLTPEQRQLLEQMQADMRQQPTQLVEVPWNEQTPEQRQQTLQRQRQAQQLAE---QQR 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  274 SQPQPSEPTKPIQQQtsakpssgpTKPSPQQPdstkVTSQTAPPTKPSSQQpgPAKQPSQQPARQGApvKPSPQQTGPPK 353
Cdd:PRK10927   168 LAQQSRTTEQSWQQQ---------TRTSQAAP----VQAQPRQSKPASTQQ--PYQDLLQTPAHTTA--QSKPQQAAPVT 230

                          250       260       270
                   ....*....|....*....|....*....|...
gi 2032737686  354 QPSQQPgpeKPSAQQAGPAKQPPQPGSGKPPPQ 386
Cdd:PRK10927   231 RAADAP---KPTAEKKDERRWMVQCGSFRGAEQ 260
PDZ4_MUPP1-like cd06668
PDZ domain 4 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ...
 4538-4616 1.08e-05

PDZ domain 4 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 4 of MUPP1 and PATJ, and related domains. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, 9, and 13; consequently, MUPP1 PDZ7 and 8 align with PATJ PDZ6 and 7; and MUPP1 PDZ domains 10-12 align with PATJ PDZ domains 8-10. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like family PDZ4 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F


Pssm-ID: 467156 [Multi-domain]  Cd Length: 88  Bit Score: 46.91  E-value: 1.08e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2032737686 4538 GNGLGIRVVGGKEIpGSSGEigAYIAKILPGGNAEQTGKLVEGMQVLEWNGIPLTGKTYEEVQSIIiqqsGEAEICVRL 4616
Cdd:cd06668     13 SSGLGISLEGTVDV-EVRGH--HYIRSILPEGPVGRNGKLFSGDELLEVNGIQLLGLSHKEVVSIL----KELPPPVRL 84
C2B_Synaptotagmin-1 cd08402
C2 domain second repeat present in Synaptotagmin 1; Synaptotagmin is a membrane-trafficking ...
 5113-5222 1.18e-05

C2 domain second repeat present in Synaptotagmin 1; 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 the 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. It, like synaptotagmin-2, has an N-glycosylated N-terminus. Synaptotagmin 4, a member of class 4 synaptotagmins, is located in the brain. It functions are unknown. It, like synaptotagmin-11, has an Asp to Ser substitution in its C2A domain. 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.


Pssm-ID: 176047 [Multi-domain]  Cd Length: 136  Bit Score: 48.17  E-value: 1.18e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 5113 QLIVEILQCRNItyKFKSPDHLPDLYVKLYVvnISTQKRVIKKKTRVCRHDREPSFNETFRFSLSPagHSLQ----ILLV 5188
Cdd:cd08402     16 KLTVVILEAKNL--KKMDVGGLSDPYVKIHL--MQNGKRLKKKKTTIKKRTLNPYYNESFSFEVPF--EQIQkvhlIVTV 89

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2032737686 5189 SNGGKFMKKTLIGEAYI-----------WLDKVDLRKR-IVNWHKL 5222
Cdd:cd08402     90 LDYDRIGKNDPIGKVVLgcnatgaelrhWSDMLASPRRpIAQWHTL 135
SP2_N cd22540
N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins ...
 173-379 1.26e-05

N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. SP2 contains the least conserved DNA-binding domain within the SP subfamily of proteins, and its DNA sequence specificity differs from the other SP proteins. It localizes primarily within subnuclear foci associated with the nuclear matrix, and can activate, or in some cases, repress expression from different promoters. The transcription factor SP2 serves as a paradigm for indirect genomic binding. It does not require its DNA-binding domain for genomic DNA binding and occupies target promoters independently of whether they contain a cognate DNA-binding motif. SP2 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP2.


Pssm-ID: 411776 [Multi-domain]  Cd Length: 511  Bit Score: 51.47  E-value: 1.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  173 LISDSDTSHeeagrkQKVAPKEQGKPEEQRSpaKHPTQPQSPKPAVQQQgpVRPTVQQTESSKQQQQPGGPKQVQKPGHG 252
Cdd:cd22540    212 LVGTQDGAT------QLQLAAAPSKPSKKIR--KKSAQAAQPAVTVAEQ--VETVLIETTADNIIQAGNNLLIVQSPGTG 281

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  253 QPAdakQDQAKQPAQPRGPQKSQPQPSEPTKPIQQQTSAKPssgptkPSPQQPdSTKVTSQTAPPTKPSSQQPGPAKQPS 332
Cdd:cd22540    282 QPA---VLQQVQVLQPKQEQQVVQIPQQALRVVQAASATLP------TVPQKP-LQNIQIQNSEPTPTQVYIKTPSGEVQ 351

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2032737686  333 QQPARQGAPVKPSPQQTGPPKQPSQQP-GPEKPSAQQAGPAKQPPQPG 379
Cdd:cd22540    352 TVLLQEAPAATATPSSSTSTVQQQVTAnNGTGTSKPNYNVRKERTLPK 399
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
 4532-4603 1.39e-05

PDZ domain; PDZ domains are found in diverse signaling proteins.


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 46.12  E-value: 1.39e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2032737686 4532 KDHTVSGNGLGIRVVGGkeipGSSGEIGAYIAKILPGGNAEQTGkLVEGMQVLEWNGIPLTGKTYEEVQSII 4603
Cdd:pfam00595    3 TLEKDGRGGLGFSLKGG----SDQGDPGIFVSEVLPGGAAEAGG-LKVGDRILSINGQDVENMTHEEAVLAL 69
PDZ_syntrophin-like cd06801
PDZ domain of syntrophins, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), ...
 4526-4615 1.42e-05

PDZ domain of syntrophins, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of syntrophins (including alpha-1-syntrophin, beta-1-syntrophin, beta-2-syntrophin, gamma-1-syntrophin, and gamma-2-syntrophin), and related domains. Syntrophins play a role in recruiting various signaling molecules into signaling complexes and help provide appropriate spatiotemporal regulation of signaling pathways. They function in cytoskeletal organization and maintenance; as components of the dystrophin-glycoprotein complex (DGC), they help maintain structural integrity of skeletal muscle fibers. They link voltage-gated sodium channels to the actin cytoskeleton and the extracellular matrix, and control the localization and activity of the actin reorganizing proteins such as PI3K, PI(3,4)P2 and TAPP1. Through association with various cytoskeletal proteins within the cells, they are involved in processes such as regulation of focal adhesions, myogenesis, calcium homeostasis, and cell migration. They also have roles in synapse formation and in the organization of utrophin, acetylcholine receptor, and acetylcholinesterase at the neuromuscular synapse. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This syntrophin-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467262 [Multi-domain]  Cd Length: 83  Bit Score: 46.41  E-value: 1.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4526 KLLRDPkdhtvsGNGLGIRVVGGKE--IPgssgeigAYIAKILPGGNAEQTGKLVEGMQVLEWNGIPLTGKTYEEVQSII 4603
Cdd:cd06801      4 RVVKQD------VGGLGISIKGGAEhkMP-------ILISKIFKGQAADQTGQLFVGDAILSVNGENLEDATHDEAVQAL 70

                           90
                   ....*....|..
gi 2032737686 4604 IQQSGEAEICVR 4615
Cdd:cd06801     71 KNAGDEVTLTVK 82
PDZ3_Par3-like cd23059
PDZ domain 3 of partitioning defective 3 (Par3), and related domains; PDZ (PSD-95 ...
 4540-4603 1.46e-05

PDZ domain 3 of partitioning defective 3 (Par3), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of Par3 (or PAR3 or Par-3, also known as Atypical PKC isotype-specific-interacting protein, ASIP, Drosophila Bazooka) and related domains. Par3 is a scaffold protein involved in organizing cell polarity across animals. Par3 binds numerous molecules both for its recruitment to one pole of the cell and for downstream contributions to polarized cell function. It regulates cell polarity by targeting the Par complex proteins Par6 and atypical protein kinase C (aPKC) to specific cortical sites. Physical interactions between Par-3 and the Par complex include Par3 PDZ domain 1 binding to the Par6 PDZ domain, Par3 PDZ domain 1 and PDZ domain 3 binding the Par6's PDZ-binding motif, and an interaction with an undefined region of aPKC that requires both Par3 PDZ2 and PDZ3. The PDZ domains of Par3 have also been implicated as potential phosphoinositide signaling integrators, since its second PDZ domain binds to phosphoinositides, and the third PDZ interacts with phosphoinositide phosphatase PTEN. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Par3 family PDZ3 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467272 [Multi-domain]  Cd Length: 103  Bit Score: 46.89  E-value: 1.46e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2032737686 4540 GLGIRVVG--GKEIPGSSGEIGAYIAKILPGGNAEQTGKLVEGMQVLEWNGIPLTGKTYEEVQSII 4603
Cdd:cd23059     17 GLGVSVKGktSKEDNGGKADLGIFIKSIIHGGAASKDGRLRVNDQLIAVNGESLLGLTNSEAMETL 82
PDZ3_Scribble-like cd06702
PDZ domain 3 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 4534-4615 1.50e-05

PDZ domain 3 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of Drosophila Scribble (also known as LAP4), human Scribble homolog (also known as hScrib, LAP4, CriB1, ScrB1 and Vartul), and related domains. They belong to the LAP family, which describes proteins that contain either one or four PDZ domains and 16 LRRs (leucine-rich repeats) and function in controlling cell shape, size and subcellular protein localization. In Drosophila, the Scribble complex, comprising Scribble, discs large, and lethal giant larvae, plays a role in apico-basal cell polarity, in other forms of polarity, including regulation of the actin cytoskeleton, cell signaling and vesicular trafficking, and in tumor development. Mammalian Scribble is important in many aspects of cancer development. Scribble and its homologs can be downregulated or overexpressed in cancer; they have a role in cancer beyond their function in loss of cell polarity. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Scribble-like family PDZ3 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467186 [Multi-domain]  Cd Length: 89  Bit Score: 46.48  E-value: 1.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4534 HTVSGNG-LGIRVVGGKE---IPGSSGEIGAYIAKILPGGNAEQTGkLVEGMQVLEWNGIPLTGKTYEEVQSIIIQQSGE 4609
Cdd:cd06702      4 HLVKAGGpLGLSIVGGSDhssHPFGVDEPGIFISKVIPDGAAAKSG-LRIGDRILSVNGKDLRHATHQEAVSALLSPGQE 82


                   ....*.
gi 2032737686 4610 AEICVR 4615
Cdd:cd06702     83 IKLLVR 88
PDZ_GOPC-like cd06800
PDZ domain of Golgi-associated PDZ and coiled-coil motif-containing protein (GOPC), and ...
 4540-4614 1.52e-05

PDZ domain of Golgi-associated PDZ and coiled-coil motif-containing protein (GOPC), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of GOPC and related domains. GOPC, also known as PIST (PDZ domain protein interacting specifically with TC10), FIG (fused in glioblastoma), and CAL (CFTR-associated ligand), regulates the trafficking of a wide array of proteins, including small GTPases, receptors, and cell surface molecules such as cadherin 23 and CFTR. It may regulate CFTR chloride currents and acid-sensing ASIC3 currents by modulating cell surface expression of both channels, and may play a role in autophagy. Interaction partners of the GOPC PDZ domains include: FZD5, FZD8, ASIC3, CFTR, MUC3, ARFRP1, Ggamma13, neuroligin, and Stargazin. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This GOPC-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467261 [Multi-domain]  Cd Length: 83  Bit Score: 46.21  E-value: 1.52e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2032737686 4540 GLGIRVVGGKE--IPgssgeigAYIAKILPGGNAEQTGKLVEGMQVLEWNGIPLTGKTYEEVQSIIIQQSGEAEICV 4614
Cdd:cd06800     12 GLGISITGGKEhgVP-------ILISEIHEGQPADRCGGLYVGDAILSVNGIDLRDAKHKEAVTILSQQRGEITLEV 81
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
 201-439 1.53e-05

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 51.47  E-value: 1.53e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  201 QRSPAKHPTQPQSPKPAvqqqgPVRPTVQQTESSKQQQQPGgpkqvqkpghgqpadakqdQAKQPAQ-PRGPQKSQPQPS 279
Cdd:PLN03209   326 QRVPPKESDAADGPKPV-----PTKPVTPEAPSPPIEEEPP-------------------QPKAVVPrPLSPYTAYEDLK 381

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  280 EPTKPIQQQTSAKPssgptkPSPQQPDSTKVTSQTAPPTKPSSQQPGPAKQPSQQPARQGAPVkpSPQQTGPPKQPSQQP 359
Cdd:PLN03209   382 PPTSPIPTPPSSSP------ASSKSVDAVAKPAEPDVVPSPGSASNVPEVEPAQVEAKKTRPL--SPYARYEDLKPPTSP 453

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  360 GPEKPSAQQAGPAKQPPQPGSGKPPPQQTGLVKQVPPQAGPTKppsqtVGPTKPLAQQAGPTKPPGQQPGPEKPPQQTQA 439
Cdd:PLN03209   454 SPTAPTGVSPSVSSTSSVPAVPDTAPATAATDAAAPPPANMRP-----LSPYAVYDDLKPPTSPSPAAPVGKVAPSSTNE 528
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
247-367 1.74e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 51.31  E-value: 1.74e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  247 QKPGHGQPADAKQDQAK----QPAQPRGPQ-KSQPQPSEPTKPIQQQTSAKPSSGPTKPSPQQPDSTKVTSQTAPPTKPS 321
Cdd:PRK14971   364 QKGDDASGGRGPKQHIKpvftQPAAAPQPSaAAAASPSPSQSSAAAQPSAPQSATQPAGTPPTVSVDPPAAVPVNPPSTA 443

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2032737686  322 SQQPGPAKQPSQQPARQGAPVKPSPQQTGPPKQPSQQPGPEKPSAQ 367
Cdd:PRK14971   444 PQAVRPAQFKEEKKIPVSKVSSLGPSTLRPIQEKAEQATGNIKEAP 489
PDZ1_hSTXBP4-PDZ2_GgSTXBP4-like cd06698
PDZ1 domain of human syntaxin-binding protein 4 (STXBP4), PDZ2 domain of Gallus gallus ...
 4540-4603 1.78e-05

PDZ1 domain of human syntaxin-binding protein 4 (STXBP4), PDZ2 domain of Gallus gallus uncharacterized STXBP4 isoform X1, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of human syntaxin-binding protein 4 (STXBP4), PDZ2 domain of Gallus gallus uncharacterized STXBP4 isoform X1, and related domains. Human STXBP4 (also known as Synip) includes a single PDZ domain, a coiled-coil domain, and a WW domain (named for its two conserved tryptophans); Gallus gallus STXBP4 isoform X1 contains 2 PDZ domains (PDZ1 and PDZ2). Human STXBP4 plays a role in the translocation of transport vesicles from the cytoplasm to the plasma membrane: insulin induces the dissociation of the STXBP4 and STX4 complex liberating STX4 to interact with Vamp2, and to form the SNARE complex thereby promoting vesicle fusion. It may also play a role in the regulation of insulin release by pancreatic beta cells after stimulation by glucose. Human STXBP4 is also known to physically associate with a prominent isoform of TP63 (deltaNp63alpha 9) whose overexpression promotes squamous cell carcinoma development, and in doing so prevents degradation of this isoform by the Cdc20-APC/C complex, Itch, and RACK1. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This STXBP4-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467184 [Multi-domain]  Cd Length: 89  Bit Score: 46.14  E-value: 1.78e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2032737686 4540 GLGIRVVGGKEIPGssgEIGAYIAKILPGGNAEQTGKLVEGMQVLEWNGIPLTGKTYEEVQSII 4603
Cdd:cd06698     12 GLGLSIVGGINRPE---GPMVFIQEVIPGGDCYKDGRLRPGDQLVSINKESLIGVTLEEAKSIL 72
Amelin smart00817
Ameloblastin precursor (Amelin); This family consists of several mammalian Ameloblastin ...
 290-378 1.90e-05

Ameloblastin precursor (Amelin); This family consists of several mammalian Ameloblastin precursor (Amelin) proteins. Matrix proteins of tooth enamel consist mainly of amelogenin but also of non-amelogenin proteins, which, although their volumetric percentage is low, have an important role in enamel mineralisation. One of the non-amelogenin proteins is ameloblastin, also known as amelin and sheathlin. Ameloblastin (AMBN) is one of the enamel sheath proteins which is though to have a role in determining the prismatic structure of growing enamel crystals.


Pssm-ID: 214832 [Multi-domain]  Cd Length: 411  Bit Score: 50.66  E-value: 1.90e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686   290 SAKPSSGPTKPSPQQPDSTKVTSQTAPPTKPSSQ--QPG--PAKQPSQQPARQGAPVKPSPQQTGPPKQPSQQPGPEKPS 365
Cdd:smart00817   74 SSFPWLRPREHETQQYEYSLPVHPPPLPSQPSLQpqQPGlkPFLQPTALPTNQATPQKNGPQPPMHLGQPPLQQAELPMI 153

                            90
                    ....*....|...
gi 2032737686   366 AQQAGPAKQPPQP 378
Cdd:smart00817  154 PPQVAPSDKPPQT 166
PDZ3_ZO1-like_domain cd06729
PDZ domain 3 of Zonula Occludens-1 (ZO-1), homologs ZO-2 and ZO-3, and related domains; PDZ ...
 4538-4599 1.96e-05

PDZ domain 3 of Zonula Occludens-1 (ZO-1), homologs ZO-2 and ZO-3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of ZO-1, -2, -3 and related domains. Zonula occludens proteins (ZO-1, ZO-2, ZO-3) are multi-PDZ domain proteins involved in the maintenance and biogenesis of multi-protein networks at the cytoplasmic surface of intercellular contacts in epithelial and endothelial cells. They have three N-terminal PDZ domains, PDZ1-3, followed by a Src homology-3 (SH3) domain and a guanylate kinase (GuK)-like domain. Among protein-protein interactions for all ZO proteins is the binding of the first PDZ domain (PDZ1) to the C-termini of claudins , and the homo- and hetero-dimerization of ZO-proteins via their second PDZ domain (PDZ2), which takes place by symmetrical domain swapping of the first two beta-strands of PDZ2. At the cell level, ZO-1 and ZO-2 are involved in polarity maintenance, gene transcription, cell proliferation, and tumor cell metastasis. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This ZO family PDZ3 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467211 [Multi-domain]  Cd Length: 82  Bit Score: 45.64  E-value: 1.96e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2032737686 4538 GNGLGIRVVGGKEIpgssgeiGAYIAKILPGGNAEQTGkLVEGMQVLEWNGIPLTGKTYEEV 4599
Cdd:cd06729     10 GGSVGLRLAGGNDV-------GIFVAGVQEGSPAEKQG-LQEGDQILKVNGVDFRNLTREEA 63
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 141-453 2.10e-05

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 51.24  E-value: 2.10e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  141 EDQKPSMMPSFLSEANPLSAVTSVVnkfnPFDLISDSDTSHeeAGRKQKVApkeqgkpeeqrSPAKHPTQPQSPKPAVQQ 220
Cdd:PRK10263   538 EPIKSSLKAPSVAAVPPVEAAAAVS----PLASGVKKATLA--TGAAATVA-----------APVFSLANSGGPRPQVKE 600

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  221 Q-GPV--RPTVQQTESSKQQQQPGGPKQVQKPGHGQPADAKQDQAKQPAQPRGPQKSQPQPSEPTKPIQQQTSAKPSSGP 297
Cdd:PRK10263   601 GiGPQlpRPKRIRVPTRRELASYGIKLPSQRAAEEKAREAQRNQYDSGDQYNDDEIDAMQQDELARQFAQTQQQRYGEQY 680

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  298 TKPSPQQP--DSTKVTSQTAPPTKPSSQQPGPAKQPSQQPARQGAPVKPSPQQT---GPPKQPSQQPG--PEKPSAQQAG 370
Cdd:PRK10263   681 QHDVPVNAedADAAAEAELARQFAQTQQQRYSGEQPAGANPFSLDDFEFSPMKAlldDGPHEPLFTPIvePVQQPQQPVA 760

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  371 PAKQPPQPGSGKPPPQQTGLVKQVPPQAGPTKPPSQTVGPTKPLAQQAGPTKPPGQQPGPE---KPPQQTQAgANQPTET 447
Cdd:PRK10263   761 PQQQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQqpvAPQPQYQQ-PQQPVAP 839


                   ....*.
gi 2032737686  448 APKKTF 453
Cdd:PRK10263   840 QPQDTL 845
C2C_Tricalbin-like cd04045
C2 domain third repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are ...
 4736-4867 2.14e-05

C2 domain third repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are present in Tricalbin, a yeast homolog of Synaptotagmin, which is involved in membrane trafficking and sorting. 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.


Pssm-ID: 176010 [Multi-domain]  Cd Length: 120  Bit Score: 46.81  E-value: 2.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4736 GNLIIHILQARNLAPRDNNGYSDPFVKVYLlpgRGQVmvvqnasaeyKRRTKYIQKSLNPEWNQtVIYknISVEQLKKK- 4814
Cdd:cd04045      1 GVLRLHIRKANDLKNLEGVGKIDPYVRVLV---NGIV----------KGRTVTISNTLNPVWDE-VLY--VPVTSPNQKi 64

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2032737686 4815 TLEvtVWDYDRFSSNDFLGEVLIELSSISQLDNTPRWYP---LKEQSENIDHGKSH 4867
Cdd:cd04045     65 TLE--VMDYEKVGKDRSLGSVEINVSDLIKKNEDGKYVEyddEEERLKRLLSLKGV 118
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
535-736 2.32e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 51.03  E-value: 2.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  535 PPSAKPSPQPQPVqkkdvtPKPDPSQAADSKRPPPqkkqtqlPGSPPVKSKQPRAEPTDISQQTDATPKSDQVKPTQAED 614
Cdd:PRK12323   374 PATAAAAPVAQPA------PAAAAPAAAAPAPAAP-------PAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQAS 440

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  615 KQKQPSVQKPTADSVSTSVAAEQKQdLAGPRPPTqqkVTDSPKPELAKPSQDTHPAGDKPdsKPVPQVSRQKSDPKFASQ 694
Cdd:PRK12323   441 ARGPGGAPAPAPAPAAAPAAAARPA-AAGPRPVA---AAAAAAPARAAPAAAPAPADDDP--PPWEELPPEFASPAPAQP 514

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 2032737686  695 PGARPDAKAQKPIDPTQTKDDPKKLPTKPAPKPDTKPAPKGP 736
Cdd:PRK12323   515 DAAPAGWVAESIPDPATADPDDAFETLAPAPAAAPAPRAAAA 556
PDZ1_ZO1-like cd06727
PDZ domain 1 of Zonula Occludens-1 (ZO-1), homologs ZO-2 and ZO-3, and related domains; PDZ ...
 4534-4615 2.45e-05

PDZ domain 1 of Zonula Occludens-1 (ZO-1), homologs ZO-2 and ZO-3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of ZO-1, -2, -3 and related domains. Zonula occludens proteins (ZO-1, ZO-2, ZO-3) are multi-PDZ domain proteins involved in the maintenance and biogenesis of multi-protein networks at the cytoplasmic surface of intercellular contacts in epithelial and endothelial cells. They have three N-terminal PDZ domains, PDZ1-3, followed by a Src homology-3 (SH3) domain and a guanylate kinase (GuK)-like domain. Among protein-protein interactions for all ZO proteins is the binding of the first PDZ domain (PDZ1) to the C-termini of claudins, and the homo- and hetero-dimerization of ZO-proteins via their second PDZ domain (PDZ2), which takes place by symmetrical domain swapping of the first two beta-strands of PDZ2. At the cell level, ZO-1 and ZO-2 are involved in polarity maintenance, gene transcription, cell proliferation, and tumor cell metastasis. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This ZO family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467209 [Multi-domain]  Cd Length: 87  Bit Score: 45.73  E-value: 2.45e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4534 HTV-----SGNGLGIRVVGGKEIPG-SSGEIGAYIAKILPGGNAEqtGKLVEGMQVLEWNGIPLTGKTYEE-VQsiIIQQ 4606
Cdd:cd06727      1 HTVtlhraPGFGFGIAVSGGRDNPHfQSGDTSIVISDVLKGGPAE--GKLQENDRVVSVNGVSMENVEHSFaVQ--ILRK 76

                           90
                   ....*....|
gi 2032737686 4607 SG-EAEICVR 4615
Cdd:cd06727     77 CGkTANITVK 86
PDZ1_LNX1_2-like cd06677
PDZ domain 1 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ ...
 4541-4605 2.48e-05

PDZ domain 1 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of LNX1 (also known as PDZ domain-containing RING finger protein 2, PDZRN2) and LNX2 (also known as PDZ domain-containing RING finger protein 1, PDZRN1), and related domains. LNX1 and LNX2 are Ring (Really Interesting New Gene) finger and PDZ domain-containing E3 ubiquitin ligases that bind to the cell fate determinant protein NUMB and mediate its ubiquitination. LNX1 can ubiquitinate a number of other ligands including PPFIA1, KLHL11, KIF7 and ERC2. LNX1 and LNX2 each have four PDZ domains. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This LNX family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467165 [Multi-domain]  Cd Length: 89  Bit Score: 45.70  E-value: 2.48e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2032737686 4541 LGIRVVGGKEIPgssgEIGAYIAKILPGGNAEQTGKLVEGMQVLEWNGIPLTGKTYEEVQSIIIQ 4605
Cdd:cd06677     17 LGISIVGGNDTP----LINIVIQEVYRDGVIARDGRLLPGDQILEVNGVDISNVTHSQARSVLRQ 77
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 195-411 2.53e-05

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 50.78  E-value: 2.53e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  195 QGKPeeQRSPAKHPTQPQSPKPavQQQGPVRPTVQQTESSKQQQQPGGPKQVQKPGHGQPadAKQDQAKQPAQPRGPQKS 274
Cdd:pfam09606  269 QGVG--GGAGQGGPGQPMGPPG--QQPGAMPNVMSIGDQNNYQQQQTRQQQQQQGGNHPA--AHQQQMNQSVGQGGQVVA 342

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  275 QPQPSEPTKPIQQqtsakpSSGPTKPSPQQPdstkvtsqtAPPTKPSSQQPGPAKQPSQQPARQGAPVKPSPQQTGpPKQ 354
Cdd:pfam09606  343 LGGLNHLETWNPG------NFGGLGANPMQR---------GQPGMMSSPSPVPGQQVRQVTPNQFMRQSPQPSVPS-PQG 406

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2032737686  355 PSQQPGPEKPSAQQAGPAKQP-PQPGSGKPPPQQtglvkQVPPQAGPTKP---PSQTVGPT 411
Cdd:pfam09606  407 PGSQPPQSHPGGMIPSPALIPsPSPQMSQQPAQQ-----RTIGQDSPGGSlntPGQSAVNS 462
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
296-664 2.58e-05

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 50.41  E-value: 2.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  296 GPTKPSPQQPdstkvTSQTAPPTKPSSQQPgPAKQPSQQPARQGAPVKPSpqQTGPPKQPSQQPGPEKPSaqQAGPAKQP 375
Cdd:COG5164      5 GPGKTGPSDP-----GGVTTPAGSQGSTKP-AQNQGSTRPAGNTGGTRPA--QNQGSTTPAGNTGGTRPA--GNQGATGP 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  376 PQPGSGKPPPQQTGlvKQVPPQAGPTKPPSQTVGPTKPlAQQAGPTKPPGQQpGPEKPPQQTQAGANQPTETAPKKtfcp 455
Cdd:COG5164     75 AQNQGGTTPAQNQG--GTRPAGNTGGTTPAGDGGATGP-PDDGGATGPPDDG-GSTTPPSGGSTTPPGDGGSTPPG---- 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  456 lctttelllhtPEKANYNTCTQCHTVVCSLCGFNPNphiteisewlclncqmqrtlGGDLAPGLGPGPQPLAPKQ-KTPI 534
Cdd:COG5164    147 -----------PGSTGPGGSTTPPGDGGSTTPPGPG--------------------GSTTPPDDGGSTTPPNKGEtGTDI 195

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  535 PPSAKPSPQPQ-PVQKKDVTPKPDPSQAADSKRPPpqkkQTQLPGSPPVKSKQPRAEPTDISQQTdatpksdqVKPTQAE 613
Cdd:COG5164    196 PTGGTPRQGPDgPVKKDDKNGKGNPPDDRGGKTGP----KDQRPKTNPIERRGPERPEAAALPAE--------LTALEAE 263

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2032737686  614 DKQKQPSVQKPTADSVSTSVAAEQKQDLAGPRPPTQQKVTDSPKPELAKPS 664
Cdd:COG5164    264 NRAANPEPATKTIPETTTVKDLATVLGKKGSDLVTNLMKKGKGTNINAALD 314
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
 283-450 2.82e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 50.63  E-value: 2.82e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  283 KPIQQQTSAKPSSGPTKPSPQQPdSTKVTSQTAPPTKPSSQQPGPAKQPSQQPArqGAPVKPSPQQTGPPKQPSQQPGPE 362
Cdd:PRK07994   360 HPAAPLPEPEVPPQSAAPAASAQ-ATAAPTAAVAPPQAPAVPPPPASAPQQAPA--VPLPETTSQLLAARQQLQRAQGAT 436

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  363 KPsaqqagPAKQPPQPGSGKPPPQQTGLVKQVPPQAGPTKPPsqtvgPTKPLAQQAGPTKPPGQQPGPE-KPPQQTQAGA 441
Cdd:PRK07994   437 KA------KKSEPAAASRARPVNSALERLASVRPAPSALEKA-----PAKKEAYRWKATNPVEVKKEPVaTPKALKKALE 505

                          170
                   ....*....|
gi 2032737686  442 NQPT-ETAPK 450
Cdd:PRK07994   506 HEKTpELAAK 515
PHA03379 PHA03379
EBNA-3A; Provisional
 319-737 2.90e-05

EBNA-3A; Provisional


Pssm-ID: 223066 [Multi-domain]  Cd Length: 935  Bit Score: 50.83  E-value: 2.90e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  319 KPSSQQPGPAKQPSQQPArqgaPVKPSPQQTGPPKQPSQQPGPEKPSAQQAGP------------AKQPPQP-GSGKPPP 385
Cdd:PHA03379   407 KASEPTYGTPRPPVEKPR----PEVPQSLETATSHGSAQVPEPPPVHDLEPGPlhdqhsmapcpvAQLPPGPlQDLEPGD 482

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  386 QQTGLVKQvpPQAGPTKPPSqtvgPTKPLAQ--QAGPTKPPGQQPGPEKPpqQTQAGANQPTET-APKKTFCPLctTTEL 462
Cdd:PHA03379   483 QLPGVVQD--GRPACAPVPA----PAGPIVRpwEASLSQVPGVAFAPVMP--QPMPVEPVPVPTvALERPVCPA--PPLI 552

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  463 LLHTPEKANyntctqchtvvcslcgfnpnpHITEISEwlclncqmqrtlggdlapglgpgpqPLAPKQKTPIPPSAkPSP 542
Cdd:PHA03379   553 AMQGPGETS---------------------GIVRVRE-------------------------RWRPAPWTPNPPRS-PSQ 585

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  543 QPQPVQKKDVTPKPDPSQAADSKRPPpqkkqtQLPGSPPvksKQPRAEPTDISQQTDATPKSDQVKPTQAEDK---QKQP 619
Cdd:PHA03379   586 MSVRDRLARLRAEAQPYQASVEVQPP------QLTQVSP---QQPMEYPLEPEQQMFPGSPFSQVADVMRAGGvpaMQPQ 656

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  620 SVQKPTADSVSTSVAAEQKQDLAGPRPP---TQQKVTDSPkpeLAKPSQDTHPAGDKPDSKPV--PQVSRQKSDPKFASQ 694
Cdd:PHA03379   657 YFDLPLQQPISQGAPLAPLRASMGPVPPvpaTQPQYFDIP---LTEPINQGASAAHFLPQQPMegPLVPERWMFQGATLS 733

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|...
gi 2032737686  695 PGARPDAKAQKPIDPTQTKDDPKKLPTKPAPKPDTKPAPKGPQ 737
Cdd:PHA03379   734 QSVRPGVAQSQYFDLPLTQPINHGAPAAHFLHQPPMEGPWVPE 776
PDZ_MPP5-like cd06798
PDZ domain of membrane palmitoylated protein 5 (MPP5), Drosophila Stardust, and related ...
 4562-4608 2.94e-05

PDZ domain of membrane palmitoylated protein 5 (MPP5), Drosophila Stardust, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MPP5, Drosophila Stardust, and related domains. MPP5 (also known as MAGUK p55 subfamily member 1, protein associated with Lin-7 1 or PALS1) and Drosophila Stardust are membrane-associated guanylate kinase (MAGUK)-like proteins that serve as signaling and scaffolding proteins, linking different proteins critical to the formation and maintenance of tight junctions (TJ) and apical-basal polarity. Apical-basal polarity determinants cluster in complexes; in particular, the Crumbs complex (Crb, MPP5, and PATJ) and the PAR/aPKC-complex (PAR-3, PAR-6, aPKC) determine the apical plasma membrane domain. Within the Crumbs complex, Crb is stabilized in the plasma membrane by MPP5, which in turn recruits PATJ and Lin-7 to the complex. MPP5 also links the Crumbs complex with the PAR/aPKC-complex. The Drosophila homolog of the Crumbs complex is the (CRB)-Stardust (Sdt)-Discs Lost (Dlt) complex. MPP5 also acts as an interaction partner for SARS-CoV envelope protein E, which results in delayed formation of TJs and dysregulation of cell polarity. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MPP5-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467259 [Multi-domain]  Cd Length: 79  Bit Score: 45.41  E-value: 2.94e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 2032737686 4562 IAKILPGGNAEQTGKLVEGMQVLEWNGIPLTGKTYEEVQSIIIQQSG 4608
Cdd:cd06798     25 ISRIVKGGAAEKSGLLHEGDEILEINGIEIRGKDVNEVCDLLADMHG 71
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 319-446 3.62e-05

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 50.10  E-value: 3.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  319 KPSSQQPGPAKQPSQQPARQGAPvKPSPQqtgPPKQPSQQPGPEKPSAQQAGPAKQPPQPGSGKPPPQQTGLVKQVPPQA 398
Cdd:PRK14951   365 KPAAAAEAAAPAEKKTPARPEAA-APAAA---PVAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVAAPAAAAPAAAPAA 440

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2032737686  399 GPT----KPPSQTVGPTKPLAQQAGPTKPPGQQPGPEKPPQQTQAGANQPTE 446
Cdd:PRK14951   441 APAavalAPAPPAQAAPETVAIPVRVAPEPAVASAAPAPAAAPAAARLTPTE 492
PRK08691 PRK08691
DNA polymerase III subunits gamma and tau; Validated
 527-725 3.84e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236333 [Multi-domain]  Cd Length: 709  Bit Score: 50.09  E-value: 3.84e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  527 APKQKTPIPPSAKPSPQPQPVQKKDVTPKPDPSQAAdskrPPPQKKQTQLPGSPPVKSKQPRAEPTDISQQTDATpksdq 606
Cdd:PRK08691   379 SPSAQTAEKETAAKKPQPRPEAETAQTPVQTASAAA----MPSEGKTAGPVSNQENNDVPPWEDAPDEAQTAAGT----- 449

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  607 vKPTQAEDKQKQPSVQKPTADSVSTSVAAEQKQDLAGPRPPTQQKVTDSPKPELAKPSQDTHPAGDKP--------DSKP 678
Cdd:PRK08691   450 -AQTSAKSIQTASEAETPPENQVSKNKAADNETDAPLSEVPSENPIQATPNDEAVETETFAHEAPAEPfygygfpdNDCP 528

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 2032737686  679 VPQVSRQKSDPKFASQPGARPDAKAQKPIDPTQTKDDPkkLPTKPAP 725
Cdd:PRK08691   529 PEDGAEIPPPDWEHAAPADTAGGGADEEAEAGGIGGNN--TPSAPPP 573
PRK11901 PRK11901
hypothetical protein; Reviewed
 281-452 3.86e-05

hypothetical protein; Reviewed


Pssm-ID: 237015 [Multi-domain]  Cd Length: 327  Bit Score: 49.30  E-value: 3.86e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  281 PTKPIQQQTSAKPS-------SGPTKPSPQQPDSTKVTSQTAPPTKPSSQQPGPAKQPSQQPARQGAPVKPSPQQTGPPK 353
Cdd:PRK11901    61 PTEHESQQSSNNAGaeknidlSGSSSLSSGNQSSPSAANNTSDGHDASGVKNTAPPQDISAPPISPTPTQAAPPQTPNGQ 140

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  354 QPSQQPG--PEKPSAQQA---GPAKQPPQPGSGKPPPQQTglvkqvppQAGPTKPPSQTVGPTKPLAQQAGPTKPPGQQP 428
Cdd:PRK11901   141 QRIELPGniSDALSQQQGqvnAASQNAQGNTSTLPTAPAT--------VAPSKGAKVPATAETHPTPPQKPATKKPAVNH 212

                          170       180
                   ....*....|....*....|....
gi 2032737686  429 GPEKPPQQTQAGANQPTETAPKKT 452
Cdd:PRK11901   213 HKTATVAVPPATSGKPKSGAASAR 236
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
283-449 4.05e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 50.26  E-value: 4.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  283 KPIQQQTSAKPSSGPTKPSPQQ-PDSTKVTSQTAPPTKPSSQQPGPAKQPSQQPARQGAPVKPSPQQTgpPKQPSQQPGP 361
Cdd:PRK12323   364 RPGQSGGGAGPATAAAAPVAQPaPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPE--ALAAARQASA 441

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  362 EKPSAQQAGPAKQPPQPGSGKPPPQqtglvkqvppqAGPTKPPSQTVGPTKPLAQQAGPTKPPGQQPGPEKPPQQTQAGA 441
Cdd:PRK12323   442 RGPGGAPAPAPAPAAAPAAAARPAA-----------AGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPA 510


                   ....*...
gi 2032737686  442 NQPTETAP 449
Cdd:PRK12323   511 PAQPDAAP 518
dnaA PRK14086
chromosomal replication initiator protein DnaA;
508-736 4.40e-05

chromosomal replication initiator protein DnaA;


Pssm-ID: 237605 [Multi-domain]  Cd Length: 617  Bit Score: 49.82  E-value: 4.40e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  508 QRTLGGDLAP--------GLGPGPQPLAPKQKTPIPPSAKPSPQPQPVQKKDVTPKPDPSQA----ADSKRPPPQKKQTQ 575
Cdd:PRK14086    59 KEVLEGRLAPiisetlsrELGRPIRIAITVDPSAGEPAPPPPHARRTSEPELPRPGRRPYEGyggpRADDRPPGLPRQDQ 138

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  576 LPGSPPV-KSKQPRAEPTDI-SQQTDATPKSDQVKPTQAEDkQKQPSVQKPTADSVSTSVAAEQKQDLAGPRPPtqqkvt 653
Cdd:PRK14086   139 LPTARPAyPAYQQRPEPGAWpRAADDYGWQQQRLGFPPRAP-YASPASYAPEQERDREPYDAGRPEYDQRRRDY------ 211

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  654 DSPKPELAKPSQDTHpagDKPDSKPvpqvsrQKSDPKFASQPGARPDAKAQKPIDPtqtkddpkKLPTKPAPKPDTKPAP 733
Cdd:PRK14086   212 DHPRPDWDRPRRDRT---DRPEPPP------GAGHVHRGGPGPPERDDAPVVPIRP--------SAPGPLAAQPAPAPGP 274


                   ...
gi 2032737686  734 KGP 736
Cdd:PRK14086   275 GEP 277
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
 327-409 4.51e-05

pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.


Pssm-ID: 468201 [Multi-domain]  Cd Length: 684  Bit Score: 50.01  E-value: 4.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  327 PAKQPSQQPARQgaPVKPSPQqtgpPKQPSQQPGPEKPSAQQAGPAKQPPQPGSGKPPPQQtglvkQVPPQAGPTKPPSQ 406
Cdd:NF033838   416 PAEQPQPAPAPQ--PEKPAPK----PEKPAEQPKAEKPADQQAEEDYARRSEEEYNRLTQQ-----QPPKTEKPAQPSTP 484


                   ...
gi 2032737686  407 TVG 409
Cdd:NF033838   485 KTG 487
C2_Perforin cd04032
C2 domain of Perforin; Perforin contains a single copy of a C2 domain in its C-terminus and ...
 4735-4841 4.64e-05

C2 domain of Perforin; Perforin contains a single copy of a C2 domain in its C-terminus and plays a role in lymphocyte-mediated cytotoxicity. Mutations in perforin leads to familial hemophagocytic lymphohistiocytosis type 2. The function of perforin is calcium dependent and the C2 domain is thought to confer this binding to target cell membranes. 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.


Pssm-ID: 175998 [Multi-domain]  Cd Length: 127  Bit Score: 46.10  E-value: 4.64e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4735 LGNLIIHILQARNLaprdnNG----YSDPFVKVYLlpgRGQVmvvqnasaeykRRTKYIQKSLNPEWNQTVIYKNISVEQ 4810
Cdd:cd04032     27 LATLTVTVLRATGL-----WGdyftSTDGYVKVFF---GGQE-----------KRTEVIWNNNNPRWNATFDFGSVELSP 87

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2032737686 4811 LKKKTLEVtvWDYDRFSSNDFLGEVLIELSS 4841
Cdd:cd04032     88 GGKLRFEV--WDRDNGWDDDLLGTCSVVPEA 116
C2C_Ferlin cd04018
C2 domain third repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and ...
 4751-4844 4.69e-05

C2 domain third repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and other proteins, such as Synaptotagmins, are implicated in facilitating the fusion process when cell membranes fuse together. There are six known human Ferlins: Dysferlin (Fer1L1), Otoferlin (Fer1L2), Myoferlin (Fer1L3), Fer1L4, Fer1L5, and Fer1L6. Defects in these genes can lead to a wide range of diseases including muscular dystrophy (dysferlin), deafness (otoferlin), and infertility (fer-1, fertilization factor-1). Structurally they have 6 tandem C2 domains, designated as (C2A-C2F) and a single C-terminal transmembrane domain, though there is a new study that disputes this and claims that there are actually 7 tandem C2 domains with another C2 domain inserted between C2D and C2E. In a subset of them (Dysferlin, Myoferlin, and Fer1) there is an additional conserved domain called DysF. 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.


Pssm-ID: 175985 [Multi-domain]  Cd Length: 151  Bit Score: 46.86  E-value: 4.69e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4751 RDNNGYSDPFVKVYLLpgrGQvmvvqnasaeyKRRTKYIQKSLNPEWNQTVIYKnisvEQLKK--KTLEVTVWDYDRFSS 4828
Cdd:cd04018     29 GEKKELVDPYVEVSFA---GQ-----------KVKTSVKKNSYNPEWNEQIVFP----EMFPPlcERIKIQIRDWDRVGN 90

                           90
                   ....*....|....*.
gi 2032737686 4829 NDFLGEVLIELSSISQ 4844
Cdd:cd04018     91 DDVIGTHFIDLSKISN 106
C2_putative_Elicitor-responsive_gene cd04049
C2 domain present in the putative elicitor-responsive gene; In plants elicitor-responsive ...
 4736-4861 5.58e-05

C2 domain present in the putative elicitor-responsive gene; In plants elicitor-responsive proteins are triggered in response to specific elicitor molecules such as glycolproteins, peptides, carbohydrates and lipids. A host of defensive responses are also triggered resulting in localized cell death. Antimicrobial secondary metabolites, such as phytoalexins, or defense-related proteins, including pathogenesis-related (PR) proteins are also produced. There is a single C2 domain present here. 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. Members have a type-II topology.


Pssm-ID: 176014 [Multi-domain]  Cd Length: 124  Bit Score: 45.79  E-value: 5.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4736 GNLIIHILQARNLAPRDNNGYSDPFVkvyLLPGRGQVmvvqnasaeykRRTKyIQKSL--NPEWNQTVIYkNISVEQLKK 4813
Cdd:cd04049      1 GTLEVLLISAKGLQDTDFLGKIDPYV---IIQCRTQE-----------RKSK-VAKGDgrNPEWNEKFKF-TVEYPGWGG 64

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2032737686 4814 KT-LEVTVWDYDRFSSNDFLGEVLIELSSISQLDNTPRWYPLKEQSENI 4861
Cdd:cd04049     65 DTkLILRIMDKDNFSDDDFIGEATIHLKGLFEEGVEPGTAELVPAKYNV 113
motB PRK05996
MotB family protein;
246-448 5.67e-05

MotB family protein;


Pssm-ID: 235665 [Multi-domain]  Cd Length: 423  Bit Score: 49.31  E-value: 5.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  246 VQKPGHGQPADAKQDQAKQpaqprgpQKSQPQPSEPTKPIQQQTSakPSSGPTKPSPQQ----PDST-----KVTSQTAP 316
Cdd:PRK05996    83 LKDPVDGAEGEQKPGKSKF-------EEDQRVEGSSAVTGDDTTR--TSGDQTNYSEADlfrnPYAVlaeiaQEVGQQAN 153

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  317 PTKP---SSQQPGPA---------KQP------SQQPARQGAPVKPSPqqtGPPKQPSQQPGPEKPSAQQAGPAKQPPQP 378
Cdd:PRK05996   154 VSAKgdgGAAQSGPAtgadggeayRDPfdpdfwSKQVEVTTAGDLLPP---GQAREQAQGAKSATAAPATVPQAAPLPQA 230

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  379 GSGKPPpqqtglvKQVPPQAGPTKppsqtvgptkplAQQAGPTKPPGQQPGPEKPPQQTQAGANQPTETA 448
Cdd:PRK05996   231 QPKKAA-------TEEELIADAKK------------AATGEPAANAAKAAKPEPMPDDQQKEAEQLQAAI 281
PDZ_Radil-like cd06690
PDZ domain of Ras-associating and dilute domain-containing protein (Radil) and related domains; ...
 4538-4609 5.81e-05

PDZ domain of Ras-associating and dilute domain-containing protein (Radil) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of Radil (also known as protein KIAA1849) and related domains. Radil is required for cell adhesion and migration of neural crest precursors during development. Radil is a component of a Rasip1-Radil-ARHGAP29 complex at endothelial cell-cell junctions. Rap1, via its effectors Radil and Rasip1 and their binding partner ArhGAP29, controls the endothelial barrier by decreasing Rho-mediated radial tension on cell-cell junctions. ArhGAP29 binds the Radil PDZ domain. The Radil PDZ domain also binds kinesin family protein 14 (KIF14); KIF14 negatively regulates Rap1-mediated inside-out integrin activation by tethering Radil on microtubules. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Radil-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467177 [Multi-domain]  Cd Length: 88  Bit Score: 44.59  E-value: 5.81e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2032737686 4538 GNGLGIRVVGGKEIPGSSGeiGAYIAKILPGGNAEQTGKLVEGMQVLEWNGIPLTGKTYEEVQSiIIQQSGE 4609
Cdd:cd06690     12 PKGLGLGLIDGLHTPLRSP--GIYIRTLVPDSPAARDGRLRLGDRILAVNGTSLVGADYQSAMD-LIRTSGD 80
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
 251-397 6.06e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 49.48  E-value: 6.06e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  251 HGQPADAKQDQAKQPAQPRGPQKSQPQPSEPTKPIQQQTSAKPSSGPTKPSPQQPDSTKVTSQTAPPTKPSSQQPGPAKQ 330
Cdd:PRK07994   360 HPAAPLPEPEVPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPASAPQQAPAVPLPETTSQLLAARQQLQRAQGATKAK 439

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2032737686  331 PSQQPARQGAPVKPSPQQTGPPKQPSQQPGPEKPSAQQAGPAKQPPQPGSGKPPPQQTGLVKQVPPQ 397
Cdd:PRK07994   440 KSEPAAASRARPVNSALERLASVRPAPSALEKAPAKKEAYRWKATNPVEVKKEPVATPKALKKALEH 506
PDZ_AFDN-like cd06789
PDZ domain of afadin (AFDN), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95) ...
 4538-4608 6.10e-05

PDZ domain of afadin (AFDN), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of afadin (AFDN, also known as ALL1-fused gene from chromosome 6 protein (AF6) and MLLT4), and related domains. AFDN belongs to the adhesion system, probably together with the E-cadherin-catenin system, that plays a role in the organization of homotypic, interneuronal, and heterotypic cell-cell adherens junctions. The AFDN PDZ domain interaction partners include poliovirus receptor-related protein PRR2/nectin, the junctional adhesion molecule (JAM), the breakpoint-cluster-region protein (BCR), connexin36 (Cx36), and a subset of Eph-related receptor tyrosine kinases; it can also bind low molecular weight ligands, in competition with a natural peptide ligand. Other AFDN-binding proteins have been identified. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This AFDN family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467251 [Multi-domain]  Cd Length: 89  Bit Score: 44.58  E-value: 6.10e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2032737686 4538 GNGLGIRVVGGKeipGS-SGEIGAYIAKILPGGNAEQTGKLVEGMQVLEWNGIPLTGKTYEEVQSiIIQQSG 4608
Cdd:cd06789     12 GNGMGLSIVAAK---GAgQDKLGIYIKSVVKGGAADLDGRLQAGDQLLSVDGHSLVGLSQERAAE-LMTKTG 79
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 119-428 6.97e-05

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 49.69  E-value: 6.97e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  119 RAPGRSPSTLSLRE-SKSRTDFKEDQKPSMMPSFLSEANPLSAVTSVVNKFNPFdlisdsdtSHEEAGRKQKVAPKEQGK 197
Cdd:PTZ00449   522 KAPGDKEGEEGEHEdSKESDEPKEGGKPGETKEGEVGKKPGPAKEHKPSKIPTL--------SKKPEFPKDPKHPKDPEE 593

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  198 PEEQRSP--AKHPTQPQSPKpavqqqgpvRPTVQQTESSKqqqqpggpkqvqkpghgqpadakqdqaKQPAQPRGPqKSQ 275
Cdd:PTZ00449   594 PKKPKRPrsAQRPTRPKSPK---------LPELLDIPKSP---------------------------KRPESPKSP-KRP 636

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  276 PQPSEPTKPIQQQTSAKPSSGPTKPSPQQP----------DSTKVTSQTAPPTKPSSQQPGPAKQPSQQPARQGAPVKPS 345
Cdd:PTZ00449   637 PPPQRPSSPERPEGPKIIKSPKPPKSPKPPfdpkfkekfyDDYLDAAAKSKETKTTVVLDESFESILKETLPETPGTPFT 716

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  346 PQQTGPPKQPSQQPGPEKPSAQQAGPAKQPPQPGSgkPPPQQTGLVKQVP---PQAGPT----KPP---SQTVGPTKPLA 415
Cdd:PTZ00449   717 TPRPLPPKLPRDEEFPFEPIGDPDAEQPDDIEFFT--PPEEERTFFHETPadtPLPDILaeefKEEdihAETGEPDEAMK 794

                          330
                   ....*....|....*..
gi 2032737686  416 QQAGPTK----PPGQQP 428
Cdd:PTZ00449   795 RPDSPSEhedkPPGDHP 811
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
300-569 7.59e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 49.46  E-value: 7.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  300 PSPQQPDSTKVTSQTAPPTKPSSQQPGPAKQPSQQPARQGAPVKPSPQQTGPPK--QPSQQPGPEKPSAQQAGPAKQPPQ 377
Cdd:PRK07003   381 PAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPPAtaDRGDDAADGDAPVPAKANARASAD 460

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  378 PGSGKPPPQQtglVKQVPPQAGPTKPpsqtvGPTKPLAQQAGPTKPPGQQPGPEKPPQQTQAGANQPTETAPKKTFCPLC 457
Cdd:PRK07003   461 SRCDERDAQP---PADSGSASAPASD-----APPDAAFEPAPRAAAPSAATPAAVPDARAPAAASREDAPAAAAPPAPEA 532

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  458 TTTELLLHTPekANYNTCTQCHTVVCSLCGfnpnphiteisewLCLNCQMQRTLGGDLAPglgPGPQPLAPKQKTPIPPS 537
Cdd:PRK07003   533 RPPTPAAAAP--AARAGGAAAALDVLRNAG-------------MRVSSDRGARAAAAAKP---AAAPAAAPKPAAPRVAV 594

                          250       260       270
                   ....*....|....*....|....*....|...
gi 2032737686  538 AKPSPQ-PQPVQKKDVTPKPDPSQAADSKRPPP 569
Cdd:PRK07003   595 QVPTPRaRAATGDAPPNGAARAEQAAESRGAPP 627
PHA03269 PHA03269
envelope glycoprotein C; Provisional
 272-385 7.61e-05

envelope glycoprotein C; Provisional


Pssm-ID: 165527 [Multi-domain]  Cd Length: 566  Bit Score: 48.96  E-value: 7.61e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  272 QKSQPQPsEPTKpiQQQTSAKPSSGPTKPSPQQPDSTKVtsqtapPTKPSSQQPGPAKQPSQQPARQGAPVkPSPQQTGP 351
Cdd:PHA03269    38 QKPDPAP-APHQ--AASRAPDPAVAPTSAASRKPDLAQA------PTPAASEKFDPAPAPHQAASRAPDPA-VAPQLAAA 107

                           90       100       110
                   ....*....|....*....|....*....|....
gi 2032737686  352 PKQPSQQPGPEKPSAQQAgPAKQPPQPGSGKPPP 385
Cdd:PHA03269   108 PKPDAAEAFTSAAQAHEA-PADAGTSAASKKPDP 140
PRK11901 PRK11901
hypothetical protein; Reviewed
 259-405 8.07e-05

hypothetical protein; Reviewed


Pssm-ID: 237015 [Multi-domain]  Cd Length: 327  Bit Score: 48.53  E-value: 8.07e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  259 QDQAKQPAQPRGPQK---------------SQPQPSEPTKPIQQQTSAKPSSGPTKPSPQQPDSTkvTSQTAPPTKPSSQ 323
Cdd:PRK11901    63 EHESQQSSNNAGAEKnidlsgssslssgnqSSPSAANNTSDGHDASGVKNTAPPQDISAPPISPT--PTQAAPPQTPNGQ 140

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  324 Q----PGP-AKQPSQQPARQGAPVK--PSPQQTGPPKQPSQQPGPEKPSAQQAGPAKQPPQPGSG-KPPPQQTGLVKQVP 395
Cdd:PRK11901   141 QrielPGNiSDALSQQQGQVNAASQnaQGNTSTLPTAPATVAPSKGAKVPATAETHPTPPQKPATkKPAVNHHKTATVAV 220

                          170
                   ....*....|
gi 2032737686  396 PQAGPTKPPS 405
Cdd:PRK11901   221 PPATSGKPKS 230
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
 325-422 8.19e-05

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 49.04  E-value: 8.19e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  325 PGPAKQPSQQPARQGAPVKPSPQQTGPPKQPSQQPGPEK-PSAQQAGPAKQPPQPGSGKPPPqqtglvkqvPPQAGPTKP 403
Cdd:PRK14950   362 PVPAPQPAKPTAAAPSPVRPTPAPSTRPKAAAAANIPPKePVRETATPPPVPPRPVAPPVPH---------TPESAPKLT 432

                           90
                   ....*....|....*....
gi 2032737686  404 PSQTVGPTKPLAQQAGPTK 422
Cdd:PRK14950   433 RAAIPVDEKPKYTPPAPPK 451
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 328-736 9.34e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 49.40  E-value: 9.34e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  328 AKQPSQQPARQGAPVKPSPQQtGPPKQPSQQPGPEKPSAQQAGPAKQPPQPGSGKPPPqqtGLVKQVPPQAGPTKPPSQT 407
Cdd:PHA03307    17 GGEFFPRPPATPGDAADDLLS-GSQGQLVSDSAELAAVTVVAGAAACDRFEPPTGPPP---GPGTEAPANESRSTPTWSL 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  408 VGPTKPLAQQAGPTKPPGQQPGPEKPPqqtqagANQPTETAPKktfcplctttelllhtpekanyntctqchtvvcslcg 487
Cdd:PHA03307    93 STLAPASPAREGSPTPPGPSSPDPPPP------TPPPASPPPS------------------------------------- 129

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  488 fnPNPHITEisewlclncqmqrtlggDLAPGLGPGPQPLAPKQKTPIPPSAKPSPQPQPVQKKDVTPKPDpsqaaDSKRP 567
Cdd:PHA03307   130 --PAPDLSE-----------------MLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPE-----ETARA 185

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  568 PPqkkqtqlPGSPPVKSKQPRAEPTDISQQTDATPKSDQVKPTQA-EDKQKQPSVQKPTADSVSTSVAAEQKQDLAGPRP 646
Cdd:PHA03307   186 PS-------SPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPApGRSAADDAGASSSDSSSSESSGCGWGPENECPLP 258

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  647 PTQQKVTDSPKPELAKPSqdtHPAGDKPDSKPV--PQVSRQKSDPKFASQPGARPDAKAQKPIDPTQTKDDPKKLPTKPA 724
Cdd:PHA03307   259 RPAPITLPTRIWEASGWN---GPSSRPGPASSSssPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSES 335

                          410
                   ....*....|..
gi 2032737686  725 pkPDTKPAPKGP 736
Cdd:PHA03307   336 --SRGAAVSPGP 345
dnaA PRK14086
chromosomal replication initiator protein DnaA;
271-452 9.44e-05

chromosomal replication initiator protein DnaA;


Pssm-ID: 237605 [Multi-domain]  Cd Length: 617  Bit Score: 49.05  E-value: 9.44e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  271 PQKSQPQPSEPTKPIQQQTSAKPSSGPTKPSPQQPDSTKVTSQTAPPTKP---------SSQQPGPAKQPSQQPARQGAP 341
Cdd:PRK14086    68 PIISETLSRELGRPIRIAITVDPSAGEPAPPPPHARRTSEPELPRPGRRPyegyggpraDDRPPGLPRQDQLPTARPAYP 147

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  342 VKPSPQQTGPPKQPSQQPGPEK------PSAQQAGPAKQPPQPGSGKPPPQQTglvkqvPPQAGPTKPPSQTVGP--TKP 413
Cdd:PRK14086   148 AYQQRPEPGAWPRAADDYGWQQqrlgfpPRAPYASPASYAPEQERDREPYDAG------RPEYDQRRRDYDHPRPdwDRP 221

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 2032737686  414 LAQQagpTKPPGQQPGPEKPPQQTQAGANQPTETAPKKT 452
Cdd:PRK14086   222 RRDR---TDRPEPPPGAGHVHRGGPGPPERDDAPVVPIR 257
C2_Smurf-like cd08382
C2 domain present in Smad ubiquitination-related factor (Smurf)-like proteins; A single C2 ...
 4742-4850 9.64e-05

C2 domain present in Smad ubiquitination-related factor (Smurf)-like proteins; A single C2 domain is found in Smurf proteins, C2-WW-HECT-domain E3s, which play an important role in the downregulation of the TGF-beta signaling pathway. Smurf proteins also regulate cell shape, motility, and polarity by degrading small guanosine triphosphatases (GTPases). 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. Members here have type-II topology.


Pssm-ID: 176028 [Multi-domain]  Cd Length: 123  Bit Score: 44.99  E-value: 9.64e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4742 ILQARNLAPRDNNGYSDPFVKVyLLPGrGQVmvvqnasaeykRRTKYIQKSLNPEWNQTviYKnISVEqlKKKTLEVTVW 4821
Cdd:cd08382      6 VLCADGLAKRDLFRLPDPFAVI-TVDG-GQT-----------HSTDVAKKTLDPKWNEH--FD-LTVG--PSSIITIQVF 67

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2032737686 4822 DYDRFSSND--FLGEVLIELSSISQLDNTPR 4850
Cdd:cd08382     68 DQKKFKKKDqgFLGCVRIRANAVLPLKDTGY 98
PDZ10_MUPP1-PDZ8_PATJ-like cd06673
PDZ domain 10 of multi-PDZ-domain protein 1 (MUPP1), domain 8 of PATJ (protein-associated ...
 4540-4599 1.04e-04

PDZ domain 10 of multi-PDZ-domain protein 1 (MUPP1), domain 8 of PATJ (protein-associated tight junction) and similar domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 10 of MUPP1, PDZ domain 8 of PATJ, and related domains. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, 9, and 13; consequently, MUPP1 PDZ7 and 8 align with PATJ PDZ6 and 7; and MUPP1 PDZ domains 10-12 align with PATJ PDZ domains 8-10. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like family PDZ10 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467161 [Multi-domain]  Cd Length: 86  Bit Score: 43.82  E-value: 1.04e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2032737686 4540 GLGIRVVGGKEIPgssgeIGA-YIAKILPGGNAEQTGKLVEGMQVLEWNGIPLTGKTYEEV 4599
Cdd:cd06673     14 GLGLSIVGGSDTL-----LGAiIIHEVYEDGAAAKDGRLWAGDQILEVNGEDLRKATHDEA 69
Aim21 pfam11489
Altered inheritance of mitochondria protein 21; This is a family of proteins conserved in ...
 203-414 1.11e-04

Altered inheritance of mitochondria protein 21; This is a family of proteins conserved in yeasts. Saccharomyces cerevisiae Aim21 may be involved in mitochondrial migration along actin filament. It may also interact with ribosomes.


Pssm-ID: 371558 [Multi-domain]  Cd Length: 677  Bit Score: 48.81  E-value: 1.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  203 SPAKHPTQPQSPKPAVQQQGPV-RPTVQQTESSKQQQQPGGPKQVQKPGHGQPADAKQDQAKQPAQPRGPQKSQPQPSEP 281
Cdd:pfam11489  426 SPSSLQLTATVSTPSNPPPRAFeTPEQETSSSSSEPSLDDQSELKSEDVKERPEVKAQRFPSRDVWEDAPESQELVTTVE 505

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  282 TKPIQQQTSAKPSSGPTKPS-PQQPDSTKVTSQTAPPT---KPSSQQPgpakqpsqqparqGAPVKPSPQQTGPPKQPSQ 357
Cdd:pfam11489  506 TPDEVKSTSPGVPTKPAIPArPKSGKPTSPTEKRKPPPvpkKPKPQIP-------------ARPAKAQPQQAGEEFKPKP 572

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2032737686  358 ----QPGPEKPSAQQAGPAKQ-PPQPGSGKPPPQQTGLVKQVPPQAGPTKPPSQTVGPTKPL 414
Cdd:pfam11489  573 rvpaRPGGSKISALRAGFASDlNGRLQLGPQAPKKVVEEDKEPSEEKGDKEEEEDTKEKAPL 634
PHA03169 PHA03169
hypothetical protein; Provisional
 196-453 1.13e-04

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 48.43  E-value: 1.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  196 GKPEEQRSPAKHPTQPQSPKPAVQQQGPVRPTVQQTESSKQQQQPGGPKQVQKPGHGQPADAKQDQAKQP------AQPR 269
Cdd:PHA03169    34 GRRRGTAARAAKPAPPAPTTSGPQVRAVAEQGHRQTESDTETAEESRHGEKEERGQGGPSGSGSESVGSPtpspsgSAEE 113

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  270 GPQKSQPQPSEPTKPIQQQTSAKPSSGPTKPSPQQP--------DSTKVTSQTAPPTKPSSQQPGPAKQPSQQPARQGAP 341
Cdd:PHA03169   114 LASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPappeshnpSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPP 193

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  342 VKPSPQQTGPPKQPSQQPGPEKPSAQQAGPAKQPPQPGSGKPPPqqTGLVKQVPPQAGPTKPPSQTVG---PTKPLAQQA 418
Cdd:PHA03169   194 QSETPTSSPPPQSPPDEPGEPQSPTPQQAPSPNTQQAVEHEDEP--TEPEREGPPFPGHRSHSYTVVGwkpSTRPGGVPK 271

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 2032737686  419 GPTKPPGQQPGPEKPPQQTQAGANQPTETAPKKTF 453
Cdd:PHA03169   272 LCLRCTSHPSHRSRLPEGQQSEDKVPRKYQARRRF 306
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
 312-414 1.15e-04

Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem to regulate formation of crystallites during the secretory stage of tooth enamel development and are thought to play a major role in the structural organisation and mineralisation of developing enamel. The extracellular matrix of the developing enamel comprises two major classes of protein: the hydrophobic amelogenins and the acidic enamelins. Circular dichroism studies of porcine amelogenin have shown that the protein consists of 3 discrete folding units: the N-terminal region appears to contain beta-strand structures, while the C-terminal region displays characteristics of a random coil conformation. Subsequent studies on the bovine protein have indicated the amelogenin structure to contain a repetitive beta-turn segment and a "beta-spiral" between Gln112 and Leu138, which sequester a (Pro, Leu, Gln) rich region. The beta-spiral offers a probable site for interactions with Ca2+ ions. Muatations in the human amelogenin gene (AMGX) cause X-linked hypoplastic amelogenesis imperfecta, a disease characterised by defective enamel. A 9bp deletion in exon 2 of AMGX results in the loss of codons for Ile5, Leu6, Phe7 and Ala8, and replacement by a new threonine codon, disrupting the 16-residue (Met1-Ala16) amelogenin signal peptide.


Pssm-ID: 197891 [Multi-domain]  Cd Length: 165  Bit Score: 45.94  E-value: 1.15e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686   312 SQTAPPTKPSSQQPGPAKQPSQQPARQGAPVKPSPQQtgPPKQPSQQPGPEKPSAQQAGPAKQPPQPGSGKPPPQQTGLV 391
Cdd:smart00818   43 SQQHPPTHTLQPHHHIPVLPAQQPVVPQQPLMPVPGQ--HSMTPTQHHQPNLPQPAQQPFQPQPLQPPQPQQPMQPQPPV 120

                            90       100
                    ....*....|....*....|...
gi 2032737686   392 KQVPPQagPTKPPSQTVGPTKPL 414
Cdd:smart00818  121 HPIPPL--PPQPPLPPMFPMQPL 141
VCX_VCY pfam15231
Variable charge X/Y family; The variable charge X/Y (VCX/VCY) family of proteins has members ...
 252-372 1.19e-04

Variable charge X/Y family; The variable charge X/Y (VCX/VCY) family of proteins has members on the Human X and Y chromosomes, is expressed in male germ calls and may play a role in spermatogenesis or in sex ratio distortion.


Pssm-ID: 434553 [Multi-domain]  Cd Length: 130  Bit Score: 45.18  E-value: 1.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  252 GQPADAKQdqakqpaQPRGPQKSQPQPSEPTKPIQQQTSAKPSsGPTKPSPQQPDSTKVTSQTAPPTKPSSQQPGPAKQP 331
Cdd:pfam15231    9 GPPAKAKE-------AGKRKSISLLSFQDPKKKEGKRAKAGKA-GRGGKRGKKAAAKKMAAVGAPEAESGPAAPGPSDQP 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2032737686  332 SQQPARQGAPVKPSPQQTGPPKQP-SQQPGPEKPSAQQAGPA 372
Cdd:pfam15231   81 SQELPPCELPPEEEPVSEGTQHDPlSQESELEDPLNQESEPE 122
C2A_SLP-1_2 cd08393
C2 domain first repeat present in Synaptotagmin-like proteins 1 and 2; All Slp members ...
 5097-5222 1.24e-04

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.


Pssm-ID: 176039 [Multi-domain]  Cd Length: 125  Bit Score: 44.73  E-value: 1.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 5097 GEIKIALKKEMKTdgEQLIVEILQCRNITYKFKSPDHlPDLYVKLYVVNISTqkRVIKKKTRVCRHDREPSFNETFRFSL 5176
Cdd:cd08393      2 GSVQFALDYDPKL--RELHVHVIQCQDLAAADPKKQR-SDPYVKTYLLPDKS--NRGKRKTSVKKKTLNPVFNETLRYKV 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 2032737686 5177 SPAGHSLQILLVS--NGGKFMKKTLIGEAYIWLDKVDLRKRIVNWHKL 5222
Cdd:cd08393     77 EREELPTRVLNLSvwHRDSLGRNSFLGEVEVDLGSWDWSNTQPTWYPL 124
Androgen_recep pfam02166
Androgen receptor;
246-448 1.27e-04

Androgen receptor;


Pssm-ID: 426632 [Multi-domain]  Cd Length: 501  Bit Score: 48.38  E-value: 1.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  246 VQKPGHGQPADAKqdqAKQPAQPRGPQKSQPQPSEPTKPIQQQTSakpssgptkpsPQQPDSTKVTSQTAPPTKPSSQQP 325
Cdd:pfam02166   29 IQNPGPRHPEAAG---GAAPPGARLQHQQQQQQQVPQQPQQQESS-----------PRQPQASVQPQQAGDDGSPPAHNR 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  326 GPAKQPSQQPARQGAPVKPSPQQTGPPKQPSqQPGPEKPSAQQAGPAKQPPQPGsgkPPPQQTGLVKQVPPQAGPTKPP- 404
Cdd:pfam02166   95 GPAGYLALEDDEQPQPSQAQPAAECCPENGC-VPEPGAAAAAGKGLPQQAVAPA---APDDDDSAAPSTLSLLGPSFPGl 170

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 2032737686  405 SQTVGPTKPLAQQAGpTKPPGQQPGPEKPPQQTQAGANQPTETA 448
Cdd:pfam02166  171 SGCSADLKDILAEAG-TMQLLQQQQQEHHHQQHQHQQQQQQEAA 213
C2B_Synaptotagmin-12 cd08406
C2 domain second repeat present in Synaptotagmin 12; Synaptotagmin is a membrane-trafficking ...
 5112-5178 1.32e-04

C2 domain second repeat present in Synaptotagmin 12; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Synaptotagmin 12, a member of class 6 synaptotagmins, is located in the brain. It functions are unknown. It, like synaptotagmins 8 and 13, do not have any consensus Ca2+ binding sites. 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.


Pssm-ID: 176051 [Multi-domain]  Cd Length: 136  Bit Score: 45.17  E-value: 1.32e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2032737686 5112 EQLIVEILQCRNITYKFKSPDHlpDLYVKLYVvnISTQKRVIKKKTRVCRHDREPSFNETFRFSLSP 5178
Cdd:cd08406     15 ERLTVVVVKARNLVWDNGKTTA--DPFVKVYL--LQDGRKISKKKTSVKRDDTNPIFNEAMIFSVPA 77
C2B_Synaptotagmin-4 cd08404
C2 domain second repeat present in Synaptotagmin 4; Synaptotagmin is a membrane-trafficking ...
 5097-5222 1.37e-04

C2 domain second repeat present in Synaptotagmin 4; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Synaptotagmin 4, a member of class 4 synaptotagmins, is located in the brain. It functions are unknown. It, like synaptotagmin-11, has an Asp to Ser substitution in its C2A domain. 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.


Pssm-ID: 176049 [Multi-domain]  Cd Length: 136  Bit Score: 45.11  E-value: 1.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 5097 GEIKIALKKEMKTDgeQLIVEILQCRNITykfKSPDHLP-DLYVKLYVvnISTQKRVIKKKTRVCRHDREPSFNETFRFS 5175
Cdd:cd08404      2 GELLLSLCYQPTTN--RLTVVVLKARHLP---KMDVSGLaDPYVKVNL--YYGKKRISKKKTHVKKCTLNPVFNESFVFD 74

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2032737686 5176 LSPAG--HSLQILLVSNGGKFMKKTLIGEAYI-----------WLDKVD-LRKRIVNWHKL 5222
Cdd:cd08404     75 IPSEEleDISVEFLVLDSDRVTKNEVIGRLVLgpkasgsgghhWKEVCNpPRRQIAEWHML 135
PDZ3_LNX1_2-like cd06679
PDZ domain 3 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ ...
 4541-4615 1.48e-04

PDZ domain 3 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of LNX1 (also known as PDZ domain-containing RING finger protein 2, PDZRN2) and LNX2 (also known as PDZ domain-containing RING finger protein 1, PDZRN1), and related domains. LNX1 and LNX2 are Ring (Really Interesting New Gene) finger and PDZ domain-containing E3 ubiquitin ligases that bind to the cell fate determinant protein NUMB and mediate its ubiquitination. LNX1 can ubiquitinate a number of other ligands including PPFIA1, KLHL11, KIF7 and ERC2. LNX1 and LNX2 each have four PDZ domains. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This LNX family PDZ3 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467167 [Multi-domain]  Cd Length: 88  Bit Score: 43.39  E-value: 1.48e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2032737686 4541 LGIRVVGGKEIPgsSGEIGAYIAKILPGGNAEQTGKLVEGMQVLEWNGIPLTGKTYEEVQSIIIQQSGEAEICVR 4615
Cdd:cd06679     13 LGISVAGGRGSR--RGDLPIYVTNVQPDGCLGRDGRIKKGDVLLSINGISLTNLSHSEAVAVLKASAASSSIVLK 85
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
262-455 1.53e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 48.33  E-value: 1.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  262 AKQPAQPRG----PQKSQPQPSEPTKPIQQQTSAKPSSGPTKPSPQQPDSTKVTSQtAPPTKPSSQQPGPAKQPSQQPAR 337
Cdd:PRK12323   362 AFRPGQSGGgagpATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAAR-AVAAAPARRSPAPEALAAARQAS 440

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  338 QGAPVKPSPQQTGPPKQPSQQPGPekPSAQQAGPAKQPPQPGSGKPPPQQTGLVKQVPPQAGPTKPPSQTVGPTKPLAQQ 417
Cdd:PRK12323   441 ARGPGGAPAPAPAPAAAPAAAARP--AAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAP 518

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 2032737686  418 AGPTKPPGQQPGPEKPPQQTQAGANQPTET-APKKTFCP 455
Cdd:PRK12323   519 AGWVAESIPDPATADPDDAFETLAPAPAAApAPRAAAAT 557
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 306-710 1.55e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 48.63  E-value: 1.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  306 DSTKVTSQTAPPTKPSSQQPgPAKQPSQQPARQGAPVKPSPQQTGPPKQPSQQPGPEKPSAQQAGPAKQPPQPGS-GKPP 384
Cdd:PHA03307    52 AVTVVAGAAACDRFEPPTGP-PPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASpPPSP 130

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  385 pqqtglvkqvPPQAGPTKPPSQTVGPTkPLAQQAGPTKPPGQQPGPEKPPQQTQAGANQPTETAPkktfcplctttelll 464
Cdd:PHA03307   131 ----------APDLSEMLRPVGSPGPP-PAASPPAAGASPAAVASDAASSRQAALPLSSPEETAR--------------- 184

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  465 htpekanyntctqchtvvcslCGFNPNPhiteisewlclncqmqrtlggdlAPGLGPGPQPLAPKQKTPIPPSAKPSPQP 544
Cdd:PHA03307   185 ---------------------APSSPPA-----------------------EPPPSTPPAAASPRPPRRSSPISASASSP 220

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  545 QPVQKKDvtPKPDPSQAADSKRPPPQKK-------QTQLPGSPPVKSKQPRAEP-TDISQQTDATPKSDQvKPTQAEDKQ 616
Cdd:PHA03307   221 APAPGRS--AADDAGASSSDSSSSESSGcgwgpenECPLPRPAPITLPTRIWEAsGWNGPSSRPGPASSS-SSPRERSPS 297

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  617 KQPSVQK-PTADSVSTSVAAEQKQDLAGPRPPTQQKvtDSPKPELAKPSQDTHPAGDKPDSKPVPQVSRQKSdpkfASQP 695
Cdd:PHA03307   298 PSPSSPGsGPAPSSPRASSSSSSSRESSSSSTSSSS--ESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRK----RPRP 371

                          410
                   ....*....|....*
gi 2032737686  696 GARPDAKAQKPIDPT 710
Cdd:PHA03307   372 SRAPSSPAASAGRPT 386
PRK11633 PRK11633
cell division protein DedD; Provisional
 297-388 1.61e-04

cell division protein DedD; Provisional


Pssm-ID: 236940 [Multi-domain]  Cd Length: 226  Bit Score: 46.53  E-value: 1.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  297 PTKPSP---QQPDSTKVTSQTAPPTKPSSQ----QPGPAKQPSQQPARQGAP---VKPSPQQTGPPKQPSQQPGPEKPSA 366
Cdd:PRK11633    42 PLVPKPgdrDEPDMMPAATQALPTQPPEGAaeavRAGDAAAPSLDPATVAPPntpVEPEPAPVEPPKPKPVEKPKPKPKP 121

                           90       100
                   ....*....|....*....|..
gi 2032737686  367 QQAGPAKQPPQPGSgKPPPQQT 388
Cdd:PRK11633   122 QQKVEAPPAPKPEP-KPVVEEK 142
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 512-733 1.78e-04

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 48.15  E-value: 1.78e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  512 GGDLAPGLGPGPQPLAPKQKTPIPPSAKPSP--QPQPVQKKDVTPKPDPSQAADSKRPPPQKKQTQLPGSP--------P 581
Cdd:PTZ00449   515 EASGLPPKAPGDKEGEEGEHEDSKESDEPKEggKPGETKEGEVGKKPGPAKEHKPSKIPTLSKKPEFPKDPkhpkdpeeP 594

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  582 VKSKQPRAEPTDISQQTDATPKSDQV-----KPTQAEDKQKQPSVQKPtadsvSTSVAAEQKQDLAGPRPPTQQKVTDSP 656
Cdd:PTZ00449   595 KKPKRPRSAQRPTRPKSPKLPELLDIpkspkRPESPKSPKRPPPPQRP-----SSPERPEGPKIIKSPKPPKSPKPPFDP 669

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  657 K------PELAKPSQDTHPAGDKPDSKPVPQVSRQKSDPKFASQPGARPDAKAQK-PIDPTQTKDDPKKlPTKPAPKPDT 729
Cdd:PTZ00449   670 KfkekfyDDYLDAAAKSKETKTTVVLDESFESILKETLPETPGTPFTTPRPLPPKlPRDEEFPFEPIGD-PDAEQPDDIE 748


                   ....
gi 2032737686  730 KPAP 733
Cdd:PTZ00449   749 FFTP 752
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
 1420-1669 1.81e-04

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 48.12  E-value: 1.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1420 KETSKKDTISQESPPSPSDLAKLESTVLSILEAQASTLSDEKSAKSKE-----PSETYGEQTKDQLKTKPLPVTPESYSP 1494
Cdd:PTZ00108  1147 VEEKEIAKEQRLKSKTKGKASKLRKPKLKKKEKKKKKSSADKSKKASVvgnskRVDSDEKRKLDDKPDNKKSNSSGSDQE 1226

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1495 DEEDLKAIKEGEGTIAEEGKGAASSQ-ADYKEEHEGDDM--SARRQQRYDSVEDSSESENSPVPRRKRRTSVGSSSSDEY 1571
Cdd:PTZ00108  1227 DDEEQKTKPKKSSVKRLKSKKNNSSKsSEDNDEFSSDDLskEGKPKNAPKRVSAVQYSPPPPSKRPDGESNGGSKPSSPT 1306

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1572 KRDDsqgsgdeEDFIRKQILEMSADEDASgsdddefirnqLKEISAAESQKKEEVKSKAKGTAGKHRRMARKSSAGYDED 1651
Cdd:PTZ00108  1307 KKKV-------KKRLEGSLAALKKKKKSE-----------KKTARKKKSKTRVKQASASQSSRLLRRPRKKKSDSSSEDD 1368

                          250
                   ....*....|....*...
gi 2032737686 1652 AGRRHSWHDDDDETFDES 1669
Cdd:PTZ00108  1369 DDSEVDDSEDEDDEDDED 1386
PDZ4_INAD-like cd23065
PDZ domain 4 of inactivation-no-after-potential D (INAD), and related domains; PDZ (PSD-95 ...
 4536-4614 1.85e-04

PDZ domain 4 of inactivation-no-after-potential D (INAD), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 4 of INAD, and related domains. INAD assembles key enzymes of the Drosophila compound eye photo-transduction pathway into a supramolecular complex, supporting efficient and fast light signaling. It contains 5 PDZ domains arranged in tandem (PDZ1-PDZ5) which independently bind various proteins. INAD PDZ2 binds eye-specific protein kinase C, INAD PDZ3 binds transient receptor potential (TRP) channel, and INAD PDZ4,5 tandem binds NORPA (phospholipase Cbeta, PLCbeta). Mutations of the inaD gene that lead to disruption of each of these interactions impair fly photo signal transduction. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This INAD-like family PDZ4 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467278 [Multi-domain]  Cd Length: 82  Bit Score: 43.27  E-value: 1.85e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2032737686 4536 VSGNGLGIRVVGGKEipgsSGEIGAYIAKILPGGNAEQTGKLVEGMQVLEWNGIPLTGKTYEEVQSIIIQQSGEAEICV 4614
Cdd:cd23065      6 TDKSPLGVSVVGGKN----HVTTGCIITHIYPNSIVAADKRLKVFDQILDINGTKVHVMTTLKVHQLFHKTYEKAVTLV 80
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 188-348 1.93e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 48.06  E-value: 1.93e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  188 QKVAPKEQGKPEEQRSPAKHPTQPQSPKPAVQQQGPV-----RPTVQQTESSKQQQQPGGPKQVQKPGHGQPADAKQDQA 262
Cdd:PRK07764   623 APAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVpdasdGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPA 702

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  263 KQPAQPRGPQKSQPQPSEPTKPIQQQTSAKPSSGPTKPSPQQPDstkvtSQTAPPTKPSSQQPGPAKQPSQQPARQGAPV 342
Cdd:PRK07764   703 PAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPD-----DPPDPAGAPAQPPPPPAPAPAAAPAAAPPPS 777


                   ....*.
gi 2032737686  343 KPSPQQ 348
Cdd:PRK07764   778 PPSEEE 783
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 248-379 1.98e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 47.79  E-value: 1.98e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  248 KPGHGQPADAKQdQAKQPAQP-RGPQKSQPQPSEPTKPIQQQTSAKPSSGPTKPSPQQPDSTKVTSQTAPPTKPSSQQPG 326
Cdd:PRK14951   365 KPAAAAEAAAPA-EKKTPARPeAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVAAPAAAAPAAAPAAAPA 443

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2032737686  327 PAKQPSQQPARQGAPVKPSPQQTGPPKQPSQQPGPekPSAQQAGPAKQPPQPG 379
Cdd:PRK14951   444 AVALAPAPPAQAAPETVAIPVRVAPEPAVASAAPA--PAAAPAAARLTPTEEG 494
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
512-722 2.03e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 47.95  E-value: 2.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  512 GGDLAP---GLGPGPQPlAPKQKTPIPPSAKPSPQPQPVQKKDVTPKPDPSQAADSKRPPP------QKKQTQLPGSPPV 582
Cdd:PRK12323   369 GGGAGPataAAAPVAQP-APAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPapealaAARQASARGPGGA 447

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  583 KSKQPRAEPTDISQQTDATPKSDQVKPTQAEDKQKQPSVQKPTADSVSTSVAAEQKQDLAGPRP------PTQQKVTDSP 656
Cdd:PRK12323   448 PAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPaqpdaaPAGWVAESIP 527

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2032737686  657 KPELAKPSQDTHPAGDKPDSKPVPQVSRQKsdpkfASQPGARPDAKAQKPIDPTQTKDDP---KKLPTK 722
Cdd:PRK12323   528 DPATADPDDAFETLAPAPAAAPAPRAAAAT-----EPVVAPRPPRASASGLPDMFDGDWPalaARLPVR 591
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
203-348 2.73e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 47.46  E-value: 2.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  203 SPAKHPTQPQspKPAVQQQGPVRPTVQQTESSkqqqqpggpkqVQKPGHGQPADAKQDQAKQPAQPRGPQKSQPQPsEPT 282
Cdd:PRK14971   370 SGGRGPKQHI--KPVFTQPAAAPQPSAAAAAS-----------PSPSQSSAAAQPSAPQSATQPAGTPPTVSVDPP-AAV 435

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2032737686  283 kPIQQQTSAKPSSGPTKPSPQQPDSTKVTSQTAPPTKpssqqpGPAKQPSQQPARQGAPVKPSPQQ 348
Cdd:PRK14971   436 -PVNPPSTAPQAVRPAQFKEEKKIPVSKVSSLGPSTL------RPIQEKAEQATGNIKEAPTGTQK 494
PHA01929 PHA01929
putative scaffolding protein
 308-425 2.77e-04

putative scaffolding protein


Pssm-ID: 177328  Cd Length: 306  Bit Score: 46.59  E-value: 2.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  308 TKVTSQTAPPTKPS-SQQPGPAKQPSQQPARQGAPVKPS-PQQTGPPKQ---PSQQPGPEKPSAQQAGPAKQ-PPQPGSG 381
Cdd:PHA01929     1 TTQNEQQLPPGLAGlVANVPPAAAPTPQPNPVIQPQAPVqPGQPGAPQQlaiPTQQPQPVPTSAMTPHVVQQaPAQPAPA 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2032737686  382 KPPPQQTGLVKQVPPQAGPTKPPSQTVGPTKPLAQQAGPTKPPG 425
Cdd:PHA01929    81 APPAAGAALPEALEVPPPPAFTPNGEIVGTLAGNLEGDPQLAPS 124
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 338-462 2.80e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 47.40  E-value: 2.80e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  338 QGAPVKPSPQQTGPPKQPSQQ-PGPEKPSAQQAGPAKQPPQPGSGKPPPQQtgLVKQVPPQAGPTKPPSQTVGPTKPLAQ 416
Cdd:PRK14951   367 AAAAEAAAPAEKKTPARPEAAaPAAAPVAQAAAAPAPAAAPAAAASAPAAP--PAAAPPAPVAAPAAAAPAAAPAAAPAA 444

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2032737686  417 QAGPTKPPGQ-QPGPEKPPQQTQA--GANQPTETAPKKTFCPLCTTTEL 462
Cdd:PRK14951   445 VALAPAPPAQaAPETVAIPVRVAPepAVASAAPAPAAAPAAARLTPTEE 493
C2A_Synaptotagmin-14_16 cd08389
C2A domain first repeat present in Synaptotagmins 14 and 16; Synaptotagmin 14 and 16 are ...
 5112-5212 3.04e-04

C2A domain first repeat present in Synaptotagmins 14 and 16; Synaptotagmin 14 and 16 are membrane-trafficking proteins in specific tissues outside the brain. Both of these contain C-terminal tandem C2 repeats, but only Synaptotagmin 14 has an N-terminal transmembrane domain and a putative fatty-acylation site. 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 and this is indeed the case here. 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.


Pssm-ID: 176035 [Multi-domain]  Cd Length: 124  Bit Score: 43.77  E-value: 3.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 5112 EQLIVEILQCRNITYKFKSPdhlpdlyvklyvvNISTQKRV----IKK---KTRVcRHDREPSFNETFRFS-LSP---AG 5180
Cdd:cd08389     16 RKLTVTVIRAQDIPTKDRGG-------------ASSWQVHLvllpSKKqraKTKV-QRGPNPVFNETFTFSrVEPeelNN 81

                           90       100       110
                   ....*....|....*....|....*....|..
gi 2032737686 5181 HSLQILLVSNgGKFMKKTLIGEAYIWLDKVDL 5212
Cdd:cd08389     82 MALRFRLYGV-ERMRKERLIGEKVVPLSQLNL 112
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
189-418 3.09e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 47.18  E-value: 3.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  189 KVAPKEQGKPEEQRSPA--KHPTQPQSPKPAVQQQGPVRPTVQQTESSKQQQQPGGPKQVQKPGHGQPADAKQD------ 260
Cdd:PRK12323   378 AAAPVAQPAPAAAAPAAaaPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPApapaaa 457

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  261 ----QAKQPAQPRGPQKSQPQPSEPTKPIQQQTSAKPSSGP--------TKPSPQQPDSTKVTSQTAPPTKPSSQQPGPA 328
Cdd:PRK12323   458 paaaARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPweelppefASPAPAQPDAAPAGWVAESIPDPATADPDDA 537

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  329 KqPSQQPARQGAPVKPSPQQTgppkQPSQQPGPEKPSAQQAGPAKQPPQPGSGKPPPqQTGLVKQVPPQAGPTKPPSQTV 408
Cdd:PRK12323   538 F-ETLAPAPAAAPAPRAAAAT----EPVVAPRPPRASASGLPDMFDGDWPALAARLP-VRGLAQQLARQSELAGVEGDTV 611

                          250
                   ....*....|
gi 2032737686  409 GPTKPLAQQA 418
Cdd:PRK12323   612 RLRVPVPALA 621
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
 521-665 3.11e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 47.17  E-value: 3.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  521 PGPQPLAPKQKTPIPPSAKPSPQPQPVQkkdvtPKPDPSQAADSKRPPPQKKQTQLPGSPPVKSKQPRAEPTDISQQTDA 600
Cdd:PRK07994   364 PLPEPEVPPQSAAPAASAQATAAPTAAV-----APPQAPAVPPPPASAPQQAPAVPLPETTSQLLAARQQLQRAQGATKA 438

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2032737686  601 TPKsdqvKPTQAEDKQKQPSVQKPTADSVSTSVAAEQKQDLAGPRPPTQQKVTDSPKPELAKPSQ 665
Cdd:PRK07994   439 KKS----EPAAASRARPVNSALERLASVRPAPSALEKAPAKKEAYRWKATNPVEVKKEPVATPKA 499
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
 297-427 3.14e-04

polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 47.11  E-value: 3.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  297 PTKPSPQQPdSTKVTSQTAPPTKpssqQPGPAKQPSQQPAR-QGAPVKPSPQQTGPPKQPSqqpGPEKPSAQQAGPAKQp 375
Cdd:TIGR01628  380 PRMRQLPMG-SPMGGAMGQPPYY----GQGPQQQFNGQPLGwPRMSMMPTPMGPGGPLRPN---GLAPMNAVRAPSRNA- 450

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2032737686  376 pQPGSGKPPPQ----QTGLVKQVPPQAGPTKPPSQTVGPTKPLAQQAGPTKPPGQQ 427
Cdd:TIGR01628  451 -QNAAQKPPMQpvmyPPNYQSLPLSQDLPQPQSTASQGGQNKKLAQVLASATPQMQ 505
COG3416 COG3416
Uncharacterized conserved protein, DUF2076 domain [Function unknown];
326-380 3.49e-04

Uncharacterized conserved protein, DUF2076 domain [Function unknown];


Pssm-ID: 442642 [Multi-domain]  Cd Length: 237  Bit Score: 45.78  E-value: 3.49e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2032737686  326 GPAKQPSQQPARQGAPVKPSPQQTGPPKQPSQQPGPEKPsaQQAGPAKQPPQPGS 380
Cdd:COG3416     93 GQRPPPAPQPSQPGPQQQPAPPSGPWGQAAPQQPGYGQP--QYGQPAAGPSGGGG 145
C2F_Ferlin cd08374
C2 domain sixth repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and ...
 4809-4844 3.50e-04

C2 domain sixth repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and other proteins, such as Synaptotagmins, are implicated in facilitating the fusion process when cell membranes fuse together. There are six known human Ferlins: Dysferlin (Fer1L1), Otoferlin (Fer1L2), Myoferlin (Fer1L3), Fer1L4, Fer1L5, and Fer1L6. Defects in these genes can lead to a wide range of diseases including muscular dystrophy (dysferlin), deafness (otoferlin), and infertility (fer-1, fertilization factor-1). Structurally they have 6 tandem C2 domains, designated as (C2A-C2F) and a single C-terminal transmembrane domain, though there is a new study that disputes this and claims that there are actually 7 tandem C2 domains with another C2 domain inserted between C2D and C2E. In a subset of them (Dysferlin, Myoferlin, and Fer1) there is an additional conserved domain called DysF. 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 sixth C2 repeat, C2E, and has a type-II topology.


Pssm-ID: 176020  Cd Length: 133  Bit Score: 43.81  E-value: 3.50e-04
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 2032737686 4809 EQLKKKTLEVTVWDYDRFSSNDFLGEVLIELSSISQ 4844
Cdd:cd08374     88 EYKIPPKLTLQVWDNDKFSPDDFLGSLELDLSILPR 123
C2A_Synaptotagmin-4-11 cd08388
C2A domain first repeat present in Synaptotagmins 4 and 11; Synaptotagmin is a ...
 5114-5212 3.83e-04

C2A domain first repeat present in Synaptotagmins 4 and 11; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Synaptotagmins 4 and 11, class 4 synaptotagmins, are located in the brain. Their functions are unknown. They are distinguished from the other synaptotagmins by having and Asp to Ser substitution in their C2A 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.


Pssm-ID: 176034 [Multi-domain]  Cd Length: 128  Bit Score: 43.49  E-value: 3.83e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 5114 LIVEILQCRNITYKfKSPDHLPDLYVKLYVVNiSTQKRVikkKTRVCRHDREPSFNETFRFSLSPAGH----SLQILLVS 5189
Cdd:cd08388     18 LLVNIIECRDLPAM-DEQSGTSDPYVKLQLLP-EKEHKV---KTRVLRKTRNPVYDETFTFYGIPYNQlqdlSLHFAVLS 92

                           90       100
                   ....*....|....*....|...
gi 2032737686 5190 NgGKFMKKTLIGEAYIWLDKVDL 5212
Cdd:cd08388     93 F-DRYSRDDVIGEVVCPLAGADL 114
C2_cPLA2 cd04036
C2 domain present in cytosolic PhosphoLipase A2 (cPLA2); A single copy of the C2 domain is ...
 5113-5179 4.62e-04

C2 domain present in cytosolic PhosphoLipase A2 (cPLA2); A single copy of the C2 domain is present in cPLA2 which releases arachidonic acid from membranes initiating the biosynthesis of potent inflammatory mediators such as prostaglandins, leukotrienes, and platelet-activating factor. 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. Members of this cd have a type-II topology.


Pssm-ID: 176001 [Multi-domain]  Cd Length: 119  Bit Score: 43.02  E-value: 4.62e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2032737686 5113 QLIVEILQCRNIT-YKFKSPdhlPDLYVKLYVVNISTQKrvikKKTRVCRHDREPSFNETFRFSLSPA 5179
Cdd:cd04036      1 LLTVRVLRATNITkGDLLST---PDCYVELWLPTASDEK----KRTKTIKNSINPVWNETFEFRIQSQ 61
DUF4045 pfam13254
Domain of unknown function (DUF4045); This presumed domain is functionally uncharacterized. ...
 525-716 4.65e-04

Domain of unknown function (DUF4045); This presumed domain is functionally uncharacterized. This domain family is found in bacteria and eukaryotes, and is typically between 384 and 430 amino acids in length.


Pssm-ID: 433066 [Multi-domain]  Cd Length: 415  Bit Score: 46.31  E-value: 4.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  525 PLAPKQKtpippsAKPSPQPQPVQKKDVTP------KPDPSQAADSKRPPPQK-KQTQLPGS----PPVKSKQPRAEPTD 593
Cdd:pfam13254  161 PESPKPK------AQPSQPAQPAWMKELNKirqsraSVDLGRPNSFKEVTPVGlMRSPAPGGhsksPSVSGISADSSPTK 234

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  594 ISQQTDATPKSDQVKPTQAEDKQKQPSVQKPTADSVSTSVAAEQKQDLAGPRPPTQQKVTDSPKPELAKPSQDTHPAGDK 673
Cdd:pfam13254  235 EEPSEEADTLSTDKEQSPAPTSASEPPPKTKELPKDSEEPAAPSKSAEASTEKKEPDTESSPETSSEKSAPSLLSPVSKA 314

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 2032737686  674 PDSKPVPQVSRQKSDPKFASQPGA---RPDAKAQKPIDPTQTKDDP 716
Cdd:pfam13254  315 SIDKPLSSPDRDPLSPKPKPQSPPkdfRANLRSREVPKDKSKKDEP 360
PDZ7_PDZD2-PDZ4_hPro-IL-16-like cd06763
PDZ domain 7 of PDZ domain containing 2 (PDZD2), PDZ domain 4 of human pro-interleukin-16 ...
 4540-4603 4.81e-04

PDZ domain 7 of PDZ domain containing 2 (PDZD2), PDZ domain 4 of human pro-interleukin-16 (isoform 1, 1332 AA), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 7 of PDZD2, also known as KIAA0300, PIN-1, PAPIN, activated in prostate cancer (AIPC) and PDZ domain-containing protein 3 (PDZK3). PDZD2 has seven PDZ domains. PDZD2 is expressed at exceptionally high levels in the pancreas and certain cancer tissues, such as prostate cancer. It promotes the proliferation of insulinoma cells and is upregulated during prostate tumorigenesis. In osteosarcoma (OS), the microRNA miR-363 acts as a tumor suppressor by inhibiting PDZD2. This family include the PDZ domain of the secreted mature form of human interleukin-16 (IL-16); this is the fourth PDZ domain (PDZ4) of human pro-interleukin-16 (isoform 1, also known as nPro-Il-16). Precursor IL-16 is cleaved to produce pro-IL-16 and C-terminal mature IL-16. Pro-IL-16 functions as a regulator of T cell growth; mature IL-16 is a CD4 ligand that induces chemotaxis and CD25 expression in CD4+ T cells. IL-16 bioactivity has been closely associated with the progression of several different cancers PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PDZD2-like family PDZ7 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467244 [Multi-domain]  Cd Length: 86  Bit Score: 41.83  E-value: 4.81e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2032737686 4540 GLGIRVVGGKEIPgsSGEIGAYIAKILPGGNAEQTGKLVEGMQVLEWNGIPLTGKTYEEVQSII 4603
Cdd:cd06763     12 GLGFSLEGGKGSP--LGDRPLTIKRIFKGGAAEQSGVLQVGDEILQINGTSLQGLTRFEAWNII 73
C2A_RasGAP cd08383
C2 domain (first repeat) of Ras GTPase activating proteins (GAPs); RasGAPs suppress Ras ...
 4738-4854 5.20e-04

C2 domain (first repeat) of Ras GTPase activating proteins (GAPs); RasGAPs suppress Ras function by enhancing the GTPase activity of Ras proteins resulting in the inactive GDP-bound form of Ras. In this way it can control cellular proliferation and differentiation. The proteins here all contain either a single C2 domain or two tandem C2 domains, a Ras-GAP domain, and a pleckstrin homology (PH)-like 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. Members here have a type-I topology.


Pssm-ID: 176029 [Multi-domain]  Cd Length: 117  Bit Score: 43.02  E-value: 5.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4738 LIIHILQARNLAPRdnnGYSDPFVKVYLlpgrGQVMVVqnasaeykrRTKYIQKsLNPEWNQTVIYKNISVEqLKKKTLE 4817
Cdd:cd08383      2 LRLRILEAKNLPSK---GTRDPYCTVSL----DQVEVA---------RTKTVEK-LNPFWGEEFVFDDPPPD-VTFFTLS 63

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 2032737686 4818 VTVWDYDRFSSNDFLGEVlielsSISQLDN---TPRWYPL 4854
Cdd:cd08383     64 FYNKDKRSKDRDIVIGKV-----ALSKLDLgqgKDEWFPL 98
PHA03247 PHA03247
large tegument protein UL36; Provisional
 566-1093 5.68e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.86  E-value: 5.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  566 RPPPQKKQTQLPGSPPVKSKQPRAEPtdisqqtDATPKSDQVKPTQAEDKqkqpsvqkPTADSVSTSVAA------EQKQ 639
Cdd:PHA03247  2481 RRPAEARFPFAAGAAPDPGGGGPPDP-------DAPPAPSRLAPAILPDE--------PVGEPVHPRMLTwirgleELAS 2545

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  640 DLAGPRPPtqqkvtdsPKPELAKPsqdthPAGDKpdSKPVPQVSRQKSDPKFASQpGARPDAKAQ--KPIDPTQTKDDPK 717
Cdd:PHA03247  2546 DDAGDPPP--------PLPPAAPP-----AAPDR--SVPPPRPAPRPSEPAVTSR-ARRPDAPPQsaRPRAPVDDRGDPR 2609

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  718 KLPTKPAPKPDT---KPAPKGPQAGAGPKAAPAQPAPQPQPPQKTPEQPRRFSLNLGGITDAPKPQPTTPQETVTgklfg 794
Cdd:PHA03247  2610 GPAPPSPLPPDThapDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPR----- 2684

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  795 fgasffsqasnlistagqtgsQPSGPPPPAPAAKQPQPPAQPPAPQAAPKEAAQAQPLPKAVPVKKEAKP-LTTEKSEPS 873
Cdd:PHA03247  2685 ---------------------RRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPaLPAAPAPPA 2743

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  874 KVDGVLTKGSDlEKKPGLAKDSKPLAAEAKKPDGLSEPEKASQPEMSCPLCKTGLNIGSKDPPNFNTCTECKKVVCNLC- 952
Cdd:PHA03247  2744 VPAGPATPGGP-ARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAa 2822

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  953 ----GFNPMPHIAEVQEWLCLN-CQTQRAMSGQLGDMGkvPLLKPGPSQPT-SKPAAPPQKR----PVPAVSHS------ 1016
Cdd:PHA03247  2823 spagPLPPPTSAQPTAPPPPPGpPPPSLPLGGSVAPGG--DVRRRPPSRSPaAKPAAPARPPvrrlARPAVSRStesfal 2900

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1017 ------PQKTSTPPTPAAAKPKEEPGVQKEAPKLQQGRLEKTLSADKIQQGI---QKEDAKPKQGKLVKAPSADKIQHAS 1087
Cdd:PHA03247  2901 ppdqpeRPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAgepSGAVPQPWLGALVPGRVAVPRFRVP 2980


                   ....*.
gi 2032737686 1088 QKEDPR 1093
Cdd:PHA03247  2981 QPAPSR 2986
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
 342-433 5.94e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 46.34  E-value: 5.94e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  342 VKPSPQQTGPPKQPSQQPGPEKPsaqqaGPAKQPPQPGSGKPPPQqtglvKQVPPQAGPTKPPSQTVGPTKPLAQQAGPT 421
Cdd:PRK14950   361 VPVPAPQPAKPTAAAPSPVRPTP-----APSTRPKAAAAANIPPK-----EPVRETATPPPVPPRPVAPPVPHTPESAPK 430

                           90
                   ....*....|..
gi 2032737686  422 KPPGQQPGPEKP 433
Cdd:PRK14950   431 LTRAAIPVDEKP 442
Pneumo_att_G pfam05539
Pneumovirinae attachment membrane glycoprotein G;
254-459 6.30e-04

Pneumovirinae attachment membrane glycoprotein G;


Pssm-ID: 114270 [Multi-domain]  Cd Length: 408  Bit Score: 45.81  E-value: 6.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  254 PADAKQDQAKQPAQPRGPQKSQP-QPSEPTKPIQQQTSAKPSSGPTKPSPQQPDSTKVTSQTAPPTKPSSQQPGPAKQPS 332
Cdd:pfam05539  187 PTYPSQVTPQSQPATQGHQTATAnQRLSSTEPVGTQGTTTSSNPEPQTEPPPSQRGPSGSPQHPPSTTSQDQSTTGDGQE 266

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  333 QQPARQGAPVKPSPQQTgppkqpsqqpgpekpsAQQAGPAKQPPQPGSGKPPPQQTGLVkQVPPQAGPTKPPSQTVGPTK 412
Cdd:pfam05539  267 HTQRRKTPPATSNRRSP----------------HSTATPPPTTKRQETGRPTPRPTATT-QSGSSPPHSSPPGVQANPTT 329

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 2032737686  413 plaqQAGPTKPPGQQPGPEKPPQQTqaGANQPTETAPKKTFCPLCTT 459
Cdd:pfam05539  330 ----QNLVDCKELDPPKPNSICYGV--GIYNEALPRGCDIVVPLCST 370
C2B_SLP_1-2-3-4 cd04020
C2 domain second repeat present in Synaptotagmin-like proteins 1-4; All Slp members basically ...
 5097-5175 6.70e-04

C2 domain second repeat present in Synaptotagmin-like proteins 1-4; 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. 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.


Pssm-ID: 175987 [Multi-domain]  Cd Length: 162  Bit Score: 43.47  E-value: 6.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 5097 GEIKIALK----------KEMKTDGEQLIVEILQCRNITYKfKSPDHLpDLYVKLYVvnISTQKRVIKKKTRVCRHDREP 5166
Cdd:cd04020      2 GELKVALKyvppesegalKSKKPSTGELHVWVKEAKNLPAL-KSGGTS-DSFVKCYL--LPDKSKKSKQKTPVVKKSVNP 77


                   ....*....
gi 2032737686 5167 SFNETFRFS 5175
Cdd:cd04020     78 VWNHTFVYD 86
PRK10927 PRK10927
cell division protein FtsN;
276-451 6.70e-04

cell division protein FtsN;


Pssm-ID: 236797 [Multi-domain]  Cd Length: 319  Bit Score: 45.44  E-value: 6.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  276 PQPSEPTKPIQQQTSAKPS-SGPTKPS-------PQQ--PDSTKVTSQTAPPTKpssQQPgpaKQPSQQPARQGAPVKPs 345
Cdd:PRK10927    77 PKPEERWRYIKELESRQPGvRAPTEPSaggevktPEQltPEQRQLLEQMQADMR---QQP---TQLVEVPWNEQTPEQR- 149

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  346 pQQTGPPKQPSQQPGPEKPSAQQAGPAKQPPQpgsgkpppQQTGLVKQVPPQAGPTKP-PSQTVGPTKPLAQQAGPTKpp 424
Cdd:PRK10927   150 -QQTLQRQRQAQQLAEQQRLAQQSRTTEQSWQ--------QQTRTSQAAPVQAQPRQSkPASTQQPYQDLLQTPAHTT-- 218

                          170       180
                   ....*....|....*....|....*..
gi 2032737686  425 gQQPGPEKPPQQTQAgANQPTETAPKK 451
Cdd:PRK10927   219 -AQSKPQQAAPVTRA-ADAPKPTAEKK 243
PHA03247 PHA03247
large tegument protein UL36; Provisional
 190-416 6.88e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.47  E-value: 6.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  190 VAPKEQGKPEEQRSPAKHPTQPQSPKPAVQQQGPVRPTVQQTESSKQQQQPGGPKQVQKPGHGQPADAKQDQAKQPAQPR 269
Cdd:PHA03247   261 VGEGADRAPETARGATGPPPPPEAAAPNGAAAPPDGVWGAALAGAPLALPAPPDPPPPAPAGDAEEEDDEDGAMEVVSPL 340

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  270 G----------PQKSQPQPSEPTKpIQQQTS----AKPSSGPTKPSPQQPDS-TKVTSQTAPPTKPSSQQPGPAKQPSQQ 334
Cdd:PHA03247   341 PrprqhyplgfPKRRRPTWTPPSS-LEDLSAgrhhPKRASLPTRKRRSARHAaTPFARGPGGDDQTRPAAPVPASVPTPA 419

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  335 PARQGAPVKPSPQQTGPPKQPSQQPGPEKPsaqqagPAKQPPQPGSGKPPPQQTGLVKQVPPQAGPTKPPSQtvgPTKPL 414
Cdd:PHA03247   420 PTPVPASAPPPPATPLPSAEPGSDDGPAPP------PERQPPAPATEPAPDDPDDATRKALDALRERRPPEP---PGADL 490


                   ..
gi 2032737686  415 AQ 416
Cdd:PHA03247   491 AE 492
PDZ3_MUPP1-like cd06791
PDZ domain 3 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ...
 4538-4618 7.58e-04

PDZ domain 3 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of MUPP1 and PATJ, and related domains. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, 9, and 13; consequently, MUPP1 PDZ7 and 8 align with PATJ PDZ6 and 7; and MUPP1 PDZ domains 10-12 align with PATJ PDZ domains 8-10. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467253 [Multi-domain]  Cd Length: 89  Bit Score: 41.45  E-value: 7.58e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4538 GNGLGIRVVGGKEIPGSSGEIGAYIAKILPGGNAEQTGKLVEGMQVLEWNGIPLTGKTYEEVQSiIIQQSGEaeiCVRLD 4617
Cdd:cd06791     11 EQGLGITIAGYVGEKASGELSGIFVKSIIPGSAADQDGRIQVNDQIIAVDGVNLQGFTNQEAVE-VLRNTGQ---VVHLT 86


                   .
gi 2032737686 4618 L 4618
Cdd:cd06791     87 L 87
C2B_Synaptotagmin-15 cd08409
C2 domain second repeat present in Synaptotagmin 15; Synaptotagmin is a membrane-trafficking ...
 5097-5222 7.70e-04

C2 domain second repeat present in Synaptotagmin 15; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. It is thought to be involved in the trafficking and exocytosis of secretory vesicles in non-neuronal tissues and is Ca2+ independent. Human synaptotagmin 15 has 2 alternatively spliced forms that encode proteins with different C-termini. The larger, SYT15a, contains a N-terminal TM region, a putative fatty-acylation site, and 2 tandem C terminal C2 domains. The smaller, SYT15b, lacks the C-terminal portion of the second C2 domain. Unlike most other synaptotagmins it is nearly absent in the brain and rather is found in the heart, lungs, skeletal muscle, and testis. 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.


Pssm-ID: 176054 [Multi-domain]  Cd Length: 137  Bit Score: 42.71  E-value: 7.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 5097 GEIKIALKKEMKTDgeQLIVEILQCRNItyKFKSPDHLpDLYVKLYVVNISTQkrVIKKKTRVCRHDREPSFNETFRFSL 5176
Cdd:cd08409      2 GDIQISLTYNPTLN--RLTVVVLRARGL--RQLDHAHT-SVYVKVSLMIHNKV--VKTKKTEVVDGAASPSFNESFSFKV 74

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2032737686 5177 SPAGHSLQILLVS--NGGKFMKKTLIGEAYI-------------WLDKV-DLRKRIVNWHKL 5222
Cdd:cd08409     75 TSRQLDTASLSLSvmQSGGVRKSKLLGRVVLgpfmyargkelehWNDMLsKPKELIKRWHAL 136
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 252-408 8.04e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 46.32  E-value: 8.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  252 GQPADAKQDQAKQPAQPRGPQKSQPQPSEPTKPIQQQTSAKPSSGPTKPSPQQPDSTKVTSQTAPPTKPSSQQPGPAKQP 331
Cdd:PHA03307   797 RRPGRLRRSGPAADAASRTASKRKSRSHTPDGGSESSGPARPPGAAARPPPARSSESSKSKPAAAGGRARGKNGRRRPRP 876

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2032737686  332 SQQPARQGAPVKPSPQQTGPPkqpsqqPGPEKPSAQQAGPAKQPPQPgSGKPPPQqtGLVKQVPPQAGPTKPPSQTV 408
Cdd:PHA03307   877 PEPRARPGAAAPPKAAAAAPP------AGAPAPRPRPAPRVKLGPMP-PGGPDPR--GGFRRVPPGDLHTPAPSAAA 944
kgd PRK12270
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ...
 286-373 8.26e-04

multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;


Pssm-ID: 237030 [Multi-domain]  Cd Length: 1228  Bit Score: 46.04  E-value: 8.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  286 QQQTSAKPSSGPTKPSPQQPDSTKVTSQTAPPTKPSSQQPGPAKQPSQQPARQGAPVKPSPQQTGPPKQPSQQPGPEKPS 365
Cdd:PRK12270    34 ADYGPGSTAAPTAAAAAAAAAASAPAAAPAAKAPAAPAPAPPAAAAPAAPPKPAAAAAAAAAPAAPPAAAAAAAPAAAAV 113

                           90
                   ....*....|..
gi 2032737686  366 AQQA----GPAK 373
Cdd:PRK12270   114 EDEVtplrGAAA 125
dnaA PRK14086
chromosomal replication initiator protein DnaA;
186-416 8.30e-04

chromosomal replication initiator protein DnaA;


Pssm-ID: 237605 [Multi-domain]  Cd Length: 617  Bit Score: 45.97  E-value: 8.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  186 RKQKVAPKEQGKPEEQRSPAKHPTQPQSPKPAVQQQGPVRPTvqqtesskqqqqpggpkqvqkpghgqpadakqdqaKQP 265
Cdd:PRK14086   100 PHARRTSEPELPRPGRRPYEGYGGPRADDRPPGLPRQDQLPT-----------------------------------ARP 144

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  266 AQPRGPQKSQPQ--PSEPTKPIQQQTSAkpssGPTKPSPQqpdstkvTSQTAPPTKPSSQQPGPAKQPSQQPARQGAPVK 343
Cdd:PRK14086   145 AYPAYQQRPEPGawPRAADDYGWQQQRL----GFPPRAPY-------ASPASYAPEQERDREPYDAGRPEYDQRRRDYDH 213

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2032737686  344 PSPQQTGPPKQPSQQPGPEkpsaqqagPAKQPPQPGSGKPPPQQTGLVKQVPPQAG--PTKPPSQTVGPTKPLAQ 416
Cdd:PRK14086   214 PRPDWDRPRRDRTDRPEPP--------PGAGHVHRGGPGPPERDDAPVVPIRPSAPgpLAAQPAPAPGPGEPTAR 280
C2C_MCTP_PRT_plant cd04019
C2 domain third repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); ...
 4740-4865 8.37e-04

C2 domain third repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); plant subset; MCTPs are involved in Ca2+ signaling at the membrane. Plant-MCTPs are composed of a variable N-terminal sequence, four C2 domains, two transmembrane regions (TMRs), and a short C-terminal sequence. It is one of four protein classes that are anchored to membranes via a transmembrane region; the others being synaptotagmins, extended synaptotagmins, and ferlins. MCTPs are the only membrane-bound C2 domain proteins that contain two functional TMRs. MCTPs are unique in that they bind Ca2+ but not phospholipids. 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.


Pssm-ID: 175986 [Multi-domain]  Cd Length: 150  Bit Score: 43.04  E-value: 8.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4740 IHILQARNLAPRDNNGYSDPFVKVYLLpgrGQVmvvqnasaeykRRTKYIQ-KSLNPEWNQTVI---------YKNISVE 4809
Cdd:cd04019      4 VTVIEAQDLVPSDKNRVPEVFVKAQLG---NQV-----------LRTRPSQtRNGNPSWNEELMfvaaepfedHLILSVE 69

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4810 QLKKKTLEVTVwdydrfssndflGEVLIELSSISQ-LDNTP---RWYPLkEQSENIDHGK 4865
Cdd:cd04019     70 DRVGPNKDEPL------------GRAVIPLNDIERrVDDRPvpsRWFSL-ERPGGAMEQK 116
PDZ3_FL-whirlin-like cd06742
PDZ domain 3 of the full-length isoform of whirlin, PDZ domain 1 of the short isoform of ...
 4541-4603 8.54e-04

PDZ domain 3 of the full-length isoform of whirlin, PDZ domain 1 of the short isoform of whirlin, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of the full-length isoform of whirlin, PDZ domain 1 of the short isoform of whirlin, and related domains. Whirlin is an essential protein for developmental pathways in photoreceptor cells of the retina and hair cells of the inner ear. The full-length whirlin isoform has two harmonin N-like domains, three PDZ domains, a proline-rich region, and a PDZ-binding motif. Whirlin isoforms may form different complexes at the periciliary membrane complex (PMC) in photoreceptors, and the stereociliary tip and base in inner ear hair cells. It interacts with ADGRV1 and usherin at the PMC; with SANS and RpgrORF15 at the connecting cilium in photoreceptors; with EPS8, MYO15A, p55, and CASK proteins at the stereociliary tip of inner ear hair cells; and with ADGRV1, usherin, and PDZD7 at the stereociliary base in inner ear hair cells. Mutations in the gene encoding whirlin (WHRN; also known as USH2D and DFNB31), have been found to cause either USH2 subtype (USH2D) or autosomal recessive non-syndromic deafness type 31 (DFNB31). Whirlin is the key protein in the USH2 complex (whirlin, usherin and GPR98) which recruits other USH2 causative proteins at the periciliary membrane in photoreceptors and the ankle link of the stereocilia in hair cells. Whirlin's interaction with espin, another stereociliary protein, may be important for the architecture of the USH2 complex. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This whirlin family PDZ3 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F


Pssm-ID: 467224 [Multi-domain]  Cd Length: 91  Bit Score: 41.57  E-value: 8.54e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2032737686 4541 LGIRVVGGkeipGSSGEIGAYIAKILPGGNAEQTGKLVEGMQVLEWNGIPLTGKTYEEVQSII 4603
Cdd:cd06742     13 LGIAIEGG----ANTKQPLPRVINIQRGGSAHNCGGLKVGHVILEVNGTSLRGLEHREAARLI 71
C2A_Tricalbin-like cd04044
C2 domain first repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are ...
 4735-4844 8.54e-04

C2 domain first repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are present in Tricalbin, a yeast homolog of Synaptotagmin, which is involved in membrane trafficking and sorting. 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-II topology.


Pssm-ID: 176009 [Multi-domain]  Cd Length: 124  Bit Score: 42.54  E-value: 8.54e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4735 LGNLIIHILQARNLAPRDN-NGYSDPFVkvyllpgrgqVMVVQNASAEykRRTKYIQKSLNPEWNQTviyKNISVEQLKK 4813
Cdd:cd04044      1 IGVLAVTIKSARGLKGSDIiGGTVDPYV----------TFSISNRREL--ARTKVKKDTSNPVWNET---KYILVNSLTE 65

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2032737686 4814 KtLEVTVWDYDRFSSNDFLGEVLIELSSISQ 4844
Cdd:cd04044     66 P-LNLTVYDFNDKRKDKLIGTAEFDLSSLLQ 95
G_path_suppress pfam15991
G-protein pathway suppressor; This family of proteins inhibits G-protein- and ...
 247-386 8.67e-04

G-protein pathway suppressor; This family of proteins inhibits G-protein- and mitogen-activated protein kinase-mediated signal transduction.


Pssm-ID: 464961 [Multi-domain]  Cd Length: 272  Bit Score: 44.91  E-value: 8.67e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  247 QKPGHGQPADAKQDQAKQPAQPRGPQKSQP--QPSEPTKPIQQQTSAKPSSGPTKPSPQQPDSTKV--TSQTAPPTkpss 322
Cdd:pfam15991  125 QQHPGPQVGVLKRTRSPSPPVQQQAYYKQPafSPGYAEHGQQKHDDGRRGYDVARFGSWNKSTAQYppSGQLFYPT---- 200

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2032737686  323 QQPGPAKQPSQQPARQGAPVKPSPQQTGP-------PKQPSQQPGPEKPSAQQAGPAKQPPQPGSGKPPPQ 386
Cdd:pfam15991  201 HQYLPPPQTQGQADARLQTIYPQPGYALPlqqqyehANQPSPFVSSSPLKQMQSPKAGPGPQPMQLSVLHI 271
DUF1720 pfam08226
Domain of unknown function (DUF1720); This domain is found in different combinations with ...
 346-419 8.81e-04

Domain of unknown function (DUF1720); This domain is found in different combinations with cortical patch components EF hand, SH3 and ENTH and is therefore likely to be involved in cytoskeletal processes. This family contains many hypothetical proteins.


Pssm-ID: 369766 [Multi-domain]  Cd Length: 75  Bit Score: 40.89  E-value: 8.81e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2032737686  346 PQQTGPPKQPSQQPGPEKPSAQQAGPAKQPPQPGSGKPPPQQTGLVKQVPPQAGPTKPPSQtvgPTKPLAQQAG 419
Cdd:pfam08226    3 PQQTGYMPPQQQQPQQTQQPLQPQPTGFMPQQQTGQGLQPQPTGMGQFQPLQPQQTGFQPQ---AQQGLQPQAT 73
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
 265-374 9.01e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 45.57  E-value: 9.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  265 PAQPRGPQKSQPQPSEPTKpiqqqtsaKPSSGPTKPSPQQPDSTKVTSQTAPPTKPssqqpgpakqpsqqPARQGAPVKP 344
Cdd:PRK14950   365 APQPAKPTAAAPSPVRPTP--------APSTRPKAAAAANIPPKEPVRETATPPPV--------------PPRPVAPPVP 422

                           90       100       110
                   ....*....|....*....|....*....|
gi 2032737686  345 SPQQTGPPKQPSQQPGPEKPSAQQAGPAKQ 374
Cdd:PRK14950   423 HTPESAPKLTRAAIPVDEKPKYTPPAPPKE 452
C2B_Synaptotagmin-14_16 cd08408
C2 domain second repeat present in Synaptotagmins 14 and 16; Synaptotagmin 14 and 16 are ...
 4724-4860 9.65e-04

C2 domain second repeat present in Synaptotagmins 14 and 16; Synaptotagmin 14 and 16 are membrane-trafficking proteins in specific tissues outside the brain. Both of these contain C-terminal tandem C2 repeats, but only Synaptotagmin 14 has an N-terminal transmembrane domain and a putative fatty-acylation site. 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 and this is indeed the case here. 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.


Pssm-ID: 176053 [Multi-domain]  Cd Length: 138  Bit Score: 42.74  E-value: 9.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4724 EIQLQINYDKHLGNLIIHILQARNLAPRDNNGYSDPFVKVYLLPGRGQVMVVQNASAeykRRTKYiqkslNPEWNQTVIY 4803
Cdd:cd08408      3 ELLLGLEYNALTGRLSVEVIKGSNFKNLAMNKAPDTYVKLTLLNSDGQEISKSKTSI---RRGQP-----DPEFKETFVF 74

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2032737686 4804 KnISVEQLKKKTLEVTVWDYDRFSSNDFLGEVLIELSSISQlDNTPRWYPLKEQSEN 4860
Cdd:cd08408     75 Q-VALFQLSEVTLMFSVYNKRKMKRKEMIGWFSLGLNSSGE-EEEEHWNEMKESKGQ 129
PRK10856 PRK10856
cytoskeleton protein RodZ;
262-366 1.01e-03

cytoskeleton protein RodZ;


Pssm-ID: 236776 [Multi-domain]  Cd Length: 331  Bit Score: 45.02  E-value: 1.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  262 AKQPAQPRGPQKSQPQPSEPTKPIQQQTSakPSSGPTKPSPQQPDSTKVTSQTAPPTKPSSQ-QPGPAKQPSQQPARQGA 340
Cdd:PRK10856   147 ADQSSAELSQNSGQSVPLDTSTTTDPATT--PAPAAPVDTTPTNSQTPAVATAPAPAVDPQQnAVVAPSQANVDTAATPA 224

                           90       100
                   ....*....|....*....|....*.
gi 2032737686  341 PVKPSPQQTGPPkQPSQQPGPEKPSA 366
Cdd:PRK10856   225 PAAPATPDGAAP-LPTDQAGVSTPAA 249
PRK10819 PRK10819
transport protein TonB; Provisional
 299-434 1.01e-03

transport protein TonB; Provisional


Pssm-ID: 236768 [Multi-domain]  Cd Length: 246  Bit Score: 44.29  E-value: 1.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  299 KPSPQQPDS-TKVTSQTAPPTKPSSQQPGPAKQPSQQPARQGAPVKPSPQQTGPPK-----QPSQQPGPEKPSAQQAGPA 372
Cdd:PRK10819    41 LPAPAQPISvTMVAPADLEPPQAVQPPPEPVVEPEPEPEPIPEPPKEAPVVIPKPEpkpkpKPKPKPKPVKKVEEQPKRE 120

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2032737686  373 KQPPQPGSGKPPPQqtglvkqvPPQAGPTKPPSQTVGPTKPLAQQAGPTkpPGQQPGPEKPP 434
Cdd:PRK10819   121 VKPVEPRPASPFEN--------TAPARPTSSTATAAASKPVTSVSSGPR--ALSRNQPQYPA 172
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
 202-372 1.07e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 45.63  E-value: 1.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  202 RSPAKHPTQPQSPKPAVQQQGPVRPTVQQTESSKqqqqpggpkqvqkpghGQPADAKQDQAKQPAQPRGPQKSQPQPSEP 281
Cdd:PRK07994   355 RMLAFHPAAPLPEPEVPPQSAAPAASAQATAAPT----------------AAVAPPQAPAVPPPPASAPQQAPAVPLPET 418

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  282 TKPI----QQQTSAKPSSGPTKPSPQQPDSTK-VTSQTAPPTKPSSQQPGPAKQPSQQPARQGAPVKPSPQQTGP---PK 353
Cdd:PRK07994   419 TSQLlaarQQLQRAQGATKAKKSEPAAASRARpVNSALERLASVRPAPSALEKAPAKKEAYRWKATNPVEVKKEPvatPK 498

                          170
                   ....*....|....*....
gi 2032737686  354 QPSQQPGPEKPSAQQAGPA 372
Cdd:PRK07994   499 ALKKALEHEKTPELAAKLA 517
PRK12757 PRK12757
cell division protein FtsN; Provisional
 322-452 1.08e-03

cell division protein FtsN; Provisional


Pssm-ID: 237191 [Multi-domain]  Cd Length: 256  Bit Score: 44.26  E-value: 1.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  322 SQQPGPakqPSQQPARQGAPVKPSPQQTGPPKQPSQQpgpekpsaQQAGPAKQPPQ----PGSGKPPPQQTGLVkQVPPQ 397
Cdd:PRK12757    57 NRQIGV---PTPTEPSAGGEVNSPTQLTDEQRQLLEQ--------MQADMRQQPTQlsevPYNEQTPQVPRSTV-QIQQQ 124

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2032737686  398 AGPTKPPSQTV--GPTKPLAQQAGPTKPPGQQPGPEKPPQQTQAGANQPTETAPKKT 452
Cdd:PRK12757   125 AQQQQPPATTAqpQPVTPPRQTTAPVQPQTPAPVRTQPAAPVTQAVEAPKVEAEKEK 181
ftsN TIGR02223
cell division protein FtsN; FtsN is a poorly conserved protein active in cell division in a ...
 273-441 1.08e-03

cell division protein FtsN; FtsN is a poorly conserved protein active in cell division in a number of Proteobacteria. The N-terminal 30 residue region tends to by Lys/Arg-rich, and is followed by a membrane-spanning region. This is followed by an acidic low-complexity region of variable length and a well-conserved C-terminal domain of two tandem regions matched by pfam05036 (Sporulation related repeat), found in several cell division and sporulation proteins. The role of FtsN as a suppressor for other cell division mutations is poorly understood; it may involve cell wall hydrolysis. [Cellular processes, Cell division]


Pssm-ID: 274041 [Multi-domain]  Cd Length: 298  Bit Score: 44.68  E-value: 1.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  273 KSQPQPSEPTKPIQQQTSAKPSSGPTKPSPQQPDSTKVTSQTAP------PTKPSSQQPgPAKQPSQQPARQGAPVKPSP 346
Cdd:TIGR02223   49 TESKQANEPETLQPKNQTENGETAADLPPKPEERWSYIEELEARevlindPEEPSNGGG-VEESAQLTAEQRQLLEQMQA 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  347 QQTGPPKQ----PSQQPGPEKPSAQQAGPAKQPPQPGSGKPPPQQT-----GLVKQVPPQAGPTKPPSQTVGPTKPLAQQ 417
Cdd:TIGR02223  128 DMRAAEKVlataPSEQTVAVEARKQTAEKKPQKARTAEAQKTPVETekiasKVKEAKQKQKALPKQTAETQSNSKPIETA 207

                          170       180
                   ....*....|....*....|....*..
gi 2032737686  418 AGPTKPPGQQPGPEKPPQQT---QAGA 441
Cdd:TIGR02223  208 PKADKADKTKPKPKEKAERAaalQCGA 234
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 261-400 1.09e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 45.48  E-value: 1.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  261 QAKQPAQPRGPQKSqpqpsePTKPIQQQTSAKPSSGPtkPSPQQPDSTKVTSQTAPPTKPSSQQPGPAKQPSqqPARQGA 340
Cdd:PRK14951   367 AAAAEAAAPAEKKT------PARPEAAAPAAAPVAQA--AAAPAPAAAPAAAASAPAAPPAAAPPAPVAAPA--AAAPAA 436

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  341 PVKPSPQQTGPPKQPSQQPGPEkpsaQQAGPAKQPPQPGSGKPPPQQTGLVKQVPPQAGP 400
Cdd:PRK14951   437 APAAAPAAVALAPAPPAQAAPE----TVAIPVRVAPEPAVASAAPAPAAAPAAARLTPTE 492
Amelin smart00817
Ameloblastin precursor (Amelin); This family consists of several mammalian Ameloblastin ...
 320-443 1.13e-03

Ameloblastin precursor (Amelin); This family consists of several mammalian Ameloblastin precursor (Amelin) proteins. Matrix proteins of tooth enamel consist mainly of amelogenin but also of non-amelogenin proteins, which, although their volumetric percentage is low, have an important role in enamel mineralisation. One of the non-amelogenin proteins is ameloblastin, also known as amelin and sheathlin. Ameloblastin (AMBN) is one of the enamel sheath proteins which is though to have a role in determining the prismatic structure of growing enamel crystals.


Pssm-ID: 214832 [Multi-domain]  Cd Length: 411  Bit Score: 44.88  E-value: 1.13e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686   320 PSSQQP--GPAKQPSQQpARQGAPVKPSPQQTGPPKQPsQQPGpEKPSAQ-------QAGPAKQPPQPG--SGKPPPQQT 388
Cdd:smart00817   72 PHSSFPwlRPREHETQQ-YEYSLPVHPPPLPSQPSLQP-QQPG-LKPFLQptalptnQATPQKNGPQPPmhLGQPPLQQA 148

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2032737686   389 GLvKQVPPQAGPTKPPSQTV-------GPTKPLAQQAGPTKPPGQQPGPEKPPQQ-----TQAGANQ 443
Cdd:smart00817  149 EL-PMIPPQVAPSDKPPQTElplydfaDPQNPLLFQIAHLMSRGPMPQNKQQHLYpglfyMSYGANQ 214
PHA03264 PHA03264
envelope glycoprotein D; Provisional
 315-409 1.16e-03

envelope glycoprotein D; Provisional


Pssm-ID: 223029 [Multi-domain]  Cd Length: 416  Bit Score: 45.00  E-value: 1.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  315 APPTKPSSQQPGPAKQPSQQPARQGAPVKPSPqqtGPPKQPSQQPGPEKPSAQQAGPAKQPPQPGSGKPP-------PQQ 387
Cdd:PHA03264   265 EPPPAPSGGSPAPPGDDRPEAKPEPGPVEDGA---PGRETGGEGEGPEPAGRDGAAGGEPKPGPPRPAPDadrpegwPSL 341

                           90       100
                   ....*....|....*....|..
gi 2032737686  388 TGLVKQVPPQAGPTKPPSQTVG 409
Cdd:PHA03264   342 EAITFPPPTPATPAVPRARPVI 363
PDZ1_harmonin cd06737
PDZ domain 1 of harmonin isoforms a, b, and c, and related domains; PDZ (PSD-95 (Postsynaptic ...
 4524-4607 1.18e-03

PDZ domain 1 of harmonin isoforms a, b, and c, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of harmonin isoforms a, b, and c, and related domains. Harmonin (also known as Usher Type 1C, PDZ-73 and AIE-75) is a key organizer of the Usher (USH) protein interactome. USH syndrome is the leading cause of hereditary sensory deaf-blindness in humans; three clinically distinct types of USH have been identified, type 1 to 3. The gene encoding harmonin (USH1C) is the causative gene for the USH type 1C phenotype. There are at least 10 alternatively spliced isoforms of harmonin, which are divided into three subclasses (a, b, and c). All isoforms contain the first two PDZ domains and the first coiled-coil domain. The a and b isoforms all have a third PDZ domain. The different PDZ domains are responsible for interactions with all known Usher syndrome type 1 proteins, and most Usher syndrome type 2 proteins. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This harmonin family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467219 [Multi-domain]  Cd Length: 85  Bit Score: 40.70  E-value: 1.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4524 RLKLLRDPKDHtvsGNGLGIRVVGGKEIpgssgEIGAYIAKILPGGNAEQTGkLVEGMQVLEWNGIPLTGKTYEEVQSII 4603
Cdd:cd06737      1 KLRLVRLDRRG---PESLGFSVRGGLEH-----GCGLFVSHVSPGSQADNKG-LRVGDEIVRINGYSISQCTHEEVINLI 71


                   ....
gi 2032737686 4604 IQQS 4607
Cdd:cd06737     72 KTKK 75
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
 337-451 1.20e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 45.24  E-value: 1.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  337 RQGAPVKPSPQQTGPPkQPSQQPGPEKPSAQQAGPAKQPPQPGSGKPPPQqtglvkqvpPQAGPTKPPSQTVGPTKPLAQ 416
Cdd:PRK07994   362 AAPLPEPEVPPQSAAP-AASAQATAAPTAAVAPPQAPAVPPPPASAPQQA---------PAVPLPETTSQLLAARQQLQR 431

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2032737686  417 QAGPTKPPGQQPGPEKPPQQTQAG---------ANQPTETAPKK 451
Cdd:PRK07994   432 AQGATKAKKSEPAAASRARPVNSAlerlasvrpAPSALEKAPAK 475
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
 521-615 1.31e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 45.19  E-value: 1.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  521 PGPQPLAPKQKTPIPPSAKPSPQPQPVQKKDVTPKPDPSQAAdskrPPPQKKQTQLPGSPPVKSKQPRAEP-TDISQQTD 599
Cdd:PRK14950   364 PAPQPAKPTAAAPSPVRPTPAPSTRPKAAAAANIPPKEPVRE----TATPPPVPPRPVAPPVPHTPESAPKlTRAAIPVD 439

                           90
                   ....*....|....*.
gi 2032737686  600 ATPKSDQVKPTQAEDK 615
Cdd:PRK14950   440 EKPKYTPPAPPKEEEK 455
PDZ1_PTPN13-like cd23072
PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), and related ...
 4523-4603 1.31e-03

PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of PTPN13 [also known as Fas-associated protein-tyrosine phosphatase 1 (FAP-1), protein-tyrosine phosphatase 1E (PTP-E1), and protein-tyrosine phosphatase (PTPL1)], and related domains. PTPN13 regulates negative apoptotic signaling and mediates phosphoinositide 3-kinase (PI3K) signaling. PTPN13 has five PDZ domains. Proteins known to interact with PTPN13 PDZ domains include: PLEKHA1 and PLEKHA2 via PTPN13-PDZ domain 1, Fas receptor and thyroid receptor-interacting protein 6 via PTPN13-PDZ domain 2, nerve growth factor receptor and protein kinase N2 via PTPN13-PDZ domain 3, PDZ and LIM domain 4 (PDLIM4) via PTPN13-PDZ domains 2 and 4, and brain calpain-2 via PTPN13-PDZ domains 3, 4 and 5. Calpain-2-mediated PTPN13 fragments may be involved in abnormal tau aggregation and increased risk for Alzheimer's disease. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PTPN13 family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467285 [Multi-domain]  Cd Length: 92  Bit Score: 40.94  E-value: 1.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4523 TRLKLLRDPKdhtvsgNGLGIRVVGGkEIPGSSgEIGAYIAKILPGGNAEQTGKLVEGMQVLEWNGIPLTGKTYEEVQSI 4602
Cdd:cd23072      3 TLVNLKKDAK------YGLGFQIVGG-EKSGRL-DLGIFISSITPGGPADLDGRLKPGDRLISVNDVSLEGLSHDAAVEI 74


                   .
gi 2032737686 4603 I 4603
Cdd:cd23072     75 L 75
PHA03369 PHA03369
capsid maturational protease; Provisional
 179-447 1.39e-03

capsid maturational protease; Provisional


Pssm-ID: 223061 [Multi-domain]  Cd Length: 663  Bit Score: 44.99  E-value: 1.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  179 TSHEEAGRKQKVAPKEQGKPEEQRSPAKHPTQ---PQSPKPAVQQQGPVRPTVQQTESSKQQQQPGGPKQVQKPGhgQPA 255
Cdd:PHA03369   337 TINGLKAHNEILKTASLTAPSRVLAAAAKVAViaaPQTHTGPADRQRPQRPDGIPYSVPARSPMTAYPPVPQFCG--DPG 414

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  256 DAKQDQAKQPAQPRGPQKSQPQPSEPTKPIQQQTSAKPSSGPTKPSPQQ-----------PDSTKVTSQTAPPTKP---- 320
Cdd:PHA03369   415 LVSPYNPQSPGTSYGPEPVGPVPPQPTNPYVMPISMANMVYPGHPQEHGherkrkrggelKEELIETLKLVKKLKEeqes 494

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  321 -------------------SSQQPGPAKQPSQQPARQGAPVKPSP-QQTGPP----------KQPSQQPGPEKPSAQQAG 370
Cdd:PHA03369   495 lakeleatahkseikkiaeSEFKNAGAKTAAANIEPNCSADAAAPaTKRARPetkteleavvRFPYQIRNMESPAFVHSF 574

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  371 PAKQPPQPGSGKPPPQQT--GLVKQVPPQAGPT-KPPSQTVGPTKPLAQQAGPTKPP-----GQQPGPEKPPQQTQAGAN 442
Cdd:PHA03369   575 TSTTLAAAAGQGSDTAEAlaGAIETLLTQASAQpAGLSLPAPAVPVNASTPASTPPPlapqePPQPGTSAPSLETSLPQQ 654


                   ....*
gi 2032737686  443 QPTET 447
Cdd:PHA03369   655 KPVLS 659
PRK12757 PRK12757
cell division protein FtsN; Provisional
 286-366 1.42e-03

cell division protein FtsN; Provisional


Pssm-ID: 237191 [Multi-domain]  Cd Length: 256  Bit Score: 43.88  E-value: 1.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  286 QQQTSAK--PSSGPTKPSPQQP-DSTKVTSQTAPPTKPSSQQPGPAKQPSQQPARQGAPVKPSPQQTGPPKQPSQQPGPE 362
Cdd:PRK12757    97 QQPTQLSevPYNEQTPQVPRSTvQIQQQAQQQQPPATTAQPQPVTPPRQTTAPVQPQTPAPVRTQPAAPVTQAVEAPKVE 176


                   ....
gi 2032737686  363 KPSA 366
Cdd:PRK12757   177 AEKE 180
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
 301-413 1.46e-03

Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem to regulate formation of crystallites during the secretory stage of tooth enamel development and are thought to play a major role in the structural organisation and mineralisation of developing enamel. The extracellular matrix of the developing enamel comprises two major classes of protein: the hydrophobic amelogenins and the acidic enamelins. Circular dichroism studies of porcine amelogenin have shown that the protein consists of 3 discrete folding units: the N-terminal region appears to contain beta-strand structures, while the C-terminal region displays characteristics of a random coil conformation. Subsequent studies on the bovine protein have indicated the amelogenin structure to contain a repetitive beta-turn segment and a "beta-spiral" between Gln112 and Leu138, which sequester a (Pro, Leu, Gln) rich region. The beta-spiral offers a probable site for interactions with Ca2+ ions. Muatations in the human amelogenin gene (AMGX) cause X-linked hypoplastic amelogenesis imperfecta, a disease characterised by defective enamel. A 9bp deletion in exon 2 of AMGX results in the loss of codons for Ile5, Leu6, Phe7 and Ala8, and replacement by a new threonine codon, disrupting the 16-residue (Met1-Ala16) amelogenin signal peptide.


Pssm-ID: 197891 [Multi-domain]  Cd Length: 165  Bit Score: 42.85  E-value: 1.46e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686   301 SPQQPDSTKVTSQTAPPTKPsSQQPGPAKQPS-QQPARQgaPVKPSPQQTGPPKQPSQQP-GPEKPSAQQAGPAKQPPQP 378
Cdd:smart00818   43 SQQHPPTHTLQPHHHIPVLP-AQQPVVPQQPLmPVPGQH--SMTPTQHHQPNLPQPAQQPfQPQPLQPPQPQQPMQPQPP 119

                            90       100       110
                    ....*....|....*....|....*....|....*
gi 2032737686   379 GSGKPPPQqtglvkqvPPQAGPTKPPSQTVGPTKP 413
Cdd:smart00818  120 VHPIPPLP--------PQPPLPPMFPMQPLPPLLP 146
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 1333-1683 1.55e-03

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 45.29  E-value: 1.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1333 GISQVVLKAEKAQEAEI---PVQTAPLPGTDHVEAVREKIEKEDDKSDTSSSQQqkspqglSDTGYSSDGISSSLGEIPS 1409
Cdd:NF033609   538 GIDKPVVPEQPDEPGEIepiPEDSDSDPGSDSGSDSSNSDSGSDSGSDSTSDSG-------SDSASDSDSASDSDSASDS 610

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1410 HIPTDEKDLLKETSKKDTISQESPPSPSDlakLESTVLSILEAQASTLSDEKSAkSKEPSETYGEQTKDQLKTKPLPVTP 1489
Cdd:NF033609   611 DSASDSDSASDSDSASDSDSASDSDSASD---SDSDSDSDSDSDSDSDSDSDSD-SDSDSDSDSDSDSDSDSDSDSDSDS 686

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1490 ESYSPDEEDLKAIKEGEGTIAEEGKGAASSQADYKEEHEGDDmsarrqqryDSVEDSSESENSPVPRRKRRTSVGSSSSD 1569
Cdd:NF033609   687 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS---------DSDSDSDSDSDSDSDSDSDSDSDSDSDSD 757

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1570 EYKRDDSQGSGDEEDfirkqilEMSADEDA-SGSDDDEFIRNQLKEISAAESQKKEEVKSKAKGTAGKHRRMARKSSAGY 1648
Cdd:NF033609   758 SDSDSDSDSDSDSDS-------DSDSDSDSdSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 830

                          330       340       350
                   ....*....|....*....|....*....|....*
gi 2032737686 1649 DEDAGRRHSWHDDDDETFDESPEPKYRESKSQDSE 1683
Cdd:NF033609   831 DSDSDSDSDSDSDSDSDSDSDSDSDSESDSNSDSE 865
PRK14954 PRK14954
DNA polymerase III subunits gamma and tau; Provisional
 292-383 1.63e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184918 [Multi-domain]  Cd Length: 620  Bit Score: 44.93  E-value: 1.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  292 KPSSGpTKPSP-QQPDSTKVTSQTAPPTKPSSQQPGPAKQPSQQPArqgapVKPSPQQTGPPKQpsQQPGPEKPSAQQAG 370
Cdd:PRK14954   375 RNDGG-VAPSPaGSPDVKKKAPEPDLPQPDRHPGPAKPEAPGARPA-----ELPSPASAPTPEQ--QPPVARSAPLPPSP 446

                           90
                   ....*....|...
gi 2032737686  371 PAKQPPQPGSGKP 383
Cdd:PRK14954   447 QASAPRNVASGKP 459
Cornifin pfam02389
Cornifin (SPRR) family; SPRR genes (formerly SPR) encode a novel class of polypeptides (small ...
 201-333 1.66e-03

Cornifin (SPRR) family; SPRR genes (formerly SPR) encode a novel class of polypeptides (small proline rich proteins) that are strongly induced during differentiation of human epidermal keratinocytes in vitro and in vivo. The most characteriztic feature of the SPRR gene family resides in the structure of the central segments of the encoded polypeptides that are built up from tandemly repeated units of either eight (SPRR1 and SPRR3) or nine (SPRR2) amino acids with the general consensus XKXPEPXX where X is any amino acid. In order to avoid bacterial contamination due to the high polar-nature of the HMM the threshold has been set very high.


Pssm-ID: 280537 [Multi-domain]  Cd Length: 135  Bit Score: 41.96  E-value: 1.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  201 QRSPAKHPTQPQSPKPAVQQ-QGPVRPTVqqTESSKQQQQPGGPKQVQKPGHGQPADAKQDQAKQPAQPRGPQKSQ---P 276
Cdd:pfam02389    1 HQQQVKQPCQPPPQEPCVPTtKEPCHSKV--PEPCNPKVPEPCCPKVPEPCCPKVPEPCCPKVPEPCCPKVPEPCYpkvP 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2032737686  277 QPSEPTKPIQQQTSAKPSSGPTKPSPQQPDSTKVTSQTAPPTKPSSQQPGPAKQPSQ 333
Cdd:pfam02389   79 EPCSPKVPEPCHPKAPEPCHPKVPEPCYPKAPEPCQPKVPEPCPSTVTPGPAQQKTK 135
PDZ11_MUPP1-PDZ9_PATJ-like cd06674
PDZ domain 11 of MUPP1 of multi-PDZ-domain protein 1 (MUPP1), domain 9 of PATJ ...
 4537-4599 1.66e-03

PDZ domain 11 of MUPP1 of multi-PDZ-domain protein 1 (MUPP1), domain 9 of PATJ (protein-associated tight junction) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 11 of MUPP1, PDZ domain 9 of PATJ, and related domains. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, 9, and 13; consequently, MUPP1 PDZ7 and 8 align with PATJ PDZ6 and 7; and MUPP1 PDZ domains 10-12 align with PATJ PDZ domains 8-10. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like family PDZ11 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467162 [Multi-domain]  Cd Length: 87  Bit Score: 40.34  E-value: 1.66e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2032737686 4537 SGNGLGIRVVGGKEipgssgEIGAYIAKILPGGNAEQTGKLVEGMQVLEWNGIPLTGKTYEEV 4599
Cdd:cd06674     12 PGRGLGLSIVGKRN------DTGVFVSDIVKGGAADADGRLMQGDQILSVNGEDVRNASQEAA 68
PRK12373 PRK12373
NADH-quinone oxidoreductase subunit E;
278-430 1.77e-03

NADH-quinone oxidoreductase subunit E;


Pssm-ID: 237082 [Multi-domain]  Cd Length: 400  Bit Score: 44.41  E-value: 1.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  278 PSEPTKPIQQQTSAKPSSGPT-----KPSPQQPDSTKVTSQTAPPTKpssQQPGPAKQPSQQPARQGAPVKPSPQQTGPP 352
Cdd:PRK12373   175 PVVKPGPQIGRYASEPAGGLTslteeAGKARYNASKALAEDIGDTVK---RIDGTEVPLLAPWQGDAAPVPPSEAARPKS 251

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2032737686  353 KQPSQQPGPEKPSAQQAGPAKQppqpgsgkpppqqtglvKQVPPQAGPTKPPSQTVGPTKPLAQQAGPTKPP-GQQPGP 430
Cdd:PRK12373   252 ADAETNAALKTPATAPKAAAKN-----------------AKAPEAQPVSGTAAAEPAPKEAAKAAAAAAKPAlEDKPRP 313
PDZ5_MAGI-1_3-like cd06735
PDZ domain 5 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ...
 4527-4608 1.83e-03

PDZ domain 5 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 5 of MAGI1, 2, 3 (MAGI is also known as Membrane-associated guanylate kinase, WW and PDZ domain-containing protein) and related domains. MAGI proteins have been implicated in the control of cell migration and invasion through altering the activity of phosphatase and tensin homolog (PTEN) and modulating Akt signaling. Four MAGI proteins have been identified (MAGI1-3 and MAGIX). MAGI1-3 have 6 PDZ domains and bind to the C-terminus of PTEN via their PDZ2 domain. MAGIX has a single PDZ domain that is related to MAGI1-3 PDZ domain 5, and belongs to this MAGI1,2,3-like family. Other binding partners for MAGI1 include JAM4, C-terminal tail of high risk HPV-18 E6, megalin, TRAF6, Kir4.1 (basolateral K+ channel subunit), and cadherin 23; for MAGI2, include DASM1, dendrin, axin, beta- and delta-catenin, neuroligin, hyperpolarization-activated cation channels, beta1-adrenergic receptors, NMDA receptor, and TARPs; and for MAGI3 includes LPA2. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MAGI family PDZ5 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467217 [Multi-domain]  Cd Length: 84  Bit Score: 40.25  E-value: 1.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4527 LLRDPKdhtvsGNGLGIRvvGGKEipgsSGEIGAYIAKILPGGNAEQTGKLVEGMQVLEWNGIPLTGKTYEevQSI-IIQ 4605
Cdd:cd06735      6 LERGPK-----GFGFSIR--GGRE----YNNMPLYVLRLAEDGPAQRDGRLRVGDQILEINGESTQGMTHA--QAIeLIR 72


                   ...
gi 2032737686 4606 QSG 4608
Cdd:cd06735     73 SGG 75
valS PRK14900
valyl-tRNA synthetase; Provisional
 301-437 1.85e-03

valyl-tRNA synthetase; Provisional


Pssm-ID: 237855 [Multi-domain]  Cd Length: 1052  Bit Score: 44.98  E-value: 1.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  301 SPQQPDST-KVTSQTAPPTKPSSQQPGPAKQPSQQPARQGAPVKPSPQQTGPPKQ--PSQQPGPEKPSAQQAGPAKQPPQ 377
Cdd:PRK14900   904 SGSEANSArRDTMEIQNEQKPTQDGPAAEAQPAQENTVVESAEKAVAAVSEAAQQaaTAVASGIEKVAEAVRKTVRRSVK 983

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  378 PGSGKPPPQQTGLVKQVPPQAGPTKPPSQTVGPTKPLAQQAGPTKPPGQQPGPEKPPQQT 437
Cdd:PRK14900   984 KAAATRAAMKKKVAKKAPAKKAAAKKAAAKKAAAKKKVAKKAPAKKVARKPAAKKAAKKP 1043
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
501-656 1.96e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 44.77  E-value: 1.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  501 LCLNCQMQRTLGGDLAPGLGPGPQPLAPKQKTPI---PPSAKPSPQPQPVQKKDVTPKPDPSQAadskrppPQKKQTQLP 577
Cdd:PRK14971   354 LTLIQLAQLTQKGDDASGGRGPKQHIKPVFTQPAaapQPSAAAAASPSPSQSSAAAQPSAPQSA-------TQPAGTPPT 426

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2032737686  578 GSPPVKSKQPRAEPTDISQQTDATPKSDQVKPTQAEDKQKQPSVQKPTADSvstsvAAEQKQDLAGPRPPTQQKVTDSP 656
Cdd:PRK14971   427 VSVDPPAAVPVNPPSTAPQAVRPAQFKEEKKIPVSKVSSLGPSTLRPIQEK-----AEQATGNIKEAPTGTQKEIFTEE 500
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
 335-402 2.00e-03

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 44.52  E-value: 2.00e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2032737686  335 PARQGAPVKPSPQQTGPPKQPSQQPGPEKPSAQQAGPAKQPPQPGSGKP----PPQQTGLVKQ----VPPQAGPTK 402
Cdd:PRK01297    13 EAEQPAPAPPSPAAAPAPPPPAKTAAPATKAAAPAAAAPRAEKPKKDKPrrerKPKPASLWKLedfvVEPQEGKTR 88
PDZ2_GRIP1-2-like cd06681
PDZ domain 2 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
 4565-4610 2.31e-03

PDZ domain 2 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR) binding proteins GRIP1 (ABP/GRIP2) and GRIP2, and related domains. GRIP1 and GRIP2 each have 7 PDZ domains. The interaction of GRIP1 and GRIP2 with GluA2/3 (AMPAR subunit) regulates AMPAR trafficking and synaptic targeting. GRIP1 has an essential role in regulating AMPAR trafficking during synaptic plasticity and learning and memory. GRIP1 and GRIP2 interact with a variety of other proteins associated with protein trafficking and internalization, for example GRIP1 also interacts with KIF5 (also known as kinesin 1), EphB receptors, scaffold protein liprin-alpha, and the rasGEF GRASP-1. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This GRIP family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467169 [Multi-domain]  Cd Length: 89  Bit Score: 40.29  E-value: 2.31e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2032737686 4565 ILPGGNAEQTGKLVEGMQVLEWNGIPLTGKTYEEVQSIIIQQSGEA 4610
Cdd:cd06681     37 VRPGGPADREGTIKPGDRLLSVDGISLHGATHAEAMSILKQCGQEA 82
COG5038 COG5038
Ca2+-dependent lipid-binding protein, contains C2 domain [General function prediction only];
4735-4844 2.47e-03

Ca2+-dependent lipid-binding protein, contains C2 domain [General function prediction only];


Pssm-ID: 227371 [Multi-domain]  Cd Length: 1227  Bit Score: 44.36  E-value: 2.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4735 LGNLIIHILQARNLAPRDN--NGYSDPFVkVYLLPGRgqvmvvqnasaeYKRRTKYIQKSLNPEWNQTvIYknISVEQLK 4812
Cdd:COG5038    435 IGVVEVKIKSAEGLKKSDStiNGTVDPYI-TVTFSDR------------VIGKTRVKKNTLNPVWNET-FY--ILLNSFT 498

                           90       100       110
                   ....*....|....*....|....*....|..
gi 2032737686 4813 KKtLEVTVWDYDRFSSNDFLGEVLIELSSISQ 4844
Cdd:COG5038    499 DP-LNLSLYDFNSFKSDKVVGSTQLDLALLHQ 529
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
 259-397 2.50e-03

polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 44.03  E-value: 2.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  259 QDQAKQpAQPRGPQKSQPQPSEPTKPIQQQTSakpsSGPTKPSPQQPDSTKVTSQtapptKPSSQQPGPAKQPsQQPARQ 338
Cdd:TIGR01628  372 QDQFMQ-LQPRMRQLPMGSPMGGAMGQPPYYG----QGPQQQFNGQPLGWPRMSM-----MPTPMGPGGPLRP-NGLAPM 440

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2032737686  339 GAPVKPSPQQTGPPKQPSQQPGPEKPSAQQAGPAKQPPQP----GSGKPPPQQTGLVKQVPPQ 397
Cdd:TIGR01628  441 NAVRAPSRNAQNAAQKPPMQPVMYPPNYQSLPLSQDLPQPqstaSQGGQNKKLAQVLASATPQ 503
PHA03247 PHA03247
large tegument protein UL36; Provisional
 260-470 2.52e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.54  E-value: 2.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  260 DQAKQPAQPRGPQKSQPQPSEPTKPIQQQTS-----------AKPSSGPTKPSP------QQPDSTKVTSQTAPPTKPSS 322
Cdd:PHA03247   266 DRAPETARGATGPPPPPEAAAPNGAAAPPDGvwgaalagaplALPAPPDPPPPApagdaeEEDDEDGAMEVVSPLPRPRQ 345

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  323 QQPG-------PAKQPSQQPARQGAPVKPSPQQTGPPKQPSQQPGPEKPSAQQAG----PAKQPPQPGSGKPPPQQTGLV 391
Cdd:PHA03247   346 HYPLgfpkrrrPTWTPPSSLEDLSAGRHHPKRASLPTRKRRSARHAATPFARGPGgddqTRPAAPVPASVPTPAPTPVPA 425

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  392 KQVPPQAGPTKP--PSQTVGPTKPLAQQAGPTKPPGQQPGPEKPPQQT--QAGANQPTETapkktfcPLCTTTELLLHTP 467
Cdd:PHA03247   426 SAPPPPATPLPSaePGSDDGPAPPPERQPPAPATEPAPDDPDDATRKAldALRERRPPEP-------PGADLAELLGRHP 498


                   ...
gi 2032737686  468 EKA 470
Cdd:PHA03247   499 DTA 501
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
310-448 2.59e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 44.46  E-value: 2.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  310 VTSQTAPPTKPSSQQPGPAKQPSQQPArQGAPVKPSPQQTGPPKQPSQQPGPekPSAQQAGPAKQPPqPGSGKPPPQQTG 389
Cdd:PRK07003   362 VTGGGAPGGGVPARVAGAVPAPGARAA-AAVGASAVPAVTAVTGAAGAALAP--KAAAAAAATRAEA-PPAAPAPPATAD 437

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2032737686  390 LVKQVPPQAGPTKPPSQTVGPTKPLAQQAGPTKPPGQQPGPEKPPQQTQAGANQPTETA 448
Cdd:PRK07003   438 RGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRA 496
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
372-661 2.73e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 44.10  E-value: 2.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  372 AKQPPQPGSGK-PPPQQTGLVKQVPPQAGP----TKPPSQTVGPTKPLAQQAGPTKPPGQQPGPEKPPQQTQAGANQpte 446
Cdd:PRK12323   362 AFRPGQSGGGAgPATAAAAPVAQPAPAAAApaaaAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQ--- 438

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  447 tapkktfcplctttelllhtpekanyntctqchtvvcslcgfnpnphiteisewlclncqmqrtlGGDLAPGLGPGPQPL 526
Cdd:PRK12323   439 -----------------------------------------------------------------ASARGPGGAPAPAPA 453

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  527 APKQKTPIPPSAKPSPQPQPVQKKDVTPKPDP---SQAADSKRPPPQKKQTQLPGSPPVKSKQPRAEPTDISQQTDATPK 603
Cdd:PRK12323   454 PAAAPAAAARPAAAGPRPVAAAAAAAPARAAPaaaPAPADDDPPPWEELPPEFASPAPAQPDAAPAGWVAESIPDPATAD 533

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2032737686  604 SDQVKPTQAEDKQKQPSvqkPTADSVSTSVAAEQKQDLAGPRPPTqqkVTDSPKPELA 661
Cdd:PRK12323   534 PDDAFETLAPAPAAAPA---PRAAAATEPVVAPRPPRASASGLPD---MFDGDWPALA 585
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 262-439 3.38e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 44.01  E-value: 3.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  262 AKQPAQPRGPQKSQPQPSEPTKPIQQQTSAKPSSGPTKPSPQqpdstkVTSQTAPPTKPSSQQPGPAKQPSQQPARQGAP 341
Cdd:PHA03307   769 AEALALLEPAEPQRGAGSSPPVRAEAAFRRPGRLRRSGPAAD------AASRTASKRKSRSHTPDGGSESSGPARPPGAA 842

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  342 VKPSPQQTGPPKQPSQQPGPEKPSAQQAGPAKQPP----QPGSGKPPPQQTGLVKQVPPQAGPTKPPSQTVGPTKP--LA 415
Cdd:PHA03307   843 ARPPPARSSESSKSKPAAAGGRARGKNGRRRPRPPepraRPGAAAPPKAAAAAPPAGAPAPRPRPAPRVKLGPMPPggPD 922

                          170       180
                   ....*....|....*....|....
gi 2032737686  416 QQAGPTKPPgqqPGPEKPPQQTQA 439
Cdd:PHA03307   923 PRGGFRRVP---PGDLHTPAPSAA 943
ftsN TIGR02223
cell division protein FtsN; FtsN is a poorly conserved protein active in cell division in a ...
 529-714 3.42e-03

cell division protein FtsN; FtsN is a poorly conserved protein active in cell division in a number of Proteobacteria. The N-terminal 30 residue region tends to by Lys/Arg-rich, and is followed by a membrane-spanning region. This is followed by an acidic low-complexity region of variable length and a well-conserved C-terminal domain of two tandem regions matched by pfam05036 (Sporulation related repeat), found in several cell division and sporulation proteins. The role of FtsN as a suppressor for other cell division mutations is poorly understood; it may involve cell wall hydrolysis. [Cellular processes, Cell division]


Pssm-ID: 274041 [Multi-domain]  Cd Length: 298  Bit Score: 43.14  E-value: 3.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  529 KQKTPIPPSAKPSPQPQPVQKKDVTPKPDpSQAADSKrpPPQKKQTQLPGSPPVKSKQPRAEPTDISQQTDAtpksdqvK 608
Cdd:TIGR02223   52 KQANEPETLQPKNQTENGETAADLPPKPE-ERWSYIE--ELEAREVLINDPEEPSNGGGVEESAQLTAEQRQ-------L 121

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  609 PTQAEDKQKQPSVQKPTADSVSTSVAAEQKQDLAGPRPPTQQKVTDSPKPELAKpsQDTHPAGDKPDSKPVPQVSRQKSd 688
Cdd:TIGR02223  122 LEQMQADMRAAEKVLATAPSEQTVAVEARKQTAEKKPQKARTAEAQKTPVETEK--IASKVKEAKQKQKALPKQTAETQ- 198

                          170       180
                   ....*....|....*....|....*.
gi 2032737686  689 PKFASQPGARPDAKAQKPIDPTQTKD 714
Cdd:TIGR02223  199 SNSKPIETAPKADKADKTKPKPKEKA 224
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
 524-727 3.43e-03

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 43.88  E-value: 3.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  524 QPLAPKQKTPIPPSAKPSPQpqpVQKKDVTPKPDPSQAADSKRPPPQKKQTQLPGSPPVKSKQPRAEPTDISQQTDATPK 603
Cdd:PTZ00108  1156 QRLKSKTKGKASKLRKPKLK---KKEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQK 1232

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  604 SDQVKPTQAEDKQKQPSVQKPTADSVSTSVAAEQKQDLAGPRPPTQQKVTDSPKP--ELAKPSQDTHPAGDKPDSKPVPQ 681
Cdd:PTZ00108  1233 TKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPpsKRPDGESNGGSKPSSPTKKKVKK 1312

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 2032737686  682 VSRQKSDPKFASQPGARPDAKAQKpiDPTQTKDDPKKLPTKPAPKP 727
Cdd:PTZ00108  1313 RLEGSLAALKKKKKSEKKTARKKK--SKTRVKQASASQSSRLLRRP 1356
PDZ_PDLIM-like cd06753
PDZ domain of PDZ-LIM family proteins, and related domains; PDZ (PSD-95 (Postsynaptic density ...
 4542-4603 3.58e-03

PDZ domain of PDZ-LIM family proteins, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of PDZ-LIM family proteins including PDLIM1-7, and related domains. PDZ-LIM family proteins (also known as Zasp PDZ domain proteins) are involved in the rearrangement of the actin cytoskeleton; they mediate association with the cytoskeleton through alpha-actinin as well as with other proteins involved in signal transduction pathways. Members of this family include PDLIM1 (also known as C-terminal LIM domain protein 1, elfin, LIM domain protein CLP-36), PDLIM2 (also known as PDZ-LIM protein mystique), PDLIM3 (also known as actinin-associated LIM protein, alpha-actinin-2-associated LIM protein, ALP), PDLIM4 (also known as LIM protein RIL, Reversion-induced LIM protein), PDLIM5 (also known as enigma homolog, ENH, enigma-like PDZ and LIM domains protein), PDLIM6 (also known as LIM domain-binding protein 3, ZASP, Cypher, Oracle), and PDLIM7 (also known as PDZ and LIM domain protein 7, LIM mineralization protein, LMP; protein enigma). PDLIM1 has been shown to negatively regulate NF-kappaB-mediated signaling in the cytoplasm. PDLIM7 negatively regulates p53 through binding murine double minute 2 (MDM2). The PDZ domains of PDZ-LIM family proteins PDLIM1, 2, 3, 5, 6, 7 have been shown to bind actin. Other PDZ-LIM family PDZ domain binding partners include thyroid receptor interacting protein-6 (PDLIM4-PDZ), the LIM domain of PDLIM4 (PDLIM4-PDZ), tropomyosin (PDLIM7-PDZ), myotilin and calsarcin 1 (PDLIM6-PDZ), and proteins from the myotilin and FATZ (calsarcin/myozenin) families (PDLIM1, 3, 4, 6 PDZ domains). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PDLIM-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467235 [Multi-domain]  Cd Length: 79  Bit Score: 39.44  E-value: 3.58e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2032737686 4542 GIRVVGGKE--IPgssgeigAYIAKILPGGNAEQTGkLVEGMQVLEWNGIPLTGKTYEEVQSII 4603
Cdd:cd06753     11 GFRLQGGKDfnQP-------LTISRVTPGGKAAQAN-LRPGDVILAINGESTEGMTHLEAQNKI 66
SOBP pfam15279
Sine oculis-binding protein; SOBP is associated with syndromic and nonsyndromic intellectual ...
 262-434 3.76e-03

Sine oculis-binding protein; SOBP is associated with syndromic and nonsyndromic intellectual disability. It carries a zinc-finger of the zf-C2H2 type at the N-terminus, and a highly characteriztic C-terminal PhPhPhPhPhPh motif. The deduced 873-amino acid protein contains an N-terminal nuclear localization signal (NLS), followed by 2 FCS-type zinc finger motifs, a proline-rich region (PR1), a putative RNA-binding motif region, and a C-terminal NLS embedded in a second proline-rich motif. SOBP is expressed in various human tissues, including developing mouse brain at embryonic day 14. In postnatal and adult mouse brain SOBP is expressed in all neurons, with intense staining in the limbic system. Highest expression is in layer V cortical neurons, hippocampus, pyriform cortex, dorsomedial nucleus of thalamus, amygdala, and hypothalamus. Postnatal expression of SOBP in the limbic system corresponds to a time of active synaptogenesis. the family is also referred to as Jackson circler, JXC1. In seven affected siblings from a consanguineous Israeli Arab family with mental retardation, anterior maxillary protrusion, and strabismus mutations were found in this protein.


Pssm-ID: 464609 [Multi-domain]  Cd Length: 325  Bit Score: 43.26  E-value: 3.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  262 AKQPAQ-PRGPQKSQPQPSEPTKPIQQQT------SAKPSSGPTKPSPQQPDSTKVTSQTAPP----TKPSSQQPGPAKQ 330
Cdd:pfam15279  123 SKLLAPkPHEPPSLPPPPLPPKKGRRHRPglhpplGRPPGSPPMSMTPRGLLGKPQQHPPPSPlpafMEPSSMPPPFLRP 202

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  331 PSQQPARQgapvkpSPQQTGPPKQPSQQPGPEKPSAQQAGPAKQP---------PQPGSGKPPPQQTGLVKQVPPQAGPT 401
Cdd:pfam15279  203 PPSIPQPN------SPLSNPMLPGIGPPPKPPRNLGPPSNPMHRPpfsphhpppPPTPPGPPPGLPPPPPRGFTPPFGPP 276

                          170       180       190
                   ....*....|....*....|....*....|...
gi 2032737686  402 KPPsqtvGPTKPLAQQAGPTKPPgqqPGPEKPP 434
Cdd:pfam15279  277 FPP----VNMMPNPPEMNFGLPS---LAPLVPP 302
PRK14954 PRK14954
DNA polymerase III subunits gamma and tau; Provisional
 324-413 3.88e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184918 [Multi-domain]  Cd Length: 620  Bit Score: 43.78  E-value: 3.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  324 QPGPAKQPSqqPARQGAPVKPSPQQtgPPKQPSQQPGPEKPSAQQAGPAKQpPQPGSGKPPPQQTGLVKQVPPQAGPTKP 403
Cdd:PRK14954   375 RNDGGVAPS--PAGSPDVKKKAPEP--DLPQPDRHPGPAKPEAPGARPAEL-PSPASAPTPEQQPPVARSAPLPPSPQAS 449

                           90
                   ....*....|
gi 2032737686  404 PSQTVGPTKP 413
Cdd:PRK14954   450 APRNVASGKP 459
PDZ1_FL-whirlin cd06740
PDZ domain 1 of the full-length isoform of whirlin and related domains; PDZ (PSD-95 ...
 4523-4603 3.91e-03

PDZ domain 1 of the full-length isoform of whirlin and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of the full-length isoform of whirlin and related domains. Whirlin is an essential protein for developmental pathways in photoreceptor cells of the retina and hair cells of the inner ear. The full-length whirlin isoform has two harmonin N-like domains, three PDZ domains, a proline-rich region, and a PDZ-binding motif. Whirlin isoforms may form different complexes at the periciliary membrane complex (PMC) in photoreceptors, and the stereociliary tip and base in inner ear hair cells. It interacts with ADGRV1 and usherin at the PMC; with SANS and RpgrORF15 at the connecting cilium in photoreceptors; with EPS8, MYO15A, p55, and CASK proteins at the stereociliary tip of inner ear hair cells; and with ADGRV1, usherin, and PDZD7 at the stereociliary base in inner ear hair cells. Mutations in the gene encoding whirlin (WHRN; also known as USH2D and DFNB31), have been found to cause either USH2 subtype (USH2D) or autosomal recessive non-syndromic deafness type 31 (DFNB31). Whirlin is the key protein in the USH2 complex (whirlin, usherin and GPR98) which recruits other USH2 causative proteins at the periciliary membrane in photoreceptors and the ankle link of the stereocilia in hair cells. Whirlin's interaction with espin, another stereociliary protein, may be important for the architecture of the USH2 complex. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This whirlin family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467222 [Multi-domain]  Cd Length: 82  Bit Score: 39.27  E-value: 3.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4523 TRLKLLRDPKDHTvsgnGLGIRVVGGKEipgsSGeIGAYIAKILPGGNAEQTGkLVEGMQVLEWNGIPLTGKTYEEVQSI 4602
Cdd:cd06740      1 VRQVTLKRSKSHE----GLGFSIRGGAE----HG-VGIYVSLVEPGSLAEKEG-LRVGDQILRVNDVSFEKVTHAEAVKI 70


                   .
gi 2032737686 4603 I 4603
Cdd:cd06740     71 L 71
Not5 COG5665
CCR4-NOT transcriptional regulation complex, NOT5 subunit [Transcription];
252-452 4.07e-03

CCR4-NOT transcriptional regulation complex, NOT5 subunit [Transcription];


Pssm-ID: 444384 [Multi-domain]  Cd Length: 874  Bit Score: 43.88  E-value: 4.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  252 GQPADAKQDQAKQPAQPRGPQKSQPQPSEPTKPIQQQTSAKPSSGPTKPSPQQPDSTKVTSQTAPPTKPSSQQPGPAKQP 331
Cdd:COG5665    269 GGTTPPSTNQLTTSNTPTSTAKAQPQPPTKKQPAKEPPSDTASGNPSAPSVLINSDSPTSEDPATASVPTTEETTAFTTP 348

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  332 SQQPARQGAPVKPSPQqtgpPKQPSQQPGPEKPSAQQAGPA---------KQPPQPGSGKPPPQQTGLVKQV----PPQA 398
Cdd:COG5665    349 SSVPSTPAEKDTPATD----LATPVSPTPPETSVDKKVSPDsatsstkseKEGGTASSPMPPNIAIGAKDDVdatdPSQE 424

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2032737686  399 GPTKPPSQTVGPTKPLAQQAGPTKPPgqQPGPEKPPQQTQAGANQPTETAPKKT 452
Cdd:COG5665    425 AKEYTKNAPMTPEADSAPESSVRTEA--SPSAGSDLEPENTTLRDPAPNAIPPP 476
C2B_Munc13-like cd04009
C2 domain second repeat in Munc13 (mammalian uncoordinated)-like proteins; C2-like domains are ...
 5112-5210 4.16e-03

C2 domain second repeat in Munc13 (mammalian uncoordinated)-like proteins; C2-like domains are thought to be involved in phospholipid binding in a Ca2+ independent manner in both Unc13 and Munc13. Caenorabditis elegans Unc13 has a central domain with sequence similarity to PKC, which includes C1 and C2-related domains. Unc13 binds phorbol esters and DAG with high affinity in a phospholipid manner. Mutations in Unc13 results in abnormal neuronal connections and impairment in cholinergic neurotransmission in the nematode. Munc13 is the mammalian homolog which are expressed in the brain. There are 3 isoforms (Munc13-1, -2, -3) and are thought to play a role in neurotransmitter release and are hypothesized to be high-affinity receptors for phorbol esters. Unc13 and Munc13 contain both C1 and C2 domains. There are two C2 related domains present, one central and one at the carboxyl end. Munc13-1 contains a third C2-like domain. Munc13 interacts with syntaxin, synaptobrevin, and synaptotagmin suggesting a role for these as scaffolding 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 third C2 repeat, C2C, and has a type-II topology.


Pssm-ID: 175976 [Multi-domain]  Cd Length: 133  Bit Score: 40.68  E-value: 4.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 5112 EQLIVEILQCRNItykfKSPD--HLPDLYVKLYVVNISTQKRVIKKKTRVCRHDREPSFNETFRFSLSPAGHSLQ----- 5184
Cdd:cd04009     16 QSLRVEILNARNL----LPLDsnGSSDPFVKVELLPRHLFPDVPTPKTQVKKKTLFPLFDESFEFNVPPEQCSVEgalll 91

                           90       100
                   ....*....|....*....|....*..
gi 2032737686 5185 -ILLVSNggKFMKKTLIGEAYIWLDKV 5210
Cdd:cd04009     92 fTVKDYD--LLGSNDFEGEAFLPLNDI 116
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 517-660 4.50e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 43.55  E-value: 4.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  517 PGLGPGPQPLAPKqKTPIPPSA-KPSPQPQPVqkkdvtpkpdPSQAADSKRPPPqkKQTQLPGSPPVKSKQPRAEPTDIS 595
Cdd:PRK14951   366 PAAAAEAAAPAEK-KTPARPEAaAPAAAPVAQ----------AAAAPAPAAAPA--AAASAPAAPPAAAPPAPVAAPAAA 432

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2032737686  596 QQTDATPKSdqvkPTQAEDKQKQPSVQKPTADSVSTSVAAEQKQDLAGPRPPTQQKVTDSPKPEL 660
Cdd:PRK14951   433 APAAAPAAA----PAAVALAPAPPAQAAPETVAIPVRVAPEPAVASAAPAPAAAPAAARLTPTEE 493
PDZ1_Dlg1-2-4-like cd06723
PDZ domain 1 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg) ...
 4538-4577 4.59e-03

PDZ domain 1 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of Drosophila Dlg1, human Dlg1,2, and 4 and related domains. Dlg1 (also known as synapse-associated protein Dlg197 or SAP-97), Dlg2 (also known as channel-associated protein of synapse-110, postsynaptic density protein 93, or PSD-93), Dlg4 (also known as postsynaptic density protein 95, PSD-95, synapse-associated protein 90, or SAP-90) each have 3 PDZ domains and belong to the membrane-associated guanylate kinase family. Dlg1 regulates antigen receptor signaling and cell polarity in lymphocytes, B-cell proliferation and antibody production, and TGFalpha bioavailability; its PDZ3 domain binds pro-TGFalpha, and its PDZ2 domain binds the TACE metalloprotease responsible for cleaving pro-TGFalpha to a soluble form. Dlg2 is involved in N-methyl-D-aspartate (NMDA) receptor signaling. It regulates surface expression of NMDA receptors in dorsal horn neurons of the spinal cord, and it also interacts with NMDA receptor subunits and with Shaker-type K+ channel subunits to cluster into a channel complex. Dlg4 PDZ1 domain binds NMDA receptors, and its PDZ2 domain binds neuronal nitric oxide synthase (nNOS), forming a complex in neurons. The Drosophila Scribble complex (Scribble, Dlg, and lethal giant larvae) plays a role in apico-basal cell polarity, and in other forms of polarity, including regulation of the actin cytoskeleton, cell signaling and vesicular trafficking, and in tumor development. Postsynaptic targeting of Drosophila DLG requires interactions mediated by the first two PDZ domains. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Dlg-like family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467206 [Multi-domain]  Cd Length: 89  Bit Score: 39.22  E-value: 4.59e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 2032737686 4538 GNGLGIRVVGGKEIPGSSGEIGAYIAKILPGGNAEQTGKL 4577
Cdd:cd06723     10 NSGLGFSIAGGTDNPHIGDDPSIYITKIIPGGAAAADGRL 49
PRK11633 PRK11633
cell division protein DedD; Provisional
 515-568 4.72e-03

cell division protein DedD; Provisional


Pssm-ID: 236940 [Multi-domain]  Cd Length: 226  Bit Score: 41.91  E-value: 4.72e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2032737686  515 LAPGLGPGPQPLAPKQKTPIPPSAKPSPQPQPVQKKDV--TPKPDPSQAADSKRPP 568
Cdd:PRK11633    90 VAPPNTPVEPEPAPVEPPKPKPVEKPKPKPKPQQKVEAppAPKPEPKPVVEEKAAP 145
kgd PRK12270
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ...
 300-375 4.75e-03

multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;


Pssm-ID: 237030 [Multi-domain]  Cd Length: 1228  Bit Score: 43.73  E-value: 4.75e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2032737686  300 PSPQQPDSTKVTSQTAPPTKPSSQQPGPAKQPSQQPARQGAPVKPSPQQTGPPKQPSQQPGPEKPSAQQAGPAKQP 375
Cdd:PRK12270    40 STAAPTAAAAAAAAAASAPAAAPAAKAPAAPAPAPPAAAAPAAPPKPAAAAAAAAAPAAPPAAAAAAAPAAAAVED 115
CCDC47 pfam07946
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ...
 3782-3845 4.80e-03

PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of the PAT complex, an endoplasmic reticulum (ER)-resident membrane multiprotein complex that facilitates multi-pass membrane proteins insertion into membranes. The PAT complex, formed by CCDC47 and Asterix proteins, acts as an intramembrane chaperone by directly interacting with nascent transmembrane domains (TMDs), releasing its substrates upon correct folding, and is needed for optimal biogenesis of multi-pass membrane proteins. CCDC47 is required to maintain the stability of Asterix. CCDC47 is associated with various membrane-associated processes and is component of a ribosome-associated ER translocon complex involved in multi-pass membrane protein transport into the ER membrane and biogenesis. It is also involved in the regulation of calcium ion homeostasis in the ER, being also required for proper protein degradation via the ERAD (ER-associated degradation) pathway.


Pssm-ID: 462322  Cd Length: 323  Bit Score: 42.55  E-value: 4.80e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2032737686 3782 ARAKILQDIDRELDLVERESAKLRKKQAELDEEEKEIDaklrylEMGINRRKEALLKEREKRER 3845
Cdd:pfam07946  265 TREEEIEKIKKAAEEERAEEAQEKKEEAKKKEREEKLA------KLSPEEQRKYEEKERKKEQR 322
PDZ1_MAGI-1_3-like cd06731
PDZ domain 1 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ...
 4540-4613 4.83e-03

PDZ domain 1 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of MAGI1, 2, 3 (MAGI is also known as Membrane-associated guanylate kinase, WW and PDZ domain-containing protein) and related domains. MAGI proteins have been implicated in the control of cell migration and invasion through altering the activity of phosphatase and tensin homolog (PTEN) and modulating Akt signaling. Four MAGI proteins have been identified (MAGI1-3 and MAGIX). MAGI1-3 have 6 PDZ domains and bind to the C-terminus of PTEN via their PDZ2 domain. MAGIX has a single PDZ domain that is related to MAGI1-3 PDZ domain 5. Other binding partners for MAGI1 include JAM4, C-terminal tail of high risk HPV-18 E6, megalin, TRAF6, Kir4.1 (basolateral K+ channel subunit), and cadherin 23; for MAGI2, include DASM1, dendrin, axin, beta- and delta-catenin, neuroligin, hyperpolarization-activated cation channels, beta1-adrenergic receptors, NMDA receptor, and TARPs; and for MAGI3 includes LPA2. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MAGI family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as beta-strands A, -B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467213 [Multi-domain]  Cd Length: 85  Bit Score: 39.12  E-value: 4.83e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2032737686 4540 GLGIRVVGGKEipgsSGEIgAYIAKILPGGNAEQTGKLVEGMQVLEWNGIPLTGKTYEEV----QSIIIQQSGEAEIC 4613
Cdd:cd06731     12 GFGFTIIGGDE----PDEF-LQIKSVVPDGPAALDGKLRTGDVLVSVNDTCVLGYTHADVvklfQSIPIGQSVNLEVC 84
PLN02226 PLN02226
2-oxoglutarate dehydrogenase E2 component
 526-606 5.34e-03

2-oxoglutarate dehydrogenase E2 component


Pssm-ID: 177871 [Multi-domain]  Cd Length: 463  Bit Score: 42.82  E-value: 5.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  526 LAPKQKTPIPPSAKPSPQPQPVQKKDVTPKPDPSQAADSKRPPPQKKQTQLPGSPPvKSKQPRAEPTDISQQTDATPKSD 605
Cdd:PLN02226   175 VTPSQKIPETTDPKPSPPAEDKQKPKVESAPVAEKPKAPSSPPPPKQSAKEPQLPP-KERERRVPMTRLRKRVATRLKDS 253


                   .
gi 2032737686  606 Q 606
Cdd:PLN02226   254 Q 254
C2A_RIM1alpha cd04031
C2 domain first repeat contained in Rab3-interacting molecule (RIM) proteins; RIMs are ...
 5095-5175 5.35e-03

C2 domain first repeat contained in Rab3-interacting molecule (RIM) proteins; RIMs are believed to organize specialized sites of the plasma membrane called active zones. They also play a role in controlling neurotransmitter release, plasticity processes, as well as memory and learning. RIM contains an N-terminal zinc finger domain, a PDZ domain, and two C-terminal C2 domains (C2A, C2B). 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. Members here have a type-I topology and do not bind Ca2+.


Pssm-ID: 175997 [Multi-domain]  Cd Length: 125  Bit Score: 40.31  E-value: 5.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 5095 VMGEIKIALKKEMKTdgEQLIVEILQCRNItykfKSPDH--LPDLYVKLYVVNISTQKRviKKKTRVCRHDREPSFNETF 5172
Cdd:cd04031      1 ITGRIQIQLWYDKVT--SQLIVTVLQARDL----PPRDDgsLRNPYVKVYLLPDRSEKS--KRRTKTVKKTLNPEWNQTF 72


                   ...
gi 2032737686 5173 RFS 5175
Cdd:cd04031     73 EYS 75
PRK11633 PRK11633
cell division protein DedD; Provisional
 298-386 5.36e-03

cell division protein DedD; Provisional


Pssm-ID: 236940 [Multi-domain]  Cd Length: 226  Bit Score: 41.91  E-value: 5.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  298 TKPSPQQPDSTKVTSQTAPPTKPSSQQPGPAKQPSQQPARQGAPVKPSPQQTGPPKQPSQQPGPEKPSAQQAGPAKQPPQ 377
Cdd:PRK11633    60 TQALPTQPPEGAAEAVRAGDAAAPSLDPATVAPPNTPVEPEPAPVEPPKPKPVEKPKPKPKPQQKVEAPPAPKPEPKPVV 139


                   ....*....
gi 2032737686  378 pgSGKPPPQ 386
Cdd:PRK11633   140 --EEKAAPT 146
kgd PRK12270
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ...
 306-383 5.44e-03

multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;


Pssm-ID: 237030 [Multi-domain]  Cd Length: 1228  Bit Score: 43.34  E-value: 5.44e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2032737686  306 DSTKVTSQTAPPTKPSSQQPGPAKQPSQQPARQGAPVKPSPQQTGPPKQPSQQP-GPEKPSAQQAGPAKQPPQPGSGKP 383
Cdd:PRK12270    37 GPGSTAAPTAAAAAAAAAASAPAAAPAAKAPAAPAPAPPAAAAPAAPPKPAAAAaAAAAPAAPPAAAAAAAPAAAAVED 115
PHA03291 PHA03291
envelope glycoprotein I; Provisional
 246-362 5.47e-03

envelope glycoprotein I; Provisional


Pssm-ID: 223033 [Multi-domain]  Cd Length: 401  Bit Score: 42.63  E-value: 5.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  246 VQKPGHGQPADAKQDQAKQPAQPRGPQKSQPQPSEPTKPiqQQTSAKPSSGPTKPSPQQPdstkvtsqtAPPTKPSSQQP 325
Cdd:PHA03291   173 AAPPLGEGSADGSCDPALPLSAPRLGPADVFVPATPRPT--PRTTASPETTPTPSTTTSP---------PSTTIPAPSTT 241

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2032737686  326 GPAKQPSQQPARQGAPVKPSPqQTGPPKQPSQQPGPE 362
Cdd:PHA03291   242 IAAPQAGTTPEAEGTPAPPTP-GGGEAPPANATPAPE 277
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
 188-403 5.54e-03

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 42.99  E-value: 5.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  188 QKVAPKEqgkPEEQRSPAKHPTQPQSPKPAV--QQQGPVRPTVQQTESSKQQQQPGGPKQVQKPGHGQPADAKQ-----D 260
Cdd:PLN03209   326 QRVPPKE---SDAADGPKPVPTKPVTPEAPSppIEEEPPQPKAVVPRPLSPYTAYEDLKPPTSPIPTPPSSSPAssksvD 402

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  261 QAKQPAQPRGPQKSQPQPSEP-TKPIQQQT-SAKPSSG---------PTKPSPQQPD--STKVTSQTAPPTKPSSQQPGP 327
Cdd:PLN03209   403 AVAKPAEPDVVPSPGSASNVPeVEPAQVEAkKTRPLSPyaryedlkpPTSPSPTAPTgvSPSVSSTSSVPAVPDTAPATA 482

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2032737686  328 AKQPSQQPARQGAPVkpSPQQTGPPKQPSQQPGPEKPSAQQAGPAK-QPPQPGSGKPPPQQTGLVKQVPPQAGPTKP 403
Cdd:PLN03209   483 ATDAAAPPPANMRPL--SPYAVYDDLKPPTSPSPAAPVGKVAPSSTnEVVKVGNSAPPTALADEQHHAQPKPRPLSP 557
kgd PRK12270
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ...
 315-402 5.58e-03

multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;


Pssm-ID: 237030 [Multi-domain]  Cd Length: 1228  Bit Score: 43.34  E-value: 5.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  315 APPTKPSSQQPGPAKQPSQQPARQGAPVKPSPQQTGPPKQ-PSQQPGPEKPSAQQAGPAKQPPQPgsGKPPPQQTGLVKQ 393
Cdd:PRK12270    39 GSTAAPTAAAAAAAAAASAPAAAPAAKAPAAPAPAPPAAAaPAAPPKPAAAAAAAAAPAAPPAAA--AAAAPAAAAVEDE 116


                   ....*....
gi 2032737686  394 VPPQAGPTK 402
Cdd:PRK12270   117 VTPLRGAAA 125
SSDP pfam04503
Single-stranded DNA binding protein, SSDP; This is a family of eukaryotic single-stranded DNA ...
 204-449 5.60e-03

Single-stranded DNA binding protein, SSDP; This is a family of eukaryotic single-stranded DNA binding proteins with specificity to a pyrimidine-rich element found in the promoter region of the alpha2(I) collagen gene.


Pssm-ID: 461334 [Multi-domain]  Cd Length: 293  Bit Score: 42.25  E-value: 5.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  204 PAKHPTQPQSPKPAVQQQGPVRPTVQQTESSKQQQqpggpkqvqkpghgQPADAKQDQAKQPAQPRGPQkSQP-----QP 278
Cdd:pfam04503   19 AAPSPVMGQMPPGDGMPGGPMPPGFFQSPPSHPSS--------------QPSPHAQPPPHNPATMMGPH-SQPfmgprYP 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  279 SEPTKPIQQQTSAKPSSGPTKPSPQQPDSTKvtsqtapptkPSSQQPGPAKQPSQQ---PARQG--APVKP---SPQQTG 350
Cdd:pfam04503   84 GGPRPSVRMPQQGNDFNGPPGQQPMMPNSMD----------PTRPGGHPNMGGPMQrmnPPRGPgmGPMGPqsyGPGMRG 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  351 PPKQPSQQPGPEKPSAQQAGPAKQPPQPGSGKPPPQQTGlvkqvppqagptKPPSQTVGPtkplaqqaGPTKPPGQQPGP 430
Cdd:pfam04503  154 PPPNSTDGPGGMPPMNMGPGGRRPWPQPNASNPLPYSSS------------SPGSYGGPP--------GGGGPPGPTPIM 213

                          250
                   ....*....|....*....
gi 2032737686  431 EKPPQQTQAGANQPTETAP 449
Cdd:pfam04503  214 PSPQDSTNSGENMYTLMNP 232
KREPA2 cd23959
Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of ...
 257-457 5.67e-03

Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of the parasitic protozoan's KREPA RNA editing catalytic complex (RECC). Kinetoplastid RNA editing (KRE) proteins occur as pairs or sets of related proteins in multiple complexes. KREPA complex is composed of six components (KREPA1-6), which share a conserved C-terminal region containing an oligonucleotide-binding (OB)-fold-like domain. KREPAs are responsible for the site-specific insertion and deletion of U nucleotides in the kinetoplastid mitochondria pre-messenger RNA. Apart from the conserved C-terminal OB-fold domain, KREPA1, KREPA2, and KREPA3 contain two conserved C2H2 zinc-finger domains. KREPA2 and kinetoplastid RNA editing ligase 1 (KREL1) are specific for ligation post-U-deletion and are paralogous to KREL2 and KREPA1 that are specific for ligation post-U-insertion. KREPA2, is critical for RECC stability and KREL1 integration into the complex.


Pssm-ID: 467780 [Multi-domain]  Cd Length: 424  Bit Score: 42.93  E-value: 5.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  257 AKQDQAKQPaqPRGPQKSQPQPSePTKPIQQQTSAKPSSGPTKPSPQQPDSTKV----TSQTAPPTKPSS---------- 322
Cdd:cd23959     48 ARPSDQEEP--LYGAVSPEGENP-FDGPGLVTASTVSDCYVGNANFYEVDMSDAfamaPDESLGPFRAARvpnpfsasss 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  323 ---QQPGPAKQPSQQPARQGAPVK-----PSPQQTGPPKQPSQQPGPEKPSAQQAGPAKQPPQPGSGKPPPQQTglvkqv 394
Cdd:cd23959    125 tqrETHKTAQVAPPKAEPQTAPVTpfgqlPMFGQHPPPAKPLPAAAAAQQSSASPGEVASPFASGTVSASPFAT------ 198

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2032737686  395 ppqAGPTKPPSQTVGPTKPLAQQAGPTKPPGQqpgpekpPQQTQAGANQPTETAPKKTFCPLC 457
Cdd:cd23959    199 ---ATDTAPSSGAPDGFPAEASAPSPFAAPAS-------AASFPAAPVANGEAATPTHACTIC 251
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
 1008-1375 6.15e-03

pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.


Pssm-ID: 468201 [Multi-domain]  Cd Length: 684  Bit Score: 43.08  E-value: 6.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1008 RPVPAVSHSPQKTSTPpTPAAAKPKEEPGVQKEAPKLQQGRLEKTLSADKIQQGIQKEDAKpKQGKLVKAPSADKIQHAS 1087
Cdd:NF033838    43 GNNPTVTSSGNESQKE-HAKEVESHLEKILSEIQKSLDKRKHTQNVALNKKLSDIKTEYLY-ELNVLKEKSEAELTSKTK 120

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1088 QKEDPRIQQTK------LTKTASYDRVLQEVQK--EDEKLQEAKLAKTSSADKILHRVQKEDIKLQEAKLakvpsadKIL 1159
Cdd:NF033838   121 KELDAAFEQFKkdtlepGKKVAEATKKVEEAEKkaKDQKEEDRRNYPTNTYKTLELEIAESDVEVKKAEL-------ELV 193

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1160 QGIQKEDPKLQQMKMAKAlsadKIQlAAQREDTKLQEVKLPKAASVDKIQHGTQKDIKLQHEKIKKTSSVDKiqeegQKE 1239
Cdd:NF033838   194 KEEAKEPRDEEKIKQAKA----KVE-SKKAEATRLEKIKTDREKAEEEAKRRADAKLKEAVEKNVATSEQDK-----PKR 263

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1240 ETKlqRGKLSKTPSADK------IPATATADQKIPLSTLEEDKETVLPEKSTPHPE----DKKEE------------ITA 1297
Cdd:NF033838   264 RAK--RGVLGEPATPDKkendakSSDSSVGEETLPSPSLKPEKKVAEAEKKVEEAKkkakDQKEEdrrnyptntyktLEL 341

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1298 EIKDR-----------VAEEKAEVEAPYKGLQAKEEEDVKKEDLT--TGISQVVLKAE-----KAQE--------AEIPv 1351
Cdd:NF033838   342 EIAESdvkvkeaelelVKEEAKEPRNEEKIKQAKAKVESKKAEATrlEKIKTDRKKAEeeakrKAAEedkvkekpAEQP- 420

                          410       420       430
                   ....*....|....*....|....*....|
gi 2032737686 1352 QTAPLPGTDH------VEAVREKIEKEDDK 1375
Cdd:NF033838   421 QPAPAPQPEKpapkpeKPAEQPKAEKPADQ 450
PDZ3_DLG5-like cd06767
PDZ domain 3 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density ...
 4530-4606 6.18e-03

PDZ domain 3 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of Drosophila and mammalian Dlg5, and related domains. Dlg5 is a scaffold protein with multiple conserved functions that are independent of each other in regulating growth, cell polarity, and cell adhesion. It has a coiled-coil domain, 4 PDZ domains and a MAGUK domain (an SH3 domain next to a non-catalytically active guanylate kinase domain). Deregulation of Dlg5 has been implicated in the malignancy of several cancer types. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Dlg5-like family PDZ3 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467248 [Multi-domain]  Cd Length: 82  Bit Score: 38.85  E-value: 6.18e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2032737686 4530 DPKDHTV--SGNGLGIRVVGGKeipgsSGeiGAYIAKILPGGNAEQTGkLVEGMQVLEWNGIPLTGKTYEEVQSIIIQQ 4606
Cdd:cd06767      2 EPRHVSIekGSEPLGISIVSGE-----NG--GIFVSSVTEGSLAHQAG-LEYGDQLLEVNGINLRNATEQQAALILRQC 72
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
 515-663 6.77e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 42.93  E-value: 6.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  515 LAPGLGPGPQPLAPKQKTPIPPSAKPSP-QPQPVQKKDVTPKPDPSQAADSkRPPPQKKQTQLPGSPPVKSKQPRAEPTD 593
Cdd:PRK07994   375 AAPAASAQATAAPTAAVAPPQAPAVPPPpASAPQQAPAVPLPETTSQLLAA-RQQLQRAQGATKAKKSEPAAASRARPVN 453

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  594 ISQQTDAtPKSDQVKPTQAEDKQKQPSVQKPTAdsvstsVAAEQKQDLAGPRPPTQQkVTDSPKPELAKP 663
Cdd:PRK07994   454 SALERLA-SVRPAPSALEKAPAKKEAYRWKATN------PVEVKKEPVATPKALKKA-LEHEKTPELAAK 515
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
 308-558 7.09e-03

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 42.61  E-value: 7.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  308 TKVTSQTAPPTKPSSqqpgpAKQPSQQPARQGAPVKPSPQQT-GPPKQPSQQPGPEKPSA--QQAGPAKQP-PQPGSGKP 383
Cdd:PLN03209   321 AKIPSQRVPPKESDA-----ADGPKPVPTKPVTPEAPSPPIEeEPPQPKAVVPRPLSPYTayEDLKPPTSPiPTPPSSSP 395

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  384 --PPQQTGLVKQVPPQAGPTKPPSQTVGPTKPL---AQQAGPTKPPGQQPGpEKPPqqtqagaNQPTETAPKKTfCPLCT 458
Cdd:PLN03209   396 asSKSVDAVAKPAEPDVVPSPGSASNVPEVEPAqveAKKTRPLSPYARYED-LKPP-------TSPSPTAPTGV-SPSVS 466

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  459 TTELLLHTPEKA--NYNTCTQCHtvvcslcgfnPNPHITEISEWLclncqmqrtLGGDLAPGLGPGPQPLAPKQKTPIPP 536
Cdd:PLN03209   467 STSSVPAVPDTApaTAATDAAAP----------PPANMRPLSPYA---------VYDDLKPPTSPSPAAPVGKVAPSSTN 527

                          250       260
                   ....*....|....*....|....*..
gi 2032737686  537 SAKP----SPQPQPVQKKD-VTPKPDP 558
Cdd:PLN03209   528 EVVKvgnsAPPTALADEQHhAQPKPRP 554
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
 288-387 7.17e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 42.87  E-value: 7.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  288 QTSAKPSSGPTKPSPQQPDSTKVTSQTAPPTKPSSqqPGPAKQPSQQPARQGAPVKPSPQQTGPPKQPSQQPGPEkPSAQ 367
Cdd:PRK14950   357 EALLVPVPAPQPAKPTAAAPSPVRPTPAPSTRPKA--AAAANIPPKEPVRETATPPPVPPRPVAPPVPHTPESAP-KLTR 433

                           90       100
                   ....*....|....*....|
gi 2032737686  368 QAGPAKQPPQPGSGKPPPQQ 387
Cdd:PRK14950   434 AAIPVDEKPKYTPPAPPKEE 453
PRK10905 PRK10905
cell division protein DamX; Validated
 254-425 7.63e-03

cell division protein DamX; Validated


Pssm-ID: 236792 [Multi-domain]  Cd Length: 328  Bit Score: 42.23  E-value: 7.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  254 PADAKQDQAKQPAQPRGPQKSQPQP------SEPTKPIQQQTSAKPSSGPTKPSPQQPdstkVTSQTAPPTKPSSQQPgp 327
Cdd:PRK10905    75 PISSTPTQGQTPVATDGQQRVEVQGdlnnalTQPQNQQQLNNVAVNSTLPTEPATVAP----VRNGNASRQTAKTQTA-- 148

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  328 AKQPSQQPARQGAPVKPspqqtgppkqpsqqpgpEKPSAQQAGPAKQPPQPGSGKPPPQQTGLVKQVPPQAGPTKPPSQT 407
Cdd:PRK10905   149 ERPATTRPARKQAVIEP-----------------KKPQATAKTEPKPVAQTPKRTEPAAPVASTKAPAATSTPAPKETAT 211

                          170
                   ....*....|....*...
gi 2032737686  408 VGPTKPLAQQAGPTKPPG 425
Cdd:PRK10905   212 TAPVQTASPAQTTATPAA 229
KLF9_13_N-like cd21975
Kruppel-like factor (KLF) 9, KLF13, KLF14, KLF16, and similar proteins; Kruppel/Krueppel-like ...
 325-451 7.70e-03

Kruppel-like factor (KLF) 9, KLF13, KLF14, KLF16, and similar proteins; Kruppel/Krueppel-like transcription factors (KLFs) belong to a family of proteins, called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. KLF9, KLF10, KLF11, KLF13, KLF14, and KLF16 share a conserved alpha-helical motif AA/VXXL that mediates their binding to Sin3A and their activities as transcriptional repressors. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the related N-terminal domains of KLF9, KLF13, KLF14, KLF16, and similar proteins.


Pssm-ID: 409240 [Multi-domain]  Cd Length: 163  Bit Score: 40.44  E-value: 7.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  325 PGP--AKQPSQQPARQGAPVKPSPQQTGPPKQPSQQPGPEKPSA-------QQAGPAKQPPQPG----SGKPPPQQTGLV 391
Cdd:cd21975     23 PDPegAGLAAGLDVRATREVAKGPGPPGPAWKPDGADSPGLVTAaphllaaNVLAPLRGPSVEGssleSGDADMGSDSDV 102

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  392 KQVPPQAGPTKPPSQTVGPTKPLAQQAGPtkPPGQQPGPEKPPQQTQAGANQPTETAPKK 451
Cdd:cd21975    103 APASGAAASTSPESSSDAASSPSPLSLLH--PGEAGLEPERPRPRVRRGVRRRGVTPAAK 160
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
 335-432 8.01e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 42.49  E-value: 8.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  335 PARQGAPVKPSPQQTgPPKQPSQQPGPEKPSAQQAGPAKQPPQPGSGKPPPQQtglvkqvPPQAGPTKPPSQTVGPTKPL 414
Cdd:PRK14950   362 PVPAPQPAKPTAAAP-SPVRPTPAPSTRPKAAAAANIPPKEPVRETATPPPVP-------PRPVAPPVPHTPESAPKLTR 433

                           90
                   ....*....|....*...
gi 2032737686  415 AQQAGPTKPPGQQPGPEK 432
Cdd:PRK14950   434 AAIPVDEKPKYTPPAPPK 451
PHA03419 PHA03419
E4 protein; Provisional
 273-394 8.52e-03

E4 protein; Provisional


Pssm-ID: 223079 [Multi-domain]  Cd Length: 200  Bit Score: 41.09  E-value: 8.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  273 KSQPQPSEPTKPiQQQTSAKPSSGPTKPSPQQPDSTKVTSQTAPPtkPSSQQPGPAKQPSQQPARQGAPVKPSPQQTG-- 350
Cdd:PHA03419    46 ETGYPFCPPTTP-HPSSQPPPCPPSPGHPPQTNDTHEKDLALQPP--PGGKKKEKKKKETEKPAQGGEKPDQGPEAKGeg 122

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2032737686  351 ---PPKQPSQQPGPEKPSAQqaGPAKQPPQPGSGKPPPQQTGLVKQV 394
Cdd:PHA03419   123 eghEPEDPPPEDTPPPPGGE--GEVEGGPSPGPGPGPLDQEGLLPGV 167
SP4_N cd22536
N-terminal domain of transcription factor Specificity Protein (SP) 4; Specificity Proteins ...
 287-446 8.64e-03

N-terminal domain of transcription factor Specificity Protein (SP) 4; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. Human SP4 is a risk gene of multiple psychiatric disorders including schizophrenia, bipolar disorder, and major depression. SP4 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP4.


Pssm-ID: 411773 [Multi-domain]  Cd Length: 623  Bit Score: 42.60  E-value: 8.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  287 QQTSAKPSSGPTKPSPQQPDSTKVTSQTAPPTKPSSQQPGPAKQPSQQPARQGAPVKPSPQ-QTGPPKQPSQQPGPEKPS 365
Cdd:cd22536    275 QLVSTPITTASVSTMPESPSSSTTCTTTASTSLTSSDTLVSSAETGQYASTAASSERTEEEpQTSAAESEAQSSSQLQSN 354

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  366 AQQAGP--AKQPPQPGSGKPPPQQTGLVKQvppqagptkPPSQTVGPTKPLAQQAGPTKPPGQQPGPEKPPQQTQAGANq 443
Cdd:cd22536    355 GLQNVQdqSNSLQQVQIVGQPILQQIQIQQ---------PQQQIIQAIQPQSFQLQSGQTIQTIQQQPLQNVQLQAVQS- 424


                   ...
gi 2032737686  444 PTE 446
Cdd:cd22536    425 PTQ 427
PDZ4_GRIP1-2-like cd06686
PDZ domain 4 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
 4539-4617 8.65e-03

PDZ domain 4 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR) binding proteins GRIP1 (ABP/GRIP2) and GRIP2, and related domains. GRIP1 and GRIP2 each have 7 PDZ domains. The interaction of GRIP1 and GRIP2 with GluA2/3 (AMPAR subunit) regulates AMPAR trafficking and synaptic targeting. GRIP1 has an essential role in regulating AMPAR trafficking during synaptic plasticity and learning and memory. GRIP1 and GRIP2 interact with a variety of other proteins associated with protein trafficking and internalization, for example GRIP1 also interacts with KIF5 (also known as kinesin 1), EphB receptors, scaffold protein liprin-alpha, and the rasGEF GRASP-1. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This GRIP family PDZ4 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467174 [Multi-domain]  Cd Length: 99  Bit Score: 38.87  E-value: 8.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 4539 NGLGIRVVGG---KEIPGSSgeigAYIAKILPGGNAEQTGKLVEGMQVLEWNGIPLTGKTYEEVQSIIIQQSGEAEICVR 4615
Cdd:cd06686     18 KGFGIQLQGGvfaTETLSSP----PLISFIEPDSPAERCGVLQVGDRVLSINGIPTEDRTLEEANQLLRDSASKVTLEIE 93


                   ..
gi 2032737686 4616 LD 4617
Cdd:cd06686     94 FD 95
Herpes_TAF50 pfam03326
Herpesvirus transcription activation factor (transactivator); This family includes EBV BRLF1 ...
 291-674 8.73e-03

Herpesvirus transcription activation factor (transactivator); This family includes EBV BRLF1 and similar ORF 50 proteins from other herpesviruses.


Pssm-ID: 308764 [Multi-domain]  Cd Length: 568  Bit Score: 42.38  E-value: 8.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  291 AKPSSGPTKPSPQQPDSTK----VTSQTAPPTKPSSQQPGPAKQPSQQPArQGAPVKPSPQQTgppkqpSQQPGPEKPSA 366
Cdd:pfam03326  200 MGPDGGLSHPAGSFFAFTDelesLIRDPEPRYQPSPTMPQQALKPGAQSS-DTSGVSDTEQSA------RQTATAEPQRL 272

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  367 QQAGPAKQPPQPGSGKPP----PQQTGLVKQVPPQAGPTKPPSQTVGPTKPLAQQAGPTKPpgqqpgPEKPPQQTQAGAn 442
Cdd:pfam03326  273 QAPGFSRSTSRPARGQTAqyflAAQQHGVVSLFPSTATLVPIAGSTGVTEVVSYGHNSTSP------SSTPCPSTAVTE- 345

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  443 qptETAPKKTFCPLCTTTELLLHTPEKANYNTCTQCHTVVCSLCGFNPNPHITEISEwlclncqmqrtlggdlapglgpg 522
Cdd:pfam03326  346 ---ADHQTEPEVPWIATAHQESDQRPIGPGPEKPTFLPPVGGKQFFQGLRDSRSTSF----------------------- 399

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  523 pQPLAPKQkTPIPPSAKPSPQPQPVQKKDVTPKPDPSQaadsKRPPPQKKQTQLPGSP--PVKSKQPRAEPTDISQQTDA 600
Cdd:pfam03326  400 -LTAPEAT-SAISDVFQGTEVCQPKRIRALHPPGSPSA----NRPLPSSLAPTPTGPVhePGSSLTPATVPQPLDAAPVA 473

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  601 TPK-SDQVKPTQAEDKQKQ--------------PSVQKPTADSVSTSVAAEQKQDLAGPRPPTQQKVTDS----PKPELA 661
Cdd:pfam03326  474 TPEaSHELQPPDEETPQPLdedqalcgqqdashPPPRGQLDELTTTLESMTEDLNLDSPLSPEDNEILETilndLYPEER 553

                          410
                   ....*....|...
gi 2032737686  662 KPSQDTHPAGDKP 674
Cdd:pfam03326  554 RQQEQQHSQGEEA 566
PDZ2_PDZD7-like cd10834
PDZ domain 2 of the canonical isoform 1 of PDZ domain containing 7 (PDZD7), and related ...
 4535-4589 9.09e-03

PDZ domain 2 of the canonical isoform 1 of PDZ domain containing 7 (PDZD7), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of the long isoform 1 of PDZD7, and related domains. PDZD7 is critical for the organization of Usher syndrome type 2 (USH2) complex. Usher syndrome is the leading cause of hereditary sensory deaf-blindness in humans; USH2 is the most common sub-type. Formation of the USH2 complex is based upon heterodimerization between PDZD7 and whirlin (another PDZ domain-containing protein) and a subsequent dynamic interplay between USH2 proteins via their multiple PDZ domains. The PDZD7 PDZ2 domain binds GPR98 (also known as VLGR1) and usherin (USH2A). PDZD7 and whirlin form heterodimers through their multiple PDZ domains; whirlin and PDZD7 interact with usherin and GPR98 to form an interdependent ankle link complex. PDZD7 also interacts with myosin VIIa. PDZD7 also forms homodimers through its PDZ2 domain. Various isoforms of PDZD7 produced by alternative splicing have been identified; this subgroup includes the second PDZ domain of the canonical isoform of PDZD7- isoform 1. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PDZD7-like family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467270 [Multi-domain]  Cd Length: 85  Bit Score: 38.52  E-value: 9.09e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2032737686 4535 TVSGNGLGIRVVGGKEIPgssgeIGAYIAKILPGGNAEQTGkLVEGMQVLEWNGI 4589
Cdd:cd10834      9 TSDDYCLGFNIRGGSEYG-----LGIYVSKVDPGGLAEQNG-IKVGDQILAVNGV 57
PRK12757 PRK12757
cell division protein FtsN; Provisional
 258-386 9.11e-03

cell division protein FtsN; Provisional


Pssm-ID: 237191 [Multi-domain]  Cd Length: 256  Bit Score: 41.57  E-value: 9.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  258 KQDQAkQPAQPRGPQKSQ---PQPSE--------PTKPIQQQTSAKPSSGPTKPSP-------------------QQPDS 307
Cdd:PRK12757    23 KKEEA-PLLPNHKPRTGNglpPKPEErwryikelENRQIGVPTPTEPSAGGEVNSPtqltdeqrqlleqmqadmrQQPTQ 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  308 -TKVTSQTAPPTKPSSQ-QPGPAKQPSQQPAR--QGAPVKPsPQQTGPPKQPSQQPGPEKPSAQQAGPAKQPPQPGSGKP 383
Cdd:PRK12757   102 lSEVPYNEQTPQVPRSTvQIQQQAQQQQPPATtaQPQPVTP-PRQTTAPVQPQTPAPVRTQPAAPVTQAVEAPKVEAEKE 180


                   ...
gi 2032737686  384 PPQ 386
Cdd:PRK12757   181 KEQ 183
TFIIF_alpha pfam05793
Transcription initiation factor IIF, alpha subunit (TFIIF-alpha); Transcription initiation ...
 1498-1692 9.96e-03

Transcription initiation factor IIF, alpha subunit (TFIIF-alpha); Transcription initiation factor IIF, alpha subunit (TFIIF-alpha) or RNA polymerase II-associating protein 74 (RAP74) is the large subunit of transcription factor IIF (TFIIF), which is essential for accurate initiation and stimulates elongation by RNA polymerase II.


Pssm-ID: 310411 [Multi-domain]  Cd Length: 528  Bit Score: 42.24  E-value: 9.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1498 DLKAIKEGEGTIAEEGKGAASSQADYKEEHEGDDMSARRQQRYDSVEDSSESENSPVP---------RRKRRTSVGSSSS 1568
Cdd:pfam05793  189 PAAFGEHDEETEGEKGGGGRGKDLKIKDLEGDDEDDGDESDKGGEDGDEEKKKKKKKKlaknkkkldDDKKKKRGGDDDA 268

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686 1569 DEYKRDDSQGSGDEEDFIrkqilemsADEDASGSD--------DDEFIRNQLKEISAAESQKKEEVKS----------KA 1630
Cdd:pfam05793  269 FEYDSDDGDDEGREEDYI--------SDSSASGNDpeeredklSPEEPAKGEIEQSDDSEESEEEKNEeegklskkgkKA 340

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2032737686 1631 KGTAGKHRRMARKSSAGYDEDagrrhswHDDDDETFDESPEPKYRESKSQDSEELAVSGGGG 1692
Cdd:pfam05793  341 KKLKGKKNGKDKSESSDGDDS-------DDSDIDDEDSVPLFTAKKKKEPKKEEPVDSGPSS 395
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
 281-449 9.97e-03

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 42.22  E-value: 9.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  281 PTKPIQQQTSAKPSSgptKPSPQQPDSTKVTSqtapPTKPSSQQPGPAKQPSQQPARQGAPVKPSP-------QQTGPPK 353
Cdd:PLN03209   312 PLTPMEELLAKIPSQ---RVPPKESDAADGPK----PVPTKPVTPEAPSPPIEEEPPQPKAVVPRPlspytayEDLKPPT 384

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032737686  354 QPSqqPGPEKPSAQQAGPAKQPPQPGSGKPPPqQTGLVKQVpPQAGPTKPPSQTVGPTKPLAQQAG---PTKPPGQQPGP 430
Cdd:PLN03209   385 SPI--PTPPSSSPASSKSVDAVAKPAEPDVVP-SPGSASNV-PEVEPAQVEAKKTRPLSPYARYEDlkpPTSPSPTAPTG 460

                          170
                   ....*....|....*....
gi 2032737686  431 EKPPQQTQAGANQPTETAP 449
Cdd:PLN03209   461 VSPSVSSTSSVPAVPDTAP 479
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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