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Conserved domains on  [gi|1201829585|ref|XP_021240130|]
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protein piccolo isoform X8 [Numida meleagris]

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 ...
 4720-4845 1.17e-69

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: 230.60  E-value: 1.17e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4720 ITGEIQLQINYDKHLGNLIIHILQARNLAPRDNNGYSDPFVKVYLLPGRGAEYKRRTKYVQKSLNPEWNQTVIYKNISTE 4799
Cdd:cd04031      1 ITGRIQIQLWYDKVTSQLIVTVLQARDLPPRDDGSLRNPYVKVYLLPDRSEKSKRRTKTVKKTLNPEWNQTFEYSNVRRE 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1201829585 4800 QLKKKTLEVTVWDYDRFSSNDFLGEVLIDLSSvSQLDNTPRWYPLK 4845
Cdd:cd04031     81 TLKERTLEVTVWDYDRDGENDFLGEVVIDLAD-ALLDDEPHWYPLQ 125
PDZ_RIM-like cd06714
PDZ domain of Rab3-interacting molecule 1 (RIM), RIM2, piccolo and related domains; PDZ ...
 4520-4614 3.20e-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: 171.20  E-value: 3.20e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4520 PHARLKLLRDPKDHTVSGNGLGIRVVGGKEIPgsSGEIGAYIAKVLPGGSAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQ 4599
Cdd:cd06714      3 LIGRIILQRDPKDGSVSGNGLGLKVVGGKMTE--SGRLGAYVTKVKPGSVADTVGHLREGDEVLEWNGISLQGKTFEEVQ 80

                           90
                   ....*....|....*
gi 1201829585 4600 NIIIQQCGEAEICVR 4614
Cdd:cd06714     81 DIISQSKGEVELVVS 95
FYVE1_PCLO cd15774
FYVE-related domain 1 found in protein piccolo; Protein piccolo, also termed aczonin, is a ...
 446-507 4.98e-43

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: 152.11  E-value: 4.98e-43
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1201829585  446 TFCPLCTTTELLLHVPEKANYNTCTQCHTVVCSLCGFNPNPHITEIKEWLCLNCQMQRALGG 507
Cdd:cd15774      1 TICPLCKTTELLLHTPEKANYNTCTQCQTTVCSLCGFNPNPHITEKKEWLCLNCQMQRALGG 62
FYVE2_PCLO cd15776
FYVE-related domain 2 found in protein piccolo; Protein piccolo, also termed aczonin, is a ...
 914-977 2.22e-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: 150.60  E-value: 2.22e-42
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1201829585  914 VSCPLCKTGLNIGSKDPPNFNTCTECKKVVCNLCGFNPMPHIAEVQEWLCLNCQTQRAMSGQLG 977
Cdd:cd15776      1 LLCPLCKTELNIGSKDPPNFNTCTECKKTVCNLCGFNPTPHLTEVKEWLCLNCQTQRAMSGQLG 64
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 232-862 6.42e-17

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 89.61  E-value: 6.42e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  232 PQQQQPGEPKQIQKPGPSHQ-GDSKVEQPKQPPQPRGPQKSQLQQSEPTKPVQ----------QQTSAKPSVGPTKPLPQ 300
Cdd:PHA03247  2478 PVYRRPAEARFPFAAGAAPDpGGGGPPDPDAPPAPSRLAPAILPDEPVGEPVHprmltwirglEELASDDAGDPPPPLPP 2557

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  301 QPDSAkTSSQASPPTKPSSQQSGPVKQPSQ-------QPARQGGPVKPSaqqaGPPKQQPGSEKPSAQQTGPAKQPLQTG 373
Cdd:PHA03247  2558 AAPPA-APDRSVPPPRPAPRPSEPAVTSRArrpdappQSARPRAPVDDR----GDPRGPAPPSPLPPDTHAPDPPPPSPS 2632

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  374 PGKPPLQQTGPVKQVPPQAGPTKPSSQTAGATKSVAQQpglTKPPGPQSGPEKPSQQKQASAAQPVESTPKKtfcplctt 453
Cdd:PHA03247  2633 PAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRL---GRAAQASSPPQRPRRRAARPTVGSLTSLADP-------- 2701

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  454 telllHVPEKANyntctqchtvvcslcgfNPNPHITEIKEWLCLNCqmqralggdlASGHGPGPQLPPPKQKTPTPTSTA 533
Cdd:PHA03247  2702 -----PPPPPTP-----------------EPAPHALVSATPLPPGP----------AAARQASPALPAAPAPPAVPAGPA 2749

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  534 KPSPQSQPGQKKDASPKPDPSQQADSKKPvPQKKQPSMPGSPPVKSKQTDAEPSDTFQQIDPTPKSDQAKPTQAEEKQNQ 613
Cdd:PHA03247  2750 TPGGPARPARPPTTAGPPAPAPPAAPAAG-PPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPL 2828

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  614 PsvqkPTTDTVPTSAAPGVkqdlADPRPPLTQQKVTDSPKPETTKPPADTHPAgdKPDSKPLPQVSRQksdPKLASQSGS 693
Cdd:PHA03247  2829 P----PPTSAQPTAPPPPP----GPPPPSLPLGGSVAPGGDVRRRPPSRSPAA--KPAAPARPPVRRL---ARPAVSRST 2895

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  694 KSDAKTQKAVEPAQVRDDPKKLQTKSAPKPDTKPAPKGPQAGTGPKPMSAQPAPQPQQPQKTPEQSRRFSLNLGGITDVP 773
Cdd:PHA03247  2896 ESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVP 2975

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  774 K---PQPTTPQET---VTGKLFGFGAS-IFSQASSL---ISTAGQPGS--QTSGPAPPAAKQPQPPSQPTASQAPPKEAT 841
Cdd:PHA03247  2976 RfrvPQPAPSREApasSTPPLTGHSLSrVSSWASSLalhEETDPPPVSlkQTLWPPDDTEDSDADSLFDSDSERSDLEAL 3055

                          650       660
                   ....*....|....*....|.
gi 1201829585  842 QAQPLPKAAPTKKETKPLASE 862
Cdd:PHA03247  3056 DPLPPEPHDPFAHEPDPATPE 3076
C2 super family cl14603
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 5026-5151 1.60e-14

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: 73.08  E-value: 1.60e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 5026 GEIKIALkkEMKTDGEQLIVEILQCRNITykFKSPDHLPDLYVKLYVvnISTQKRVIKKKTRVCRHDREPSFNETFRFSL 5105
Cdd:cd04030      3 GRIQLTI--RYSSQRQKLIVTVHKCRNLP--PCDSSDIPDPYVRLYL--LPDKSKSTRRKTSVKKDNLNPVFDETFEFPV 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1201829585 5106 SPAGHSLQILLVS--NGGKFM--KKTLIGEAYVWLDKVDLRKRIVNWHKL 5151
Cdd:cd04030     77 SLEELKRRTLDVAvkNSKSFLsrEKKLLGQVLIDLSDLDLSKGFTQWYDL 126
PTZ00121 super family cl31754
MAEBL; Provisional
 1022-1643 3.94e-09

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 63.62  E-value: 3.94e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 1022 AATKPKEEPGVQKEVPKLQQGKLEKTL-------SADKIQQGIQKEDAKSKQGKLFKTPSADKIQRvsQKEDSRLQQTKL 1094
Cdd:PTZ00121  1333 AAKKKAEEAKKAAEAAKAEAEAAADEAeaaeekaEAAEKKKEEAKKKADAAKKKAEEKKKADEAKK--KAEEDKKKADEL 1410

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 1095 TKTPSSDKilhgaQKEDAKFQESKLAKTSSADKilhgVQKEDIKVQEAKlAKIPSADKILHGVQK--EDPKLQQMKmAKA 1172
Cdd:PTZ00121  1411 KKAAAAKK-----KADEAKKKAEEKKKADEAKK----KAEEAKKADEAK-KKAEEAKKAEEAKKKaeEAKKADEAK-KKA 1479

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 1173 LSADKIQPAAQK-EDPQLQGVRLSKAVSADKIQHGIQKEDLNLQHVKTEKTSVEKIQEEAQKEELKLQQEKLSKTLSEDK 1251
Cdd:PTZ00121  1480 EEAKKADEAKKKaEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKK 1559

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 1252 IPATVSSDQKkpsRKFEEDK-----KPELLEKSTPHPEDKKEQITAETKDRVAEQKAEVEAPCDKLHEKKEEDVKKEGLT 1326
Cdd:PTZ00121  1560 AEEKKKAEEA---KKAEEDKnmalrKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVE 1636

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 1327 TgipqmvSKTEKAEEEKTPVQVSRLPRSDHVEAVREKMEKEDDKSDTSSSQQQKSPQGLSDTGYSSDgissslgeipshi 1406
Cdd:PTZ00121  1637 Q------LKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKE------------- 1697

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 1407 pSDEKDLTRESSKKdtisQESPPSPSDLAKLESTVLSILEAQASTLADEKSVKRKELHEAYSDQTKDQHKTKPLPVTPES 1486
Cdd:PTZ00121  1698 -AEEAKKAEELKKK----EAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEE 1772

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 1487 YSS----------DEEDLESIQEGERTIaADGKGGSSSrtdyKEEGGGDDTP---ARRQRYDS----VEDSSES---ENS 1546
Cdd:PTZ00121  1773 IRKekeavieeelDEEDEKRRMEVDKKI-KDIFDNFAN----IIEGGKEGNLvinDSKEMEDSaikeVADSKNMqleEAD 1847

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 1547 PVPRRKRRASVGSSSSDEYKQDDSQGSGDEEDFIrKQIIEmsADEDASGSEDD---EFIRNQLK----EISVTESQKKEE 1619
Cdd:PTZ00121  1848 AFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDE-EEIEE--ADEIEKIDKDDierEIPNNNMAgknnDIIDDKLDKDEY 1924

                          650       660
                   ....*....|....*....|....
gi 1201829585 1620 VKSKAKGTAGKHRRMARKSSAGYD 1643
Cdd:PTZ00121  1925 IKRDAEETREEIIKISKKDMCIND 1948
PRK10263 super family cl35903
DNA translocase FtsK; Provisional
 162-299 3.42e-06

DNA translocase FtsK; Provisional


The actual alignment was detected with superfamily member PRK10263:

Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 53.94  E-value: 3.42e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  162 KFNPFDLISDsDAAHE---------EAGRKQKVTQKDQGKPEEQRglAKHPSQQQSPklvqqQGPVKPTPQQTESSKPVP 232
Cdd:PRK10263   728 EFSPMKALLD-DGPHEplftpivepVQQPQQPVAPQQQYQQPQQP--VAPQPQYQQP-----QQPVAPQPQYQQPQQPVA 799

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1201829585  233 QQQQPGEPKQIQKPGPSHQgdskveqpkQPPQPRGPQKSQLQQSEPTKPVQQQT----------SAKPSVGPTKPLP 299
Cdd:PRK10263   800 PQPQYQQPQQPVAPQPQYQ---------QPQQPVAPQPQYQQPQQPVAPQPQDTllhpllmrngDSRPLHKPTTPLP 867
CCDC47 super family cl46382
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ...
 3776-3839 4.77e-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: 4.77e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1201829585 3776 ARAKILQDIDRELDLVERESAKLRKKQAELDEEEKEIDaklrylEMGINRRKEALLKEREKRER 3839
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 ...
 4720-4845 1.17e-69

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: 230.60  E-value: 1.17e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4720 ITGEIQLQINYDKHLGNLIIHILQARNLAPRDNNGYSDPFVKVYLLPGRGAEYKRRTKYVQKSLNPEWNQTVIYKNISTE 4799
Cdd:cd04031      1 ITGRIQIQLWYDKVTSQLIVTVLQARDLPPRDDGSLRNPYVKVYLLPDRSEKSKRRTKTVKKTLNPEWNQTFEYSNVRRE 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1201829585 4800 QLKKKTLEVTVWDYDRFSSNDFLGEVLIDLSSvSQLDNTPRWYPLK 4845
Cdd:cd04031     81 TLKERTLEVTVWDYDRDGENDFLGEVVIDLAD-ALLDDEPHWYPLQ 125
PDZ_RIM-like cd06714
PDZ domain of Rab3-interacting molecule 1 (RIM), RIM2, piccolo and related domains; PDZ ...
 4520-4614 3.20e-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: 171.20  E-value: 3.20e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4520 PHARLKLLRDPKDHTVSGNGLGIRVVGGKEIPgsSGEIGAYIAKVLPGGSAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQ 4599
Cdd:cd06714      3 LIGRIILQRDPKDGSVSGNGLGLKVVGGKMTE--SGRLGAYVTKVKPGSVADTVGHLREGDEVLEWNGISLQGKTFEEVQ 80

                           90
                   ....*....|....*
gi 1201829585 4600 NIIIQQCGEAEICVR 4614
Cdd:cd06714     81 DIISQSKGEVELVVS 95
FYVE1_PCLO cd15774
FYVE-related domain 1 found in protein piccolo; Protein piccolo, also termed aczonin, is a ...
 446-507 4.98e-43

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: 152.11  E-value: 4.98e-43
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1201829585  446 TFCPLCTTTELLLHVPEKANYNTCTQCHTVVCSLCGFNPNPHITEIKEWLCLNCQMQRALGG 507
Cdd:cd15774      1 TICPLCKTTELLLHTPEKANYNTCTQCQTTVCSLCGFNPNPHITEKKEWLCLNCQMQRALGG 62
FYVE2_PCLO cd15776
FYVE-related domain 2 found in protein piccolo; Protein piccolo, also termed aczonin, is a ...
 914-977 2.22e-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: 150.60  E-value: 2.22e-42
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1201829585  914 VSCPLCKTGLNIGSKDPPNFNTCTECKKVVCNLCGFNPMPHIAEVQEWLCLNCQTQRAMSGQLG 977
Cdd:cd15776      1 LLCPLCKTELNIGSKDPPNFNTCTECKKTVCNLCGFNPTPHLTEVKEWLCLNCQTQRAMSGQLG 64
zf-piccolo pfam05715
Piccolo Zn-finger; This (predicted) Zinc finger is found in the bassoon and piccolo proteins. ...
 914-972 5.84e-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: 5.84e-37
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  914 VSCPLCK-TGLNIGSKDPPNFNTCTECKKVVCNLCGFNPMPHIAEVQEWLCLNCQTQRAM 972
Cdd:pfam05715    1 TLCPLCKtTELNVGSKEPPNYNTCTECKSQVCNLCGFNPTPHLTEKKEWLCLNCQTQRAL 60
zf-piccolo pfam05715
Piccolo Zn-finger; This (predicted) Zinc finger is found in the bassoon and piccolo proteins. ...
 446-505 6.37e-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: 6.37e-37
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  446 TFCPLCTTTELLLHVPEKANYNTCTQCHTVVCSLCGFNPNPHITEIKEWLCLNCQMQRAL 505
Cdd:pfam05715    1 TLCPLCKTTELNVGSKEPPNYNTCTECKSQVCNLCGFNPTPHLTEKKEWLCLNCQTQRAL 60
C2 pfam00168
C2 domain;
4735-4844 1.79e-33

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 126.28  E-value: 1.79e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4735 GNLIIHILQARNLAPRDNNGYSDPFVKVYLLPGrgaEYKRRTKYVQKSLNPEWNQTVIYkNISTEQlkKKTLEVTVWDYD 4814
Cdd:pfam00168    1 GRLTVTVIEAKNLPPKDGNGTSDPYVKVYLLDG---KQKKKTKVVKNTLNPVWNETFTF-SVPDPE--NAVLEIEVYDYD 74

                           90       100       110
                   ....*....|....*....|....*....|
gi 1201829585 4815 RFSSNDFLGEVLIDLSSVSQLDNTPRWYPL 4844
Cdd:pfam00168   75 RFGRDDFIGEVRIPLSELDSGEGLDGWYPL 104
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 4737-4841 1.41e-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: 112.58  E-value: 1.41e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  4737 LIIHILQARNLAPRDNNGYSDPFVKVYLLPGRGAeyKRRTKYVQKSLNPEWNQTVIYKNISTEqlkKKTLEVTVWDYDRF 4816
Cdd:smart00239    2 LTVKIISARNLPPKDKGGKSDPYVKVSLDGDPKE--KKKTKVVKNTLNPVWNETFEFEVPPPE---LAELEIEVYDKDRF 76

                            90       100
                    ....*....|....*....|....*
gi 1201829585  4817 SSNDFLGEVLIDLSSVSQLDNTPRW 4841
Cdd:smart00239   77 GRDDFIGQVTIPLSDLLLGGRHEKL 101
PHA03247 PHA03247
large tegument protein UL36; Provisional
 232-862 6.42e-17

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 89.61  E-value: 6.42e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  232 PQQQQPGEPKQIQKPGPSHQ-GDSKVEQPKQPPQPRGPQKSQLQQSEPTKPVQ----------QQTSAKPSVGPTKPLPQ 300
Cdd:PHA03247  2478 PVYRRPAEARFPFAAGAAPDpGGGGPPDPDAPPAPSRLAPAILPDEPVGEPVHprmltwirglEELASDDAGDPPPPLPP 2557

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  301 QPDSAkTSSQASPPTKPSSQQSGPVKQPSQ-------QPARQGGPVKPSaqqaGPPKQQPGSEKPSAQQTGPAKQPLQTG 373
Cdd:PHA03247  2558 AAPPA-APDRSVPPPRPAPRPSEPAVTSRArrpdappQSARPRAPVDDR----GDPRGPAPPSPLPPDTHAPDPPPPSPS 2632

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  374 PGKPPLQQTGPVKQVPPQAGPTKPSSQTAGATKSVAQQpglTKPPGPQSGPEKPSQQKQASAAQPVESTPKKtfcplctt 453
Cdd:PHA03247  2633 PAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRL---GRAAQASSPPQRPRRRAARPTVGSLTSLADP-------- 2701

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  454 telllHVPEKANyntctqchtvvcslcgfNPNPHITEIKEWLCLNCqmqralggdlASGHGPGPQLPPPKQKTPTPTSTA 533
Cdd:PHA03247  2702 -----PPPPPTP-----------------EPAPHALVSATPLPPGP----------AAARQASPALPAAPAPPAVPAGPA 2749

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  534 KPSPQSQPGQKKDASPKPDPSQQADSKKPvPQKKQPSMPGSPPVKSKQTDAEPSDTFQQIDPTPKSDQAKPTQAEEKQNQ 613
Cdd:PHA03247  2750 TPGGPARPARPPTTAGPPAPAPPAAPAAG-PPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPL 2828

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  614 PsvqkPTTDTVPTSAAPGVkqdlADPRPPLTQQKVTDSPKPETTKPPADTHPAgdKPDSKPLPQVSRQksdPKLASQSGS 693
Cdd:PHA03247  2829 P----PPTSAQPTAPPPPP----GPPPPSLPLGGSVAPGGDVRRRPPSRSPAA--KPAAPARPPVRRL---ARPAVSRST 2895

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  694 KSDAKTQKAVEPAQVRDDPKKLQTKSAPKPDTKPAPKGPQAGTGPKPMSAQPAPQPQQPQKTPEQSRRFSLNLGGITDVP 773
Cdd:PHA03247  2896 ESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVP 2975

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  774 K---PQPTTPQET---VTGKLFGFGAS-IFSQASSL---ISTAGQPGS--QTSGPAPPAAKQPQPPSQPTASQAPPKEAT 841
Cdd:PHA03247  2976 RfrvPQPAPSREApasSTPPLTGHSLSrVSSWASSLalhEETDPPPVSlkQTLWPPDDTEDSDADSLFDSDSERSDLEAL 3055

                          650       660
                   ....*....|....*....|.
gi 1201829585  842 QAQPLPKAAPTKKETKPLASE 862
Cdd:PHA03247  3056 DPLPPEPHDPFAHEPDPATPE 3076
C2C_KIAA1228 cd04030
C2 domain third repeat present in uncharacterized human KIAA1228-like proteins; KIAA proteins ...
 5026-5151 1.60e-14

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: 73.08  E-value: 1.60e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 5026 GEIKIALkkEMKTDGEQLIVEILQCRNITykFKSPDHLPDLYVKLYVvnISTQKRVIKKKTRVCRHDREPSFNETFRFSL 5105
Cdd:cd04030      3 GRIQLTI--RYSSQRQKLIVTVHKCRNLP--PCDSSDIPDPYVRLYL--LPDKSKSTRRKTSVKKDNLNPVFDETFEFPV 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1201829585 5106 SPAGHSLQILLVS--NGGKFM--KKTLIGEAYVWLDKVDLRKRIVNWHKL 5151
Cdd:cd04030     77 SLEELKRRTLDVAvkNSKSFLsrEKKLLGQVLIDLSDLDLSKGFTQWYDL 126
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 5042-5148 1.40e-13

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: 69.82  E-value: 1.40e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  5042 QLIVEILQCRNITYKFKSpdHLPDLYVKLYVVNistqKRVIKKKTRVCRHDREPSFNETFRFSLSPAGHSLQILLVSNGG 5121
Cdd:smart00239    1 TLTVKIISARNLPPKDKG--GKSDPYVKVSLDG----DPKEKKKTKVVKNTLNPVWNETFEFEVPPPELAELEIEVYDKD 74

                            90       100
                    ....*....|....*....|....*..
gi 1201829585  5122 KFMKKTLIGEAYVWLDKVDLRKRIVNW 5148
Cdd:smart00239   75 RFGRDDFIGQVTIPLSDLLLGGRHEKL 101
C2 pfam00168
C2 domain;
5042-5151 7.10e-13

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 67.73  E-value: 7.10e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 5042 QLIVEILQCRNITYKFKSPdhLPDLYVKLYVvnistQKRVIKKKTRVCRHDREPSFNETFRFSLSPAGHSLQILLVSNGG 5121
Cdd:pfam00168    2 RLTVTVIEAKNLPPKDGNG--TSDPYVKVYL-----LDGKQKKKTKVVKNTLNPVWNETFTFSVPDPENAVLEIEVYDYD 74

                           90       100       110
                   ....*....|....*....|....*....|
gi 1201829585 5122 KFMKKTLIGEAYVWLDKVDLRKRIVNWHKL 5151
Cdd:pfam00168   75 RFGRDDFIGEVRIPLSELDSGEGLDGWYPL 104
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 4536-4614 1.15e-11

Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF (relatively well conserved tetrapeptide in these domains). Some PDZs have been shown to bind C-terminal polypeptides; others appear to bind internal (non-C-terminal) polypeptides. Different PDZs possess different binding specificities.


Pssm-ID: 214570 [Multi-domain]  Cd Length: 85  Bit Score: 63.55  E-value: 1.15e-11
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1201829585  4536 SGNGLGIRVVGGKEIPGssgeiGAYIAKVLPGGSAEQTGkLIEGMQVLEWNGIPLTGKTYEEVQNIIIQQCGEAEICVR 4614
Cdd:smart00228   10 GGGGLGFSLVGGKDEGG-----GVVVSSVVPGSPAAKAG-LRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVTLTVL 82
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 213-449 3.06e-11

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: 70.57  E-value: 3.06e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  213 QQQGPVKPTPQQTESSKPVPQQQQPGEPKQIQKPGP-------SHQGDSKVEQPKQPPQPRGPQKSQLQQSePTKPVQQQ 285
Cdd:pfam03154  164 QQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPtpsapsvPPQGSPATSQPPNQTQSTAAPHTLIQQT-PTLHPQRL 242

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  286 TSAKPsvgPTKPLPQQPDSAKTSSQASP--------PTKPSSQQSGPVKQPSQQPARQGGPVKPSAQQAGPP-------- 349
Cdd:pfam03154  243 PSPHP---PLQPMTQPPPPSQVSPQPLPqpslhgqmPPMPHSLQTGPSHMQHPVPPQPFPLTPQSSQSQVPPgpspaapg 319

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  350 -----KQQPGSEKPSAQQTGPAKQPLQTGPGKPPLQQTGPVKQVPPQAGPTKPSSQTAGATKSVAQQPGLTKPP------ 418
Cdd:pfam03154  320 qsqqrIHTPPSQSQLQSQQPPREQPLPPAPLSMPHIKPPPTTPIPQLPNPQSHKHPPHLSGPSPFQMNSNLPPPpalkpl 399

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1201829585  419 ------GPQSGPEKP------SQQKQASAAQPVESTPKKTFCP 449
Cdd:pfam03154  400 sslsthHPPSAHPPPlqlmpqSQQLPPPPAQPPVLTQSQSLPP 442
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 534-779 5.80e-10

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: 65.56  E-value: 5.80e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  534 KPSPQSQPGQkkdasPKPDPSQQADSKKPVPQKKQPSMPGSPPVKSKQTDAEPSDTFQQIDPTPksDQAKPtqaeEKQNQ 613
Cdd:NF033839   300 QPSPQPEKKE-----VKPEPETPKPEVKPQLEKPKPEVKPQPEKPKPEVKPQLETPKPEVKPQP--EKPKP----EVKPQ 368

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  614 PSVQKPTTDTVPTSAAPGVKQDLADPRPPLtqqkvtdSPKPETTKPPADTHPAGDKPDSKPLPQVSRQ--KSDPKLASQS 691
Cdd:NF033839   369 PEKPKPEVKPQPETPKPEVKPQPEKPKPEV-------KPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPevKPQPEKPKPE 441

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  692 GSKSDAKTQKAVEPAQVRDDPKKLQTKSAPKPDTKPAPKGPQAGTGPKPMSAQPAPQPQQPQKTPEQSRRFSLNLGGITD 771
Cdd:NF033839   442 VKPQPEKPKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEKPKPDNSKPQADDKKPSTPNNLSKDKQPSNQASTNEKATNK 521


                   ....*...
gi 1201829585  772 VPKPQPTT 779
Cdd:NF033839   522 PKKSLPST 529
COG5038 COG5038
Ca2+-dependent lipid-binding protein, contains C2 domain [General function prediction only];
4735-4834 8.85e-10

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


Pssm-ID: 227371 [Multi-domain]  Cd Length: 1227  Bit Score: 65.55  E-value: 8.85e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4735 GNLIIHILQARNLAPRDNNGYSDPFVKVYLlpgrGAEYKRRTKYVQKSLNPEWNQTviykniSTEQLKKKT---LEVTVW 4811
Cdd:COG5038   1040 GYLTIMLRSGENLPSSDENGYSDPFVKLFL----NEKSVYKTKVVKKTLNPVWNEE------FTIEVLNRVkdvLTINVN 1109

                           90       100
                   ....*....|....*....|...
gi 1201829585 4812 DYDRFSSNDFLGEVLIDLSSVSQ 4834
Cdd:COG5038   1110 DWDSGEKNDLLGTAEIDLSKLEP 1132
PTZ00121 PTZ00121
MAEBL; Provisional
 1022-1643 3.94e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 63.62  E-value: 3.94e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 1022 AATKPKEEPGVQKEVPKLQQGKLEKTL-------SADKIQQGIQKEDAKSKQGKLFKTPSADKIQRvsQKEDSRLQQTKL 1094
Cdd:PTZ00121  1333 AAKKKAEEAKKAAEAAKAEAEAAADEAeaaeekaEAAEKKKEEAKKKADAAKKKAEEKKKADEAKK--KAEEDKKKADEL 1410

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 1095 TKTPSSDKilhgaQKEDAKFQESKLAKTSSADKilhgVQKEDIKVQEAKlAKIPSADKILHGVQK--EDPKLQQMKmAKA 1172
Cdd:PTZ00121  1411 KKAAAAKK-----KADEAKKKAEEKKKADEAKK----KAEEAKKADEAK-KKAEEAKKAEEAKKKaeEAKKADEAK-KKA 1479

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 1173 LSADKIQPAAQK-EDPQLQGVRLSKAVSADKIQHGIQKEDLNLQHVKTEKTSVEKIQEEAQKEELKLQQEKLSKTLSEDK 1251
Cdd:PTZ00121  1480 EEAKKADEAKKKaEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKK 1559

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 1252 IPATVSSDQKkpsRKFEEDK-----KPELLEKSTPHPEDKKEQITAETKDRVAEQKAEVEAPCDKLHEKKEEDVKKEGLT 1326
Cdd:PTZ00121  1560 AEEKKKAEEA---KKAEEDKnmalrKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVE 1636

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 1327 TgipqmvSKTEKAEEEKTPVQVSRLPRSDHVEAVREKMEKEDDKSDTSSSQQQKSPQGLSDTGYSSDgissslgeipshi 1406
Cdd:PTZ00121  1637 Q------LKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKE------------- 1697

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 1407 pSDEKDLTRESSKKdtisQESPPSPSDLAKLESTVLSILEAQASTLADEKSVKRKELHEAYSDQTKDQHKTKPLPVTPES 1486
Cdd:PTZ00121  1698 -AEEAKKAEELKKK----EAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEE 1772

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 1487 YSS----------DEEDLESIQEGERTIaADGKGGSSSrtdyKEEGGGDDTP---ARRQRYDS----VEDSSES---ENS 1546
Cdd:PTZ00121  1773 IRKekeavieeelDEEDEKRRMEVDKKI-KDIFDNFAN----IIEGGKEGNLvinDSKEMEDSaikeVADSKNMqleEAD 1847

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 1547 PVPRRKRRASVGSSSSDEYKQDDSQGSGDEEDFIrKQIIEmsADEDASGSEDD---EFIRNQLK----EISVTESQKKEE 1619
Cdd:PTZ00121  1848 AFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDE-EEIEE--ADEIEKIDKDDierEIPNNNMAgknnDIIDDKLDKDEY 1924

                          650       660
                   ....*....|....*....|....
gi 1201829585 1620 VKSKAKGTAGKHRRMARKSSAGYD 1643
Cdd:PTZ00121  1925 IKRDAEETREEIIKISKKDMCIND 1948
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 182-460 2.06e-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: 60.55  E-value: 2.06e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  182 KQKVTQKDQGKPEEQRGLAKHPSQQQSPKLVQQQGPVKPTPQQTESsKPVPQQQQPGEPKQIQKPGPSHQGDSKVEQPKQ 261
Cdd:NF033839   276 KKGLTQDTPKEPGNKKPSAPKPGMQPSPQPEKKEVKPEPETPKPEV-KPQLEKPKPEVKPQPEKPKPEVKPQLETPKPEV 354

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  262 PPQPRGPQKSqlQQSEPTKPvqqqtsaKPSVGPtKPLPQQPDSAKTSSQASPPTKPSSQQSGPVKQPsqQPARQGGPVKP 341
Cdd:NF033839   355 KPQPEKPKPE--VKPQPEKP-------KPEVKP-QPETPKPEVKPQPEKPKPEVKPQPEKPKPEVKP--QPEKPKPEVKP 422

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  342 sAQQAGPPKQQPGSEKPSAQqtgPAKQPLQTGPGKPPLQQTgPVKQVPPQAGPTKPSSQTAGAT---KSVAQQPGLTKPP 418
Cdd:NF033839   423 -QPEKPKPEVKPQPEKPKPE---VKPQPEKPKPEVKPQPET-PKPEVKPQPEKPKPEVKPQPEKpkpDNSKPQADDKKPS 497

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1201829585  419 GPQSGPEKPSQQKQASAAQPVESTPKKTFCPLCTTTELLLHV 460
Cdd:NF033839   498 TPNNLSKDKQPSNQASTNEKATNKPKKSLPSTGSISNLALEI 539
PBP1 COG5180
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ...
 171-428 1.88e-07

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


Pssm-ID: 444064 [Multi-domain]  Cd Length: 548  Bit Score: 57.38  E-value: 1.88e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  171 DSDAAHEEAGRKQKVTQKD--QGKPEEQRGLAKHPSQQqspklVQQQGPVKPTPQQTESSKPVPQQQQPGE--PKQIQKP 246
Cdd:COG5180    190 DALKDSPEKLDRPKVEVKDeaQEEPPDLTGGADHPRPE-----AASSPKVDPPSTSEARSRPATVDAQPEMrpPADAKER 264

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  247 GPSHQGDSKVEQPKQPPQPRGPQKSQLQQSEPTKPVQQQTSAKPSVgPTKPLPQQPDSAKTSSQASPPTKPSSQqsgPVK 326
Cdd:COG5180    265 RRAAIGDTPAAEPPGLPVLEAGSEPQSDAPEAETARPIDVKGVASA-PPATRPVRPPGGARDPGTPRPGQPTER---PAG 340

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  327 QPsQQPARQGGPVKPSAQQAGPPKQQPG-SEKPSAQQTGPAKQPLQTGPGKPPLQQTGPVKQVPPQ--AGPTKPSSQTAG 403
Cdd:COG5180    341 VP-EAASDAGQPPSAYPPAEEAVPGKPLeQGAPRPGSSGGDGAPFQPPNGAPQPGLGRRGAPGPPMgaGDLVQAALDGGG 419

                          250       260
                   ....*....|....*....|....*..
gi 1201829585  404 ATKSVAQQP--GLTKPPGPQSGPEKPS 428
Cdd:COG5180    420 RETASLGGAagGAGQGPKADFVPGDAE 446
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
 4531-4602 5.67e-07

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


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 49.97  E-value: 5.67e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1201829585 4531 KDHTVSGNGLGIRVVGGkeipGSSGEIGAYIAKVLPGGSAEQTGkLIEGMQVLEWNGIPLTGKTYEEVQNII 4602
Cdd:pfam00595    3 TLEKDGRGGLGFSLKGG----SDQGDPGIFVSEVLPGGAAEAGG-LKVGDRILSINGQDVENMTHEEAVLAL 69
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 162-299 3.42e-06

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 53.94  E-value: 3.42e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  162 KFNPFDLISDsDAAHE---------EAGRKQKVTQKDQGKPEEQRglAKHPSQQQSPklvqqQGPVKPTPQQTESSKPVP 232
Cdd:PRK10263   728 EFSPMKALLD-DGPHEplftpivepVQQPQQPVAPQQQYQQPQQP--VAPQPQYQQP-----QQPVAPQPQYQQPQQPVA 799

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1201829585  233 QQQQPGEPKQIQKPGPSHQgdskveqpkQPPQPRGPQKSQLQQSEPTKPVQQQT----------SAKPSVGPTKPLP 299
Cdd:PRK10263   800 PQPQYQQPQQPVAPQPQYQ---------QPQQPVAPQPQYQQPQQPVAPQPQDTllhpllmrngDSRPLHKPTTPLP 867
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 500-784 4.06e-06

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: 53.23  E-value: 4.06e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  500 QMQRALGGDLASGHGPGPQLPPPKQKTPTPTSTAKPSPQSQPGQKKDASPKPDPSQQADSKKP----------------- 562
Cdd:NF033839   142 KFEKDSSSSSSSGSSTKPETPQPENPEHQKPTTPAPDTKPSPQPEGKKPSVPDINQEKEKAKLavatymskilddiqkhh 221

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  563 ------------VPQKKQPSMPGSPPVKSKQTDAEPSDTFQQIDPTP-------KSDQAKPTQAEEKQNQPSVQKPTTDT 623
Cdd:NF033839   222 lqkekhrqivalIKELDELKKQALSEIDNVNTKVEIENTVHKIFADMdavvtkfKKGLTQDTPKEPGNKKPSAPKPGMQP 301

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  624 VPTSAAPGVKQDLADP----RPPLTQQKVTDSPKPETTKPPADTHPAGDKPDSKPLPQVSRQKSDPKLasqSGSKSDAKT 699
Cdd:NF033839   302 SPQPEKKEVKPEPETPkpevKPQLEKPKPEVKPQPEKPKPEVKPQLETPKPEVKPQPEKPKPEVKPQP---EKPKPEVKP 378

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  700 QKAVEPAQVRDDPkklqtkSAPKPDTKPAPKGPQAGTGPKPMSAQPAPQPQQPQKTPEQSRRfslnLGGITDVPKPQPTT 779
Cdd:NF033839   379 QPETPKPEVKPQP------EKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQ----PEKPKPEVKPQPEK 448


                   ....*
gi 1201829585  780 PQETV 784
Cdd:NF033839   449 PKPEV 453
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 268-714 5.42e-06

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: 52.85  E-value: 5.42e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  268 PQKSQLQQSEPTKPVQQQTSAKPSVGPTKPLPQQPDSAKTSSQASPPTKPSSQQSGPVKQPSQQPARQGGPVKPSAQQAG 347
Cdd:NF033839   159 PETPQPENPEHQKPTTPAPDTKPSPQPEGKKPSVPDINQEKEKAKLAVATYMSKILDDIQKHHLQKEKHRQIVALIKELD 238

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  348 PPKQQPGSE----KPSAQQTGPAKQPLQTGPGKPPLQQTGPVKQVPPQAGPTKPSsqtagatksvAQQPGLTKPPGPQSG 423
Cdd:NF033839   239 ELKKQALSEidnvNTKVEIENTVHKIFADMDAVVTKFKKGLTQDTPKEPGNKKPS----------APKPGMQPSPQPEKK 308

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  424 PEKPSQQKQASAAQPVESTPKKTFCPlctttelllhVPEKanyntctqchtvvcslcgfnPNPHITeikewlclncqmqr 503
Cdd:NF033839   309 EVKPEPETPKPEVKPQLEKPKPEVKP----------QPEK--------------------PKPEVK-------------- 344

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  504 alggdlasghgpgPQLPPPKQKTPTPTSTAKPSPQSQPgQKKDASPKPDPSQQADSKKPVPQKKQPSMPGSPPVKSKQTD 583
Cdd:NF033839   345 -------------PQLETPKPEVKPQPEKPKPEVKPQP-EKPKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEKPKPEVK 410

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  584 AEPSDtfqqidPTPKSDQAKPTQAEEKQNQPSVQKPTTDTVPTSAAPGVKQDLADPRPPLtqqkvtdSPKPETTKPPADT 663
Cdd:NF033839   411 PQPEK------PKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPETPKPEV-------KPQPEKPKPEVKP 477

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1201829585  664 HPAGDKPD-SKPLPQVSRQKSDPKLasqsgSKSDAKTQKAVEPAQVRDDPKK 714
Cdd:NF033839   478 QPEKPKPDnSKPQADDKKPSTPNNL-----SKDKQPSNQASTNEKATNKPKK 524
SP2_N cd22540
N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins ...
 217-443 3.49e-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: 50.31  E-value: 3.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  217 PVKPTPQQTESSKPVPQQQQPG----------------EPKQIQKPGPSHQGDSKVEQPKQP---PQPRGPQKSQLQQSE 277
Cdd:cd22540     51 PPQPTPRKLVPIKPAPLPLGPGknsigflsakgniiqlQGSQLSSSAPGGQQVFAIQNPTMIikgSQTRSSTNQQYQISP 130

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  278 PTKPVQQQT-SAKPSVGP--------TKPLPQQPDSAKTSSQASP-PTKPSSQQSGPVKQPSQQPARQGG-------PVK 340
Cdd:cd22540    131 QIQAAGQINnSGQIQIIPgtnqaiitPVQVLQQPQQAHKPVPIKPaPLQTSNTNSASLQVPGNVIKLQSGgnvaltlPVN 210

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  341 PSAQQAGPPKQQPGSEKPSAQQTGPAKQPLQTGPGKPPLQQtgpvkQVPPQA-GPTKPSSQTAGATKSVAQQPGLTKPPG 419
Cdd:cd22540    211 NLVGTQDGATQLQLAAAPSKPSKKIRKKSAQAAQPAVTVAE-----QVETVLiETTADNIIQAGNNLLIVQSPGTGQPAV 285

                          250       260
                   ....*....|....*....|....
gi 1201829585  420 PQsgpekPSQQKQASAAQPVESTP 443
Cdd:cd22540    286 LQ-----QVQVLQPKQEQQVVQIP 304
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 30-391 5.82e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 49.60  E-value: 5.82e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585   30 QPLVPAGVEADLSQLSEEERRQIAAVMSRAQGLPRGNLAGAEPPPMQRHPDLDTSRHPRQPGKPPDPGPGlsksRTVDVL 109
Cdd:PRK07764   440 APPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAPAGADDA----ATLRER 515

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  110 KTEQRA--PGRSPSSISLRESKSRtdFKEDQKPSMMPSFlseANPLSAvtSVVNKFNPFDLIsdSDAAHEEAGRKQKV-- 185
Cdd:PRK07764   516 WPEILAavPKRSRKTWAILLPEAT--VLGVRGDTLVLGF---STGGLA--RRFASPGNAEVL--VTALAEELGGDWQVea 586

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  186 ---TQKDQGKPEEQRGLAKHPSQQQSPKLVQQQGPVKPTPQQTESSkPVPQQQQPGEPKQIQKPGPSHQGDSKVEQPKQP 262
Cdd:PRK07764   587 vvgPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGA-AAAPAEASAAPAPGVAAPEHHPKHVAVPDASDG 665

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  263 PQPRGPQKSQLQQSEPTkpvqqqtsakPSVGPTKPLPQQPDSAKTSSQASPPTKPSSQQSGPVKQPSQQPARQGGPVkPS 342
Cdd:PRK07764   666 GDGWPAKAGGAAPAAPP----------PAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPS-PA 734

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1201829585  343 AQQAGPPKQQPGSEKPSAQQTGPAKQPLQTGPGKPPLQQTGPVKQVPPQ 391
Cdd:PRK07764   735 ADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEE 783
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
 205-302 2.32e-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: 45.17  E-value: 2.32e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585   205 QQQSPKLVQQQGPVKPTPQQteSSKPVPQQQQPGEPKQIQKPGPSHQG--DSKVEQPKQPPQPRGPQKSQ-LQQSEPTKP 281
Cdd:smart00818   36 HHQIIPVSQQHPPTHTLQPH--HHIPVLPAQQPVVPQQPLMPVPGQHSmtPTQHHQPNLPQPAQQPFQPQpLQPPQPQQP 113

                            90       100
                    ....*....|....*....|.
gi 1201829585   282 VQQQtsakPSVGPTKPLPQQP 302
Cdd:smart00818  114 MQPQ----PPVHPIPPLPPQP 130
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 1363-1677 1.66e-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: 44.90  E-value: 1.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 1363 KMEKEDDKSDTSSSQQQKSPQGLSDTGYSSDGISSSLGEIPSHIPSDEKDLTRESSKKDTISQESPPSPSDLAKLESTVL 1442
Cdd:NF033609   553 EIEPIPEDSDSDPGSDSGSDSSNSDSGSDSGSDSTSDSGSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSAS 632

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 1443 SILEAQASTLADEKSVKRKELHEAYSDQTKDQHKTKPLPVTPESYSSDEEDLESIQEGERTIAADGKGGSSSRTDYKEEG 1522
Cdd:NF033609   633 DSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 712

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 1523 GGDDTPARRQRYDSVEDSSESENSPVPRRKRRASVGSSSSDEYKQDDSQGSGDEEDfirKQIIEMSADEDA-SGSEDDEF 1601
Cdd:NF033609   713 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS---DSDSDSDSDSDSdSDSDSDSD 789

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1201829585 1602 IRNQLKEISVTESQKKEEVKSKAKGTAGKHRRMARKSSAGYDEDAGRRHSWHDDDDETFDESPEPKYRETKSQDGE 1677
Cdd:NF033609   790 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSESDSNSDSE 865
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
 203-352 1.77e-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: 44.80  E-value: 1.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  203 PSQQQSPKLVQQQGPVKPTPQQTESSKPVPQQQQPGEPKQIQKPGPShqgdskveQPKQPPQPRGpqksqlqqsePTKPV 282
Cdd:TIGR01628  380 PRMRQLPMGSPMGGAMGQPPYYGQGPQQQFNGQPLGWPRMSMMPTPM--------GPGGPLRPNG----------LAPMN 441

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1201829585  283 QQQTSAKPSVGPTKPLPQQPDSAktssqaspptkPSSQQSGPVKQPSQQPAR---QGGPVKPSAQ--QAGPPKQQ 352
Cdd:TIGR01628  442 AVRAPSRNAQNAAQKPPMQPVMY-----------PPNYQSLPLSQDLPQPQStasQGGQNKKLAQvlASATPQMQ 505
CCDC47 pfam07946
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ...
 3776-3839 4.77e-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: 4.77e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1201829585 3776 ARAKILQDIDRELDLVERESAKLRKKQAELDEEEKEIDaklrylEMGINRRKEALLKEREKRER 3839
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 ...
 4720-4845 1.17e-69

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: 230.60  E-value: 1.17e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4720 ITGEIQLQINYDKHLGNLIIHILQARNLAPRDNNGYSDPFVKVYLLPGRGAEYKRRTKYVQKSLNPEWNQTVIYKNISTE 4799
Cdd:cd04031      1 ITGRIQIQLWYDKVTSQLIVTVLQARDLPPRDDGSLRNPYVKVYLLPDRSEKSKRRTKTVKKTLNPEWNQTFEYSNVRRE 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1201829585 4800 QLKKKTLEVTVWDYDRFSSNDFLGEVLIDLSSvSQLDNTPRWYPLK 4845
Cdd:cd04031     81 TLKERTLEVTVWDYDRDGENDFLGEVVIDLAD-ALLDDEPHWYPLQ 125
PDZ_RIM-like cd06714
PDZ domain of Rab3-interacting molecule 1 (RIM), RIM2, piccolo and related domains; PDZ ...
 4520-4614 3.20e-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: 171.20  E-value: 3.20e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4520 PHARLKLLRDPKDHTVSGNGLGIRVVGGKEIPgsSGEIGAYIAKVLPGGSAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQ 4599
Cdd:cd06714      3 LIGRIILQRDPKDGSVSGNGLGLKVVGGKMTE--SGRLGAYVTKVKPGSVADTVGHLREGDEVLEWNGISLQGKTFEEVQ 80

                           90
                   ....*....|....*
gi 1201829585 4600 NIIIQQCGEAEICVR 4614
Cdd:cd06714     81 DIISQSKGEVELVVS 95
FYVE1_PCLO cd15774
FYVE-related domain 1 found in protein piccolo; Protein piccolo, also termed aczonin, is a ...
 446-507 4.98e-43

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: 152.11  E-value: 4.98e-43
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1201829585  446 TFCPLCTTTELLLHVPEKANYNTCTQCHTVVCSLCGFNPNPHITEIKEWLCLNCQMQRALGG 507
Cdd:cd15774      1 TICPLCKTTELLLHTPEKANYNTCTQCQTTVCSLCGFNPNPHITEKKEWLCLNCQMQRALGG 62
FYVE2_PCLO cd15776
FYVE-related domain 2 found in protein piccolo; Protein piccolo, also termed aczonin, is a ...
 914-977 2.22e-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: 150.60  E-value: 2.22e-42
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1201829585  914 VSCPLCKTGLNIGSKDPPNFNTCTECKKVVCNLCGFNPMPHIAEVQEWLCLNCQTQRAMSGQLG 977
Cdd:cd15776      1 LLCPLCKTELNIGSKDPPNFNTCTECKKTVCNLCGFNPTPHLTEVKEWLCLNCQTQRAMSGQLG 64
zf-piccolo pfam05715
Piccolo Zn-finger; This (predicted) Zinc finger is found in the bassoon and piccolo proteins. ...
 914-972 5.84e-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: 5.84e-37
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  914 VSCPLCK-TGLNIGSKDPPNFNTCTECKKVVCNLCGFNPMPHIAEVQEWLCLNCQTQRAM 972
Cdd:pfam05715    1 TLCPLCKtTELNVGSKEPPNYNTCTECKSQVCNLCGFNPTPHLTEKKEWLCLNCQTQRAL 60
zf-piccolo pfam05715
Piccolo Zn-finger; This (predicted) Zinc finger is found in the bassoon and piccolo proteins. ...
 446-505 6.37e-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: 6.37e-37
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  446 TFCPLCTTTELLLHVPEKANYNTCTQCHTVVCSLCGFNPNPHITEIKEWLCLNCQMQRAL 505
Cdd:pfam05715    1 TLCPLCKTTELNVGSKEPPNYNTCTECKSQVCNLCGFNPTPHLTEKKEWLCLNCQTQRAL 60
FYVE2_BSN_PCLO cd15772
FYVE-related domain 2 found in protein bassoon and piccolo; This family includes protein ...
 914-977 7.64e-37

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: 134.77  E-value: 7.64e-37
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1201829585  914 VSCPLCKTGLNIGSKDPPNFNTCTECKKVVCNLCGFNPMPHIAEVQEWLCLNCQTQRAMSGQLG 977
Cdd:cd15772      1 VTCPLCKTELNVGSKEPPNYNTCTQCHTQVCNLCGFNPTPHLVEKKEWLCLNCQTQRLMSGGLG 64
FYVE1_BSN_PCLO cd15771
FYVE-related domain 1 found in protein bassoon and piccolo; This family includes protein ...
 446-507 4.00e-36

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: 132.43  E-value: 4.00e-36
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1201829585  446 TFCPLCTTTELLLHVPeKANYNTCTQCHTVVCSLCGFNPNPHITEIKEWLCLNCQMQRALGG 507
Cdd:cd15771      1 TLCPLCNTTELTLHVP-KPNFNTCTQCHTTVCNQCGFNPNPHLTEVKEWLCLNCQMQRALGM 61
C2A_SLP cd08521
C2 domain first repeat present in Synaptotagmin-like proteins; All Slp members basically share ...
 4722-4844 1.03e-34

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: 130.84  E-value: 1.03e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4722 GEIQLQINYDKHLGNLIIHILQARNLAPRDN-NGYSDPFVKVYLLPGRGAEYKRRTKYVQKSLNPEWNQTVIYKnISTEQ 4800
Cdd:cd08521      1 GEIEFSLSYNYKTGSLEVHIKECRNLAYADEkKKRSNPYVKVYLLPDKSKQSKRKTSVKKNTTNPVFNETLKYH-ISKSQ 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1201829585 4801 LKKKTLEVTVWDYDRFSSNDFLGEVLIDLSSVSQLDNTPRWYPL 4844
Cdd:cd08521     80 LETRTLQLSVWHHDRFGRNTFLGEVEIPLDSWDLDSQQSEWYPL 123
FYVE2_BSN cd15775
FYVE-related domain 2 found in protein bassoon; Protein bassoon, also termed zinc finger ...
 913-977 9.83e-34

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: 125.80  E-value: 9.83e-34
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1201829585  913 KVSCPLCKTGLNIGSKDPPNFNTCTECKKVVCNLCGFNPMPHIAEVQEWLCLNCQTQRAMSGQLG 977
Cdd:cd15775      1 RVTCPLCKTELNVGSTEPPNYNTCTSCRTQVCNLCGFNPTPHLVEKNEWLCLNCQTQRLLEGSLG 65
C2 pfam00168
C2 domain;
4735-4844 1.79e-33

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 126.28  E-value: 1.79e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4735 GNLIIHILQARNLAPRDNNGYSDPFVKVYLLPGrgaEYKRRTKYVQKSLNPEWNQTVIYkNISTEQlkKKTLEVTVWDYD 4814
Cdd:pfam00168    1 GRLTVTVIEAKNLPPKDGNGTSDPYVKVYLLDG---KQKKKTKVVKNTLNPVWNETFTF-SVPDPE--NAVLEIEVYDYD 74

                           90       100       110
                   ....*....|....*....|....*....|
gi 1201829585 4815 RFSSNDFLGEVLIDLSSVSQLDNTPRWYPL 4844
Cdd:pfam00168   75 RFGRDDFIGEVRIPLSELDSGEGLDGWYPL 104
FYVE1_BSN cd15773
FYVE-related domain 1 found in protein bassoon; Protein bassoon, also termed zinc finger ...
 443-506 4.67e-32

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: 120.96  E-value: 4.67e-32
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1201829585  443 PKKTFCPLCTTTELLlHVPEKANYNTCTQCHTVVCSLCGFNPNPHITEIKEWLCLNCQMQRALG 506
Cdd:cd15773      1 PSSTLCPICNTTELT-SFPSQPNFNTCTQCHNKVCNQCGFNPNPHLTEVKEWLCLNCQMQRALG 63
C2A_SLP-1_2 cd08393
C2 domain first repeat present in Synaptotagmin-like proteins 1 and 2; All Slp members ...
 4722-4845 1.12e-31

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: 122.16  E-value: 1.12e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4722 GEIQLQINYDKHLGNLIIHILQARNLAPRD-NNGYSDPFVKVYLLPGRGAEYKRRTKYVQKSLNPEWNQTVIYKnISTEQ 4800
Cdd:cd08393      2 GSVQFALDYDPKLRELHVHVIQCQDLAAADpKKQRSDPYVKTYLLPDKSNRGKRKTSVKKKTLNPVFNETLRYK-VEREE 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1201829585 4801 LKKKTLEVTVWDYDRFSSNDFLGEVLIDLSSVSQLDNTPRWYPLK 4845
Cdd:cd08393     81 LPTRVLNLSVWHRDSLGRNSFLGEVEVDLGSWDWSNTQPTWYPLQ 125
C2B_SLP_1-2-3-4 cd04020
C2 domain second repeat present in Synaptotagmin-like proteins 1-4; All Slp members basically ...
 4709-4841 1.97e-31

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: 122.82  E-value: 1.97e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4709 PTEATKSASHPITGEIQlqinydkhlgnliIHILQARNLAPRDNNGYSDPFVKVYLLPGRGAEYKRRTKYVQKSLNPEWN 4788
Cdd:cd04020     14 ESEGALKSKKPSTGELH-------------VWVKEAKNLPALKSGGTSDSFVKCYLLPDKSKKSKQKTPVVKKSVNPVWN 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1201829585 4789 QTVIYKNISTEQLKKKTLEVTVWDYDRFSSNDFLGEVLIDLSSVSQLDNTPRW 4841
Cdd:cd04020     81 HTFVYDGVSPEDLSQACLELTVWDHDKLSSNDFLGGVRLGLGTGKSYGQAVDW 133
C2_PKC_alpha_gamma cd04026
C2 domain in Protein Kinase C (PKC) alpha and gamma; A single C2 domain is found in PKC alpha ...
 4722-4849 9.63e-31

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: 119.67  E-value: 9.63e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4722 GEIQLQINYDKhlGNLIIHILQARNLAPRDNNGYSDPFVKVYLLPGRGAEYKRRTKYVQKSLNPEWNQTVIYKniSTEQL 4801
Cdd:cd04026      2 GRIYLKISVKD--NKLTVEVREAKNLIPMDPNGLSDPYVKLKLIPDPKNETKQKTKTIKKTLNPVWNETFTFD--LKPAD 77

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1201829585 4802 KKKTLEVTVWDYDRFSSNDFLGEvlidLS-SVSQLDNTPR--WYPLKEQSE 4849
Cdd:cd04026     78 KDRRLSIEVWDWDRTTRNDFMGS----LSfGVSELIKMPVdgWYKLLNQEE 124
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 4737-4844 3.35e-30

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: 117.17  E-value: 3.35e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4737 LIIHILQARNLAPRDNNGYSDPFVKVYLLPGRgaeyKRRTKYVQKSLNPEWNQTVIYKNISTeqlKKKTLEVTVWDYDRF 4816
Cdd:cd00030      1 LRVTVIEARNLPAKDLNGKSDPYVKVSLGGKQ----KFKTKVVKNTLNPVWNETFEFPVLDP---ESDTLTVEVWDKDRF 73

                           90       100
                   ....*....|....*....|....*....
gi 1201829585 4817 SSNDFLGEVLIDLSSV-SQLDNTPRWYPL 4844
Cdd:cd00030     74 SKDDFLGEVEIPLSELlDSGKEGELWLPL 102
C2B_PI3K_class_II cd08381
C2 domain second repeat present in class II phosphatidylinositol 3-kinases (PI3Ks); There are ...
 4721-4845 3.71e-30

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: 117.78  E-value: 3.71e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4721 TGEIQLQINYDKhlGNLIIHILQARNLAPRDNNgYSDPFVKVYLLPGRGAEYKRRTKYVQKSLNPEWNQTVIYKNISTEQ 4800
Cdd:cd08381      1 GGQVKLSISYKN--GTLFVMVMHAKNLPLLDGS-DPDPYVKTYLLPDPQKTTKRKTKVVRKTRNPTFNEMLVYDGLPVED 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1201829585 4801 LKKKTLEVTVWDYDRFSSNDFLGEVLIDLSSVSQLDNTPRWYPLK 4845
Cdd:cd08381     78 LQQRVLQVSVWSHDSLVENEFLGGVCIPLKKLDLSQETEKWYPLG 122
C2B_Rabphilin_Doc2 cd08384
C2 domain second repeat present in Rabphilin and Double C2 domain; Rabphilin is found neurons ...
 4724-4831 9.07e-30

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: 117.06  E-value: 9.07e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4724 IQLQINYDKHLGNLIIHILQARNLAPRDNNGYSDPFVKVYLLPGRGAEYKRRTKYVQKSLNPEWNQTVIYKnISTEQLKK 4803
Cdd:cd08384      2 ILVSLMYNTQRRGLIVGIIRCVNLAAMDANGYSDPFVKLYLKPDAGKKSKHKTQVKKKTLNPEFNEEFFYD-IKHSDLAK 80

                           90       100
                   ....*....|....*....|....*...
gi 1201829585 4804 KTLEVTVWDYDRFSSNDFLGEVLIDLSS 4831
Cdd:cd08384     81 KTLEITVWDKDIGKSNDYIGGLQLGINA 108
C2A_Synaptotagmin-1-5-6-9-10 cd08385
C2A domain first repeat present in Synaptotagmins 1, 5, 6, 9, and 10; Synaptotagmin is a ...
 4722-4841 2.20e-29

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: 115.44  E-value: 2.20e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4722 GEIQLQINYDKHLGNLIIHILQARNLAPRDNNGYSDPFVKVYLLPGRGAEYKrrTKYVQKSLNPEWNQTVIYKNISTEqL 4801
Cdd:cd08385      3 GKLQFSLDYDFQSNQLTVGIIQAADLPAMDMGGTSDPYVKVYLLPDKKKKFE--TKVHRKTLNPVFNETFTFKVPYSE-L 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1201829585 4802 KKKTLEVTVWDYDRFSSNDFLGEVLIDLSSVSQLDNTPRW 4841
Cdd:cd08385     80 GNKTLVFSVYDFDRFSKHDLIGEVRVPLLTVDLGHVTEEW 119
C2A_Synaptotagmin-7 cd08386
C2A domain first repeat present in Synaptotagmin 7; Synaptotagmin is a membrane-trafficking ...
 4722-4845 8.75e-29

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: 113.96  E-value: 8.75e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4722 GEIQLQINYDKHLGNLIIHILQARNLAPRDNNGYSDPFVKVYLLPGRGaeYKRRTKYVQKSLNPEWNQTVIYKNISTEQL 4801
Cdd:cd08386      3 GRIQFSVSYDFQESTLTLKILKAVELPAKDFSGTSDPFVKIYLLPDKK--HKLETKVKRKNLNPHWNETFLFEGFPYEKL 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1201829585 4802 KKKTLEVTVWDYDRFSSNDFLGEVLIDLSSVSQLDNTPRWYPLK 4845
Cdd:cd08386     81 QQRVLYLQVLDYDRFSRNDPIGEVSLPLNKVDLTEEQTFWKDLK 124
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 4737-4841 1.41e-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: 112.58  E-value: 1.41e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  4737 LIIHILQARNLAPRDNNGYSDPFVKVYLLPGRGAeyKRRTKYVQKSLNPEWNQTVIYKNISTEqlkKKTLEVTVWDYDRF 4816
Cdd:smart00239    2 LTVKIISARNLPPKDKGGKSDPYVKVSLDGDPKE--KKKTKVVKNTLNPVWNETFEFEVPPPE---LAELEIEVYDKDRF 76

                            90       100
                    ....*....|....*....|....*
gi 1201829585  4817 SSNDFLGEVLIDLSSVSQLDNTPRW 4841
Cdd:smart00239   77 GRDDFIGQVTIPLSDLLLGGRHEKL 101
C2A_Rabphilin_Doc2 cd04035
C2 domain first repeat present in Rabphilin and Double C2 domain; Rabphilin is found neurons ...
 4722-4830 2.02e-28

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: 112.76  E-value: 2.02e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4722 GEIQLQINYDKHLGNLIIHILQARNLAPRDNNGYSDPFVKVYLLPGRGAEYKRRTKYVQKSLNPEWNQTVIYKNISTEQL 4801
Cdd:cd04035      2 GTLEFTLLYDPANSALHCTIIRAKGLKAMDANGLSDPYVKLNLLPGASKATKLRTKTVHKTRNPEFNETLTYYGITEEDI 81

                           90       100
                   ....*....|....*....|....*....
gi 1201829585 4802 KKKTLEVTVWDYDRFsSNDFLGEVLIDLS 4830
Cdd:cd04035     82 QRKTLRLLVLDEDRF-GNDFLGETRIPLK 109
C2C_KIAA1228 cd04030
C2 domain third repeat present in uncharacterized human KIAA1228-like proteins; KIAA proteins ...
 4721-4845 2.24e-27

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: 110.06  E-value: 2.24e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4721 TGEIQLQINYDKHLGNLIIHILQARNLAPRDNNGYSDPFVKVYLLPGRGAEYKRRTKYVQKSLNPEWNQTVIYkNISTEQ 4800
Cdd:cd04030      2 LGRIQLTIRYSSQRQKLIVTVHKCRNLPPCDSSDIPDPYVRLYLLPDKSKSTRRKTSVKKDNLNPVFDETFEF-PVSLEE 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1201829585 4801 LKKKTLEVTVWDYDRFSS--NDFLGEVLIDLSSVSQLDNTPRWYPLK 4845
Cdd:cd04030     81 LKRRTLDVAVKNSKSFLSreKKLLGQVLIDLSDLDLSKGFTQWYDLT 127
FYVE_BSN_PCLO cd15751
FYVE-related domain found in protein bassoon and piccolo; This family includes protein bassoon ...
 916-972 8.22e-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: 8.22e-27
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1201829585  916 CPLCK-TGLNIGSKDPPNFNTCTECKKVVCNLCGFNPMPHIAEVQEWLCLNCQTQRAM 972
Cdd:cd15751      3 CPLCGtSELPLGSKSPPNYNTCTDCKNRVCNQCGFNSTPPVTKVKEWLCLNCQKKRAL 60
C2A_SLP-4_5 cd04029
C2 domain first repeat present in Synaptotagmin-like proteins 4 and 5; All Slp members ...
 4721-4844 1.02e-26

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: 107.91  E-value: 1.02e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4721 TGEIQLQINYDKHLGNLIIHILQARNLAPRDNNGY-SDPFVKVYLLPGRGAEYKRRTKYVQKSLNPEWNQTVIYKnISTE 4799
Cdd:cd04029      1 SGEILFSLSYDYKTQSLNVHVKECRNLAYGDEAKKrSNPYVKTYLLPDKSRQSKRKTSIKRNTTNPVYNETLKYS-ISHS 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1201829585 4800 QLKKKTLEVTVWDYDRFSSNDFLGEVLIDLSSvSQLDN-TPRWYPL 4844
Cdd:cd04029     80 QLETRTLQLSVWHYDRFGRNTFLGEVEIPLDS-WNFDSqHEECLPL 124
FYVE1_PCLO cd15774
FYVE-related domain 1 found in protein piccolo; Protein piccolo, also termed aczonin, is a ...
 916-974 5.51e-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: 5.51e-26
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  916 CPLCK-TGLNIGSKDPPNFNTCTECKKVVCNLCGFNPMPHIAEVQEWLCLNCQTQRAMSG 974
Cdd:cd15774      3 CPLCKtTELLLHTPEKANYNTCTQCQTTVCSLCGFNPNPHITEKKEWLCLNCQMQRALGG 62
FYVE2_BSN_PCLO cd15772
FYVE-related domain 2 found in protein bassoon and piccolo; This family includes protein ...
 448-509 1.22e-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: 102.80  E-value: 1.22e-25
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1201829585  448 CPLCTTtELLLHVPEKANYNTCTQCHTVVCSLCGFNPNPHITEIKEWLCLNCQMQRALGGDL 509
Cdd:cd15772      3 CPLCKT-ELNVGSKEPPNYNTCTQCHTQVCNLCGFNPTPHLVEKKEWLCLNCQTQRLMSGGL 63
FYVE2_BSN cd15775
FYVE-related domain 2 found in protein bassoon; Protein bassoon, also termed zinc finger ...
 445-510 1.67e-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: 1.67e-25
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1201829585  445 KTFCPLCTTtELLLHVPEKANYNTCTQCHTVVCSLCGFNPNPHITEIKEWLCLNCQMQRALGGDLA 510
Cdd:cd15775      1 RVTCPLCKT-ELNVGSTEPPNYNTCTSCRTQVCNLCGFNPTPHLVEKNEWLCLNCQTQRLLEGSLG 65
C2A_Synaptotagmin-8 cd08387
C2A domain first repeat present in Synaptotagmin 8; Synaptotagmin is a membrane-trafficking ...
 4721-4845 2.11e-25

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: 104.02  E-value: 2.11e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4721 TGEIQLQINYDKHLGNLIIHILQARNLAPRDNNGYSDPFVKVYLLPGRGAEykRRTKYVQKSLNPEWNQTVIYKnISTEQ 4800
Cdd:cd08387      2 RGELHFSLEYDKDMGILNVKLIQARNLQPRDFSGTADPYCKVRLLPDRSNT--KQSKIHKKTLNPEFDESFVFE-VPPQE 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1201829585 4801 LKKKTLEVTVWDYDRFSSNDFLGEVLIDLSSVSQLDNTPRWYPLK 4845
Cdd:cd08387     79 LPKRTLEVLLYDFDQFSRDECIGVVELPLAEVDLSEKLDLWRKIQ 123
FYVE1_BSN_PCLO cd15771
FYVE-related domain 1 found in protein bassoon and piccolo; This family includes protein ...
 916-974 2.28e-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: 2.28e-25
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1201829585  916 CPLCKTGLNIGSKDPPNFNTCTECKKVVCNLCGFNPMPHIAEVQEWLCLNCQTQRAMSG 974
Cdd:cd15771      3 CPLCNTTELTLHVPKPNFNTCTQCHTTVCNQCGFNPNPHLTEVKEWLCLNCQMQRALGM 61
C2B_Synaptotagmin cd00276
C2 domain second repeat present in Synaptotagmin; Synaptotagmin is a membrane-trafficking ...
 4722-4844 1.12e-24

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: 102.66  E-value: 1.12e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4722 GEIQLQINYDKHLGNLIIHILQARNLAPRDNNGYSDPFVKVYLLPGRGAEYKRRTKYVQKSLNPEWNQTVIYkNISTEQL 4801
Cdd:cd00276      1 GELLLSLSYLPTAERLTVVVLKARNLPPSDGKGLSDPYVKVSLLQGGKKLKKKKTSVKKGTLNPVFNEAFSF-DVPAEQL 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1201829585 4802 KKKTLEVTVWDYDRFSSNDFLGEVLIDLSSVS-------QLDNTPR-----WYPL 4844
Cdd:cd00276     80 EEVSLVITVVDKDSVGRNEVIGQVVLGPDSGGeelehwnEMLASPRkpiarWHKL 134
FYVE_BSN_PCLO cd15751
FYVE-related domain found in protein bassoon and piccolo; This family includes protein bassoon ...
 448-506 1.65e-24

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: 99.45  E-value: 1.65e-24
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1201829585  448 CPLCTTTELLLHVPEKANYNTCTQCHTVVCSLCGFNPNPHITEIKEWLCLNCQMQRALG 506
Cdd:cd15751      3 CPLCGTSELPLGSKSPPNYNTCTDCKNRVCNQCGFNSTPPVTKVKEWLCLNCQKKRALG 61
FYVE1_BSN cd15773
FYVE-related domain 1 found in protein bassoon; Protein bassoon, also termed zinc finger ...
 916-972 2.78e-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: 99.00  E-value: 2.78e-24
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1201829585  916 CPLCKTGLNIGSKDPPNFNTCTECKKVVCNLCGFNPMPHIAEVQEWLCLNCQTQRAM 972
Cdd:cd15773      6 CPICNTTELTSFPSQPNFNTCTQCHNKVCNQCGFNPNPHLTEVKEWLCLNCQMQRAL 62
FYVE2_PCLO cd15776
FYVE-related domain 2 found in protein piccolo; Protein piccolo, also termed aczonin, is a ...
 448-509 1.23e-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: 97.06  E-value: 1.23e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1201829585  448 CPLCTTtELLLHVPEKANYNTCTQCHTVVCSLCGFNPNPHITEIKEWLCLNCQMQRALGGDL 509
Cdd:cd15776      3 CPLCKT-ELNIGSKDPPNFNTCTECKKTVCNLCGFNPTPHLTEVKEWLCLNCQTQRAMSGQL 63
C2B_Synaptotagmin-7 cd08405
C2 domain second repeat present in Synaptotagmin 7; Synaptotagmin is a membrane-trafficking ...
 4722-4827 4.54e-23

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: 97.87  E-value: 4.54e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4722 GEIQLQINYDKHLGNLIIHILQARNLAPRDNNGYSDPFVKVYLLPGRGAEYKRRTKYVQKSLNPEWNQTVIYkNISTEQL 4801
Cdd:cd08405      2 GELLLSLCYNPTANRITVNIIKARNLKAMDINGTSDPYVKVWLMYKDKRVEKKKTVIKKRTLNPVFNESFIF-NIPLERL 80

                           90       100
                   ....*....|....*....|....*.
gi 1201829585 4802 KKKTLEVTVWDYDRFSSNDFLGEVLI 4827
Cdd:cd08405     81 RETTLIITVMDKDRLSRNDLIGKIYL 106
C2B_Synaptotagmin-1 cd08402
C2 domain second repeat present in Synaptotagmin 1; Synaptotagmin is a membrane-trafficking ...
 4722-4827 4.44e-22

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: 95.16  E-value: 4.44e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4722 GEIQLQINYDKHLGNLIIHILQARNLAPRDNNGYSDPFVKVYLLPGRGAEYKRRTKYVQKSLNPEWNQTVIYKnISTEQL 4801
Cdd:cd08402      2 GDICFSLRYVPTAGKLTVVILEAKNLKKMDVGGLSDPYVKIHLMQNGKRLKKKKTTIKKRTLNPYYNESFSFE-VPFEQI 80

                           90       100
                   ....*....|....*....|....*.
gi 1201829585 4802 KKKTLEVTVWDYDRFSSNDFLGEVLI 4827
Cdd:cd08402     81 QKVHLIVTVLDYDRIGKNDPIGKVVL 106
C2B_Munc13-like cd04009
C2 domain second repeat in Munc13 (mammalian uncoordinated)-like proteins; C2-like domains are ...
 4722-4838 4.94e-21

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: 91.92  E-value: 4.94e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4722 GEIQLQINYDKHLGNLIIHILQARNLAPRDNNGYSDPFVKVYLLPGR---GAEyKRRTKYVQKSLNPEWNQTvIYKNIST 4798
Cdd:cd04009      3 GVLTVKAYYRASEQSLRVEILNARNLLPLDSNGSSDPFVKVELLPRHlfpDVP-TPKTQVKKKTLFPLFDES-FEFNVPP 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1201829585 4799 EQLKKK--TLEVTVWDYDRFSSNDFLGEVLIDLSSVSQLDNT 4838
Cdd:cd04009     81 EQCSVEgaLLLFTVKDYDLLGSNDFEGEAFLPLNDIPGVEDT 122
C2A_Synaptotagmin-like cd04024
C2 domain first repeat present in Synaptotagmin-like proteins; Synaptotagmin is a ...
 4735-4856 9.67e-20

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: 88.25  E-value: 9.67e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4735 GNLIIHILQARNLAPRD--NNGYSDPFVKVYLlpgrGAEyKRRTKYVQKSLNPEWNqtvIYKNISTEQLKKKTLEVTVWD 4812
Cdd:cd04024      1 GVLRVHVVEAKDLAAKDrsGKGKSDPYAILSV----GAQ-RFKTQTIPNTLNPKWN---YWCEFPIFSAQNQLLKLILWD 72

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1201829585 4813 YDRFSSNDFLGEVLIDLSSV---SQLDNTPRWYPLKEQSENIDHGKS 4856
Cdd:cd04024     73 KDRFAGKDYLGEFDIALEEVfadGKTGQSDKWITLKSTRPGKTSVVS 119
C2A_Synaptotagmin-15-17 cd08390
C2A domain first repeat present in Synaptotagmins 15 and 17; Synaptotagmin is a ...
 4722-4832 1.83e-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: 87.31  E-value: 1.83e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4722 GEIQLQINYDKHLGNLIIHILQARNLAPRD-NNGYSDPFVKVYLLPgrgaEYKRR--TKYVQKSLNPEWNQTVIYKnIST 4798
Cdd:cd08390      1 GRLWFSVQYDLEEEQLTVSLIKARNLPPRTkDVAHCDPFVKVCLLP----DERRSlqSKVKRKTQNPNFDETFVFQ-VSF 75

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1201829585 4799 EQLKKKTLEVTVWDYDRFSSNDFLGEVLIDLSSV 4832
Cdd:cd08390     76 KELQRRTLRLSVYDVDRFSRHCIIGHVLFPLKDL 109
C2D_Tricalbin-like cd04040
C2 domain fourth repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are ...
 4737-4847 1.66e-18

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: 84.16  E-value: 1.66e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4737 LIIHILQARNLAPRDNNGYSDPFVKVYLlpgRGAE-YKrrTKYVQKSLNPEWNQTViyknisTEQLKKKT---LEVTVWD 4812
Cdd:cd04040      1 LTVDVISAENLPSADRNGKSDPFVKFYL---NGEKvFK--TKTIKKTLNPVWNESF------EVPVPSRVravLKVEVYD 69

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1201829585 4813 YDRFSSNDFLGEVLIDLSSVSQLDNTPRWYPLKEQ 4847
Cdd:cd04040     70 WDRGGKDDLLGSAYIDLSDLEPEETTELTLPLDGQ 104
C2A_Synaptotagmin-4-11 cd08388
C2A domain first repeat present in Synaptotagmins 4 and 11; Synaptotagmin is a ...
 4722-4832 3.44e-18

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: 83.55  E-value: 3.44e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4722 GEIQLQINYDKHLGNLIIHILQARNLAPRD-NNGYSDPFVKVYLLPGRgaEYKRRTKYVQKSLNPEWNQTVIYKNISTEQ 4800
Cdd:cd08388      3 GTLFFSLRYNSEKKALLVNIIECRDLPAMDeQSGTSDPYVKLQLLPEK--EHKVKTRVLRKTRNPVYDETFTFYGIPYNQ 80

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1201829585 4801 LKKKTLEVTVWDYDRFSSNDFLGEVLIDLSSV 4832
Cdd:cd08388     81 LQDLSLHFAVLSFDRYSRDDVIGEVVCPLAGA 112
C2E_Ferlin cd04037
C2 domain fifth repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and ...
 4739-4829 1.18e-17

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: 82.21  E-value: 1.18e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4739 IHILQARNLAPRDNNGYSDPFVKVYLlpgRGAEYKRRTKYVQKSLNPEWNQTVIyknISTEQLKKKTLEVTVWDYDRFSS 4818
Cdd:cd04037      4 VYVVRARNLQPKDPNGKSDPYLKIKL---GKKKINDRDNYIPNTLNPVFGKMFE---LEATLPGNSILKISVMDYDLLGS 77

                           90
                   ....*....|.
gi 1201829585 4819 NDFLGEVLIDL 4829
Cdd:cd04037     78 DDLIGETVIDL 88
C2A_MCTP_PRT_plant cd04022
C2 domain first repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); ...
 4737-4848 3.59e-17

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: 80.84  E-value: 3.59e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4737 LIIHILQARNLAPRDNNGYSDPFVKVYLLpgrgaEYKRRTKYVQKSLNPEWNQTVIYKNISTEQLKKKTLEVTVWDYDRF 4816
Cdd:cd04022      2 LVVEVVDAQDLMPKDGQGSSSAYVELDFD-----GQKKRTRTKPKDLNPVWNEKLVFNVSDPSRLSNLVLEVYVYNDRRS 76

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1201829585 4817 S-SNDFLGEVLIDLSS-VSQLDNTPRWYPLKEQS 4848
Cdd:cd04022     77 GrRRSFLGRVRISGTSfVPPSEAVVQRYPLEKRG 110
C2D_Ferlin cd04017
C2 domain fourth repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and ...
 4739-4860 5.05e-17

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: 80.66  E-value: 5.05e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4739 IHILQARNLAPRDNNGYSDPFVKVYLLpgrgaEYKRRTKYVQKSLNPEWNQTVIYKNI----STEQLKKK--TLEVTVWD 4812
Cdd:cd04017      5 AYIYQARDLLAADKSGLSDPFARVSFL-----NQSQETEVIKETLSPTWDQTLIFDEVelygSPEEIAQNppLVVVELFD 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1201829585 4813 YDRFSSNDFLGEVLID--LSSVSQLDNTP--RWYPLKeqsenidHGKSHSGQ 4860
Cdd:cd04017     80 QDSVGKDEFLGRSVAKplVKLDLEEDFPPklQWFPIY-------KGGQSAGE 124
PHA03247 PHA03247
large tegument protein UL36; Provisional
 232-862 6.42e-17

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 89.61  E-value: 6.42e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  232 PQQQQPGEPKQIQKPGPSHQ-GDSKVEQPKQPPQPRGPQKSQLQQSEPTKPVQ----------QQTSAKPSVGPTKPLPQ 300
Cdd:PHA03247  2478 PVYRRPAEARFPFAAGAAPDpGGGGPPDPDAPPAPSRLAPAILPDEPVGEPVHprmltwirglEELASDDAGDPPPPLPP 2557

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  301 QPDSAkTSSQASPPTKPSSQQSGPVKQPSQ-------QPARQGGPVKPSaqqaGPPKQQPGSEKPSAQQTGPAKQPLQTG 373
Cdd:PHA03247  2558 AAPPA-APDRSVPPPRPAPRPSEPAVTSRArrpdappQSARPRAPVDDR----GDPRGPAPPSPLPPDTHAPDPPPPSPS 2632

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  374 PGKPPLQQTGPVKQVPPQAGPTKPSSQTAGATKSVAQQpglTKPPGPQSGPEKPSQQKQASAAQPVESTPKKtfcplctt 453
Cdd:PHA03247  2633 PAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRL---GRAAQASSPPQRPRRRAARPTVGSLTSLADP-------- 2701

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  454 telllHVPEKANyntctqchtvvcslcgfNPNPHITEIKEWLCLNCqmqralggdlASGHGPGPQLPPPKQKTPTPTSTA 533
Cdd:PHA03247  2702 -----PPPPPTP-----------------EPAPHALVSATPLPPGP----------AAARQASPALPAAPAPPAVPAGPA 2749

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  534 KPSPQSQPGQKKDASPKPDPSQQADSKKPvPQKKQPSMPGSPPVKSKQTDAEPSDTFQQIDPTPKSDQAKPTQAEEKQNQ 613
Cdd:PHA03247  2750 TPGGPARPARPPTTAGPPAPAPPAAPAAG-PPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPL 2828

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  614 PsvqkPTTDTVPTSAAPGVkqdlADPRPPLTQQKVTDSPKPETTKPPADTHPAgdKPDSKPLPQVSRQksdPKLASQSGS 693
Cdd:PHA03247  2829 P----PPTSAQPTAPPPPP----GPPPPSLPLGGSVAPGGDVRRRPPSRSPAA--KPAAPARPPVRRL---ARPAVSRST 2895

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  694 KSDAKTQKAVEPAQVRDDPKKLQTKSAPKPDTKPAPKGPQAGTGPKPMSAQPAPQPQQPQKTPEQSRRFSLNLGGITDVP 773
Cdd:PHA03247  2896 ESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVP 2975

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  774 K---PQPTTPQET---VTGKLFGFGAS-IFSQASSL---ISTAGQPGS--QTSGPAPPAAKQPQPPSQPTASQAPPKEAT 841
Cdd:PHA03247  2976 RfrvPQPAPSREApasSTPPLTGHSLSrVSSWASSLalhEETDPPPVSlkQTLWPPDDTEDSDADSLFDSDSERSDLEAL 3055

                          650       660
                   ....*....|....*....|.
gi 1201829585  842 QAQPLPKAAPTKKETKPLASE 862
Cdd:PHA03247  3056 DPLPPEPHDPFAHEPDPATPE 3076
PHA03247 PHA03247
large tegument protein UL36; Provisional
 203-742 1.59e-16

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 88.46  E-value: 1.59e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  203 PSQQQSPKLvqQQGPVKPTPQQTESSKPVPQQQQPGEPKQIQKPGPSHQGDSKVEQPKQPPQPRGpQKSQLQQSEPTKPV 282
Cdd:PHA03247  2592 PPQSARPRA--PVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRD-DPAPGRVSRPRRAR 2668

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  283 QQQTSAKPSVGPTKPLPQ--QPDSAKTSSQASPPTKPSSQQSGPvkqPSQQPARQGGPVKPSAQQAGPPKqqPGSEKPSA 360
Cdd:PHA03247  2669 RLGRAAQASSPPQRPRRRaaRPTVGSLTSLADPPPPPPTPEPAP---HALVSATPLPPGPAAARQASPAL--PAAPAPPA 2743

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  361 QQTGPAKQPLQTGPGKPPLQqTGPVKQVPPqAGPTKPSSQTAGATKSVAQQPGLTKPPGPQSGPEKPSQQKQASAAQPVE 440
Cdd:PHA03247  2744 VPAGPATPGGPARPARPPTT-AGPPAPAPP-AAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPA 2821

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  441 STPKKtfcPLCTTTELLLHVPEKANyntctqchtvvcslcgfNPNPHITEIKEWLclncqmqrALGGDLASGHGPGPQLP 520
Cdd:PHA03247  2822 ASPAG---PLPPPTSAQPTAPPPPP-----------------GPPPPSLPLGGSV--------APGGDVRRRPPSRSPAA 2873

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  521 PPKQKTPTPTS-------TAKPSPQSQPGQKKDASPKPDPSQQADSKKPVPQKKQPSMPGSPPVKSK-----QTDAEPSD 588
Cdd:PHA03247  2874 KPAAPARPPVRrlarpavSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQpplapTTDPAGAG 2953

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  589 TFQQIDPTPKSDQAKPTQAEEKQNQPSVQKPTTDTVPTSAAPgvKQDLADPRppLTQQKVTDSPKPETTKPPAD----TH 664
Cdd:PHA03247  2954 EPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASSTPP--LTGHSLSR--VSSWASSLALHEETDPPPVSlkqtLW 3029

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  665 PAGDKPDSKPlpqvsrqksdpklASQSGSKSDAKTQKAVEPaqvrdDPKKLQTKSAPKPDTKPAPKGPQAGT----GPKP 740
Cdd:PHA03247  3030 PPDDTEDSDA-------------DSLFDSDSERSDLEALDP-----LPPEPHDPFAHEPDPATPEAGARESPssqfGPPP 3091


                   ..
gi 1201829585  741 MS 742
Cdd:PHA03247  3092 LS 3093
C2A_C2C_Synaptotagmin_like cd08391
C2 domain first and third repeat in Synaptotagmin-like proteins; Synaptotagmin is a ...
 4735-4857 2.11e-16

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: 78.49  E-value: 2.11e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4735 GNLIIHILQARNLAPRDNN------GYSDPFVKVyllpgRGAEYKRRTKYVQKSLNPEWNQT---VIYknisteQLKKKT 4805
Cdd:cd08391      1 GVLRIHVIEAQDLVAKDKFvgglvkGKSDPYVIV-----RVGAQTFKSKVIKENLNPKWNEVyeaVVD------EVPGQE 69

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1201829585 4806 LEVTVWDYDRfSSNDFLGEVLIDLSSVSQLDNTPRWYPLkeqsENIDHGKSH 4857
Cdd:cd08391     70 LEIELFDEDP-DKDDFLGRLSIDLGSVEKKGFIDEWLPL----EDVKSGRLH 116
C2A_SLP-3 cd08392
C2 domain first repeat present in Synaptotagmin-like protein 3; All Slp members basically ...
 4721-4845 2.45e-16

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: 78.33  E-value: 2.45e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4721 TGEIQLQINYDKHLGNLIIHILQARNLAPRDNNGYS-DPFVKVYLLPGRGAEYKRRTKYVQKSLNPEWNQTVIYKnISTE 4799
Cdd:cd08392      1 TGEIEFALHYNFRTSCLEITIKACRNLAYGDEKKKKcHPYVKVCLLPDKSHNSKRKTAVKKGTVNPVFNETLKYV-VEAD 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1201829585 4800 QLKKKTLEVTVWDYDRFSSNDFLGEVLIDLSSVSQLDNTP---RWYPLK 4845
Cdd:cd08392     80 LLSSRQLQVSVWHSRTLKRRVFLGEVLIPLADWDFEDTDSqrfLWYPLN 128
C2C_MCTP_PRT cd08377
C2 domain third repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); ...
 4735-4848 2.74e-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: 78.11  E-value: 2.74e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4735 GNLIIHILQARNLAPRDNNGYSDPFVKVYLLPGRgaeykRRTKYVQKSLNPEWNQTVIY--KNISTeqlkkkTLEVTVWD 4812
Cdd:cd08377      1 GFLQVKVIRASGLAAADIGGKSDPFCVLELVNAR-----LQTHTIYKTLNPEWNKIFTFpiKDIHD------VLEVTVYD 69

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1201829585 4813 YDRFSSNDFLGEVLIDLSSVSqlDNTPRWYPLKEQS 4848
Cdd:cd08377     70 EDKDKKPEFLGKVAIPLLSIK--NGERKWYALKDKK 103
C2B_RasA1_RasA4 cd04025
C2 domain second repeat present in RasA1 and RasA4; RasA1 and RasA4 are GAP1s (GTPase ...
 4740-4844 2.83e-16

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: 77.91  E-value: 2.83e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4740 HILQARNLAPRDNNGYSDPFVKVYlLPGRGAEykrrTKYVQKSLNPEWNQTVIYKNISTEQLKkktLEVTVWDYDRFSSN 4819
Cdd:cd04025      5 HVLEARDLAPKDRNGTSDPFVRVF-YNGQTLE----TSVVKKSCYPRWNEVFEFELMEGADSP---LSVEVWDWDLVSKN 76

                           90       100
                   ....*....|....*....|....*
gi 1201829585 4820 DFLGEVLIDLSSVSQLDNTPRWYPL 4844
Cdd:cd04025     77 DFLGKVVFSIQTLQQAKQEEGWFRL 101
C2B_RasGAP cd08675
C2 domain second repeat of Ras GTPase activating proteins (GAPs); RasGAPs suppress Ras ...
 4737-4853 9.81e-16

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: 77.03  E-value: 9.81e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4737 LIIHILQARNLAPRdNNGYSDPFVKVYLLPGRGAEYKRrTKYVQKSLNPEWNQTVIY------------KNISTEQLKKK 4804
Cdd:cd08675      1 LSVRVLECRDLALK-SNGTCDPFARVTLNYSSKTDTKR-TKVKKKTNNPRFDEAFYFeltigfsyekksFKVEEEDLEKS 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1201829585 4805 TLEVTVWDYDRFSSNDFLGEVLIDLSSVSQLDNTPRWYPLKEQSENIDH 4853
Cdd:cd08675     79 ELRVELWHASMVSGDDFLGEVRIPLQGLQQAGSHQAWYFLQPREAPGTR 127
C2B_RIM1alpha cd04028
C2 domain second repeat contained in Rab3-interacting molecule (RIM) proteins; RIMs are ...
 4719-4844 2.03e-15

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: 76.27  E-value: 2.03e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4719 PITGEIQLQINYDKhlGNLIIHILQARNLAPRDNNGY-SDPFVKVYLLPGRGAEYKRRTKYVQKSLNPEWNQTVIYKnis 4797
Cdd:cd04028     15 PSMGDIQLGLYDKK--GQLEVEVIRARGLVQKPGSKVlPAPYVKVYLLEGKKCIAKKKTKIARKTLDPLYQQQLVFD--- 89

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1201829585 4798 tEQLKKKTLEVTVW-DYDRFSSNDFLGEVLIDLSSVSQLDNTPRWYPL 4844
Cdd:cd04028     90 -VSPTGKTLQVIVWgDYGRMDKKVFMGVAQILLDDLDLSNLVIGWYKL 136
PDZ_canonical cd00136
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs ...
 4536-4614 3.22e-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: 3.22e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1201829585 4536 SGNGLGIRVVGGKEIPGssgeiGAYIAKVLPGGSAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQNIIIQQCGEAEICVR 4614
Cdd:cd00136      8 PGGGLGFSIRGGKDGGG-----GIFVSRVEPGGPAARDGRLRVGDRILEVNGVSLEGLTHEEAVELLKSAGGEVTLTVR 81
C2B_Synaptotagmin-4 cd08404
C2 domain second repeat present in Synaptotagmin 4; Synaptotagmin is a membrane-trafficking ...
 4722-4827 5.84e-15

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: 74.77  E-value: 5.84e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4722 GEIQLQINYDKHLGNLIIHILQARNLAPRDNNGYSDPFVKVYLLPGRGAEYKRRTKYVQKSLNPEWNQTVIYkNISTEQL 4801
Cdd:cd08404      2 GELLLSLCYQPTTNRLTVVVLKARHLPKMDVSGLADPYVKVNLYYGKKRISKKKTHVKKCTLNPVFNESFVF-DIPSEEL 80

                           90       100
                   ....*....|....*....|....*.
gi 1201829585 4802 KKKTLEVTVWDYDRFSSNDFLGEVLI 4827
Cdd:cd08404     81 EDISVEFLVLDSDRVTKNEVIGRLVL 106
C2A_MCTP_PRT cd04042
C2 domain first repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); ...
 4737-4853 6.70e-15

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: 74.23  E-value: 6.70e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4737 LIIHILQARNLAPRDNNGYSDPFVKVYLlpGRGAEYKRRTKYvqKSLNPEWNQTVIyknISTEQLKKKtLEVTVWDYDRF 4816
Cdd:cd04042      2 LDIHLKEGRNLAARDRGGTSDPYVKFKY--GGKTVYKSKTIY--KNLNPVWDEKFT---LPIEDVTQP-LYIKVFDYDRG 73

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1201829585 4817 SSNDFLGEVLIDLSSVSQldNTPRWYPLKEQSENIDH 4853
Cdd:cd04042     74 LTDDFMGSAFVDLSTLEL--NKPTEVKLKLEDPNSDE 108
C2B_MCTP_PRT_plant cd08378
C2 domain second repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); ...
 4737-4844 7.20e-15

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: 73.89  E-value: 7.20e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4737 LIIHILQARNLAPrdnnGYSDPFVKVyllpgRGAEYKRRTKYVQKSLNPEWNQTVIyknISTEQLKKKTLEVTVWDYDrF 4816
Cdd:cd08378      2 LYVRVVKARGLPA----NSNDPVVEV-----KLGNYKGSTKAIERTSNPEWNQVFA---FSKDRLQGSTLEVSVWDKD-K 68

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1201829585 4817 SSNDFLGEVLIDLSSV-------SQLdnTPRWYPL 4844
Cdd:cd08378     69 AKDDFLGGVCFDLSEVptrvppdSPL--APQWYRL 101
C2B_Synaptotagmin-3-5-6-9-10 cd08403
C2 domain second repeat present in Synaptotagmins 3, 5, 6, 9, and 10; Synaptotagmin is a ...
 4722-4844 8.01e-15

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: 74.47  E-value: 8.01e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4722 GEIQLQINYDKHLGNLIIHILQARNLAPRDNNGYSDPFVKVYLLpGRGAEYKRRTKYVQKS-LNPEWNQTVIYkNISTEQ 4800
Cdd:cd08403      1 GELMFSLCYLPTAGRLTLTIIKARNLKAMDITGFSDPYVKVSLM-CEGRRLKKKKTSVKKNtLNPTYNEALVF-DVPPEN 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1201829585 4801 LKKKTLEVTVWDYDRFSSNDFLGEVLIDLSSVSQ--------LDN----TPRWYPL 4844
Cdd:cd08403     79 VDNVSLIIAVVDYDRVGHNELIGVCRVGPNADGQgrehwnemLANprkpIAQWHQL 134
C2C_KIAA1228 cd04030
C2 domain third repeat present in uncharacterized human KIAA1228-like proteins; KIAA proteins ...
 5026-5151 1.60e-14

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: 73.08  E-value: 1.60e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 5026 GEIKIALkkEMKTDGEQLIVEILQCRNITykFKSPDHLPDLYVKLYVvnISTQKRVIKKKTRVCRHDREPSFNETFRFSL 5105
Cdd:cd04030      3 GRIQLTI--RYSSQRQKLIVTVHKCRNLP--PCDSSDIPDPYVRLYL--LPDKSKSTRRKTSVKKDNLNPVFDETFEFPV 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1201829585 5106 SPAGHSLQILLVS--NGGKFM--KKTLIGEAYVWLDKVDLRKRIVNWHKL 5151
Cdd:cd04030     77 SLEELKRRTLDVAvkNSKSFLsrEKKLLGQVLIDLSDLDLSKGFTQWYDL 126
C2A_fungal cd04041
C2 domain first repeat; fungal group; C2 domains were first identified in Protein Kinase C ...
 4735-4848 2.42e-14

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: 72.29  E-value: 2.42e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4735 GNLIIHILQARNLAPRDNN-GYSDPFVKVYLlpGRGAEYKRRTKYVQKSLNPEWNQTVIYKNISTEQLKKKTLEVTVWDY 4813
Cdd:cd04041      1 GVLVVTIHRATDLPKADFGtGSSDPYVTASF--AKFGKPLYSTRIIRKDLNPVWEETWFVLVTPDEVKAGERLSCRLWDS 78

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1201829585 4814 DRFSSNDFLGEVLIDLSSvsqLDNTPRWYPLKEQS 4848
Cdd:cd04041     79 DRFTADDRLGRVEIDLKE---LIEDRNWMGRREDG 110
C2B_MCTP_PRT cd08376
C2 domain second repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); ...
 4739-4846 5.62e-14

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: 71.13  E-value: 5.62e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4739 IHILQARNLAPRDNNGYSDPFVKVYLlpgrGAEyKRRTKYVQKSLNPEWnqtviyknisTEQL-------KKKTLEVTVW 4811
Cdd:cd08376      4 IVLVEGKNLPPMDDNGLSDPYVKFRL----GNE-KYKSKVCSKTLNPQW----------LEQFdlhlfddQSQILEIEVW 68

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1201829585 4812 DYDRFSSNDFLGEVLIDLSSVSQLDNTPRWYPLKE 4846
Cdd:cd08376     69 DKDTGKKDEFIGRCEIDLSALPREQTHSLELELED 103
C2B_RIM1alpha cd04028
C2 domain second repeat contained in Rab3-interacting molecule (RIM) proteins; RIMs are ...
 5022-5156 8.21e-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: 71.65  E-value: 8.21e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 5022 TQVMGEIKIALkkeMKTDGeQLIVEILQCRNITYKFKSpDHLPDLYVKLYVVniSTQKRVIKKKTRVCRHDREPSFNETF 5101
Cdd:cd04028     14 SPSMGDIQLGL---YDKKG-QLEVEVIRARGLVQKPGS-KVLPAPYVKVYLL--EGKKCIAKKKTKIARKTLDPLYQQQL 86

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1201829585 5102 RFSLSPAGHSLQILLVSNGGKFMKKTLIGEAYVWLDKVDLRKRIVNWHKLLVSST 5156
Cdd:cd04028     87 VFDVSPTGKTLQVIVWGDYGRMDKKVFMGVAQILLDDLDLSNLVIGWYKLFPTSS 141
C2B_Synaptotagmin-17 cd08410
C2 domain second repeat present in Synaptotagmin 17; Synaptotagmin is a membrane-trafficking ...
 4722-4827 9.78e-14

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: 71.07  E-value: 9.78e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4722 GEIQLQINYDKHLGNLIIHILQARNLAPRDNNGYSDPFVKVYLLPGRGAEYKRRTKYVQKSLNPEWNQTVIYKnISTEQL 4801
Cdd:cd08410      1 GELLLSLNYLPSAGRLNVDIIRAKQLLQTDMSQGSDPFVKIQLVHGLKLIKTKKTSCMRGTIDPFYNESFSFK-VPQEEL 79

                           90       100
                   ....*....|....*....|....*.
gi 1201829585 4802 KKKTLEVTVWDYDRFSSNDFLGEVLI 4827
Cdd:cd08410     80 ENVSLVFTVYGHNVKSSNDFIGRIVI 105
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 5042-5148 1.40e-13

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: 69.82  E-value: 1.40e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  5042 QLIVEILQCRNITYKFKSpdHLPDLYVKLYVVNistqKRVIKKKTRVCRHDREPSFNETFRFSLSPAGHSLQILLVSNGG 5121
Cdd:smart00239    1 TLTVKIISARNLPPKDKG--GKSDPYVKVSLDG----DPKEKKKTKVVKNTLNPVWNETFEFEVPPPELAELEIEVYDKD 74

                            90       100
                    ....*....|....*....|....*..
gi 1201829585  5122 KFMKKTLIGEAYVWLDKVDLRKRIVNW 5148
Cdd:smart00239   75 RFGRDDFIGQVTIPLSDLLLGGRHEKL 101
C2B_Synaptotagmin cd00276
C2 domain second repeat present in Synaptotagmin; Synaptotagmin is a membrane-trafficking ...
 5041-5151 1.89e-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: 70.30  E-value: 1.89e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 5041 EQLIVEILQCRNItyKFKSPDHLPDLYVKLYVVNisTQKRVIKKKTRVCRHDREPSFNETFRFSLSP---AGHSLQILLV 5117
Cdd:cd00276     14 ERLTVVVLKARNL--PPSDGKGLSDPYVKVSLLQ--GGKKLKKKKTSVKKGTLNPVFNEAFSFDVPAeqlEEVSLVITVV 89

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1201829585 5118 SNgGKFMKKTLIGEAYV-----------WLDKVD-LRKRIVNWHKL 5151
Cdd:cd00276     90 DK-DSVGRNEVIGQVVLgpdsggeelehWNEMLAsPRKPIARWHKL 134
C2_ArfGAP cd04038
C2 domain present in Arf GTPase Activating Proteins (GAP); ArfGAP is a GTPase activating ...
 4734-4829 5.23e-13

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: 69.28  E-value: 5.23e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4734 LGNLIIHILQARNLAPRDNNGySDPFVKVYLlpgrGAEyKRRTKYVQKSLNPEWNQ--TVIYKNIsTEQLKkktleVTVW 4811
Cdd:cd04038      1 LGLLKVRVVRGTNLAVRDFTS-SDPYVVLTL----GNQ-KVKTRVIKKNLNPVWNEelTLSVPNP-MAPLK-----LEVF 68

                           90
                   ....*....|....*...
gi 1201829585 4812 DYDRFSSNDFLGEVLIDL 4829
Cdd:cd04038     69 DKDTFSKDDSMGEAEIDL 86
PHA03247 PHA03247
large tegument protein UL36; Provisional
 189-438 6.62e-13

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 76.13  E-value: 6.62e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  189 DQGKPEEQRGLAKHPSQQqSPKLVQQQGPVKPTPQQTESSKPVPQQQ-QPGEPKQIQKPgPSHQGDSKVEQPKQP---PQ 264
Cdd:PHA03247  2703 PPPPTPEPAPHALVSATP-LPPGPAAARQASPALPAAPAPPAVPAGPaTPGGPARPARP-PTTAGPPAPAPPAAPaagPP 2780

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  265 PRG--PQKSQLQQSEPTKPVQQQTSAKPSVGPTkPLPQQPDSAKTSSQASPPTKPSSQQSGPVKQPSQQPARQGGPVKPs 342
Cdd:PHA03247  2781 RRLtrPAVASLSESRESLPSPWDPADPPAAVLA-PAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAP- 2858

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  343 aqqAGPPKQQPGSEKPSAQQTGPAKQPLQTGPGKPPLQQTGPVKQVP--PQAGPTKPSSQTAGATKSVAQQPGLTKPPGP 420
Cdd:PHA03247  2859 ---GGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPdqPERPPQPQAPPPPQPQPQPPPPPQPQPPPPP 2935

                          250
                   ....*....|....*...
gi 1201829585  421 QSGPEKPSQQKQASAAQP 438
Cdd:PHA03247  2936 PPRPQPPLAPTTDPAGAG 2953
C2 pfam00168
C2 domain;
5042-5151 7.10e-13

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 67.73  E-value: 7.10e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 5042 QLIVEILQCRNITYKFKSPdhLPDLYVKLYVvnistQKRVIKKKTRVCRHDREPSFNETFRFSLSPAGHSLQILLVSNGG 5121
Cdd:pfam00168    2 RLTVTVIEAKNLPPKDGNG--TSDPYVKVYL-----LDGKQKKKTKVVKNTLNPVWNETFTFSVPDPENAVLEIEVYDYD 74

                           90       100       110
                   ....*....|....*....|....*....|
gi 1201829585 5122 KFMKKTLIGEAYVWLDKVDLRKRIVNWHKL 5151
Cdd:pfam00168   75 RFGRDDFIGEVRIPLSELDSGEGLDGWYPL 104
C2A_SLP cd08521
C2 domain first repeat present in Synaptotagmin-like proteins; All Slp members basically share ...
 5026-5151 1.81e-12

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: 67.28  E-value: 1.81e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 5026 GEIKIALKKEMKTDGeqLIVEILQCRNITYKfKSPDHLPDLYVKLYVV-NISTQKrviKKKTRVCRHDREPSFNETFRFS 5104
Cdd:cd08521      1 GEIEFSLSYNYKTGS--LEVHIKECRNLAYA-DEKKKRSNPYVKVYLLpDKSKQS---KRKTSVKKNTTNPVFNETLKYH 74

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1201829585 5105 LSPAGHSLQILLVS--NGGKFMKKTLIGEAYVWLDKVDLRKRIVNWHKL 5151
Cdd:cd08521     75 ISKSQLETRTLQLSvwHHDRFGRNTFLGEVEIPLDSWDLDSQQSEWYPL 123
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 5043-5151 1.91e-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: 66.32  E-value: 1.91e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 5043 LIVEILQCRNITYKFKSpdHLPDLYVKLYVVNistqkrVIKKKTRVCRHDREPSFNETFRFSLSPAGHSLQILLVSNGGK 5122
Cdd:cd00030      1 LRVTVIEARNLPAKDLN--GKSDPYVKVSLGG------KQKFKTKVVKNTLNPVWNETFEFPVLDPESDTLTVEVWDKDR 72

                           90       100       110
                   ....*....|....*....|....*....|
gi 1201829585 5123 FMKKTLIGEAYVWLDKV-DLRKRIVNWHKL 5151
Cdd:cd00030     73 FSKDDFLGEVEIPLSELlDSGKEGELWLPL 102
C2_KIAA0528-like cd08688
C2 domain found in the Human KIAA0528 cDNA clone; The members of this CD are named after the ...
 4739-4844 2.11e-12

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: 66.56  E-value: 2.11e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4739 IHILQARNLAPRD-NNGYSDPFVKVYLLpgrGAEYKrrTKYVQKSLNPEWNQTVIYKNISTEQLKKKTLEVTVWDYDRFS 4817
Cdd:cd08688      3 VRVVAARDLPVMDrSSDLTDAFVEVKFG---STTYK--TDVVKKSLNPVWNSEWFRFEVDDEELQDEPLQIRVMDHDTYS 77

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1201829585 4818 SNDFLGEVLIDLS------SVSQLDNtprWYPL 4844
Cdd:cd08688     78 ANDAIGKVYIDLNplllkdSVSQISG---WFPI 107
PDZ1_GgSTXBP4-like cd06692
PDZ1 domain of Gallus gallus uncharacterized syntaxin-binding protein 4 (STXBP4) isoform X1, ...
 4538-4602 7.62e-12

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: 64.16  E-value: 7.62e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1201829585 4538 NGLGIRVVGGKEiPGSSGEIGAYIAKVLPGGSAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQNII 4602
Cdd:cd06692      8 KGLGIKIIGGYR-ENTGEEFGIFIKRILPGGLAATDGRLKEGDLILEVNGESLQGVTNERAVSIL 71
PHA03247 PHA03247
large tegument protein UL36; Provisional
 514-1023 8.59e-12

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 72.66  E-value: 8.59e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  514 GPGPQLPPPKQKTPTPTSTAKPSPQSQPgqkkdaspkPDPSQQADSKKP--VPQKKQPSMPGSP---PVKSKQTDAEPSD 588
Cdd:PHA03247  2550 DPPPPLPPAAPPAAPDRSVPPPRPAPRP---------SEPAVTSRARRPdaPPQSARPRAPVDDrgdPRGPAPPSPLPPD 2620

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  589 TfQQIDPTPKSDQAKPTQAEEKQNQPSVQKPTTDTVPTSAAPGVKQDLADPRPPLTQQKVTDSPKPETTKPP-------A 661
Cdd:PHA03247  2621 T-HAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTvgsltslA 2699

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  662 DTHPAGDKPDSKPLPQVSRQKSDPKLASQSGSKSDAKTQKA--------VEPAQVRDDPKKLQTKSAPKPDTKPAPKGPQ 733
Cdd:PHA03247  2700 DPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAppavpagpATPGGPARPARPPTTAGPPAPAPPAAPAAGP 2779

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  734 AGTGPKPMSAQPAPQPQQPQKTPEQS--------RRFSLNLGGITDVPKPQPTTPQETVTGKlfgfgASIFSQASSLIST 805
Cdd:PHA03247  2780 PRRLTRPAVASLSESRESLPSPWDPAdppaavlaPAAALPPAASPAGPLPPPTSAQPTAPPP-----PPGPPPPSLPLGG 2854

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  806 AGQPGSQTS--GPAPPAAKQPQPPSQPTA---SQAPPKEATQAQPLPKAAPTKKETKPLASEKL---EPMAADSTLTTKG 877
Cdd:PHA03247  2855 SVAPGGDVRrrPPSRSPAAKPAAPARPPVrrlARPAVSRSTESFALPPDQPERPPQPQAPPPPQpqpQPPPPPQPQPPPP 2934

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  878 SDLEKKPSLAKDSKPQAAEAKKPAELSEQEKASQP-KVSCPLCKTGLNIGSKDPPNFNTCTECKKVVCNLCGF------- 949
Cdd:PHA03247  2935 PPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPgRVAVPRFRVPQPAPSREAPASSTPPLTGHSLSRVSSWasslalh 3014

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  950 ---NPMPHIAEVQEWLCLNCQTQRAMSGQLGDMGKVPLPKLGPSQP-VSKPPATPQKQPVPAVSH--SPQKTSTPPTPAA 1023
Cdd:PHA03247  3015 eetDPPPVSLKQTLWPPDDTEDSDADSLFDSDSERSDLEALDPLPPePHDPFAHEPDPATPEAGAreSPSSQFGPPPLSA 3094
C2A_Munc13-like cd08676
C2 domain first repeat in Munc13 (mammalian uncoordinated)-like proteins; C2-like domains are ...
 4737-4844 1.04e-11

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: 65.86  E-value: 1.04e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4737 LIIHILQARNLAPRDNNGYSDPFVKVYLLPGRG------------------------AEYKRRTKYVQKSLNPEWNQTVI 4792
Cdd:cd08676     30 LKVTVIEAKGLLAKDVNGFSDPYCMLGIVPASRernsekskkrkshrkkavlkdtvpAKSIKVTEVKPQTLNPVWNETFR 109

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1201829585 4793 YKnisTEQLKKKTLEVTVWDYDrfssNDFLGEVLIDLSSVSQlDNTPRWYPL 4844
Cdd:cd08676    110 FE---VEDVSNDQLHLDIWDHD----DDFLGCVNIPLKDLPS-CGLDSWFKL 153
C2_fungal_Inn1p-like cd08681
C2 domain found in fungal Ingression 1 (Inn1) proteins; Saccharomyces cerevisiae Inn1 ...
 4735-4850 1.05e-11

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: 64.96  E-value: 1.05e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4735 GNLIIHILQARNLAPRDNNGYSDPFVKVyllpgRGAEYKRRTKYVQKS-LNPEWNQTVIYkNISTEqlKKKTLEVTVWDy 4813
Cdd:cd08681      1 GTLVVVVLKARNLPNKRKLDKQDPYCVL-----RIGGVTKKTKTDFRGgQHPEWDEELRF-EITED--KKPILKVAVFD- 71

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1201829585 4814 DRFSSNDFLGEVLIDLSSVSQLDNTPRWYPLKEQSEN 4850
Cdd:cd08681     72 DDKRKPDLIGDTEVDLSPALKEGEFDDWYELTLKGRY 108
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 4536-4614 1.15e-11

Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF (relatively well conserved tetrapeptide in these domains). Some PDZs have been shown to bind C-terminal polypeptides; others appear to bind internal (non-C-terminal) polypeptides. Different PDZs possess different binding specificities.


Pssm-ID: 214570 [Multi-domain]  Cd Length: 85  Bit Score: 63.55  E-value: 1.15e-11
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1201829585  4536 SGNGLGIRVVGGKEIPGssgeiGAYIAKVLPGGSAEQTGkLIEGMQVLEWNGIPLTGKTYEEVQNIIIQQCGEAEICVR 4614
Cdd:smart00228   10 GGGGLGFSLVGGKDEGG-----GVVVSSVVPGSPAAKAG-LRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVTLTVL 82
C2_Intersectin cd08375
C2 domain present in Intersectin; A single instance of the C2 domain is located C terminally ...
 4735-4840 1.37e-11

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: 65.10  E-value: 1.37e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4735 GNLIIHILQARNLAPRDNNGYSDPFVKVYLlpgrgAEYKRRTKYVQKSLNPEWNQTVIYkniSTEQLKKKTLEVTVWDYD 4814
Cdd:cd08375     15 GRLMVVIVEGRDLKPCNSNGKSDPYCEVSM-----GSQEHKTKVVSDTLNPKWNSSMQF---FVKDLEQDVLCITVFDRD 86

                           90       100
                   ....*....|....*....|....*.
gi 1201829585 4815 RFSSNDFLGEVLIDLSSVSQLDNTPR 4840
Cdd:cd08375     87 FFSPDDFLGRTEIRVADILKETKESK 112
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 213-449 3.06e-11

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: 70.57  E-value: 3.06e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  213 QQQGPVKPTPQQTESSKPVPQQQQPGEPKQIQKPGP-------SHQGDSKVEQPKQPPQPRGPQKSQLQQSePTKPVQQQ 285
Cdd:pfam03154  164 QQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPtpsapsvPPQGSPATSQPPNQTQSTAAPHTLIQQT-PTLHPQRL 242

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  286 TSAKPsvgPTKPLPQQPDSAKTSSQASP--------PTKPSSQQSGPVKQPSQQPARQGGPVKPSAQQAGPP-------- 349
Cdd:pfam03154  243 PSPHP---PLQPMTQPPPPSQVSPQPLPqpslhgqmPPMPHSLQTGPSHMQHPVPPQPFPLTPQSSQSQVPPgpspaapg 319

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  350 -----KQQPGSEKPSAQQTGPAKQPLQTGPGKPPLQQTGPVKQVPPQAGPTKPSSQTAGATKSVAQQPGLTKPP------ 418
Cdd:pfam03154  320 qsqqrIHTPPSQSQLQSQQPPREQPLPPAPLSMPHIKPPPTTPIPQLPNPQSHKHPPHLSGPSPFQMNSNLPPPpalkpl 399

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1201829585  419 ------GPQSGPEKP------SQQKQASAAQPVESTPKKTFCP 449
Cdd:pfam03154  400 sslsthHPPSAHPPPlqlmpqSQQLPPPPAQPPVLTQSQSLPP 442
C2B_Munc13 cd04027
C2 domain second repeat in Munc13 (mammalian uncoordinated) proteins; C2-like domains are ...
 4737-4849 4.82e-11

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: 63.36  E-value: 4.82e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4737 LIIHILQARNLAPRDNNGYSDPFVKVYLlpgrgAEYKRRTKYVQKSLNPEWNQTVIYK-NISTEQLKkktleVTVWDYD- 4814
Cdd:cd04027      3 ISITVVCAQGLIAKDKTGTSDPYVTVQV-----GKTKKRTKTIPQNLNPVWNEKFHFEcHNSSDRIK-----VRVWDEDd 72

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1201829585 4815 --------RFS--SNDFLGEVLIDLSSVS-QLDntpRWYPLKEQSE 4849
Cdd:cd04027     73 diksrlkqKFTreSDDFLGQTIIEVRTLSgEMD---VWYNLEKRTD 115
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 172-394 1.11e-10

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: 1.11e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  172 SDAAHEEAGR--KQKVTQKDQGKPEEQRGLAKHPSQQQSPKLVQQQGPVK----------PTPQ-QTESS----KPVPQQ 234
Cdd:pfam09770   92 SDAIEEEQVRfnRQQPAARAAQSSAQPPASSLPQYQYASQQSQQPSKPVRtgyekykepePIPDlQVDASlwgvAPKKAA 171

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  235 QQPGEPKQIQKPGPSHQGDSKV-----------EQPKQPPQPRGPQKSQLQQSEPTKPVQQQTSAKPSVGPTKPLPQQPD 303
Cdd:pfam09770  172 APAPAPQPAAQPASLPAPSRKMmsleeveaamrAQAKKPAQQPAPAPAQPPAAPPAQQAQQQQQFPPQIQQQQQPQQQPQ 251

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  304 SAKTSSQASPP----TKPSSQQSGPVkQPSQQPARQGGPVKPSAQQAGP------PKQQPGSEKPSAQQTGPAKQPLQTG 373
Cdd:pfam09770  252 QPQQHPGQGHPvtilQRPQSPQPDPA-QPSIQPQAQQFHQQPPPVPVQPtqilqnPNRLSAARVGYPQNPQPGVQPAPAH 330

                          250       260
                   ....*....|....*....|.
gi 1201829585  374 PGKPplQQTGPVKQVPPQAGP 394
Cdd:pfam09770  331 QAHR--QQGSFGRQAPIITHP 349
Glutenin_hmw pfam03157
High molecular weight glutenin subunit; Members of this family include high molecular weight ...
 177-438 1.33e-10

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: 68.05  E-value: 1.33e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  177 EEAGRKQKVTQKDQGKPEEQRGLAKHPSQQQSPKLvQQQGPVKPTPQQTESSKPVPQQQQPGEPKQIQKPGPSHQG---- 252
Cdd:pfam03157  222 QQPERGQQGQQPGQGQQPGQGQQGQQPGQPQQLGQ-GQQGYYPISPQQPRQWQQSGQGQQGYYPTSLQQPGQGQSGyypt 300

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  253 ----------DSKVEQPKQPPQP----RGPQKSQLQQSEPTKPVQQQTSAKPSVGPTKPL-------------PQQPDSA 305
Cdd:pfam03157  301 sqqqagqlqqEQQLGQEQQDQQPgqgrQGQQPGQGQQGQQPAQGQQPGQGQPGYYPTSPQqpgqgqpgyyptsQQQPQQG 380

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  306 KTSSQASPPTKPSSQQSGPVKQPSQQPAR-QGGPVKPSAQQAGppKQQPGSEKPSAQQTGPAKQPlqtGPGKPPLQQTGP 384
Cdd:pfam03157  381 QQPEQGQQGQQQGQGQQGQQPGQGQQPGQgQPGYYPTSPQQSG--QGQPGYYPTSPQQSGQGQQP---GQGQQPGQEQPG 455

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1201829585  385 VKQVPPQAGPTKPSSQTAGATKSVAQQPGLTKPPGPQSGP-EKPSQQKQASAAQP 438
Cdd:pfam03157  456 QGQQPGQGQQGQQPGQPEQGQQPGQGQPGYYPTSPQQSGQgQQLGQWQQQGQGQP 510
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 323-712 1.47e-10

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 68.09  E-value: 1.47e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  323 GPVKQPSQQPARQGGPVKPSAQQAGPPKQQPGSEKPSAQQTGPAKQPLQTGPGKPPLQQTGPVKQVPPQAGPTKPSSQTA 402
Cdd:PRK07764   391 AGAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAP 470

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  403 GATKSVAQQPGLTKPPGPQSGPEkPSQQKQASAAQP--------------VESTPKKTFcplcTTTELLL-----HVPEK 463
Cdd:PRK07764   471 AAAPEPTAAPAPAPPAAPAPAAA-PAAPAAPAAPAGaddaatlrerwpeiLAAVPKRSR----KTWAILLpeatvLGVRG 545

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  464 anyNTCTQCHTVVCSLCGFNpNPHITE-----IKEWLCLNCQMQRALGGDLASGHGPGPQLPPPKQKTPTPTSTAKPSPQ 538
Cdd:PRK07764   546 ---DTLVLGFSTGGLARRFA-SPGNAEvlvtaLAEELGGDWQVEAVVGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAP 621

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  539 SQPGQKKDASPKPDPSQQADSKKPVPQKKQPSMPGSP-PVKSKQTDAEPSDTFQQI---DPTPKSDQAKPTQAEEKQNQP 614
Cdd:PRK07764   622 AAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAvPDASDGGDGWPAKAGGAApaaPPPAPAPAAPAAPAGAAPAQP 701

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  615 SVQKPTTDTVPTSAAPGVkQDLADPRPPLTQQKVTDSPKPETTKPPADTHPAGDKPDSKPLPQVSRqksdpklASQSGSK 694
Cdd:PRK07764   702 APAPAATPPAGQADDPAA-QPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAP-------AAAPAAA 773

                          410
                   ....*....|....*...
gi 1201829585  695 SDAKTQKAVEPAQVRDDP 712
Cdd:PRK07764   774 PPPSPPSEEEEMAEDDAP 791
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 261-432 2.43e-10

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: 67.37  E-value: 2.43e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  261 QPPQPRGPQKSQLQQSEPTKPVQQQTSakPSVGPTKPLP------QQPD-----SAKTSSQASPPTKPSSQQSGPvkQPS 329
Cdd:pfam09770  105 QQPAARAAQSSAQPPASSLPQYQYASQ--QSQQPSKPVRtgyekyKEPEpipdlQVDASLWGVAPKKAAAPAPAP--QPA 180

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  330 QQPARQGGPV------------------KPSAQQAGPPKQQPGSEkPSAQQTGPAKQPLQTGPGKPPLQQTGPVKQVPPQ 391
Cdd:pfam09770  181 AQPASLPAPSrkmmsleeveaamraqakKPAQQPAPAPAQPPAAP-PAQQAQQQQQFPPQIQQQQQPQQQPQQPQQHPGQ 259

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1201829585  392 AGP----TKPSSQTAGATKSVAQQPGLTKPPGPQSGPEKPSQQKQ 432
Cdd:pfam09770  260 GHPvtilQRPQSPQPDPAQPSIQPQAQQFHQQPPPVPVQPTQILQ 304
PDZ2_PDZD2-like cd06758
PDZ domain 2 of PDZ domain containing 2 (PDZD2), and related domains; PDZ (PSD-95 ...
 4531-4602 2.45e-10

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: 60.06  E-value: 2.45e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1201829585 4531 KDHTVSGN-GLGIRVVGGKeipGSS-GEIGAYIAKVLPGGSAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQNII 4602
Cdd:cd06758      4 KMHLLKEKgGLGIQITGGK---GSKrGDIGIFVAGVEEGGSADRDGRLKKGDELLMINGQSLIGLSHQEAVAIL 74
PHA03378 PHA03378
EBNA-3B; Provisional
 222-424 2.52e-10

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 67.40  E-value: 2.52e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  222 PQQTESSKPVPQQQQPGEPKQIQKPGPSHQGDSKVEQPKQPPQPR-------------GPQKSQLQQSEPTkpVQQQTSA 288
Cdd:PHA03378   590 PSYAQTPWPVPHPSQTPEPPTTQSHIPETSAPRQWPMPLRPIPMRplrmqpitfnvlvFPTPHQPPQVEIT--PYKPTWT 667

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  289 KPSVGPTKPLPQQPDSAKTSSQASPPTKPSSQQSGPVKQPSQQPARQGGPvKPSAQQAGPPKQQPGSEKPSAQQTGPAKQ 368
Cdd:PHA03378   668 QIGHIPYQPSPTGANTMLPIQWAPGTMQPPPRAPTPMRPPAAPPGRAQRP-AAATGRARPPAAAPGRARPPAAAPGRARP 746

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1201829585  369 PlQTGPGKPPLQQTGPVKQVPPQAGPTKPSSQTAGATKSVAQQ---PGLTKPPGPQSGP 424
Cdd:PHA03378   747 P-AAAPGRARPPAAAPGRARPPAAAPGAPTPQPPPQAPPAPQQrprGAPTPQPPPQAGP 804
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 204-680 2.64e-10

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 67.42  E-value: 2.64e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  204 SQQQSPKLVQQQGPVKPTPQQteSSKPVPQQQQPGEPKQIQKPGPSHQGDSKVEQPKQPPQPRGPQKSQLQQSEPTKPV- 282
Cdd:PRK10263   379 GYPQQSQYAQPAVQYNEPLQQ--PVQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQSTf 456

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  283 QQQTSAKPSVGPTKPLPQQPDSAKTSSQASPPT---KPSSQQSGPVKQP-------SQQPARQGGPVKPSAQQAGPPKQQ 352
Cdd:PRK10263   457 APQSTYQTEQTYQQPAAQEPLYQQPQPVEQQPVvepEPVVEETKPARPPlyyfeevEEKRAREREQLAAWYQPIPEPVKE 536

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  353 PGSEKPSAqqtgpakqPLQTGPGKPPLqqtGPVKQVPPQAGPTKPSSQTAGATKSVAQ-----------QPGLTKPPGPQ 421
Cdd:PRK10263   537 PEPIKSSL--------KAPSVAAVPPV---EAAAAVSPLASGVKKATLATGAAATVAApvfslansggpRPQVKEGIGPQ 605

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  422 -----------------SGPEKPSQQKQASAAQPVESTPKKTFCPLCTTTELLLHVPEKANYNTCTQCHTVVCSLCGFNP 484
Cdd:PRK10263   606 lprpkrirvptrrelasYGIKLPSQRAAEEKAREAQRNQYDSGDQYNDDEIDAMQQDELARQFAQTQQQRYGEQYQHDVP 685

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  485 -----NPHITEIKEWLCLNCQMQRALGGDLASGHGP--------GPQLPPPKQKTPTPTSTAKPSPQSQPGQKKDASPKP 551
Cdd:PRK10263   686 vnaedADAAAEAELARQFAQTQQQRYSGEQPAGANPfslddfefSPMKALLDDGPHEPLFTPIVEPVQQPQQPVAPQQQY 765

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  552 DPSQQADSkkPVPQKKQPSMPGSPPVKSKQTDAEPSDTFQQIDPtpkSDQAKPTQAEEKQNQPSVQKPTTDTVPTSAAPG 631
Cdd:PRK10263   766 QQPQQPVA--PQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQP---QQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQ 840

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1201829585  632 VKQDL--------ADPRPplTQQKVTDSPKPE-TTKPPADTHPAgdkpDSKPLPQVSR 680
Cdd:PRK10263   841 PQDTLlhpllmrnGDSRP--LHKPTTPLPSLDlLTPPPSEVEPV----DTFALEQMAR 892
C2B_PI3K_class_II cd08381
C2 domain second repeat present in class II phosphatidylinositol 3-kinases (PI3Ks); There are ...
 5064-5151 3.46e-10

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: 60.77  E-value: 3.46e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 5064 PDLYVKLYVvnISTQKRVIKKKTRVCRHDREPSFNETFRFSLSPA----GHSLQiLLVSNGGKFMKKTLIGEAYVWLDKV 5139
Cdd:cd08381     33 PDPYVKTYL--LPDPQKTTKRKTKVVRKTRNPTFNEMLVYDGLPVedlqQRVLQ-VSVWSHDSLVENEFLGGVCIPLKKL 109

                           90
                   ....*....|..
gi 1201829585 5140 DLRKRIVNWHKL 5151
Cdd:cd08381    110 DLSQETEKWYPL 121
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 186-438 5.58e-10

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: 66.19  E-value: 5.58e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  186 TQKDQGKPEEQRGLAKHPSQQQSpklVQQQGPVKPTPQQTESSKPVPQQQQP------GEPKQIQKPGPShQGDSKVEQP 259
Cdd:pfam09606  123 LLASLGRPQMPMGGAGFPSQMSR---VGRMQPGGQAGGMMQPSSGQPGSGTPnqmgpnGGPGQGQAGGMN-GGQQGPMGG 198

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  260 KQPPQPRGP----------QKSQLQQSEPTKPVQQQTSAKPSVGPTKPLPQ-QPDSAKTSSQASPPTKPSsqQSGPVKQP 328
Cdd:pfam09606  199 QMPPQMGVPgmpgpadagaQMGQQAQANGGMNPQQMGGAPNQVAMQQQQPQqQGQQSQLGMGINQMQQMP--QGVGGGAG 276

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  329 SQQPArQGGPVKPSAQQAGPPKQQPGSEKPSAQQTGPAKQPLQTGPGKP-----PLQQTGPVKQVPPQAGPTKPSSQTAG 403
Cdd:pfam09606  277 QGGPG-QPMGPPGQQPGAMPNVMSIGDQNNYQQQQTRQQQQQQGGNHPAahqqqMNQSVGQGGQVVALGGLNHLETWNPG 355

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1201829585  404 ATKSVAQQPGLTKPPGPQSGPEKPSQQKQASAAQP 438
Cdd:pfam09606  356 NFGGLGANPMQRGQPGMMSSPSPVPGQQVRQVTPN 390
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 203-430 5.63e-10

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: 66.19  E-value: 5.63e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  203 PSQQQSPKLVQQQGPVKP-TPQQTESSKPVPQQQQPGEPKQIQKPGPShQGDSKVEQPKQPPQPRGPQksQLQQSEPTKP 281
Cdd:pfam09606  166 PGSGTPNQMGPNGGPGQGqAGGMNGGQQGPMGGQMPPQMGVPGMPGPA-DAGAQMGQQAQANGGMNPQ--QMGGAPNQVA 242

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  282 VQQ-QTSAKPSVGPTKPLPQQPDSAKTSSQASPPTKPSSQQSGPVKQPSQQPARQGGPVKPS---AQQAGPPKQQPGSEK 357
Cdd:pfam09606  243 MQQqQPQQQGQQSQLGMGINQMQQMPQGVGGGAGQGGPGQPMGPPGQQPGAMPNVMSIGDQNnyqQQQTRQQQQQQGGNH 322

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  358 PSAQQTGPAKQPLQTG-----PGKPPLQQTGPVKQVPPQAGP---------TKPSSQTAGATKSVAQQPGLTKPPGPQS- 422
Cdd:pfam09606  323 PAAHQQQMNQSVGQGGqvvalGGLNHLETWNPGNFGGLGANPmqrgqpgmmSSPSPVPGQQVRQVTPNQFMRQSPQPSVp 402


                   ....*...
gi 1201829585  423 GPEKPSQQ 430
Cdd:pfam09606  403 SPQGPGSQ 410
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 534-779 5.80e-10

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: 65.56  E-value: 5.80e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  534 KPSPQSQPGQkkdasPKPDPSQQADSKKPVPQKKQPSMPGSPPVKSKQTDAEPSDTFQQIDPTPksDQAKPtqaeEKQNQ 613
Cdd:NF033839   300 QPSPQPEKKE-----VKPEPETPKPEVKPQLEKPKPEVKPQPEKPKPEVKPQLETPKPEVKPQP--EKPKP----EVKPQ 368

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  614 PSVQKPTTDTVPTSAAPGVKQDLADPRPPLtqqkvtdSPKPETTKPPADTHPAGDKPDSKPLPQVSRQ--KSDPKLASQS 691
Cdd:NF033839   369 PEKPKPEVKPQPETPKPEVKPQPEKPKPEV-------KPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPevKPQPEKPKPE 441

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  692 GSKSDAKTQKAVEPAQVRDDPKKLQTKSAPKPDTKPAPKGPQAGTGPKPMSAQPAPQPQQPQKTPEQSRRFSLNLGGITD 771
Cdd:NF033839   442 VKPQPEKPKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEKPKPDNSKPQADDKKPSTPNNLSKDKQPSNQASTNEKATNK 521


                   ....*...
gi 1201829585  772 VPKPQPTT 779
Cdd:NF033839   522 PKKSLPST 529
PDZ2-PTPN13_FRMPD2-like cd06792
PDZ domain 2 of tyrosine kinase PTPN13, FERM and PDZ domain-containing protein 2 (FRMPD2), and ...
 4538-4602 6.69e-10

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: 58.76  E-value: 6.69e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1201829585 4538 NGLGIRVVGGKEIPGSSGeiGAYIAKVLPGGSAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQNII 4602
Cdd:cd06792     12 GSLGISVTGGINTSVRHG--GIYVKSLVPGGAAEQDGRIQKGDRLLEVNGVSLEGVTHKQAVECL 74
COG5038 COG5038
Ca2+-dependent lipid-binding protein, contains C2 domain [General function prediction only];
4735-4834 8.85e-10

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


Pssm-ID: 227371 [Multi-domain]  Cd Length: 1227  Bit Score: 65.55  E-value: 8.85e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4735 GNLIIHILQARNLAPRDNNGYSDPFVKVYLlpgrGAEYKRRTKYVQKSLNPEWNQTviykniSTEQLKKKT---LEVTVW 4811
Cdd:COG5038   1040 GYLTIMLRSGENLPSSDENGYSDPFVKLFL----NEKSVYKTKVVKKTLNPVWNEE------FTIEVLNRVkdvLTINVN 1109

                           90       100
                   ....*....|....*....|...
gi 1201829585 4812 DYDRFSSNDFLGEVLIDLSSVSQ 4834
Cdd:COG5038   1110 DWDSGEKNDLLGTAEIDLSKLEP 1132
C2_Rab11-FIP_classI cd08682
C2 domain found in Rab11-family interacting proteins (FIP) class I; Rab GTPases recruit ...
 4741-4845 1.11e-09

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: 59.39  E-value: 1.11e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4741 ILQARNLAPRDNNGYSDPFVKVYLlpgrGAEyKRRTKYVQKSLNPEWNQTVIYK--NISTEQLKKKTLEVTVWDYDRFSS 4818
Cdd:cd08682      5 VLQARGLLCKGKSGTNDAYVIIQL----GKE-KYSTSVKEKTTSPVWKEECSFElpGLLSGNGNRATLQLTVMHRNLLGL 79

                           90       100
                   ....*....|....*....|....*....
gi 1201829585 4819 NDFLGEVLIDLSSVSQLDNTPR--WYPLK 4845
Cdd:cd08682     80 DKFLGQVSIPLNDLDEDKGRRRtrWFKLE 108
PHA03379 PHA03379
EBNA-3A; Provisional
 180-634 1.21e-09

EBNA-3A; Provisional


Pssm-ID: 223066 [Multi-domain]  Cd Length: 935  Bit Score: 65.08  E-value: 1.21e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  180 GRKQKVTQKDQGKPEEQRGLAKHPSQQQSPKLVQQQgpvkptpQQTESSKPVpQQQQPGePKQIQKPGPSHQGDSKVEQP 259
Cdd:PHA03379   396 KLTERAREALEKASEPTYGTPRPPVEKPRPEVPQSL-------ETATSHGSA-QVPEPP-PVHDLEPGPLHDQHSMAPCP 466

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  260 KQPPQPRGPQKSQLQQSEPTKPVQQQTSAKPSVGPTKPL--PQQPDSAKTSSQASPPTKPSSQQSGPVKQPSQQPARQGG 337
Cdd:PHA03379   467 VAQLPPGPLQDLEPGDQLPGVVQDGRPACAPVPAPAGPIvrPWEASLSQVPGVAFAPVMPQPMPVEPVPVPTVALERPVC 546

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  338 PVKPSAQQAGPpkqqpgSEKPSAQQTGPAKQPLQTGPGKPPlqqtgPVKQVPPQAGPTKPSSQTAGATKSVAQQPgltkP 417
Cdd:PHA03379   547 PAPPLIAMQGP------GETSGIVRVRERWRPAPWTPNPPR-----SPSQMSVRDRLARLRAEAQPYQASVEVQP----P 611

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  418 PGPQSGPEKPSQQKQASAAQPVESTPKKTFCPLCTTTELLLHVPEKANY---NTCTQCHTVVCSLCGFNPNPHITEIKE- 493
Cdd:PHA03379   612 QLTQVSPQQPMEYPLEPEQQMFPGSPFSQVADVMRAGGVPAMQPQYFDLplqQPISQGAPLAPLRASMGPVPPVPATQPq 691

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  494 WLCLNCQMQRALGGDLASG--HGP--GPQLPPPKQKTPtptstAKPSPQSQPGQKKDASPKPDPSQQADSKKPV-PQKKQ 568
Cdd:PHA03379   692 YFDIPLTEPINQGASAAHFlpQQPmeGPLVPERWMFQG-----ATLSQSVRPGVAQSQYFDLPLTQPINHGAPAaHFLHQ 766

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1201829585  569 PSMPGsPPVKskqtDAEPsdtFQQIDPTPKSDQAkPTQAEEKQNQPSVQKPTtdTVPTSaaPGVKQ 634
Cdd:PHA03379   767 PPMEG-PWVP----EQWM---FQGAPPSQGTDVV-QHQLDALGYVLHVLNHP--GVPVS--PAVNQ 819
PHA03378 PHA03378
EBNA-3B; Provisional
 217-443 1.35e-09

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 65.09  E-value: 1.35e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  217 PVKPTPQQTESSKPVPQQ----QQPGEPKQIQKPGPS-----------HQGDSKVEQPKQPPQ-PRGPQKSQLQQSEPTK 280
Cdd:PHA03378   646 LVFPTPHQPPQVEITPYKptwtQIGHIPYQPSPTGANtmlpiqwapgtMQPPPRAPTPMRPPAaPPGRAQRPAAATGRAR 725

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  281 PVQQQTSA--KPSVGPTKPLPQQPDSAKTSSQASPPTKPSSQQSGPvKQPSQQPARQGGPVKPSAQQAGPPKQQPGSEKP 358
Cdd:PHA03378   726 PPAAAPGRarPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAP-GAPTPQPPPQAPPAPQQRPRGAPTPQPPPQAGP 804

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  359 SAQQTGPAKQPLQTGPGKPPLQQ--TGPVKQvppqagpTKPSSQTAGAtksVAQQPGLTKPPGPQSGPEkpSQQKQASAA 436
Cdd:PHA03378   805 TSMQLMPRAAPGQQGPTKQILRQllTGGVKR-------GRPSLKKPAA---LERQAAAGPTPSPGSGTS--DKIVQAPVF 872


                   ....*..
gi 1201829585  437 QPVESTP 443
Cdd:PHA03378   873 YPPVLQP 879
PHA03247 PHA03247
large tegument protein UL36; Provisional
 541-1037 2.69e-09

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 64.19  E-value: 2.69e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  541 PGQKKDASPKPDPSQQADSKKPVPQKKQPSMPGSPPVKSKQ-----TDAEPSDT-----------FQQI------DPTPK 598
Cdd:PHA03247  2475 PGAPVYRRPAEARFPFAAGAAPDPGGGGPPDPDAPPAPSRLapailPDEPVGEPvhprmltwirgLEELasddagDPPPP 2554

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  599 SDQAKPTQAEEKQNQPS--VQKPTTDTVPTSAA-PGVKQDLADPRPPLTQQKVTDSPKPETTKPPADTHPagDKPDSKPL 675
Cdd:PHA03247  2555 LPPAAPPAAPDRSVPPPrpAPRPSEPAVTSRARrPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAP--DPPPPSPS 2632

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  676 PQVSRQKSDPKLASQSGSKSDaktqKAVEPAQVRdDPKKLQTKSAPKPDTKPaPKGPQAGTGPKPM-SAQPAPQPQQPQK 754
Cdd:PHA03247  2633 PAANEPDPHPPPTVPPPERPR----DDPAPGRVS-RPRRARRLGRAAQASSP-PQRPRRRAARPTVgSLTSLADPPPPPP 2706

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  755 TPEqsrrfslnlggitdvPKPQPTTPQETVTGKLFGFGASIFSQASSLISTAGQPGSQTSGPappaakqpqppsqPTASQ 834
Cdd:PHA03247  2707 TPE---------------PAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGG-------------PARPA 2758

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  835 APPKEATQAQPLPKAAPtkketkPLASEKLEPMAADSTLTtkgsdlEKKPSLAKDSKPQAAEAKKPAELSEQEKASQPKV 914
Cdd:PHA03247  2759 RPPTTAGPPAPAPPAAP------AAGPPRRLTRPAVASLS------ESRESLPSPWDPADPPAAVLAPAAALPPAASPAG 2826

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  915 SCPLCKTGLNIGSKDPPNFNTCTEckkvvcNLCGF----NPMPHIAEVQEWLCLNCQTQRAmsgqlgDMGKVPLPKLGPS 990
Cdd:PHA03247  2827 PLPPPTSAQPTAPPPPPGPPPPSL------PLGGSvapgGDVRRRPPSRSPAAKPAAPARP------PVRRLARPAVSRS 2894

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*...
gi 1201829585  991 -QPVSKPPATPQKQPVPAVSHSPQKTSTPPTPAATKPKEEPGVQKEVP 1037
Cdd:PHA03247  2895 tESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPP 2942
C2B_Synaptotagmin-12 cd08406
C2 domain second repeat present in Synaptotagmin 12; Synaptotagmin is a membrane-trafficking ...
 4722-4845 2.98e-09

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: 58.26  E-value: 2.98e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4722 GEIQLQINYDKHLGNLIIHILQARNLAPRDNNGYSDPFVKVYLLPGRGAEYKRRTKYVQKSLNPEWNQTVIYkNISTEQL 4801
Cdd:cd08406      2 GEILLSLSYLPTAERLTVVVVKARNLVWDNGKTTADPFVKVYLLQDGRKISKKKTSVKRDDTNPIFNEAMIF-SVPAIVL 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1201829585 4802 KKKTLEVTVWDYDRFSSNDFLGEVLI-------DLSSVSQLDNTPR-----WYPLK 4845
Cdd:cd08406     81 QDLSLRVTVAESTEDGKTPNVGHVIIgpaasgmGLSHWNQMLASLRkpvamWHPLR 136
PTZ00121 PTZ00121
MAEBL; Provisional
 1022-1643 3.94e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 63.62  E-value: 3.94e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 1022 AATKPKEEPGVQKEVPKLQQGKLEKTL-------SADKIQQGIQKEDAKSKQGKLFKTPSADKIQRvsQKEDSRLQQTKL 1094
Cdd:PTZ00121  1333 AAKKKAEEAKKAAEAAKAEAEAAADEAeaaeekaEAAEKKKEEAKKKADAAKKKAEEKKKADEAKK--KAEEDKKKADEL 1410

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 1095 TKTPSSDKilhgaQKEDAKFQESKLAKTSSADKilhgVQKEDIKVQEAKlAKIPSADKILHGVQK--EDPKLQQMKmAKA 1172
Cdd:PTZ00121  1411 KKAAAAKK-----KADEAKKKAEEKKKADEAKK----KAEEAKKADEAK-KKAEEAKKAEEAKKKaeEAKKADEAK-KKA 1479

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 1173 LSADKIQPAAQK-EDPQLQGVRLSKAVSADKIQHGIQKEDLNLQHVKTEKTSVEKIQEEAQKEELKLQQEKLSKTLSEDK 1251
Cdd:PTZ00121  1480 EEAKKADEAKKKaEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKK 1559

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 1252 IPATVSSDQKkpsRKFEEDK-----KPELLEKSTPHPEDKKEQITAETKDRVAEQKAEVEAPCDKLHEKKEEDVKKEGLT 1326
Cdd:PTZ00121  1560 AEEKKKAEEA---KKAEEDKnmalrKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVE 1636

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 1327 TgipqmvSKTEKAEEEKTPVQVSRLPRSDHVEAVREKMEKEDDKSDTSSSQQQKSPQGLSDTGYSSDgissslgeipshi 1406
Cdd:PTZ00121  1637 Q------LKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKE------------- 1697

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 1407 pSDEKDLTRESSKKdtisQESPPSPSDLAKLESTVLSILEAQASTLADEKSVKRKELHEAYSDQTKDQHKTKPLPVTPES 1486
Cdd:PTZ00121  1698 -AEEAKKAEELKKK----EAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEE 1772

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 1487 YSS----------DEEDLESIQEGERTIaADGKGGSSSrtdyKEEGGGDDTP---ARRQRYDS----VEDSSES---ENS 1546
Cdd:PTZ00121  1773 IRKekeavieeelDEEDEKRRMEVDKKI-KDIFDNFAN----IIEGGKEGNLvinDSKEMEDSaikeVADSKNMqleEAD 1847

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 1547 PVPRRKRRASVGSSSSDEYKQDDSQGSGDEEDFIrKQIIEmsADEDASGSEDD---EFIRNQLK----EISVTESQKKEE 1619
Cdd:PTZ00121  1848 AFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDE-EEIEE--ADEIEKIDKDDierEIPNNNMAgknnDIIDDKLDKDEY 1924

                          650       660
                   ....*....|....*....|....
gi 1201829585 1620 VKSKAKGTAGKHRRMARKSSAGYD 1643
Cdd:PTZ00121  1925 IKRDAEETREEIIKISKKDMCIND 1948
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 ...
 4537-4597 5.32e-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: 56.13  E-value: 5.32e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1201829585 4537 GNGLGIRVVGGKEIPgsSGEIGAYIAKVLPGGSAEQTGKLIEGMQVLEWNGIPLTGKTYEE 4597
Cdd:cd06759     11 GKGLGFSIVGGRDSP--RGPMGIYVKTIFPGGAAAEDGRLKEGDEILEVNGESLQGLTHQE 69
C2A_Synaptotagmin-14_16 cd08389
C2A domain first repeat present in Synaptotagmins 14 and 16; Synaptotagmin 14 and 16 are ...
 4722-4845 5.48e-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: 57.25  E-value: 5.48e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4722 GEIQLQINYDKHLGNLIIHILQARNLAPRDNNGYSDPFVKVYLLPGRgaEYKRRTKyVQKSLNPEWNQTVIYKNISTEQL 4801
Cdd:cd08389      3 GDLDVAFEYDPSARKLTVTVIRAQDIPTKDRGGASSWQVHLVLLPSK--KQRAKTK-VQRGPNPVFNETFTFSRVEPEEL 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1201829585 4802 KKKTLEVTVWDYDRFSSNDFLGEVLIDLSSVSQLDNTPRWYPLK 4845
Cdd:cd08389     80 NNMALRFRLYGVERMRKERLIGEKVVPLSQLNLEGETTVWLTLE 123
PDZ7_MUPP1-PD6_PATJ-like cd06671
PDZ domain 7 of multi-PDZ-domain protein 1 (MUPP1), PDZ domain 6 of PATJ (protein-associated ...
 4520-4602 6.79e-09

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: 56.17  E-value: 6.79e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4520 PHARLKLLRDPkdhtvsGNGLGIRVVGGKEI---PGSSGEI-GAYIAKVLPGGSAEQTGKLIEGMQVLEWNGIPLTGKTY 4595
Cdd:cd06671      1 PPRRVELWREP------GKSLGISIVGGRVMgsrLSNGEEIrGIFIKHVLEDSPAGRNGTLKTGDRILEVNGVDLRNATH 74


                   ....*..
gi 1201829585 4596 EEVQNII 4602
Cdd:cd06671     75 EEAVEAI 81
C2_NEDD4_NEDD4L cd04033
C2 domain present in the Human neural precursor cell-expressed, developmentally down-regulated ...
 4737-4861 1.16e-08

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: 56.59  E-value: 1.16e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4737 LIIHILQARNLAPRDNNGYSDPFVKVYLLPGRGAEY--KRRTKYVQKSLNPEWNQTVIYK-NISTEQLKkktLEvtVWDY 4813
Cdd:cd04033      2 LRVKVLAGIDLAKKDIFGASDPYVKISLYDPDGNGEidSVQTKTIKKTLNPKWNEEFFFRvNPREHRLL---FE--VFDE 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1201829585 4814 DRFSSNDFLGEVLIDLSS--VSQLDN----TPRWYPLKEQSEnidhgKSHSGQN 4861
Cdd:cd04033     77 NRLTRDDFLGQVEVPLNNlpTETPGNerryTFKDYLLRPRSS-----KSRVKGH 125
C2_PKC_alpha_gamma cd04026
C2 domain in Protein Kinase C (PKC) alpha and gamma; A single C2 domain is found in PKC alpha ...
 5026-5108 1.37e-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: 56.50  E-value: 1.37e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 5026 GEIKIalkkEMKTDGEQLIVEILQCRNITYKfkSPDHLPDLYVKLYVvnISTQKRVIKKKTRVCRHDREPSFNETFRFSL 5105
Cdd:cd04026      2 GRIYL----KISVKDNKLTVEVREAKNLIPM--DPNGLSDPYVKLKL--IPDPKNETKQKTKTIKKTLNPVWNETFTFDL 73


                   ...
gi 1201829585 5106 SPA 5108
Cdd:cd04026     74 KPA 76
C2A_Copine cd04048
C2 domain first repeat in Copine; There are 2 copies of the C2 domain present in copine, a ...
 4741-4859 1.37e-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: 56.04  E-value: 1.37e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4741 ILQARNLAPRDNNGYSDPFVKVYLLPGRGAEYKR--RTKYVQKSLNPEWNQTVI--YkNISTEQlkkkTLEVTVWDYD-- 4814
Cdd:cd04048      6 SISCRNLLDKDVLSKSDPFVVVYVKTGGSGQWVEigRTEVIKNNLNPDFVTTFTvdY-YFEEVQ----KLRFEVYDVDsk 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1201829585 4815 --RFSSNDFLGEVLIDLSS-VSQLDNTprwYPLKeqsenIDHGKSHSG 4859
Cdd:cd04048     81 skDLSDHDFLGEAECTLGEiVSSPGQK---LTLP-----LKGGKGKGT 120
C2_cPLA2 cd04036
C2 domain present in cytosolic PhosphoLipase A2 (cPLA2); A single copy of the C2 domain is ...
 4736-4833 1.45e-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: 55.73  E-value: 1.45e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4736 NLIIHILQARNLAPRDNNGYSDPFVKVYLlPGRGAEyKRRTKYVQKSLNPEWNQTVIYKnISTEQlkKKTLEVTVWDYDR 4815
Cdd:cd04036      1 LLTVRVLRATNITKGDLLSTPDCYVELWL-PTASDE-KKRTKTIKNSINPVWNETFEFR-IQSQV--KNVLELTVMDEDY 75

                           90
                   ....*....|....*...
gi 1201829585 4816 FSSnDFLGEVLIDLSSVS 4833
Cdd:cd04036     76 VMD-DHLGTVLFDVSKLK 92
C2_Kibra cd08680
C2 domain found in Human protein Kibra; Kibra is thought to be a regulator of the Salvador ...
 4724-4844 1.48e-08

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: 56.09  E-value: 1.48e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4724 IQLQINYDKHLGNLIIHILQARNLA---PRDNngySDPFVKVYLLPG-RGAEYKRRTKYVQKSLNPEWNqTVIYKNISTE 4799
Cdd:cd08680      3 VQIGLRYDSGDSSLVISVEQLRNLSalsIPEN---SKVYVRVALLPCsSSTSCLFRTKALEDQDKPVFN-EVFRVPISST 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1201829585 4800 QLKKKTLEVTVWDYDRFSSNDFLGEVLIDLSSVSQLDN-TPRWYPL 4844
Cdd:cd08680     79 KLYQKTLQVDVCSVGPDQQEECLGGAQISLADFESSEEmSTKWYNL 124
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 193-441 1.59e-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: 61.18  E-value: 1.59e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  193 PEEQRGLAKHPSQQQ---SPKLVQQQGPVKPTPQQT--ESSKPVPQQQQPGEPKQIQKPGPSHQGDSKVEQPKQPPQPRG 267
Cdd:pfam09606  220 GQQAQANGGMNPQQMggaPNQVAMQQQQPQQQGQQSqlGMGINQMQQMPQGVGGGAGQGGPGQPMGPPGQQPGAMPNVMS 299

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  268 PQKSQLQQSEPTKPVQQQtsakpsvgptkplpqqpdsaktssqaspptkpsSQQSGPVKQPSQ--QPARQGGPVKPSAQQ 345
Cdd:pfam09606  300 IGDQNNYQQQQTRQQQQQ---------------------------------QGGNHPAAHQQQmnQSVGQGGQVVALGGL 346

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  346 AGPPKQQPGSEKPsaQQTGPA--KQPLQTGPGKP----PLQQTGPVKQVPPQAGPTKPSSQTAGATKSVAQQPGLTKPPG 419
Cdd:pfam09606  347 NHLETWNPGNFGG--LGANPMqrGQPGMMSSPSPvpgqQVRQVTPNQFMRQSPQPSVPSPQGPGSQPPQSHPGGMIPSPA 424

                          250       260
                   ....*....|....*....|....
gi 1201829585  420 --PQSGPEkPSQQKQASAAQPVES 441
Cdd:pfam09606  425 liPSPSPQ-MSQQPAQQRTIGQDS 447
C2B_Synaptotagmin-15 cd08409
C2 domain second repeat present in Synaptotagmin 15; Synaptotagmin is a membrane-trafficking ...
 4721-4827 1.65e-08

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: 56.19  E-value: 1.65e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4721 TGEIQLQINYDKHLGNLIIHILQARNLAPRDNNGySDPFVKVYLLPGRGAEYKRRTKYVQKSLNPEWNQTVIYKnISTEQ 4800
Cdd:cd08409      1 LGDIQISLTYNPTLNRLTVVVLRARGLRQLDHAH-TSVYVKVSLMIHNKVVKTKKTEVVDGAASPSFNESFSFK-VTSRQ 78

                           90       100
                   ....*....|....*....|....*..
gi 1201829585 4801 LKKKTLEVTVWDYDRFSSNDFLGEVLI 4827
Cdd:cd08409     79 LDTASLSLSVMQSGGVRKSKLLGRVVL 105
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 182-460 2.06e-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: 60.55  E-value: 2.06e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  182 KQKVTQKDQGKPEEQRGLAKHPSQQQSPKLVQQQGPVKPTPQQTESsKPVPQQQQPGEPKQIQKPGPSHQGDSKVEQPKQ 261
Cdd:NF033839   276 KKGLTQDTPKEPGNKKPSAPKPGMQPSPQPEKKEVKPEPETPKPEV-KPQLEKPKPEVKPQPEKPKPEVKPQLETPKPEV 354

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  262 PPQPRGPQKSqlQQSEPTKPvqqqtsaKPSVGPtKPLPQQPDSAKTSSQASPPTKPSSQQSGPVKQPsqQPARQGGPVKP 341
Cdd:NF033839   355 KPQPEKPKPE--VKPQPEKP-------KPEVKP-QPETPKPEVKPQPEKPKPEVKPQPEKPKPEVKP--QPEKPKPEVKP 422

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  342 sAQQAGPPKQQPGSEKPSAQqtgPAKQPLQTGPGKPPLQQTgPVKQVPPQAGPTKPSSQTAGAT---KSVAQQPGLTKPP 418
Cdd:NF033839   423 -QPEKPKPEVKPQPEKPKPE---VKPQPEKPKPEVKPQPET-PKPEVKPQPEKPKPEVKPQPEKpkpDNSKPQADDKKPS 497

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1201829585  419 GPQSGPEKPSQQKQASAAQPVESTPKKTFCPLCTTTELLLHV 460
Cdd:NF033839   498 TPNNLSKDKQPSNQASTNEKATNKPKKSLPSTGSISNLALEI 539
C2_Munc13_fungal cd04043
C2 domain in Munc13 (mammalian uncoordinated) proteins; fungal group; C2-like domains are ...
 4739-4831 2.29e-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: 55.73  E-value: 2.29e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4739 IHILQARNLAPRDNNGYSDPFVKvyLLPGRGAEYKRRTKYVQKSLNPEWNQTViykNISTEQLKKKTLEVTVWDYDRFSS 4818
Cdd:cd04043      5 IRIVRAENLKADSSNGLSDPYVT--LVDTNGKRRIAKTRTIYDTLNPRWDEEF---ELEVPAGEPLWISATVWDRSFVGK 79

                           90
                   ....*....|...
gi 1201829585 4819 NDFLGEVLIDLSS 4831
Cdd:cd04043     80 HDLCGRASLKLDP 92
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
 199-438 3.75e-08

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 59.94  E-value: 3.75e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  199 LAKHPSQQQSPKlvqqqgpvkpTPQQTESSKPVPqqqqpgePKQIQKPGPSHQGDSKVEQPKQ-PPQPRGPQKSQLQQSE 277
Cdd:PLN03209   320 LAKIPSQRVPPK----------ESDAADGPKPVP-------TKPVTPEAPSPPIEEEPPQPKAvVPRPLSPYTAYEDLKP 382

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  278 PTKPVQQQTSAKPsvgptkPLPQQPDSAKTSSQASPPTKPSSQQSGPVKQPSQQPARQGGPVKPSAQQAG-PPKQQPGSE 356
Cdd:PLN03209   383 PTSPIPTPPSSSP------ASSKSVDAVAKPAEPDVVPSPGSASNVPEVEPAQVEAKKTRPLSPYARYEDlKPPTSPSPT 456

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  357 KPSAQQTGPAKQPLQTGPGKPPLQQTGPVKQVPPQAGPTKPSSQTAGATKSVAQQPGLTKPPGPQSGPEKPSQQKQASAA 436
Cdd:PLN03209   457 APTGVSPSVSSTSSVPAVPDTAPATAATDAAAPPPANMRPLSPYAVYDDLKPPTSPSPAAPVGKVAPSSTNEVVKVGNSA 536


                   ..
gi 1201829585  437 QP 438
Cdd:PLN03209   537 PP 538
PHA03378 PHA03378
EBNA-3B; Provisional
 175-740 3.78e-08

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 60.08  E-value: 3.78e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  175 AHEEAGRKQKVTQKDQGKPEeqrglakhpSQQQSPKLVQQQGPVKPTPQQTES----SKPVPQQQQPG----------EP 240
Cdd:PHA03378   425 AIEEEHRKKKAARTEQPRAT---------PHSQAPTVVLHRPPTQPLEGPTGPlsvqAPLEPWQPLPHpqvtpvilhqPP 495

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  241 KQ-IQKPGPS----HQGDSKVEQ-------PKQPPQPRGPQKS--------QLQQSEP--TKPVQQQTSAKPSVGPtkpL 298
Cdd:PHA03378   496 AQgVQAHGSMldllEKDDEDMEQrvmatllPPSPPQPRAGRRApcvytedlDIESDEPasTEPVHDQLLPAPGLGP---L 572

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  299 PQQPDSAKTSSQASPPTKPSSQQSGPVKQPSQQ---PARQGGPVKPSAQQAGPPKQQPGSEKPSAQQTGPAKQPLQTGPG 375
Cdd:PHA03378   573 QIQPLTSPTTSQLASSAPSYAQTPWPVPHPSQTpepPTTQSHIPETSAPRQWPMPLRPIPMRPLRMQPITFNVLVFPTPH 652

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  376 KPPLQQTGPVKQ--VPPQAGPTKPSSQTAGATKSVAQQPGLTKPPGPQSGPEKPsqqkqasaaqpvestpkktfcplctt 453
Cdd:PHA03378   653 QPPQVEITPYKPtwTQIGHIPYQPSPTGANTMLPIQWAPGTMQPPPRAPTPMRP-------------------------- 706

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  454 telllhvpekanyntctqchtvvcslcgfnpnphiteikewlclncqmqralggdlasghgpgPQLPPPKQKTPTPTSTA 533
Cdd:PHA03378   707 ---------------------------------------------------------------PAAPPGRAQRPAAATGR 723

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  534 KPSPQSQPG--QKKDASPKPDPSQQADSKKPVPQKKQPSmPGSPPvksKQTDAEPSDTFQ-QIDPTPksdQAKPTQAEEK 610
Cdd:PHA03378   724 ARPPAAAPGraRPPAAAPGRARPPAAAPGRARPPAAAPG-RARPP---AAAPGAPTPQPPpQAPPAP---QQRPRGAPTP 796

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  611 QNQPSVqKPTTDTVPTSAAPGVKqdlaDPRPPLTQQKVTDSPK---PETTKPPA--DTHPAGDKPD-------------- 671
Cdd:PHA03378   797 QPPPQA-GPTSMQLMPRAAPGQQ----GPTKQILRQLLTGGVKrgrPSLKKPAAleRQAAAGPTPSpgsgtsdkivqapv 871

                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1201829585  672 -----SKPLpQVSRQKSDPKLASQSgSKSDAKTQKAVEPAQVRD-DPKKLQTKSAPKPDTKPAPKGPQAGTGPKP 740
Cdd:PHA03378   872 fyppvLQPI-QVMRQLGSVRAAAAS-TVTQAPTEYTGERRGVGPmHPTDIPPSKRAKTDAYVESQPPHGGQSHSF 944
Glutenin_hmw pfam03157
High molecular weight glutenin subunit; Members of this family include high molecular weight ...
 209-740 4.00e-08

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: 59.96  E-value: 4.00e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  209 PKLVQQQGPVKPTPQQTESskpVPQQQQPGEPKQIQKPGPSHQG--DSKVEQPKQPPQ---------PRGPQKS-QLQQ- 275
Cdd:pfam03157  103 PALLQRYYPGVTSPQQVSY---YPGQASPQRPGQGQQPGQGQQWyyPTSPQQPGQWQQpgqgqqgyyPTSPQQSgQRQQp 179

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  276 SEPTKPVQQQTSAKPSVGPTKPLP---QQPDSAKTSSQASPPTKPSSQQSGPVKQPSQQPAR-QGGPVKPSAQQAGppKQ 351
Cdd:pfam03157  180 GQGQQLRQGQQGQQSGQGQPGYYPtssQQPGQLQQTGQGQQGQQPERGQQGQQPGQGQQPGQgQQGQQPGQPQQLG--QG 257

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  352 QPGSEKPSAQQTGPAKQPLQTGPGKPP--LQQTGpvkQVPPQAGPTKPSSQTAGATKSVAQQPGLTKPPGPQSGPEKPSQ 429
Cdd:pfam03157  258 QQGYYPISPQQPRQWQQSGQGQQGYYPtsLQQPG---QGQSGYYPTSQQQAGQLQQEQQLGQEQQDQQPGQGRQGQQPGQ 334

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  430 QKQ----ASAAQPVESTPKKTfcplcTTTELLLHVPEKANYNTCTQCHTVVCSLCGFNPNPHITEIKEWLCLNCQMQRAL 505
Cdd:pfam03157  335 GQQgqqpAQGQQPGQGQPGYY-----PTSPQQPGQGQPGYYPTSQQQPQQGQQPEQGQQGQQQGQGQQGQQPGQGQQPGQ 409

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  506 GgdlASGHGP-GPQLPPPKQKTPTPTSTAKPSPQSQPGQ-KKDASPKPDPSQQADSKKPVPQKKQPS---MPGSPPVKSK 580
Cdd:pfam03157  410 G---QPGYYPtSPQQSGQGQPGYYPTSPQQSGQGQQPGQgQQPGQEQPGQGQQPGQGQQGQQPGQPEqgqQPGQGQPGYY 486

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  581 QTDAEPSDTFQQIDPTPKSDQAKPTQAEEKQNQPSVQKPTTDtvPTS-AAPGVKQDLADPRPPLTQQKVTDSPKPETTKP 659
Cdd:pfam03157  487 PTSPQQSGQGQQLGQWQQQGQGQPGYYPTSPLQPGQGQPGYY--PTSpQQPGQGQQLGQLQQPTQGQQGQQSGQGQQGQQ 564

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  660 PADTHPA--------GDKPDSKPLPQVSRQKSDPKLASQSGSKSDAKTQKAVEPAQVRDDPKKLQTKSAPKPDTKPAPKg 731
Cdd:pfam03157  565 PGQGQQGqqpgqgqqGQQPGQGQQPGQGQPGYYPTSPQQSGQGQQPGQWQQPGQGQPGYYPTSSLQLGQGQQGYYPTSP- 643


                   ....*....
gi 1201829585  732 PQAGTGPKP 740
Cdd:pfam03157  644 QQPGQGQQP 652
C2A_SLP-4_5 cd04029
C2 domain first repeat present in Synaptotagmin-like proteins 4 and 5; All Slp members ...
 5026-5151 4.16e-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: 54.75  E-value: 4.16e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 5026 GEIKIALKKEMKTDGeqLIVEILQCRNITYKFKSpDHLPDLYVKLYVvnISTQKRVIKKKTRVCRHDREPSFNETFRFSL 5105
Cdd:cd04029      2 GEILFSLSYDYKTQS--LNVHVKECRNLAYGDEA-KKRSNPYVKTYL--LPDKSRQSKRKTSIKRNTTNPVYNETLKYSI 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1201829585 5106 SP---AGHSLQiLLVSNGGKFMKKTLIGEAYVWLDKVDLRKRIVNWHKL 5151
Cdd:cd04029     77 SHsqlETRTLQ-LSVWHYDRFGRNTFLGEVEIPLDSWNFDSQHEECLPL 124
PTZ00121 PTZ00121
MAEBL; Provisional
 1027-1735 6.27e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 59.77  E-value: 6.27e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 1027 KEEPGVQKEVPKLQQGKLEKtlsADKIQQGIQKEDAKSKQGKLFKTPSADKIQRVSQKEDSRLQQTKlTKTPSSDKILHG 1106
Cdd:PTZ00121  1094 EEAFGKAEEAKKTETGKAEE---ARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIA-RKAEDARKAEEA 1169

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 1107 AQKEDAKFQES-----------KLAKTSSADKILHGVQKEDI-KVQEAKLA----KIPSADKILHGVQKEDPKLQQMKMA 1170
Cdd:PTZ00121  1170 RKAEDAKKAEAarkaeevrkaeELRKAEDARKAEAARKAEEErKAEEARKAedakKAEAVKKAEEAKKDAEEAKKAEEER 1249

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 1171 KALSADKIQPAAQKEDPQLQG-VRLSKAVSADKIQHGIQKEDLNLQHVKTEKTSVEKIQ---EEAQK-EELKLQQEKLSK 1245
Cdd:PTZ00121  1250 NNEEIRKFEEARMAHFARRQAaIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKkkaEEAKKaDEAKKKAEEAKK 1329

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 1246 TLSEDKIPATvSSDQKKPSRKFEEDKKPELLEKSTPHPE-DKKEQITAETKDRVAEQKAEVEAPCDKLHEKKEEDVKKeg 1324
Cdd:PTZ00121  1330 KADAAKKKAE-EAKKAAEAAKAEAEAAADEAEAAEEKAEaAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKK-- 1406

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 1325 lTTGIPQMVSKTEKAEEEKTPVQVSRlpRSDHVEAVREKMEKEDD-KSDTSSSQQQKSPQGLSDTGYSSDGISSSLGEIP 1403
Cdd:PTZ00121  1407 -ADELKKAAAAKKKADEAKKKAEEKK--KADEAKKKAEEAKKADEaKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAK 1483

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 1404 ShipSDEKDLTRESSKKDT----ISQESPPSPSDLAKLESTvlsiLEAQASTLADEKSvKRKELHEAYSDQTKDQ----- 1474
Cdd:PTZ00121  1484 K---ADEAKKKAEEAKKKAdeakKAAEAKKKADEAKKAEEA----KKADEAKKAEEAK-KADEAKKAEEKKKADElkkae 1555

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 1475 --HKTKPLPVTPESYSSDEEDLESIQEGERTIAADGKGGSSSRTDYKEEGGGDDTPARRQRYDSVEdsSESENSPVPRRK 1552
Cdd:PTZ00121  1556 elKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIK--AEELKKAEEEKK 1633

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 1553 RRASVGSSSSDEYKQDDSQGSGDEEDFIRKQIIEMSADEDASGSEDdefIRNQLKEISVTESQ--KKEEVKSKAKGTAGK 1630
Cdd:PTZ00121  1634 KVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEE---AKKAEEDEKKAAEAlkKEAEEAKKAEELKKK 1710

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 1631 HRRMARKSSAGYDEDAGRRHSWHDDDDEtfDESPEPKYRETKSQDGEELAISGGGGLRRFKTIELNSTITSKYSETPEQQ 1710
Cdd:PTZ00121  1711 EAEEKKKAEELKKAEEENKIKAEEAKKE--AEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEE 1788

                          730       740
                   ....*....|....*....|....*
gi 1201829585 1711 kgilyfDEEPELEMESLTDSPEDRS 1735
Cdd:PTZ00121  1789 ------DEKRRMEVDKKIKDIFDNF 1807
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 217-780 6.98e-08

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 59.33  E-value: 6.98e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  217 PVKPTPQQTESSKPVPQQQQPGEPKqiqkPGPSHQGDSKVEQPKQ-PPQPRGPQKSQLQQSEPTKPVQQQTSAKPSVGPT 295
Cdd:PRK10263   339 PVTQTPPVASVDVPPAQPTVAWQPV----PGPQTGEPVIAPAPEGyPQQSQYAQPAVQYNEPLQQPVQPQQPYYAPAAEQ 414

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  296 KPlpQQPDSAKTSSQASPPTKPSSQQSGPVKQPSQQPARQGGPVKPSA-QQAGPPKQQPGSEKPSAQQTGPAKQPLQTGP 374
Cdd:PRK10263   415 PA--QQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQSTFAPQStYQTEQTYQQPAAQEPLYQQPQPVEQQPVVEP 492

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  375 gKPPLQQTGPVKqvPP-------QAGPTKPSSQTAGATKSV---AQQPGLTKPPGPQSGPEKPSQQKQASAAQPVESTPK 444
Cdd:PRK10263   493 -EPVVEETKPAR--PPlyyfeevEEKRAREREQLAAWYQPIpepVKEPEPIKSSLKAPSVAAVPPVEAAAAVSPLASGVK 569

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  445 KTfcPLCTTTELLLHVPekanyntctqchtVVCSLCGFNPNPHITEikewlclncqmqralggdlasghGPGPQLpppkq 524
Cdd:PRK10263   570 KA--TLATGAAATVAAP-------------VFSLANSGGPRPQVKE-----------------------GIGPQL----- 606

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  525 ktptptstAKPSPQSQPGQKKDASPKPD-PSQQADSKKPVPQKKQPSMPGSPPVK---------------SKQTDAEPSD 588
Cdd:PRK10263   607 --------PRPKRIRVPTRRELASYGIKlPSQRAAEEKAREAQRNQYDSGDQYNDdeidamqqdelarqfAQTQQQRYGE 678

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  589 TFQQIDPTPKSDQAKPTQAE-EKQNQPSVQKPTTDTVPTSAAP--------GVKQDLAD--PRPPLtqqkVTDSPKPETT 657
Cdd:PRK10263   679 QYQHDVPVNAEDADAAAEAElARQFAQTQQQRYSGEQPAGANPfslddfefSPMKALLDdgPHEPL----FTPIVEPVQQ 754

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  658 KPpadthpagDKPDSKPLPQVSRQKSDPKLASQSGSKSDAKTQKAVEPAQVRDDPKKLQTKSAPKPdTKPAPKGPQAGTG 737
Cdd:PRK10263   755 PQ--------QPVAPQQQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVA-PQPQYQQPQQPVA 825

                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....*..
gi 1201829585  738 PKPmsaqpapQ----PQQPQKTPEQSRRFSLNLGGITDVPKPQPTTP 780
Cdd:PRK10263   826 PQP-------QyqqpQQPVAPQPQDTLLHPLLMRNGDSRPLHKPTTP 865
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
 228-367 7.41e-08

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


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 55.43  E-value: 7.41e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  228 SKPVPQQQQPGEPKQIQKPGPSHQGDSKVEQPKQPPQPRGPQKSQLQ--QSEPTKPVQQQTSAKPSVGPTKPLPQQPDsa 305
Cdd:pfam15240   33 SEEEGQSQQGGQGPQGPPPGGFPPQPPASDDPPGPPPPGGPQQPPPQggKQKPQGPPPQGGPRPPPGKPQGPPPQGGN-- 110

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1201829585  306 ktssQASPPTKPSSQQsGPVKQPSQQPARQGGPVKPSAQQAGPPKQQPGSEKPSAQQTGPAK 367
Cdd:pfam15240  111 ----QQQGPPPPGKPQ-GPPPQGGGPPPQGGNQQGPPPPPPGNPQGPPQRPPQPGNPQGPPQ 167
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 230-443 8.88e-08

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 58.84  E-value: 8.88e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  230 PVPQQQQPGEPKQIQKPGPSHQGDskveQPKQPPQPRGPQKSQlQQSEPTKPVQQQTSAKPSVGPTKPLPQQPDSAKTSS 309
Cdd:PRK07764   590 PAPGAAGGEGPPAPASSGPPEEAA----RPAAPAAPAAPAAPA-PAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASD 664

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  310 QASP-PTKPSSQQSGPVKQPSQQPARQGGPVKPSAQQAGPPKQQPGSEKPSAQQTGPAKQPLQTGPGkpplqQTGPVKQV 388
Cdd:PRK07764   665 GGDGwPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAP-----SPAADDPV 739

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1201829585  389 PPqagPTKPSSQTAGATKSVAQQPGLTKPPGPQSGPEKPSQQKQASAAQPVESTP 443
Cdd:PRK07764   740 PL---PPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAP 791
PDZ1_FRMPD2-like cd23071
PDZ domain 1 of FERM and PDZ domain-containing protein 2 (FRMPD2), and related domains; PDZ ...
 4523-4608 1.55e-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: 1.55e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4523 RLKLLRDPKdhtvsgNGLGIRVVGGKEIpgSSGEIGAYIAKVLPGGSAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQNiI 4602
Cdd:cd23071      4 CVTLKRDPK------RGFGFVIVGGENT--GKLDLGIFIASIIPGGPAEKDGRIKPGGRLISLNNISLEGVTFNTAVK-I 74


                   ....*.
gi 1201829585 4603 IQQCGE 4608
Cdd:cd23071     75 LQNSPD 80
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 183-678 1.70e-07

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 58.16  E-value: 1.70e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  183 QKVTQKDQGK--PEEQRGLAKHPSQQQSPKlVQQQGPVKPTPQQTESSKPVPQQQQPgEPKQIQKPGPSHQGdskvEQPK 260
Cdd:PTZ00449   486 KKLIKKSKKKlaPIEEEDSDKHDEPPEGPE-ASGLPPKAPGDKEGEEGEHEDSKESD-EPKEGGKPGETKEG----EVGK 559

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  261 QPpqprGPQKSQlqqseptKPVQQQTSAKPSVGPTKPL-PQQPDSAKTSSQASPPTKPSSQQSGPVKQPSQQPARQGGPV 339
Cdd:PTZ00449   560 KP----GPAKEH-------KPSKIPTLSKKPEFPKDPKhPKDPEEPKKPKRPRSAQRPTRPKSPKLPELLDIPKSPKRPE 628

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  340 KPSAQQAGPPKQQPGS-EKPsaQQTGPAKQPLQTGPGKPPLQQTGPVK---QVPPQAGPTKPSSQTAGATKSVAQQPGLT 415
Cdd:PTZ00449   629 SPKSPKRPPPPQRPSSpERP--EGPKIIKSPKPPKSPKPPFDPKFKEKfydDYLDAAAKSKETKTTVVLDESFESILKET 706

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  416 KP--PGPQSGPEKPSQQKQASAAQPVESTPKKTFCPLCTTTELLLHVPEKANYNTCTQCHTvvcslcgfnPNPHIT--EI 491
Cdd:PTZ00449   707 LPetPGTPFTTPRPLPPKLPRDEEFPFEPIGDPDAEQPDDIEFFTPPEEERTFFHETPADT---------PLPDILaeEF 777

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  492 KEwlclncqmqralggdlasghgpgpqlpppkqktptptstakPSPQSQPGQKKDASPKPD-PSQQADSkkpvPQKKQPS 570
Cdd:PTZ00449   778 KE-----------------------------------------EDIHAETGEPDEAMKRPDsPSEHEDK----PPGDHPS 812

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  571 MPG----SPPVKSKQTDAEPSDTFQQIDPTPKSDQAKPTQA--------EEKQNQPSVQKPTTDTVPTSAapgvkqDLAD 638
Cdd:PTZ00449   813 LPKkrhrLDGLALSTTDLESDAGRIAKDASGKIVKLKRSKSfddlttveEAEEMGAEARKIVVDDDGTEA------DDED 886

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....
gi 1201829585  639 PRPPLTQQKVT---DSPKPETTKPPADTHPAG-DKPDSKPLPQV 678
Cdd:PTZ00449   887 THPPEEKHKSEvrrRRPPKKPSKPKKPSKPKKpKKPDSAFIPSI 930
PDZ3_MAGI-1_3-like cd06733
PDZ domain 3 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ...
 4538-4598 1.86e-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: 51.46  E-value: 1.86e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1201829585 4538 NGLGIRVVGGKEiPGSSGEIGAyiakVLPGGSAEQTGKLIEGMQVLEWNGIPLTGKTYEEV 4598
Cdd:cd06733     11 TGFGFRILGGTE-EGSQVSIGA----IVPGGAADLDGRLRTGDELLSVDGVNVVGASHHKV 66
PBP1 COG5180
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ...
 171-428 1.88e-07

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


Pssm-ID: 444064 [Multi-domain]  Cd Length: 548  Bit Score: 57.38  E-value: 1.88e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  171 DSDAAHEEAGRKQKVTQKD--QGKPEEQRGLAKHPSQQqspklVQQQGPVKPTPQQTESSKPVPQQQQPGE--PKQIQKP 246
Cdd:COG5180    190 DALKDSPEKLDRPKVEVKDeaQEEPPDLTGGADHPRPE-----AASSPKVDPPSTSEARSRPATVDAQPEMrpPADAKER 264

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  247 GPSHQGDSKVEQPKQPPQPRGPQKSQLQQSEPTKPVQQQTSAKPSVgPTKPLPQQPDSAKTSSQASPPTKPSSQqsgPVK 326
Cdd:COG5180    265 RRAAIGDTPAAEPPGLPVLEAGSEPQSDAPEAETARPIDVKGVASA-PPATRPVRPPGGARDPGTPRPGQPTER---PAG 340

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  327 QPsQQPARQGGPVKPSAQQAGPPKQQPG-SEKPSAQQTGPAKQPLQTGPGKPPLQQTGPVKQVPPQ--AGPTKPSSQTAG 403
Cdd:COG5180    341 VP-EAASDAGQPPSAYPPAEEAVPGKPLeQGAPRPGSSGGDGAPFQPPNGAPQPGLGRRGAPGPPMgaGDLVQAALDGGG 419

                          250       260
                   ....*....|....*....|....*..
gi 1201829585  404 ATKSVAQQP--GLTKPPGPQSGPEKPS 428
Cdd:COG5180    420 RETASLGGAagGAGQGPKADFVPGDAE 446
PHA03247 PHA03247
large tegument protein UL36; Provisional
 531-1044 1.94e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 58.03  E-value: 1.94e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  531 STAKPSPQSQPGQKKDASPKPDPSQQADS-------KKPVPQKKQPSMPGSPPVKSKQTdAEPSDTFQQIDPTPKSDQAK 603
Cdd:PHA03247  2490 FAAGAAPDPGGGGPPDPDAPPAPSRLAPAilpdepvGEPVHPRMLTWIRGLEELASDDA-GDPPPPLPPAAPPAAPDRSV 2568

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  604 PT-QAEEKQNQPSVQKpttdtvpTSAAPGVKQDLADPRPPLTQQKVTDSPKPETTKPPADTHPAGDKPDSKPLPQVSRQK 682
Cdd:PHA03247  2569 PPpRPAPRPSEPAVTS-------RARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPH 2641

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  683 SDPKLASQSGSKSDAKTQKAVEPAQVRDDPKKLQTKSAP---KPDTKPAPKGPQAGT------GPKPMSAQPAPQPQQPQ 753
Cdd:PHA03247  2642 PPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPqrpRRRAARPTVGSLTSLadppppPPTPEPAPHALVSATPL 2721

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  754 KTPEQSRRFSLNLGGITDVPKPQPTTPqetvtgklfgfgasifsqasSLISTAGQPGSQTSGPAPPAAKQPQPPSQPTAS 833
Cdd:PHA03247  2722 PPGPAAARQASPALPAAPAPPAVPAGP--------------------ATPGGPARPARPPTTAGPPAPAPPAAPAAGPPR 2781

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  834 QAPPKEATQAQPLPKAAPTKKETKPLASEKLEPMAADSTLTTKGSDLEKKPSLAKDSKPQAAEAKKPAELSEQEKASQPK 913
Cdd:PHA03247  2782 RLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGD 2861

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  914 VscplcktglnigSKDPPNFNTCTECKKvvcnlcgfNPMPHIAEVqewlclncqTQRAMSGQLGDMGKVPLPKLGPSQPV 993
Cdd:PHA03247  2862 V------------RRRPPSRSPAAKPAA--------PARPPVRRL---------ARPAVSRSTESFALPPDQPERPPQPQ 2912

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1201829585  994 SKPPATPQKQPVPAVSHSP----QKTSTPPTPAATKPKEEPGVQKEVPKLQQGKL 1044
Cdd:PHA03247  2913 APPPPQPQPQPPPPPQPQPppppPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGAL 2967
PDZ_Lin-7-like cd06796
PDZ domain of protein Lin-7 and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), ...
 4539-4614 2.30e-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: 51.28  E-value: 2.30e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1201829585 4539 GLGIRVVGGKEipgSSGEIgaYIAKVLPGGSAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQNIIIQQCGEAEICVR 4614
Cdd:cd06796     13 GLGFNVMGGKE---QNSPI--YISRIIPGGVADRHGGLKRGDQLLSVNGVSVEGEHHEKAVELLKAAQGSVKLVVR 83
C2B_RasA3 cd04010
C2 domain second repeat present in RAS p21 protein activator 3 (RasA3); RasA3 are members of ...
 4737-4859 2.34e-07

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: 53.17  E-value: 2.34e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4737 LIIHILQARNLAPrdNNGYSDPFVKVYLLPGRGAEYKRRTKYVQKSLNPEWNQTVI------------YKNISTEQLKKK 4804
Cdd:cd04010      2 LSVRVIECSDLAL--KNGTCDPYASVTLIYSNKKQDTKRTKVKKKTNNPQFDEAFYfdvtidsspekkQFEMPEEDAEKL 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1201829585 4805 TLEVTVWDYDRFSSNDFLGEVLIDLSSVSQLDNTPR-WYPLKEQSENIDHGKSHSG 4859
Cdd:cd04010     80 ELRVDLWHASMGGGDVFLGEVRIPLRGLDLQAGSHQaWYFLQPREEKSTPPGTRSS 135
PHA03378 PHA03378
EBNA-3B; Provisional
 187-414 2.34e-07

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 57.77  E-value: 2.34e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  187 QKDQGKPEEQRGLAKHPSQQQSPklvqQQGPVKPTPQQTESSKPVPQQQQPGEPKQIQKP--GPSHQGDSKVE------Q 258
Cdd:PHA03378   735 RPPAAAPGRARPPAAAPGRARPP----AAAPGRARPPAAAPGAPTPQPPPQAPPAPQQRPrgAPTPQPPPQAGptsmqlM 810

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  259 PKQPPQPRGPQKSQLQQ--------SEPTKPVQQQTSAKPSVGPTkPLPQQPDSAKTSSqaSPPTKPssqqsgPVKQPSQ 330
Cdd:PHA03378   811 PRAAPGQQGPTKQILRQlltggvkrGRPSLKKPAALERQAAAGPT-PSPGSGTSDKIVQ--APVFYP------PVLQPIQ 881

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  331 QPaRQGGPVKPSAQQAGPpkqQPGSEKPSAQQTGPAKQPLQTGPGKPPLQQTGPVKQvPPQAGPTkPSSQTAGATKSVAQ 410
Cdd:PHA03378   882 VM-RQLGSVRAAAASTVT---QAPTEYTGERRGVGPMHPTDIPPSKRAKTDAYVESQ-PPHGGQS-HSFSVIWENVSQGQ 955


                   ....
gi 1201829585  411 QPGL 414
Cdd:PHA03378   956 QQTL 959
C2A_Synaptotagmin-15-17 cd08390
C2A domain first repeat present in Synaptotagmins 15 and 17; Synaptotagmin is a ...
 5035-5151 2.42e-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: 52.64  E-value: 2.42e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 5035 EMKTDGEQLIVEILQCRNITYKFKSPDHlPDLYVKLYVvnISTQKRVikKKTRVCRHDREPSFNETFRFSLSPA---GHS 5111
Cdd:cd08390      8 QYDLEEEQLTVSLIKARNLPPRTKDVAH-CDPFVKVCL--LPDERRS--LQSKVKRKTQNPNFDETFVFQVSFKelqRRT 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1201829585 5112 LQILLVSNgGKFMKKTLIGEAYVWLDKVDLRKRIVNWHKL 5151
Cdd:cd08390     83 LRLSVYDV-DRFSRHCIIGHVLFPLKDLDLVKGGVVWRDL 121
C2_PSD cd04039
C2 domain present in Phosphatidylserine decarboxylase (PSD); PSD is involved in the ...
 4735-4839 2.97e-07

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: 51.87  E-value: 2.97e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4735 GNLIIHILQARNLAPRDN---NGYS-DPFV------KVYllpgrgaeykrRTKYVQKSLNPEWNQTVIYKNISTEqlKKK 4804
Cdd:cd04039      1 GVVFMEIKSITDLPPLKNmtrTGFDmDPFViisfgrRVF-----------RTSWRRHTLNPVFNERLAFEVYPHE--KNF 67

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1201829585 4805 TLEVTVWDYDRFSSNDFLGEVLIDLSSVSQLDNTP 4839
Cdd:cd04039     68 DIQFKVLDKDKFSFNDYVATGSLSVQELLNAAPQP 102
C2_putative_Elicitor-responsive_gene cd04049
C2 domain present in the putative elicitor-responsive gene; In plants elicitor-responsive ...
 4735-4851 3.71e-07

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: 51.95  E-value: 3.71e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4735 GNLIIHILQARNLAPRDNNGYSDPFVkvyLLPGRGAEYKRRtkyVQKSL--NPEWNQTVIYkNISTEQLKKKT-LEVTVW 4811
Cdd:cd04049      1 GTLEVLLISAKGLQDTDFLGKIDPYV---IIQCRTQERKSK---VAKGDgrNPEWNEKFKF-TVEYPGWGGDTkLILRIM 73

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1201829585 4812 DYDRFSSNDFLGEVLIDLSSVSQLDNTPRWYPLKEQSENI 4851
Cdd:cd04049     74 DKDNFSDDDFIGEATIHLKGLFEEGVEPGTAELVPAKYNV 113
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 147-441 3.77e-07

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 57.10  E-value: 3.77e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  147 LSEANPLSAVTSVVNKFNPFDLISDSD-----------AAHEEAGRKQKVTQKDQGKPEEQRGLAKHPSQQQSPKLVQQQ 215
Cdd:PHA03307    14 AAEGGEFFPRPPATPGDAADDLLSGSQgqlvsdsaelaAVTVVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLS 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  216 GPVKPTPQQTESSKPVPQQQQPGEPKQIQKPGPSHQGDSKVEQPKQPPQPRGPQKSQLQQSEPTKPVQQQTSAKPSVGPT 295
Cdd:PHA03307    94 TLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAA 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  296 KPLPQQPDSAKTSSQASPPTKPSSQQSG------PVKQPSQQPARQGGPVKPSAQQAGPPKQQPGSEKPSAQQTGPAkqP 369
Cdd:PHA03307   174 LPLSSPEETARAPSSPPAEPPPSTPPAAasprppRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWG--P 251

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1201829585  370 LQTGPGKPPlqQTGPVKQVPPQAGPTKPSSQTAGATKSVAQQPGLTKPPGP--QSGPEKPSQQKQASAAQPVES 441
Cdd:PHA03307   252 ENECPLPRP--APITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPssPGSGPAPSSPRASSSSSSSRE 323
PDZ2_MUPP1-like cd06667
PDZ domain 2 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ...
 4537-4607 3.91e-07

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: 50.74  E-value: 3.91e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1201829585 4537 GNGLGIRVVGGKeipgSSGEIgayIAKVLPGGSAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQNiIIQQCG 4607
Cdd:cd06667      9 GSGLGFGIVGGK----STGVV---VKTILPGGVADRDGRLRSGDHILQIGDTNLRGMGSEQVAQ-VLRQCG 71
C2B_Synaptotagmin-7 cd08405
C2 domain second repeat present in Synaptotagmin 7; Synaptotagmin is a membrane-trafficking ...
 5043-5151 4.24e-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: 52.42  E-value: 4.24e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 5043 LIVEILQCRNItyKFKSPDHLPDLYVKLYVvnISTQKRVIKKKTRVCRHDREPSFNETFRFSLsPAgHSLQ----ILLVS 5118
Cdd:cd08405     17 ITVNIIKARNL--KAMDINGTSDPYVKVWL--MYKDKRVEKKKTVIKKRTLNPVFNESFIFNI-PL-ERLRettlIITVM 90

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1201829585 5119 NGGKFMKKTLIGEAYV-----------WLDKV-DLRKRIVNWHKL 5151
Cdd:cd08405     91 DKDRLSRNDLIGKIYLgwksgglelkhWKDMLsKPRQPVAQWHRL 135
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
 4531-4602 5.67e-07

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


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 49.97  E-value: 5.67e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1201829585 4531 KDHTVSGNGLGIRVVGGkeipGSSGEIGAYIAKVLPGGSAEQTGkLIEGMQVLEWNGIPLTGKTYEEVQNII 4602
Cdd:pfam00595    3 TLEKDGRGGLGFSLKGG----SDQGDPGIFVSEVLPGGAAEAGG-LKVGDRILSINGQDVENMTHEEAVLAL 69
C2C_Tricalbin-like cd04045
C2 domain third repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are ...
 4735-4859 6.41e-07

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: 51.05  E-value: 6.41e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4735 GNLIIHILQARNLAPRDNNGYSDPFVKVyLLPGRgaeYKRRTKYVQKSLNPEWNQtVIYKNISTEqlkKKTLEVTVWDYD 4814
Cdd:cd04045      1 GVLRLHIRKANDLKNLEGVGKIDPYVRV-LVNGI---VKGRTVTISNTLNPVWDE-VLYVPVTSP---NQKITLEVMDYE 72

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1201829585 4815 RFSSNDFLGEVLIDLSSVSQLDNTPRWYP---LKEQSENIDHGKSHSG 4859
Cdd:cd04045     73 KVGKDRSLGSVEINVSDLIKKNEDGKYVEyddEEERLKRLLSLKGVKG 120
PDZ1_ZO1-like cd06727
PDZ domain 1 of Zonula Occludens-1 (ZO-1), homologs ZO-2 and ZO-3, and related domains; PDZ ...
 4533-4614 6.89e-07

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: 49.96  E-value: 6.89e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4533 HTV-----SGNGLGIRVVGGKEIPG-SSGEIGAYIAKVLPGGSAEqtGKLIEGMQVLEWNGIPLTGKTYEE-VQniIIQQ 4605
Cdd:cd06727      1 HTVtlhraPGFGFGIAVSGGRDNPHfQSGDTSIVISDVLKGGPAE--GKLQENDRVVSVNGVSMENVEHSFaVQ--ILRK 76

                           90
                   ....*....|
gi 1201829585 4606 CG-EAEICVR 4614
Cdd:cd06727     77 CGkTANITVK 86
PDZ4_Scribble-like cd06701
PDZ domain 4 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 4537-4601 8.81e-07

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: 50.30  E-value: 8.81e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1201829585 4537 GNGLGIRVVGGkeIPGSSG------EIGAYIAKVLPGGSAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQNI 4601
Cdd:cd06701     14 GEKLGISIRGG--AKGHAGnpldptDEGIFISKINPDGAAARDGRLKVGQRILEVNGQSLLGATHQEAVRI 82
PDZ2_DLG5-like cd06765
PDZ domain 2 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density ...
 4542-4617 1.00e-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: 49.27  E-value: 1.00e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1201829585 4542 IRVVGGKEiPGSSGEIGAYIAKVLPGGSAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQNiIIQQCGEaeiCVRLDL 4617
Cdd:cd06765      2 INLSGQKD-SGISLENGVFISRIVPGSPAAKEGSLTVGDRIIAINGIALDNKSLSECEA-LLRSCRD---SLSLSL 72
PDZ13_MUPP1-like cd06676
PDZ domain 13 of multi-PDZ-domain protein 1 (MUPP1) and related domains; PDZ (PSD-95 ...
 4539-4613 1.04e-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: 49.65  E-value: 1.04e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1201829585 4539 GLGIRVVGGKEIPgsSGEIGAYIAKVLPGGSAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQNIIIQQCGEAEICV 4613
Cdd:cd06676     10 GLGFSIVGGFGSP--HGDLPIYVKTVFEKGAAAEDGRLKRGDQILAVNGESLEGVTHEEAVNILKKTKGTVTLTV 82
PDZ2_Par3-like cd23058
PDZ domain 2 of partitioning defective 3 (Par3), and related domains; PDZ (PSD-95 ...
 4538-4598 1.27e-06

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: 49.56  E-value: 1.27e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1201829585 4538 NGLGIRVVGGKEIPGSSGEIgaYIAKVLPGGSAEQTGKLIEGMQVLEWNGIPLTGKTYEEV 4598
Cdd:cd23058     15 EGLGFSITSRDNPTGGSGPI--YIKNILPKGAAIQDGRLKAGDRLLEVNGVDVTGKTQEEV 73
PDZ3_Dlg1-2-4-like cd06795
PDZ domain 3 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg) ...
 4537-4597 1.37e-06

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: 49.28  E-value: 1.37e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1201829585 4537 GNGLGIRVVGGKEipgssGEiGAYIAKVLPGGSAEQTGKLIEGMQVLEWNGIPLTGKTYEE 4597
Cdd:cd06795     11 STGLGFNIVGGED-----GE-GIFISFILAGGPADLSGELRRGDQILSVNGVDLRNATHEQ 65
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 514-789 1.45e-06

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 55.08  E-value: 1.45e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  514 GPGPQLPPPKQKTPTPTSTAKPSPQSQPGQKKDASPKPDPSQQADSKKPVPQKKQPsmPGSPPVKSKQTDAePSDTFQQI 593
Cdd:PTZ00449   513 GPEASGLPPKAPGDKEGEEGEHEDSKESDEPKEGGKPGETKEGEVGKKPGPAKEHK--PSKIPTLSKKPEF-PKDPKHPK 589

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  594 DPTPKSDQAKPTQAEEKQNQPSVQKPTTDTVPTSaaPGVKQDLADPRPPLTQQKVTDSPKPETTKPPADTHPagdkPDSK 673
Cdd:PTZ00449   590 DPEEPKKPKRPRSAQRPTRPKSPKLPELLDIPKS--PKRPESPKSPKRPPPPQRPSSPERPEGPKIIKSPKP----PKSP 663

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  674 PLPqvsrqkSDPKLASQ---SGSKSDAKTQKAVEPAQVRDDPKKLQTKSAPK----PDTKPAPKGPQAGTGPkpmSAQPA 746
Cdd:PTZ00449   664 KPP------FDPKFKEKfydDYLDAAAKSKETKTTVVLDESFESILKETLPEtpgtPFTTPRPLPPKLPRDE---EFPFE 734

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1201829585  747 PQPQQPQKTPEQSRRFSLNLGGITDVPKPQPTTPQETVTGKLF 789
Cdd:PTZ00449   735 PIGDPDAEQPDDIEFFTPPEEERTFFHETPADTPLPDILAEEF 777
PRK10927 PRK10927
cell division protein FtsN;
126-376 1.78e-06

cell division protein FtsN;


Pssm-ID: 236797 [Multi-domain]  Cd Length: 319  Bit Score: 53.53  E-value: 1.78e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  126 RESKSRTDFKEDQKPSMMPSFLSEAnplSAVtsVVNKFNPFDLISDSDAAHEEAGRKQKVTQKD-QGKPEEQ-RGLAKHP 203
Cdd:PRK10927    16 RRKKSTSRKKQRNLPAVSPAMVAIA---AAV--LVTFIGGLYFITHHKKEESETLQSQKVTGNGlPPKPEERwRYIKELE 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  204 SQQ---QSPKLVQQQGPVKPTPQQTESSKPVPQQQQPG---EPKQIQKPGPSHQGDSKVEQPKQppqprgpQKSQLQQSE 277
Cdd:PRK10927    91 SRQpgvRAPTEPSAGGEVKTPEQLTPEQRQLLEQMQADmrqQPTQLVEVPWNEQTPEQRQQTLQ-------RQRQAQQLA 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  278 PTKPVQQQ--TSAKPSVGPTKPLPQQPdsakTSSQASPPTKPSSQQsgPVKQPSQQPARQGGpvKPSAQQAGPPKQQPGS 355
Cdd:PRK10927   164 EQQRLAQQsrTTEQSWQQQTRTSQAAP----VQAQPRQSKPASTQQ--PYQDLLQTPAHTTA--QSKPQQAAPVTRAADA 235

                          250       260
                   ....*....|....*....|.
gi 1201829585  356 EKPSAQQTGPAKQPLQTGPGK 376
Cdd:PRK10927   236 PKPTAEKKDERRWMVQCGSFR 256
C2_PLC_like cd00275
C2 domain present in Phosphoinositide-specific phospholipases C (PLC); PLCs are involved in ...
 4736-4834 1.87e-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: 1.87e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4736 NLIIHILQARNL--APRDNNGYSDPFVKVYLL-PGRGAEYKRRTKYVQK-SLNPEWNQT----VIYKNISteqlkkkTLE 4807
Cdd:cd00275      3 TLTIKIISGQQLpkPKGDKGSIVDPYVEVEIHgLPADDSAKFKTKVVKNnGFNPVWNETfefdVTVPELA-------FLR 75

                           90       100
                   ....*....|....*....|....*..
gi 1201829585 4808 VTVWDYDRFsSNDFLGEVLIDLSSVSQ 4834
Cdd:cd00275     76 FVVYDEDSG-DDDFLGQACLPLDSLRQ 101
PDZ_MPP-like cd06726
PDZ domain of membrane palmitoylated proteins (MPPs), and related domains; PDZ (PSD-95 ...
 4539-4607 1.87e-06

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: 48.80  E-value: 1.87e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1201829585 4539 GLGIRVVGGKEIpgssgeigayIAKVLPGGSAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQNIIIQQCG 4607
Cdd:cd06726     14 GATIKMEEDSVI----------VARILHGGMAHRSGLLHVGDEILEINGIPVSGKTVDELQKLLSSLSG 72
PDZ3_Scribble-like cd06702
PDZ domain 3 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 4533-4614 1.90e-06

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: 48.79  E-value: 1.90e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4533 HTVSGNG-LGIRVVGGKE---IPGSSGEIGAYIAKVLPGGSAEQTGKLIeGMQVLEWNGIPLTGKTYEEVQNIIIQQCGE 4608
Cdd:cd06702      4 HLVKAGGpLGLSIVGGSDhssHPFGVDEPGIFISKVIPDGAAAKSGLRI-GDRILSVNGKDLRHATHQEAVSALLSPGQE 82


                   ....*.
gi 1201829585 4609 AEICVR 4614
Cdd:cd06702     83 IKLLVR 88
PDZ_SYNJ2BP-like cd06709
PDZ domain of synaptojanin-2-binding protein (SYNJ2BP), and related domains; PDZ (PSD-95 ...
 4537-4601 1.94e-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: 48.83  E-value: 1.94e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1201829585 4537 GNGLGIRVVGGKEIPGSSGEIGAYIAKVLPGGSAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQNI 4601
Cdd:cd06709      9 PSGLGFNIVGGTDQPYIPNDSGIYVAKIKEDGAAAIDGRLQEGDKILEINGQSLENLTHQDAVEL 73
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 171-322 2.10e-06

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 54.71  E-value: 2.10e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  171 DSDAAHEEAGRKQKVTQKDQGKPEEQRGlaKHPSQ----QQSP-KLVQQQGPVKP--TPQQTESSKPVPQQQQPGEPKQI 243
Cdd:PRK10263   691 ADAAAEAELARQFAQTQQQRYSGEQPAG--ANPFSlddfEFSPmKALLDDGPHEPlfTPIVEPVQQPQQPVAPQQQYQQP 768

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  244 QKPGPSHQGDSKVEQPKQPP----QPRGPQKSQLQQSEPTKPVQQQTSAKPSVGPTKPLPQQpdsaktsSQASPPTKPSS 319
Cdd:PRK10263   769 QQPVAPQPQYQQPQQPVAPQpqyqQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQY-------QQPQQPVAPQP 841


                   ...
gi 1201829585  320 QQS 322
Cdd:PRK10263   842 QDT 844
C2B_Copine cd04047
C2 domain second repeat in Copine; There are 2 copies of the C2 domain present in copine, a ...
 4742-4825 2.60e-06

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: 49.10  E-value: 2.60e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4742 LQARNLAPRDNNGYSDPFVKVYLLPGRGAE---YkrRTKYVQKSLNPEWNQTviykNISTEQL----KKKTLEVTVWDYD 4814
Cdd:cd04047      7 FSGKKLDKKDFFGKSDPFLEISRQSEDGTWvlvY--RTEVIKNTLNPVWKPF----TIPLQKLcngdYDRPIKIEVYDYD 80

                           90
                   ....*....|.
gi 1201829585 4815 RFSSNDFLGEV 4825
Cdd:cd04047     81 SSGKHDLIGEF 91
PDZ1_PTPN13_FRMPD2-like cd06694
PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13),FERM and PDZ ...
 4523-4608 2.73e-06

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: 48.55  E-value: 2.73e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4523 RLKLLRDPKdhtvsgNGLGIRVVGGkEIPGSSgEIGAYIAKVLPGGSAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQNiI 4602
Cdd:cd06694      4 IVTLKKDPQ------KGLGFTIVGG-ENSGSL-DLGIFVKSIIPGGPADKDGRIKPGDRIIAINGQSLEGKTHHAAVE-I 74


                   ....*.
gi 1201829585 4603 IQQCGE 4608
Cdd:cd06694     75 IQNAPD 80
PRK14949 PRK14949
DNA polymerase III subunits gamma and tau; Provisional
 555-712 2.80e-06

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237863 [Multi-domain]  Cd Length: 944  Bit Score: 53.96  E-value: 2.80e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  555 QQADSKKPVPQKKqpsmPGSPPvKSKQTDAEPSDTfQQIDPTPKSDQAKPTQAEEKQNQPSVqKPTTDTVPTSAAPGVKQ 634
Cdd:PRK14949   632 KEGDGKKSSADRK----PKTPP-SRAPPASLSKPA-SSPDASQTSASFDLDPDFELATHQSV-PEAALASGSAPAPPPVP 704

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1201829585  635 DLADpRPPLTQQKVTDSPKPETTKPPADTHPAGDKPDSKPLPQVSRQKSDPKLASQSGSKSDAKTQKAVEPAQVRDDP 712
Cdd:PRK14949   705 DPYD-RPPWEEAPEVASANDGPNNAAEGNLSESVEDASNSELQAVEQQATHQPQVQAEAQSPASTTALTQTSSEVQDT 781
C2C_Ferlin cd04018
C2 domain third repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and ...
 4750-4834 3.06e-06

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: 50.32  E-value: 3.06e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4750 RDNNGYSDPFVKVYLlpgrgAEYKRRTKYVQKSLNPEWNQTVIYknisTEQLKK--KTLEVTVWDYDRFSSNDFLGEVLI 4827
Cdd:cd04018     29 GEKKELVDPYVEVSF-----AGQKVKTSVKKNSYNPEWNEQIVF----PEMFPPlcERIKIQIRDWDRVGNDDVIGTHFI 99


                   ....*..
gi 1201829585 4828 DLSSVSQ 4834
Cdd:cd04018    100 DLSKISN 106
PDZ12_MUPP1-like cd06675
PDZ domain 12 of multi-PDZ-domain protein 1 (MUPP1), PDZ domain 10 of protein-associated tight ...
 4526-4613 3.42e-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: 48.13  E-value: 3.42e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4526 LLRDPKDhtvsgnGLGIRVVGGKeipGSS-GEIGAYIAKVLPGGSAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQNIIIQ 4604
Cdd:cd06675      5 IKRGPQD------SLGISIAGGV---GSPlGDVPVFIAMIQPNGVAAQTGKLKVGDRIVSINGQSTDGLTHSEAVNLLKN 75


                   ....*....
gi 1201829585 4605 QCGEAEICV 4613
Cdd:cd06675     76 ASGTIILQV 84
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 162-299 3.42e-06

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 53.94  E-value: 3.42e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  162 KFNPFDLISDsDAAHE---------EAGRKQKVTQKDQGKPEEQRglAKHPSQQQSPklvqqQGPVKPTPQQTESSKPVP 232
Cdd:PRK10263   728 EFSPMKALLD-DGPHEplftpivepVQQPQQPVAPQQQYQQPQQP--VAPQPQYQQP-----QQPVAPQPQYQQPQQPVA 799

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1201829585  233 QQQQPGEPKQIQKPGPSHQgdskveqpkQPPQPRGPQKSQLQQSEPTKPVQQQT----------SAKPSVGPTKPLP 299
Cdd:PRK10263   800 PQPQYQQPQQPVAPQPQYQ---------QPQQPVAPQPQYQQPQQPVAPQPQDTllhpllmrngDSRPLHKPTTPLP 867
C2A_SLP-3 cd08392
C2 domain first repeat present in Synaptotagmin-like protein 3; All Slp members basically ...
 5025-5151 3.60e-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: 49.44  E-value: 3.60e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 5025 MGEIKIALKKEMKTdgEQLIVEILQCRNITY-KFKSPDHLPdlYVKLYVvnISTQKRVIKKKTRVCRHDREPSFNETFRF 5103
Cdd:cd08392      1 TGEIEFALHYNFRT--SCLEITIKACRNLAYgDEKKKKCHP--YVKVCL--LPDKSHNSKRKTAVKKGTVNPVFNETLKY 74

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1201829585 5104 SLSPAGHSLQILLVS--NGGKFMKKTLIGEAYVWLDKVDLRKRIV---NWHKL 5151
Cdd:cd08392     75 VVEADLLSSRQLQVSvwHSRTLKRRVFLGEVLIPLADWDFEDTDSqrfLWYPL 127
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 500-784 4.06e-06

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: 53.23  E-value: 4.06e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  500 QMQRALGGDLASGHGPGPQLPPPKQKTPTPTSTAKPSPQSQPGQKKDASPKPDPSQQADSKKP----------------- 562
Cdd:NF033839   142 KFEKDSSSSSSSGSSTKPETPQPENPEHQKPTTPAPDTKPSPQPEGKKPSVPDINQEKEKAKLavatymskilddiqkhh 221

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  563 ------------VPQKKQPSMPGSPPVKSKQTDAEPSDTFQQIDPTP-------KSDQAKPTQAEEKQNQPSVQKPTTDT 623
Cdd:NF033839   222 lqkekhrqivalIKELDELKKQALSEIDNVNTKVEIENTVHKIFADMdavvtkfKKGLTQDTPKEPGNKKPSAPKPGMQP 301

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  624 VPTSAAPGVKQDLADP----RPPLTQQKVTDSPKPETTKPPADTHPAGDKPDSKPLPQVSRQKSDPKLasqSGSKSDAKT 699
Cdd:NF033839   302 SPQPEKKEVKPEPETPkpevKPQLEKPKPEVKPQPEKPKPEVKPQLETPKPEVKPQPEKPKPEVKPQP---EKPKPEVKP 378

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  700 QKAVEPAQVRDDPkklqtkSAPKPDTKPAPKGPQAGTGPKPMSAQPAPQPQQPQKTPEQSRRfslnLGGITDVPKPQPTT 779
Cdd:NF033839   379 QPETPKPEVKPQP------EKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQ----PEKPKPEVKPQPEK 448


                   ....*
gi 1201829585  780 PQETV 784
Cdd:NF033839   449 PKPEV 453
PDZ_MPP3-MPP4-MPP7-like cd06799
PDZ domain of membrane palmitoylated proteins 3 (MPP3), MPP4, and MPP7, and related domains; ...
 4542-4607 4.28e-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: 47.62  E-value: 4.28e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1201829585 4542 IRVVGGKEIPGS-------SGEIgaYIAKVLPGGSAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQNIIIQQCG 4607
Cdd:cd06799      3 VRLVKNNEPLGAtikrdekTGAI--VVARIMRGGAADRSGLIHVGDELREVNGISVEGKDPEEVIQILANSQG 73
PDZ1_LNX1_2-like cd06677
PDZ domain 1 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ ...
 4540-4606 4.34e-06

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: 48.01  E-value: 4.34e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1201829585 4540 LGIRVVGGKEIPgssgEIGAYIAKVLPGGSAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQNIIIQQC 4606
Cdd:cd06677     17 LGISIVGGNDTP----LINIVIQEVYRDGVIARDGRLLPGDQILEVNGVDISNVTHSQARSVLRQPC 79
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 203-639 4.45e-06

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 53.45  E-value: 4.45e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  203 PSQQQSPKLVQQQGPVKPTPQQTESSKPVPQQQQPGEPKQIQKPGPSHQGDSKVEQPKQPPQPRgPQKSQLQQSEPTKPV 282
Cdd:PRK07764   365 PSASDDERGLLARLERLERRLGVAGGAGAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAA-PQPAPAPAPAPAPPS 443

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  283 QQQTSAKPSVGPTKPLPQQPDSAKTSSQASPPTKPSSQQSGPVKQPSQQPARQggPVKPSAQQAGPPKQQPGSE------ 356
Cdd:PRK07764   444 PAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAA--PAAPAAPAGADDAATLRERwpeila 521

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  357 -------------KPSAQQTGPAKQPLQTGPGKPPL------------------QQTGPVKQVPPQAGPTKPSSQTAGAT 405
Cdd:PRK07764   522 avpkrsrktwailLPEATVLGVRGDTLVLGFSTGGLarrfaspgnaevlvtalaEELGGDWQVEAVVGPAPGAAGGEGPP 601

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  406 KSVAQQPGLTKP-PGPQSGPEKPSQQKQASAAQPVESTPKKTFCPLCTTTELLLHVPEKANYNTCTQCHtvvcslcgfnp 484
Cdd:PRK07764   602 APASSGPPEEAArPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWP----------- 670

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  485 nphiteikewlclncqmqRALGGDLASGHGPGPQLPPPKQKTPTPTSTAKPSPQSQPGQKKDASPKPDPSQQADSKKPVP 564
Cdd:PRK07764   671 ------------------AKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPS 732

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1201829585  565 QKKQPSMPGSPPVKSKQTDAEPSDTFQQIDPTPKSDQAKPTQAEEKQNQPSVqkpttdTVPTSAAPGVKQDLADP 639
Cdd:PRK07764   733 PAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEE------MAEDDAPSMDDEDRRDA 801
C2B_Synaptotagmin-14_16 cd08408
C2 domain second repeat present in Synaptotagmins 14 and 16; Synaptotagmin 14 and 16 are ...
 5043-5152 4.54e-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: 4.54e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 5043 LIVEILQCRNitYKFKSPDHLPDLYVKLYVVNiSTQKRVIKKKTRVCRHDREPSFNETFRFSLSPAGHSLQILLVS--NG 5120
Cdd:cd08408     17 LSVEVIKGSN--FKNLAMNKAPDTYVKLTLLN-SDGQEISKSKTSIRRGQPDPEFKETFVFQVALFQLSEVTLMFSvyNK 93

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1201829585 5121 GKFMKKTLIG------------EAYVWLDKVDLR-KRIVNWHKLL 5152
Cdd:cd08408     94 RKMKRKEMIGwfslglnssgeeEEEHWNEMKESKgQQVCRWHTLL 138
PDZ3_PTPN13_FRMPD2-like cd06695
PDZ domain 3 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), FERM and PDZ ...
 4536-4602 4.54e-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: 48.02  E-value: 4.54e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1201829585 4536 SGNGLGIRVVGGK-EIPGSSGEIGAYIAKVLPGGSAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQNII 4602
Cdd:cd06695      9 GSSGLGFSFLGGEnNSPEDPFSGLVRIKKLFPGQPAAESGLIQEGDVILAVNGEPLKGLSYQEVLSLL 76
PDZ_AFDN-like cd06789
PDZ domain of afadin (AFDN), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95) ...
 4537-4604 4.56e-06

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: 47.67  E-value: 4.56e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1201829585 4537 GNGLGIRVVGGKeipGS-SGEIGAYIAKVLPGGSAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQNIIIQ 4604
Cdd:cd06789     12 GNGMGLSIVAAK---GAgQDKLGIYIKSVVKGGAADLDGRLQAGDQLLSVDGHSLVGLSQERAAELMTK 77
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 259-676 4.58e-06

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 53.64  E-value: 4.58e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  259 PKQPPQPRGPQKSQLQQSEPTKPVQQQTSAkpsvgPTKPLPQQPDSAKTSSQASPPTKPSSQQSGPVKQPS--QQPARQG 336
Cdd:PHA03307    67 PPTGPPPGPGTEAPANESRSTPTWSLSTLA-----PASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPdlSEMLRPV 141

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  337 GPVKPSAQQAGPPKQQPGSEKPSAQQTGPakqplqtgpgkpplqQTGPVKQVPPQAGPTKPSSQtagatksvAQQPGLTK 416
Cdd:PHA03307   142 GSPGPPPAASPPAAGASPAAVASDAASSR---------------QAALPLSSPEETARAPSSPP--------AEPPPSTP 198

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  417 PPGPQSGPEKPSQQKQASAAQPVESTPKKTFCPLctttelllhvPEKANYNTCTQCHTVVCSLCGFNPNPHITEIKEwlc 496
Cdd:PHA03307   199 PAAASPRPPRRSSPISASASSPAPAPGRSAADDA----------GASSSDSSSSESSGCGWGPENECPLPRPAPITL--- 265

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  497 LNCQMQRALGGDLASGHGPGPQLPPPKQKTPTPTSTAKPSPQSQPGqkKDASPKPDPSQQADSKKPVPQKKQPSMPGSPP 576
Cdd:PHA03307   266 PTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSS--PRASSSSSSSRESSSSSTSSSSESSRGAAVSP 343

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  577 VKSKQTDAEPSDTFQQIDPTPKSDQAKPTQAEEKQNQPSVQKPTTDTVPTSAAPGVKQD----LADPRPPLTQQKVTDSP 652
Cdd:PHA03307   344 GPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDatgrFPAGRPRPSPLDAGAAS 423

                          410       420
                   ....*....|....*....|....*
gi 1201829585  653 KPETTKPPADThPAGDK-PDSKPLP 676
Cdd:PHA03307   424 GAFYARYPLLT-PSGEPwPGSPPPP 447
C2A_Synaptotagmin-1-5-6-9-10 cd08385
C2A domain first repeat present in Synaptotagmins 1, 5, 6, 9, and 10; Synaptotagmin is a ...
 5041-5152 4.59e-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: 4.59e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 5041 EQLIVEILQCRNitykfkspdhLP--------DLYVKLYVVNIStqkrviKKK--TRVCRHDREPSFNETFRFSLSPAGH 5110
Cdd:cd08385     16 NQLTVGIIQAAD----------LPamdmggtsDPYVKVYLLPDK------KKKfeTKVHRKTLNPVFNETFTFKVPYSEL 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1201829585 5111 SLQILLVS--NGGKFMKKTLIGEAYVWLDKVDLRKRIVNWHKLL 5152
Cdd:cd08385     80 GNKTLVFSvyDFDRFSKHDLIGEVRVPLLTVDLGHVTEEWRDLE 123
PHA03418 PHA03418
hypothetical E4 protein; Provisional
 278-421 5.04e-06

hypothetical E4 protein; Provisional


Pssm-ID: 177646 [Multi-domain]  Cd Length: 230  Bit Score: 51.28  E-value: 5.04e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  278 PTKPVQQQTSAK-PSVGPTKPLPQQPDSAKTSSQASPPTK-PSSQQSGPVKQPSQQPARQGGPVKPSAQQAGPPKQQPGS 355
Cdd:PHA03418    39 PHHPNPQEDPDKnPSPPPDPPLTPRPPAQPNGHNKPPVTKqPGGEGTEEDHQAPLAADADDDPRPGKRSKADEHGPAPGR 118

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1201829585  356 EKPSAQQTGPAKQPLQTGPGKPPlQQTGPVKQVPPQAGPTKPSSQTAGATKSVAQQPGLTKPPGPQ 421
Cdd:PHA03418   119 AALAPFKLDLDQDPLHGDPDPPP-GATGGQGEEPPEGGEESQPPLGEGEGAVEGHPPPLPPAPEPK 183
PDZ3_ZO1-like_domain cd06729
PDZ domain 3 of Zonula Occludens-1 (ZO-1), homologs ZO-2 and ZO-3, and related domains; PDZ ...
 4537-4598 5.20e-06

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: 47.56  E-value: 5.20e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1201829585 4537 GNGLGIRVVGGKEIpgssgeiGAYIAKVLPGGSAEQTGkLIEGMQVLEWNGIPLTGKTYEEV 4598
Cdd:cd06729     10 GGSVGLRLAGGNDV-------GIFVAGVQEGSPAEKQG-LQEGDQILKVNGVDFRNLTREEA 63
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 268-714 5.42e-06

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: 52.85  E-value: 5.42e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  268 PQKSQLQQSEPTKPVQQQTSAKPSVGPTKPLPQQPDSAKTSSQASPPTKPSSQQSGPVKQPSQQPARQGGPVKPSAQQAG 347
Cdd:NF033839   159 PETPQPENPEHQKPTTPAPDTKPSPQPEGKKPSVPDINQEKEKAKLAVATYMSKILDDIQKHHLQKEKHRQIVALIKELD 238

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  348 PPKQQPGSE----KPSAQQTGPAKQPLQTGPGKPPLQQTGPVKQVPPQAGPTKPSsqtagatksvAQQPGLTKPPGPQSG 423
Cdd:NF033839   239 ELKKQALSEidnvNTKVEIENTVHKIFADMDAVVTKFKKGLTQDTPKEPGNKKPS----------APKPGMQPSPQPEKK 308

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  424 PEKPSQQKQASAAQPVESTPKKTFCPlctttelllhVPEKanyntctqchtvvcslcgfnPNPHITeikewlclncqmqr 503
Cdd:NF033839   309 EVKPEPETPKPEVKPQLEKPKPEVKP----------QPEK--------------------PKPEVK-------------- 344

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  504 alggdlasghgpgPQLPPPKQKTPTPTSTAKPSPQSQPgQKKDASPKPDPSQQADSKKPVPQKKQPSMPGSPPVKSKQTD 583
Cdd:NF033839   345 -------------PQLETPKPEVKPQPEKPKPEVKPQP-EKPKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEKPKPEVK 410

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  584 AEPSDtfqqidPTPKSDQAKPTQAEEKQNQPSVQKPTTDTVPTSAAPGVKQDLADPRPPLtqqkvtdSPKPETTKPPADT 663
Cdd:NF033839   411 PQPEK------PKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPETPKPEV-------KPQPEKPKPEVKP 477

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1201829585  664 HPAGDKPD-SKPLPQVSRQKSDPKLasqsgSKSDAKTQKAVEPAQVRDDPKK 714
Cdd:NF033839   478 QPEKPKPDnSKPQADDKKPSTPNNL-----SKDKQPSNQASTNEKATNKPKK 524
Androgen_recep pfam02166
Androgen receptor;
243-349 6.82e-06

Androgen receptor;


Pssm-ID: 426632 [Multi-domain]  Cd Length: 501  Bit Score: 52.24  E-value: 6.82e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  243 IQKPGPSHQGDSKveqPKQPPQPRGPQKSQLQQSEPTKPVQQQTSAKPSVGPTKPlPQQPDSAKTSSQASPPTKPSSQQS 322
Cdd:pfam02166   29 IQNPGPRHPEAAG---GAAPPGARLQHQQQQQQQVPQQPQQQESSPRQPQASVQP-QQAGDDGSPPAHNRGPAGYLALED 104

                           90       100
                   ....*....|....*....|....*...
gi 1201829585  323 GPVKQPSQ-QPARQGGPVKPSAQQAGPP 349
Cdd:pfam02166  105 DEQPQPSQaQPAAECCPENGCVPEPGAA 132
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 176-456 7.66e-06

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 52.77  E-value: 7.66e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  176 HEEAGRKQKVTQKDQGKPEEQrglaKHPSQQQSPKLVQQQGPV---KPTPQQTESSKPvpqqQQPGEPKQIQKPgpshqg 252
Cdd:PTZ00449   526 DKEGEEGEHEDSKESDEPKEG----GKPGETKEGEVGKKPGPAkehKPSKIPTLSKKP----EFPKDPKHPKDP------ 591

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  253 dskvEQPKQPPQPRGPQKSqlqqSEPTKPVQQQTSAKPSVGPTKPLPQQPDSAKTSSQASPPTKPSSQQSGPVKQPSQQP 332
Cdd:PTZ00449   592 ----EEPKKPKRPRSAQRP----TRPKSPKLPELLDIPKSPKRPESPKSPKRPPPPQRPSSPERPEGPKIIKSPKPPKSP 663

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  333 ARqggPVKPS---------AQQAGPPKQQPGSEKPSAQQTGPAKQPLQTGPGKPPLQQtgpvKQVPPQAgPTKPSSQTAG 403
Cdd:PTZ00449   664 KP---PFDPKfkekfyddyLDAAAKSKETKTTVVLDESFESILKETLPETPGTPFTTP----RPLPPKL-PRDEEFPFEP 735

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1201829585  404 ATKSVAQQPGLTKPPGPqsgPEKPSQQkqasaaqpVESTPKKTFCPLCTTTEL 456
Cdd:PTZ00449   736 IGDPDAEQPDDIEFFTP---PEEERTF--------FHETPADTPLPDILAEEF 777
PDZ2_Dlg1-2-4-like cd06724
PDZ domain 2 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg) ...
 4524-4597 8.24e-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: 46.88  E-value: 8.24e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1201829585 4524 LKLLRDPKdhtvsgnGLGIRVVGGK---EIPGSSGeigAYIAKVLPGGSAEQTGKLIEGMQVLEWNGIPLTGKTYEE 4597
Cdd:cd06724      2 IKLVKGPK-------GLGFSIAGGVgnqHIPGDNG---IYVTKIIEGGAAQKDGRLQVGDKLLAVNDVSLEEVTHEE 68
PDZ10_MUPP1-PDZ8_PATJ-like cd06673
PDZ domain 10 of multi-PDZ-domain protein 1 (MUPP1), domain 8 of PATJ (protein-associated ...
 4539-4604 8.66e-06

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: 46.90  E-value: 8.66e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1201829585 4539 GLGIRVVGGKEIPgssgeIGA-YIAKVLPGGSAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQNIIIQ 4604
Cdd:cd06673     14 GLGLSIVGGSDTL-----LGAiIIHEVYEDGAAAKDGRLWAGDQILEVNGEDLRKATHDEAINVLRQ 75
PDZ2_LNX1_2-like cd06678
PDZ domain 2 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ ...
 4533-4608 9.49e-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: 9.49e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1201829585 4533 HTVSGNGLGIRVVGGKEIPGssgeigAYIAKVLPGGSAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQNiIIQQCGE 4608
Cdd:cd06678      6 NKRDGEQLGIKLVRKKDEPG------VFILDLLEGGLAARDGRLKSDDRVLAINGQDLRHGTPEQAAQ-IIQASGE 74
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
 280-425 9.87e-06

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 52.18  E-value: 9.87e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  280 KPVQQQTSAKPSVGPTKPLPQQPDSAKTSSQASPPTK---PSSQQSGPVKQPSQQPAR------QGGPVKPSAQQAGPPK 350
Cdd:PRK07994   360 HPAAPLPEPEVPPQSAAPAASAQATAAPTAAVAPPQApavPPPPASAPQQAPAVPLPEttsqllAARQQLQRAQGATKAK 439

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1201829585  351 QqpgSEKPSAQQTGPAKQPLQTGPGKPPLQQTGPVKQVPPQAGPTKPSSQTAGATKSVAQQPGLTKPPGPQSGPE 425
Cdd:PRK07994   440 K---SEPAAASRARPVNSALERLASVRPAPSALEKAPAKKEAYRWKATNPVEVKKEPVATPKALKKALEHEKTPE 511
C2B_Synaptotagmin-1 cd08402
C2 domain second repeat present in Synaptotagmin 1; Synaptotagmin is a membrane-trafficking ...
 5042-5151 1.01e-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: 1.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 5042 QLIVEILQCRNItyKFKSPDHLPDLYVKLYVvnISTQKRVIKKKTRVCRHDREPSFNETFRFSLSPagHSLQ----ILLV 5117
Cdd:cd08402     16 KLTVVILEAKNL--KKMDVGGLSDPYVKIHL--MQNGKRLKKKKTTIKKRTLNPYYNESFSFEVPF--EQIQkvhlIVTV 89

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1201829585 5118 SNGGKFMKKTLIGEAYV-----------WLDKVDLRKR-IVNWHKL 5151
Cdd:cd08402     90 LDYDRIGKNDPIGKVVLgcnatgaelrhWSDMLASPRRpIAQWHTL 135
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
 1221-1578 1.07e-05

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 52.36  E-value: 1.07e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 1221 KTSVEKIQEEAQKEELKLqqEKLSKTLSEDkipaTVSSDQKKPSRKFEEDKKPELLEKSTphpEDKKEQITAETKDRVAE 1300
Cdd:PTZ00108  1101 KEKVEKLNAELEKKEKEL--EKLKNTTPKD----MWLEDLDKFEEALEEQEEVEEKEIAK---EQRLKSKTKGKASKLRK 1171

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 1301 QKAEVEAPcdklhekkeedvkkeglttgipqmvSKTEKAEEEKTPVQVSRLPRSDHVEAVREKMEKEDDKSDTsssqqqk 1380
Cdd:PTZ00108  1172 PKLKKKEK-------------------------KKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSN------- 1219

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 1381 spqglsdtgysSDGISSSLGEIPSHIPSDEKDlTRESSKKDTISQESPPSPSDLAKLESTVLSILEAQASTLADEKSVKR 1460
Cdd:PTZ00108  1220 -----------SSGSDQEDDEEQKTKPKKSSV-KRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPP 1287

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 1461 kelheaYSDQTKDQHKTKPLPVTPesyssdeedlesiqegerTIAADGKGGSSSRTDYKEEGGGDDTPARRQRYDS-VED 1539
Cdd:PTZ00108  1288 ------PSKRPDGESNGGSKPSSP------------------TKKKVKKRLEGSLAALKKKKKSEKKTARKKKSKTrVKQ 1343

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 1201829585 1540 SS-ESENSPVPRRKRRASVGSSSSDEYKQDDSQGSGDEED 1578
Cdd:PTZ00108  1344 ASaSQSSRLLRRPRKKKSDSSSEDDDDSEVDDSEDEDDED 1383
DUF4887 pfam16228
Domain of unknown function (DUF4887); This family consists of uncharacterized proteins around ...
 166-331 1.09e-05

Domain of unknown function (DUF4887); This family consists of uncharacterized proteins around 210 residues in length and is mainly found in various Staphylococcus species. The function of this family is unknown.


Pssm-ID: 374444 [Multi-domain]  Cd Length: 176  Bit Score: 49.16  E-value: 1.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  166 FDLISDSDAAHEEAGRKQKVTQK--DQGKPEEQRGLAKHPSQQQSPKLVQQQGPVKPTPQQTESSKPVPQQQQPGEPKQI 243
Cdd:pfam16228    2 FAFVDHSKKAKERLLDEQKQEEKekDDKDKAEKEDKKKQEEEKENNELDQQANQYQQLPQQNQQQVQPPQQQAPTKQRPA 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  244 QKPGPShQGDSKVEQPKQPPQPRGPQKSQLQQSEPTKPVQQQTSAKPSVGPTKPLPQQPDSAKTSSQASPPTKPSSQ-QS 322
Cdd:pfam16228   82 KEENDD-KAEKDAKEDKDDERKKARQDKSDDKEKKNDDDKQPAQPKPQPNKPNPKPENNQQNNNKNNQAKPQAPQNNgNS 160


                   ....*....
gi 1201829585  323 GPVKQPSQQ 331
Cdd:pfam16228  161 GNQNANSGQ 169
PDZ4_MUPP1-like cd06668
PDZ domain 4 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ...
 4537-4615 1.24e-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: 46.52  E-value: 1.24e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1201829585 4537 GNGLGIRVVGGKEIpGSSGEigAYIAKVLPGGSAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQNIIiqqcGEAEICVRL 4615
Cdd:cd06668     13 SSGLGISLEGTVDV-EVRGH--HYIRSILPEGPVGRNGKLFSGDELLEVNGIQLLGLSHKEVVSIL----KELPPPVRL 84
PDZ1_MUPP1-like cd06689
PDZ domain 1 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ...
 4536-4613 1.33e-05

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: 46.86  E-value: 1.33e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1201829585 4536 SGNGLGIRVVGGKEipGSSGEIGAYIAKVLPGGSAEQTGKLIEGMQVLEWNGIPL-TGKTYEEVQNIIIQQCGEAEICV 4613
Cdd:cd06689     24 ESGGLGFSVVGLKS--ENRGELGIFVQEIQPGSVAARDGRLKENDQILAINGQPLdQSISHQQAIAILQQAKGSVELVV 100
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
235-367 1.35e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 51.70  E-value: 1.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  235 QQPGEPKQIQKPGpshqgdskVEQPKQPPQPrgPQKSQLQQSEPTKPVQQQTSAKPSVGPTKPLPQQPDSAKTSSQASPP 314
Cdd:PRK14971   370 SGGRGPKQHIKPV--------FTQPAAAPQP--SAAAAASPSPSQSSAAAQPSAPQSATQPAGTPPTVSVDPPAAVPVNP 439

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1201829585  315 TKPSSQQSGPVKQPSQQPAR--QGGPVKPSAQQAGPPKQQPGSEKPSAQQTGPAK 367
Cdd:PRK14971   440 PSTAPQAVRPAQFKEEKKIPvsKVSSLGPSTLRPIQEKAEQATGNIKEAPTGTQK 494
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
 193-340 1.36e-05

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


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 48.88  E-value: 1.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  193 PEEQRGLAKHPSQQQSPKLVQQQGPVKPT--PQQTESSKPVPQQQQPGEPKQIQKPGPSHQGDSKVEQPKQPPQPRGPQK 270
Cdd:pfam15240   19 SSEDVSQEDSPSLISEEEGQSQQGGQGPQgpPPGGFPPQPPASDDPPGPPPPGGPQQPPPQGGKQKPQGPPPQGGPRPPP 98

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  271 SQLQQSEPTKPVQQQTSAKPSVGPTKPLPQQPDSAKTSSQASPPTKPSSQQSGPVKQPSqQPARQGGPVK 340
Cdd:pfam15240   99 GKPQGPPPQGGNQQQGPPPPGKPQGPPPQGGGPPPQGGNQQGPPPPPPGNPQGPPQRPP-QPGNPQGPPQ 167
C2_RGS-like cd08685
C2 domain of the Regulator Of G-Protein Signaling (RGS) family; This CD contains members of ...
 4722-4822 1.43e-05

C2 domain of the Regulator Of G-Protein Signaling (RGS) family; This CD contains members of the regulator of G-protein signaling (RGS) family. RGS is a GTPase activating protein which inhibits G-protein mediated signal transduction. The protein is largely cytosolic, but G-protein activation leads to translocation of this protein to the plasma membrane. A nuclear form of this protein has also been described, but its sequence has not been identified. There are multiple alternatively spliced transcript variants in this family with some members having additional domains (ex. PDZ and RGS) downstream of the 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: 176067 [Multi-domain]  Cd Length: 119  Bit Score: 47.45  E-value: 1.43e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4722 GEIQLQINYDKHlgNLIIHILQARNLaPRDNNGYSDPFVKVYLLPGRGAEYKRRTKYVQKSLNPEWNQTVIYkNISTEQL 4801
Cdd:cd08685      1 GQLKLSIEGQNR--KLTLHVLEAKGL-RSTNSGTCNSYVKISLSPDKEVRFRQKTSTVPDSANPLFHETFSF-DVNERDY 76

                           90       100
                   ....*....|....*....|.
gi 1201829585 4802 KKKTLeVTVWDYDRFSSNDFL 4822
Cdd:cd08685     77 QKRLL-VTVWNKLSKSRDSGL 96
C2B_Ferlin cd04011
C2 domain second repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and ...
 4739-4832 1.55e-05

C2 domain second 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 second C2 repeat, C2B, and has a type-II topology.


Pssm-ID: 175978 [Multi-domain]  Cd Length: 111  Bit Score: 47.19  E-value: 1.55e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4739 IHILQARNLAprdnNGYSDPFVKVYLLpgrgaEYKRRTKyVQKSLN-PEWNQTVIYK-NISTEQLKKKTLEVTVWDYDRF 4816
Cdd:cd04011      8 VRVIEARQLV----GGNIDPVVKVEVG-----GQKKYTS-VKKGTNcPFYNEYFFFNfHESPDELFDKIIKISVYDSRSL 77

                           90
                   ....*....|....*.
gi 1201829585 4817 SSNDFLGEVLIDLSSV 4832
Cdd:cd04011     78 RSDTLIGSFKLDVGTV 93
PDZ3_Par3-like cd23059
PDZ domain 3 of partitioning defective 3 (Par3), and related domains; PDZ (PSD-95 ...
 4539-4602 1.57e-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: 1.57e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1201829585 4539 GLGIRVVG--GKEIPGSSGEIGAYIAKVLPGGSAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQNII 4602
Cdd:cd23059     17 GLGVSVKGktSKEDNGGKADLGIFIKSIIHGGAASKDGRLRVNDQLIAVNGESLLGLTNSEAMETL 82
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 299-440 2.27e-05

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 50.87  E-value: 2.27e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  299 PQQPDSAKTSSQASPPTKPSSQQSGPVKQPSQQPARQGGPVKPSAQQAGPPkqqpgseKPSAQQTGPAKQPLQTGPGKPP 378
Cdd:PRK14951   366 PAAAAEAAAPAEKKTPARPEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAA-------PPAAAPPAPVAAPAAAAPAAAP 438

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1201829585  379 lqqtgpvkQVPPQAGPTKPSSQTAGATKSVAQQPGLTKPPGPQSGPEKPSQQKQASAAQPVE 440
Cdd:PRK14951   439 --------AAAPAAVALAPAPPAQAAPETVAIPVRVAPEPAVASAAPAPAAAPAAARLTPTE 492
PDZ_syntrophin-like cd06801
PDZ domain of syntrophins, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), ...
 4525-4614 2.50e-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: 45.64  E-value: 2.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4525 KLLRDPkdhtvsGNGLGIRVVGGKE--IPgssgeigAYIAKVLPGGSAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQNiI 4602
Cdd:cd06801      4 RVVKQD------VGGLGISIKGGAEhkMP-------ILISKIFKGQAADQTGQLFVGDAILSVNGENLEDATHDEAVQ-A 69

                           90
                   ....*....|...
gi 1201829585 4603 IQQCG-EAEICVR 4614
Cdd:cd06801     70 LKNAGdEVTLTVK 82
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 172-442 2.70e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 50.75  E-value: 2.70e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  172 SDAAHEEAGRKQKVTQKDQGKPEEQRGLAKHPSQQQSPKlVQQQGPVKPTPQQTESSKPVPQ--------QQQPGEPKQI 243
Cdd:PRK07764   419 AAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPP-PAAAPSAQPAPAPAAAPEPTAApapappaaPAPAAAPAAP 497

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  244 QKPGPShQGDSKVEQP----------------------KQPPQPRGPQKSQLQQSEPTKPVQQQTSAKPSV--------- 292
Cdd:PRK07764   498 AAPAAP-AGADDAATLrerwpeilaavpkrsrktwailLPEATVLGVRGDTLVLGFSTGGLARRFASPGNAevlvtalae 576

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  293 ---GPTKPLPQQPDSAKTSSQASPPTKPSSQQSGPVKQPSQQPARQGGPVKPSAQQAGPPKQQPGSEKPSAQQTGPAKQ- 368
Cdd:PRK07764   577 elgGDWQVEAVVGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKh 656

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1201829585  369 -----PLQTGPGKPPLQQTGPVKQVPPQAGPTKPSSQTAGATKSVAQQPGLTKPPGPQSGPEKPSQQKQASAAQPVEST 442
Cdd:PRK07764   657 vavpdASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAA 735
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
298-447 3.05e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 50.54  E-value: 3.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  298 LPQQPDSAKTSSQASPPTKPSSQQSGPVKQPSQQPARQggpvkPSAQQAGPPKQQPGSekPSAQQTGPAKQPLqtgpgkp 377
Cdd:PRK14971   362 LTQKGDDASGGRGPKQHIKPVFTQPAAAPQPSAAAAAS-----PSPSQSSAAAQPSAP--QSATQPAGTPPTV------- 427

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1201829585  378 PLQQTGPVKQVPPQAGPTKPSSQTAGATK--SVAQQPGLTkpPGPQSGPEKPSQQKQASAAQPVESTPKKTF 447
Cdd:PRK14971   428 SVDPPAAVPVNPPSTAPQAVRPAQFKEEKkiPVSKVSSLG--PSTLRPIQEKAEQATGNIKEAPTGTQKEIF 497
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
191-450 3.06e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 50.62  E-value: 3.06e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  191 GKPEEQRGLAKHPSQQQSPKLVQQQGPVKPTPQQTESSKPVPQQQQPGEPKQ----IQKPGPSHQGDSKVEQPKQPPQPR 266
Cdd:PRK07003   371 GVPARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRaeapPAAPAPPATADRGDDAADGDAPVP 450

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  267 GPQKSQLQQSEPTKPVQQQTSAKPSVGPTKPLPQQPDSAKtssQASPPTKPSSQQSGPVKQPSQQPARQGGPVKPSAQQA 346
Cdd:PRK07003   451 AKANARASADSRCDERDAQPPADSGSASAPASDAPPDAAF---EPAPRAAAPSAATPAAVPDARAPAAASREDAPAAAAP 527

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  347 GPPK---QQPGSEKPSAQQTGPA----------------KQPLQTGPGKPPLQQTGPVKQVPPQAGPTKPssqTAGATKS 407
Cdd:PRK07003   528 PAPEarpPTPAAAAPAARAGGAAaaldvlrnagmrvssdRGARAAAAAKPAAAPAAAPKPAAPRVAVQVP---TPRARAA 604

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1201829585  408 VAQQPGLTKPPGPQsgpekPSQQKQASAaqPVESTPKKTFCPL 450
Cdd:PRK07003   605 TGDAPPNGAARAEQ-----AAESRGAPP--PWEDIPPDDYVPL 640
C2_Perforin cd04032
C2 domain of Perforin; Perforin contains a single copy of a C2 domain in its C-terminus and ...
 4734-4833 3.46e-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: 46.49  E-value: 3.46e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4734 LGNLIIHILQARNLaprdnNG----YSDPFVKVYllpgRGAEYKRrTKYVQKSLNPEWNQTVIYKNISTEQLKKKTLEVt 4809
Cdd:cd04032     27 LATLTVTVLRATGL-----WGdyftSTDGYVKVF----FGGQEKR-TEVIWNNNNPRWNATFDFGSVELSPGGKLRFEV- 95

                           90       100
                   ....*....|....*....|....
gi 1201829585 4810 vWDYDRFSSNDFLGEVLIDLSSVS 4833
Cdd:cd04032     96 -WDRDNGWDDDLLGTCSVVPEAGV 118
SP2_N cd22540
N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins ...
 217-443 3.49e-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: 50.31  E-value: 3.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  217 PVKPTPQQTESSKPVPQQQQPG----------------EPKQIQKPGPSHQGDSKVEQPKQP---PQPRGPQKSQLQQSE 277
Cdd:cd22540     51 PPQPTPRKLVPIKPAPLPLGPGknsigflsakgniiqlQGSQLSSSAPGGQQVFAIQNPTMIikgSQTRSSTNQQYQISP 130

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  278 PTKPVQQQT-SAKPSVGP--------TKPLPQQPDSAKTSSQASP-PTKPSSQQSGPVKQPSQQPARQGG-------PVK 340
Cdd:cd22540    131 QIQAAGQINnSGQIQIIPgtnqaiitPVQVLQQPQQAHKPVPIKPaPLQTSNTNSASLQVPGNVIKLQSGgnvaltlPVN 210

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  341 PSAQQAGPPKQQPGSEKPSAQQTGPAKQPLQTGPGKPPLQQtgpvkQVPPQA-GPTKPSSQTAGATKSVAQQPGLTKPPG 419
Cdd:cd22540    211 NLVGTQDGATQLQLAAAPSKPSKKIRKKSAQAAQPAVTVAE-----QVETVLiETTADNIIQAGNNLLIVQSPGTGQPAV 285

                          250       260
                   ....*....|....*....|....
gi 1201829585  420 PQsgpekPSQQKQASAAQPVESTP 443
Cdd:cd22540    286 LQ-----QVQVLQPKQEQQVVQIP 304
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
 549-780 3.71e-05

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 50.31  E-value: 3.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  549 PKPDPSQQADSKKPVPQKKQPSMPGSP-----PVKSKQTDAEPSDTFQQID-------PTPKSDQAKPTQAEEKQnqpSV 616
Cdd:PLN03209   328 VPPKESDAADGPKPVPTKPVTPEAPSPpieeePPQPKAVVPRPLSPYTAYEdlkpptsPIPTPPSSSPASSKSVD---AV 404

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  617 QKPTTDTVPTSAAPGVKQDLADPRPPLTQQKVTDSP--KPETTKPPADTHPagdkpdSKPLPQVSRQKSDPKLASQSGSK 694
Cdd:PLN03209   405 AKPAEPDVVPSPGSASNVPEVEPAQVEAKKTRPLSPyaRYEDLKPPTSPSP------TAPTGVSPSVSSTSSVPAVPDTA 478

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  695 SDAKTQKAVEPAQVRDDPkklQTKSAPKPDTKPAPKGPQAGTGPKPMSAQPAPQPQQPQKTPEQsrrfSLNLGGITDVPK 774
Cdd:PLN03209   479 PATAATDAAAPPPANMRP---LSPYAVYDDLKPPTSPSPAAPVGKVAPSSTNEVVKVGNSAPPT----ALADEQHHAQPK 551


                   ....*.
gi 1201829585  775 PQPTTP 780
Cdd:PLN03209   552 PRPLSP 557
Androgen_recep pfam02166
Androgen receptor;
297-418 3.81e-05

Androgen receptor;


Pssm-ID: 426632 [Multi-domain]  Cd Length: 501  Bit Score: 49.93  E-value: 3.81e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  297 PLPQQPDSAKTssqASPPTKPSSQQSGPVKQPSQQPARQ-GGPVKPsaQQAGPPKQQPGSEKPSAQQTGPAKQPLQTGPG 375
Cdd:pfam02166   32 PGPRHPEAAGG---AAPPGARLQHQQQQQQQVPQQPQQQeSSPRQP--QASVQPQQAGDDGSPPAHNRGPAGYLALEDDE 106

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1201829585  376 KPPLQQTGPVKQVPPQAGPTKPSSQTAGATKSVAQQPGLTKPP 418
Cdd:pfam02166  107 QPQPSQAQPAAECCPENGCVPEPGAAAAAGKGLPQQAVAPAAP 149
PDZ2_Scribble-like cd06703
PDZ domain 2 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 4525-4602 3.94e-05

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: 45.33  E-value: 3.94e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1201829585 4525 KLLRDpkdhtvsGNGLGIRVVGGKE-IPGSSGEIGAYIAKVLPGGSAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQNII 4602
Cdd:cd06703      6 TLIRD-------GKGLGFSIAGGKGsTPFRDGDEGIFISRITEGGAADRDGKLQVGDRVLSINGVDVTEARHDQAVALL 77
C2A_SLP-1_2 cd08393
C2 domain first repeat present in Synaptotagmin-like proteins 1 and 2; All Slp members ...
 5026-5151 4.29e-05

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: 46.27  E-value: 4.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 5026 GEIKIALKKEMKTdgEQLIVEILQCRNITYKFKSPDHlPDLYVKLYVVNISTqkRVIKKKTRVCRHDREPSFNETFRFSL 5105
Cdd:cd08393      2 GSVQFALDYDPKL--RELHVHVIQCQDLAAADPKKQR-SDPYVKTYLLPDKS--NRGKRKTSVKKKTLNPVFNETLRYKV 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1201829585 5106 SPAGHSLQILLVS--NGGKFMKKTLIGEAYVWLDKVDLRKRIVNWHKL 5151
Cdd:cd08393     77 EREELPTRVLNLSvwHRDSLGRNSFLGEVEVDLGSWDWSNTQPTWYPL 124
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 ...
 4539-4602 4.41e-05

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: 44.91  E-value: 4.41e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1201829585 4539 GLGIRVVGGKEIPgsSGEIGAYIAKVLPGGSAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQNII 4602
Cdd:cd06763     12 GLGFSLEGGKGSP--LGDRPLTIKRIFKGGAAEQSGVLQVGDEILQINGTSLQGLTRFEAWNII 73
PRK10905 PRK10905
cell division protein DamX; Validated
 208-413 4.43e-05

cell division protein DamX; Validated


Pssm-ID: 236792 [Multi-domain]  Cd Length: 328  Bit Score: 49.17  E-value: 4.43e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  208 SPKLVQQQGPVKPTPQQTESskpvpQQQQPGEPKQIQKPGPShqgdSKVEQPKQPPQPRGPQKSQLQ---QSEPTKPVQQ 284
Cdd:PRK10905    41 AGNATDQANGVQPAPGTTSA-----EQTAGNTQQDVSLPPIS----STPTQGQTPVATDGQQRVEVQgdlNNALTQPQNQ 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  285 QTSAKPSVGPTkpLPQQPDSAKTSSQASPPTKPSSQQSGPvKQPSQQPARQGG---PVKPSAQQAGPPK---QQPGSEKP 358
Cdd:PRK10905   112 QQLNNVAVNST--LPTEPATVAPVRNGNASRQTAKTQTAE-RPATTRPARKQAviePKKPQATAKTEPKpvaQTPKRTEP 188

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1201829585  359 SAqQTGPAKQPLQTGPGKP-PLQQTGPVKQVPPQAGPTKP--SSQTAGATKSVAQQPG 413
Cdd:PRK10905   189 AA-PVASTKAPAATSTPAPkETATTAPVQTASPAQTTATPaaGGKTAGNVGSLKSAPS 245
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
 177-302 4.58e-05

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


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 47.34  E-value: 4.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  177 EEAGRKQKVTQKDQGKPEEQRGlAKHPSQQQSPKLVQQQGPVKPTPQQTESSKPVPQQQQPGEPKQIQKPGPSHQGDSKV 256
Cdd:pfam15240   34 EEEGQSQQGGQGPQGPPPGGFP-PQPPASDDPPGPPPPGGPQQPPPQGGKQKPQGPPPQGGPRPPPGKPQGPPPQGGNQQ 112

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1201829585  257 EQPKQPPQPRGPQksQLQQSEPTKPVQQQTSAKPSVGPTKPLPQQP 302
Cdd:pfam15240  113 QGPPPPGKPQGPP--PQGGGPPPQGGNQQGPPPPPPGNPQGPPQRP 156
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
 535-742 5.21e-05

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 49.54  E-value: 5.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  535 PSPQSQ--PGQKKDASPKP-DPSQQADSKKPvPQKKQPSMPGSPPVKSKQTDA----EPSDTFQQIDPTPKSDQAKPTQA 607
Cdd:PLN03209   352 PSPPIEeePPQPKAVVPRPlSPYTAYEDLKP-PTSPIPTPPSSSPASSKSVDAvakpAEPDVVPSPGSASNVPEVEPAQV 430

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  608 EEKQNQPsvqkpttdTVPTSAAPgvkqDLADPRPPltqqkvtdSPKPETTKPPADTHPAG--DKPDSKPLPQVSRQKSDP 685
Cdd:PLN03209   431 EAKKTRP--------LSPYARYE----DLKPPTSP--------SPTAPTGVSPSVSSTSSvpAVPDTAPATAATDAAAPP 490

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1201829585  686 KLASQSGSK----SDAKTQKAVEPAQVRDDPKKLQTKSAPK-----PDTKPAPKGPQAGTGPKPMS 742
Cdd:PLN03209   491 PANMRPLSPyavyDDLKPPTSPSPAAPVGKVAPSSTNEVVKvgnsaPPTALADEQHHAQPKPRPLS 556
C2_Smurf-like cd08382
C2 domain present in Smad ubiquitination-related factor (Smurf)-like proteins; A single C2 ...
 4741-4840 5.59e-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: 45.76  E-value: 5.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4741 ILQARNLAPRDNNGYSDPFVKVYLlpgrGAEYKRRTKYVQKSLNPEWNQTviYK-NISteqlKKKTLEVTVWDYDRFSSN 4819
Cdd:cd08382      6 VLCADGLAKRDLFRLPDPFAVITV----DGGQTHSTDVAKKTLDPKWNEH--FDlTVG----PSSIITIQVFDQKKFKKK 75

                           90       100
                   ....*....|....*....|...
gi 1201829585 4820 D--FLGEVLIDLSSVSQLDNTPR 4840
Cdd:cd08382     76 DqgFLGCVRIRANAVLPLKDTGY 98
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 ...
 4533-4611 5.77e-05

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: 44.57  E-value: 5.77e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1201829585 4533 HTVSGNGLGIRVVGgkeIPGSSGEIGAYIAKVLPGGSAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQNiIIQQCGEAEI 4611
Cdd:cd06760     10 NKEPGVGLGIGLCC---LPLENDIPGIFIHHLSPGSVAHMDGRLRRGDQILEINGTSLRNVTLNEAYA-ILSQCKPGPV 84
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 30-391 5.82e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 49.60  E-value: 5.82e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585   30 QPLVPAGVEADLSQLSEEERRQIAAVMSRAQGLPRGNLAGAEPPPMQRHPDLDTSRHPRQPGKPPDPGPGlsksRTVDVL 109
Cdd:PRK07764   440 APPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAPAGADDA----ATLRER 515

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  110 KTEQRA--PGRSPSSISLRESKSRtdFKEDQKPSMMPSFlseANPLSAvtSVVNKFNPFDLIsdSDAAHEEAGRKQKV-- 185
Cdd:PRK07764   516 WPEILAavPKRSRKTWAILLPEAT--VLGVRGDTLVLGF---STGGLA--RRFASPGNAEVL--VTALAEELGGDWQVea 586

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  186 ---TQKDQGKPEEQRGLAKHPSQQQSPKLVQQQGPVKPTPQQTESSkPVPQQQQPGEPKQIQKPGPSHQGDSKVEQPKQP 262
Cdd:PRK07764   587 vvgPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGA-AAAPAEASAAPAPGVAAPEHHPKHVAVPDASDG 665

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  263 PQPRGPQKSQLQQSEPTkpvqqqtsakPSVGPTKPLPQQPDSAKTSSQASPPTKPSSQQSGPVKQPSQQPARQGGPVkPS 342
Cdd:PRK07764   666 GDGWPAKAGGAAPAAPP----------PAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPS-PA 734

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1201829585  343 AQQAGPPKQQPGSEKPSAQQTGPAKQPLQTGPGKPPLQQTGPVKQVPPQ 391
Cdd:PRK07764   735 ADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEE 783
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
 253-400 6.20e-05

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


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 46.95  E-value: 6.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  253 DSKVEQPKQPPQPRGPQKSQLQQSE-PTKPVQQQTSAKPSVGPTKPLPQQPDSaktsSQASPPTkpssqqsgPVKQPSQQ 331
Cdd:pfam15240   20 SEDVSQEDSPSLISEEEGQSQQGGQgPQGPPPGGFPPQPPASDDPPGPPPPGG----PQQPPPQ--------GGKQKPQG 87

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1201829585  332 PARQGGPVKPSAQQAGPPKQQpGSEKPSAQQTGPAKQPLQTGPGKPPL---QQTGPVKQVPPQAGPTKPSSQ 400
Cdd:pfam15240   88 PPPQGGPRPPPGKPQGPPPQG-GNQQQGPPPPGKPQGPPPQGGGPPPQggnQQGPPPPPPGNPQGPPQRPPQ 158
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
 197-360 6.96e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 49.48  E-value: 6.96e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  197 RGLAKHPSQQQ-SPKLVQQQGPVKPTPQQTESSKPVPQQQQPGEPKQIQKPGPshqgdskveqPKQPPQPRGPQKSQLQQ 275
Cdd:PRK07994   355 RMLAFHPAAPLpEPEVPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPASAP----------QQAPAVPLPETTSQLLA 424

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  276 SEPTKPVQQQTSAKPSVGPTKPLPQQPDSAKTSSQASPPTKPSSQQSGPVKQPSQQPARQGGPVKPSAQQAGPPKQQPGS 355
Cdd:PRK07994   425 ARQQLQRAQGATKAKKSEPAAASRARPVNSALERLASVRPAPSALEKAPAKKEAYRWKATNPVEVKKEPVATPKALKKAL 504


                   ....*
gi 1201829585  356 EKPSA 360
Cdd:PRK07994   505 EHEKT 509
dnaA PRK14086
chromosomal replication initiator protein DnaA;
217-430 7.66e-05

chromosomal replication initiator protein DnaA;


Pssm-ID: 237605 [Multi-domain]  Cd Length: 617  Bit Score: 49.05  E-value: 7.66e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  217 PVKPTPQQTESSKPVPQQ-QQPGEPKQIQKPGPSHQGDSKVeqPKQPPQPRGPqksQLQQSEPTKPVQQQtSAKPSvgpt 295
Cdd:PRK14086    87 TVDPSAGEPAPPPPHARRtSEPELPRPGRRPYEGYGGPRAD--DRPPGLPRQD---QLPTARPAYPAYQQ-RPEPG---- 156

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  296 kPLPQQPDSAktSSQASPPTKPSSQQSGPVKQPSQQPARQGGPVKPSAQQAGPPKQQPGSEKPSAQQTGPAKQPLqtgPG 375
Cdd:PRK14086   157 -AWPRAADDY--GWQQQRLGFPPRAPYASPASYAPEQERDREPYDAGRPEYDQRRRDYDHPRPDWDRPRRDRTDR---PE 230

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1201829585  376 KPPLQQTgpvkqvPPQAGPTKPSSQTAGATKSVAQQPG-LTKPPGPQSGPEKPSQQ 430
Cdd:PRK14086   231 PPPGAGH------VHRGGPGPPERDDAPVVPIRPSAPGpLAAQPAPAPGPGEPTAR 280
COG5038 COG5038
Ca2+-dependent lipid-binding protein, contains C2 domain [General function prediction only];
4734-4834 8.92e-05

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


Pssm-ID: 227371 [Multi-domain]  Cd Length: 1227  Bit Score: 49.37  E-value: 8.92e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4734 LGNLIIHILQARNLAPRDN--NGYSDPFVkVYLLPGRgaeYKRRTKYVQKSLNPEWNQTvIYknISTEQLKKKtLEVTVW 4811
Cdd:COG5038    435 IGVVEVKIKSAEGLKKSDStiNGTVDPYI-TVTFSDR---VIGKTRVKKNTLNPVWNET-FY--ILLNSFTDP-LNLSLY 506

                           90       100
                   ....*....|....*....|...
gi 1201829585 4812 DYDRFSSNDFLGEVLIDLSSVSQ 4834
Cdd:COG5038    507 DFNSFKSDKVVGSTQLDLALLHQ 529
C2A_Tricalbin-like cd04044
C2 domain first repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are ...
 4734-4834 9.52e-05

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: 45.24  E-value: 9.52e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4734 LGNLIIHILQARNLAPRDN-NGYSDPFVKVYLLPGRGAEykrRTKYVQKSLNPEWNQTvIYKNISTEQLKkktLEVTVWD 4812
Cdd:cd04044      1 IGVLAVTIKSARGLKGSDIiGGTVDPYVTFSISNRRELA---RTKVKKDTSNPVWNET-KYILVNSLTEP---LNLTVYD 73

                           90       100
                   ....*....|....*....|..
gi 1201829585 4813 YDRFSSNDFLGEVLIDLSSVSQ 4834
Cdd:cd04044     74 FNDKRKDKLIGTAEFDLSSLLQ 95
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 837-1274 1.15e-04

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 48.92  E-value: 1.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  837 PKEATQAQPLPKAAPTKKET----KPLASEKLEPMAADSTLTTKGSDLEKKPSLAKDSKPQAAE--AKKPAELSEQEKAS 910
Cdd:PTZ00449   510 PPEGPEASGLPPKAPGDKEGeegeHEDSKESDEPKEGGKPGETKEGEVGKKPGPAKEHKPSKIPtlSKKPEFPKDPKHPK 589

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  911 QPKVScplcktglnIGSKDPPNFNTCTEckkvvcnlcgfNPMPHIAevqewlclncqtqramsgQLGDMGKVPLPKLGPS 990
Cdd:PTZ00449   590 DPEEP---------KKPKRPRSAQRPTR-----------PKSPKLP------------------ELLDIPKSPKRPESPK 631

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  991 QPVSKPPatPQKQPVPAVSHSPQKTSTPPTPAATKPKEEPGVQKEV-----PKLQQGKLEKT-LSADKIQQGIQKEDAKS 1064
Cdd:PTZ00449   632 SPKRPPP--PQRPSSPERPEGPKIIKSPKPPKSPKPPFDPKFKEKFyddylDAAAKSKETKTtVVLDESFESILKETLPE 709

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 1065 KQGKLFKTPSADKIQRvSQKEDSRLQQTKLTKTPSSDKILHGAQKEdakfQESKLAKTSSADKILHGVQKEDIKVQEAKl 1144
Cdd:PTZ00449   710 TPGTPFTTPRPLPPKL-PRDEEFPFEPIGDPDAEQPDDIEFFTPPE----EERTFFHETPADTPLPDILAEEFKEEDIH- 783

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 1145 AKIPSADKILH-------------GVQKEDPKLQQMKMAKALSADKIQ--PAAQKEDPQLQGVRLSKAVSADKIQHGIQK 1209
Cdd:PTZ00449   784 AETGEPDEAMKrpdspsehedkppGDHPSLPKKRHRLDGLALSTTDLEsdAGRIAKDASGKIVKLKRSKSFDDLTTVEEA 863

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1201829585 1210 EDLNlqhVKTEKTSVEKIQEEAQKEELKLQQEKlSKTLSEDKIPATVSSDQKKPSrKFEEDKKPE 1274
Cdd:PTZ00449   864 EEMG---AEARKIVVDDDGTEADDEDTHPPEEK-HKSEVRRRRPPKKPSKPKKPS-KPKKPKKPD 923
C2B_Synaptotagmin-12 cd08406
C2 domain second repeat present in Synaptotagmin 12; Synaptotagmin is a membrane-trafficking ...
 5041-5107 1.21e-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: 1.21e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1201829585 5041 EQLIVEILQCRNITYKFKSPDHlpDLYVKLYVvnISTQKRVIKKKTRVCRHDREPSFNETFRFSLSP 5107
Cdd:cd08406     15 ERLTVVVVKARNLVWDNGKTTA--DPFVKVYL--LQDGRKISKKKTSVKRDDTNPIFNEAMIFSVPA 77
PDZ_MPP5-like cd06798
PDZ domain of membrane palmitoylated protein 5 (MPP5), Drosophila Stardust, and related ...
 4561-4602 1.23e-04

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: 43.49  E-value: 1.23e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1201829585 4561 IAKVLPGGSAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQNII 4602
Cdd:cd06798     25 ISRIVKGGAAEKSGLLHEGDEILEINGIEIRGKDVNEVCDLL 66
MISS pfam15822
MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic ...
 259-449 1.26e-04

MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic MAPK-interacting and spindle-stabilising protein-like proteins. MISS is rich in prolines and has four potential MAPK-phosphorylation sites, a MAPK-docking site, a PEST sequence (PEST motif) and a bipartite nuclear localization signal. The endogenous protein accumulates during mouse meiotic maturation and is found as discrete dots on the MII spindle. MISS is the first example of a physiological MAPK-substrate that is stabilized in MII that specifically regulates MII spindle integrity during the CSF arrest.


Pssm-ID: 318115 [Multi-domain]  Cd Length: 238  Bit Score: 46.90  E-value: 1.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  259 PKQPPQprgpQKSQLQQSEPTKPVQQQTSAKPSVGPTKPlpqqpdsAKTSSQASPPTKPSSQQSGPVkqpsqqPARQGGP 338
Cdd:pfam15822    8 PEQSPA----KTSAVSNPKPGQPPQGWPGSNPWNNPSAP-------PAVPSGLPPSTAPSTVPFGPA------PTGMYPS 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  339 VKPSAQQAGPPKQQPGSEKPSAQQTGPAKQPLQTGPGkPPLQQTGPVKQVP----PQAGPTKPS----SQTAGATKSVAQ 410
Cdd:pfam15822   71 IPLTGPSPGPPAPFPPSGPSCPPPGGPYPAPTVPGPG-PIGPYPTPNMPFPelprPYGAPTDPAaaapSGPWGSMSSGPW 149

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1201829585  411 QPGLT----------KPPGPQSGPeKPSQQKQASAAQPVESTPKKTFCP 449
Cdd:pfam15822  150 APGMGgqypapnmpyPSPGPYPAV-PPPQSPGAAPPVPWGTVPPGPWGP 197
PHA03377 PHA03377
EBNA-3C; Provisional
 189-449 1.40e-04

EBNA-3C; Provisional


Pssm-ID: 177614 [Multi-domain]  Cd Length: 1000  Bit Score: 48.51  E-value: 1.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  189 DQGKPEEQRGLAKHP-------SQQQSPKLVQQQGPVKPTPQQTESSKPVPQQQQPG--EPKQIQKPGPSHQgdskveqp 259
Cdd:PHA03377   694 DAGRAQPSEESHLSSmsptqpiSHEEQPRYEDPDDPLDLSLHPDQAPPPSHQAPYSGheEPQAQQAPYPGYW-------- 765

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  260 kqppQPRGPQKSQLQQSEPTKPVQQQTSAKPSVGPTKPLPQQPdsaktssQASPPTKPSSQQsgPVKQPSQQPARQGGPV 339
Cdd:PHA03377   766 ----EPRPPQAPYLGYQEPQAQGVQVSSYPGYAGPWGLRAQHP-------RYRHSWAYWSQY--PGHGHPQGPWAPRPPH 832

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  340 kpsaqqagPPKQQPGSEKPsAQQTGPAKQPLQTGPGKPPLQQTgpvkQVPPQAGPTKPSSQTAGATKSVAQQPGLTKPPG 419
Cdd:PHA03377   833 --------LPPQWDGSAGH-GQDQVSQFPHLQSETGPPRLQLS----QVPQLPYSQTLVSSSAPSWSSPQPRAPIRPIPT 899

                          250       260       270
                   ....*....|....*....|....*....|
gi 1201829585  420 PQSGPEKPSQQKQASAAqpvesTPKKTFCP 449
Cdd:PHA03377   900 RFPPPPMPLQDSMAVGC-----DSSGTACP 924
C2A_Ferlin cd08373
C2 domain first repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and ...
 4737-4832 1.41e-04

C2 domain first 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 first C2 repeat, C2A, and has a type-II topology.


Pssm-ID: 176019 [Multi-domain]  Cd Length: 127  Bit Score: 44.55  E-value: 1.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4737 LIIHILQARNLaprdnNGYSDPFVKVYLlpgRGAeyKRRTKYVQKSLNPEWNQTV---IYKNISTEQLkkktLEVTVWDY 4813
Cdd:cd08373      1 LVVSLKNLPGL-----KGKGDRIAKVTF---RGV--KKKTRVLENELNPVWNETFewpLAGSPDPDES----LEIVVKDY 66

                           90
                   ....*....|....*....
gi 1201829585 4814 DRFSSNDFLGEVLIDLSSV 4832
Cdd:cd08373     67 EKVGRNRLIGSATVSLQDL 85
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
 234-391 1.45e-04

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


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 45.80  E-value: 1.45e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  234 QQQPGEPKQIQKPGPSHQGDSKVEQPKQPPQPRGPQKsqlqqseptkPVQQQTSAKPSVGPTKPLPQQPdsaktssqaSP 313
Cdd:pfam15240   30 SLISEEEGQSQQGGQGPQGPPPGGFPPQPPASDDPPG----------PPPPGGPQQPPPQGGKQKPQGP---------PP 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  314 PTKPSSQQSGPVKQPSQQPARQGGPVKPSAQQaGPPKQQPGSE-KPSAQQTGPAKQP-LQTGPGKPPLQQTGPvkQVPPQ 391
Cdd:pfam15240   91 QGGPRPPPGKPQGPPPQGGNQQQGPPPPGKPQ-GPPPQGGGPPpQGGNQQGPPPPPPgNPQGPPQRPPQPGNP--QGPPQ 167
PDZ_Radil-like cd06690
PDZ domain of Ras-associating and dilute domain-containing protein (Radil) and related domains; ...
 4537-4602 1.51e-04

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: 43.43  E-value: 1.51e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1201829585 4537 GNGLGIRVVGGKEIPGSSGeiGAYIAKVLPGGSAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQNII 4602
Cdd:cd06690     12 PKGLGLGLIDGLHTPLRSP--GIYIRTLVPDSPAARDGRLRLGDRILAVNGTSLVGADYQSAMDLI 75
C2F_Ferlin cd08374
C2 domain sixth repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and ...
 4798-4834 1.56e-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: 44.58  E-value: 1.56e-04
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1201829585 4798 TEQLKKKTLEVTVWDYDRFSSNDFLGEVLIDLSSVSQ 4834
Cdd:cd08374     87 TEYKIPPKLTLQVWDNDKFSPDDFLGSLELDLSILPR 123
PDZ_PDLIM-like cd06753
PDZ domain of PDZ-LIM family proteins, and related domains; PDZ (PSD-95 (Postsynaptic density ...
 4541-4602 1.56e-04

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: 43.29  E-value: 1.56e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1201829585 4541 GIRVVGGKE--IPgssgeigAYIAKVLPGGSAEQTGkLIEGMQVLEWNGIPLTGKTYEEVQNII 4602
Cdd:cd06753     11 GFRLQGGKDfnQP-------LTISRVTPGGKAAQAN-LRPGDVILAINGESTEGMTHLEAQNKI 66
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 535-1101 1.81e-04

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 48.16  E-value: 1.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  535 PSPQSQPGQKKDASPKpdPSQQADSKKPVPQKKQPSMPGSPPVKSKQTDAEPSDTFQQID---PTPKSDQAKPTQAEEKQ 611
Cdd:PRK10263   375 PAPEGYPQQSQYAQPA--VQYNEPLQQPVQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPyyaPAPEQPVAGNAWQAEEQ 452

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  612 NQPSVQKPTTDTVPTSAAPgVKQDLADPRPPLTQQKVTDSPKP--ETTKPpadthpagdkpdSKPlPQVSRQKSDPKLAS 689
Cdd:PRK10263   453 QSTFAPQSTYQTEQTYQQP-AAQEPLYQQPQPVEQQPVVEPEPvvEETKP------------ARP-PLYYFEEVEEKRAR 518

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  690 QSgSKSDAKTQKAVEPAQvrdDPKKLQTKSAPKPDTKPAPKGPQAGTGPKPMSAQPAPQPQQPQKTPeQSRRFSLNLGGi 769
Cdd:PRK10263   519 ER-EQLAAWYQPIPEPVK---EPEPIKSSLKAPSVAAVPPVEAAAAVSPLASGVKKATLATGAAATV-AAPVFSLANSG- 592

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  770 tdVPKPQ------PTTPQET-----VTGKLFGFGASIFSQasslistagqpgsqtsgpappaakqpqppsqpTASQAPPK 838
Cdd:PRK10263   593 --GPRPQvkegigPQLPRPKrirvpTRRELASYGIKLPSQ--------------------------------RAAEEKAR 638

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  839 EATQAQPLPKAAPTKKETKPLASEKLEPMAADSTLTTKGSDLEKKPSLAKDSKPQAAEakkpAELSEQEKASQPKVSCPL 918
Cdd:PRK10263   639 EAQRNQYDSGDQYNDDEIDAMQQDELARQFAQTQQQRYGEQYQHDVPVNAEDADAAAE----AELARQFAQTQQQRYSGE 714

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  919 CKTGLNIGSKDppNFNtcteckkvvcnlcgFNPMPHIAEvqewlclncqtqramsgqlgDMGKVPL--PKLGP-SQPVSK 995
Cdd:PRK10263   715 QPAGANPFSLD--DFE--------------FSPMKALLD--------------------DGPHEPLftPIVEPvQQPQQP 758

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  996 PPATPQKQPVPAVSHSPQKTSTPPTPAATKPKEEPGVQKEVPKLQQGKLEKTLSADKIQQGIQKEDAKSKQGKLFKTPSA 1075
Cdd:PRK10263   759 VAPQQQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVA 838

                          570       580       590
                   ....*....|....*....|....*....|..
gi 1201829585 1076 DKIQR------VSQKEDSRLQQTKLTKTPSSD 1101
Cdd:PRK10263   839 PQPQDtllhplLMRNGDSRPLHKPTTPLPSLD 870
PHA01929 PHA01929
putative scaffolding protein
 205-329 1.90e-04

putative scaffolding protein


Pssm-ID: 177328  Cd Length: 306  Bit Score: 46.97  E-value: 1.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  205 QQQSPKLVQQQGPVKPTPQQTESSKPVPQQQQPGEPKQIQKPgpshqgdSKVEQPKQPPQPrGPQKSQLQQSEPTKPVQQ 284
Cdd:PHA01929     6 QQLPPGLAGLVANVPPAAAPTPQPNPVIQPQAPVQPGQPGAP-------QQLAIPTQQPQP-VPTSAMTPHVVQQAPAQP 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1201829585  285 QTSAKPSVGPTKP--LPQQPDSAKTSSQASPPTKPSSQQSGPVKQPS 329
Cdd:PHA01929    78 APAAPPAAGAALPeaLEVPPPPAFTPNGEIVGTLAGNLEGDPQLAPS 124
PDZ1_hSTXBP4-PDZ2_GgSTXBP4-like cd06698
PDZ1 domain of human syntaxin-binding protein 4 (STXBP4), PDZ2 domain of Gallus gallus ...
 4539-4602 1.92e-04

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: 43.06  E-value: 1.92e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1201829585 4539 GLGIRVVGGKEIPGssgEIGAYIAKVLPGGSAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQNII 4602
Cdd:cd06698     12 GLGLSIVGGINRPE---GPMVFIQEVIPGGDCYKDGRLRPGDQLVSINKESLIGVTLEEAKSIL 72
C2B_Synaptotagmin-4 cd08404
C2 domain second repeat present in Synaptotagmin 4; Synaptotagmin is a membrane-trafficking ...
 5026-5151 1.99e-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: 44.73  E-value: 1.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 5026 GEIKIALKKEMKTDgeQLIVEILQCRNITykfKSPDHLP-DLYVKLYVvnISTQKRVIKKKTRVCRHDREPSFNETFRFS 5104
Cdd:cd08404      2 GELLLSLCYQPTTN--RLTVVVLKARHLP---KMDVSGLaDPYVKVNL--YYGKKRISKKKTHVKKCTLNPVFNESFVFD 74

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1201829585 5105 LSPAG--HSLQILLVSNGGKFMKKTLIGEA-----------YVWLDKVD-LRKRIVNWHKL 5151
Cdd:cd08404     75 IPSEEleDISVEFLVLDSDRVTKNEVIGRLvlgpkasgsggHHWKEVCNpPRRQIAEWHML 135
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 177-319 2.06e-04

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: 47.72  E-value: 2.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  177 EEAGRKQKVTQKDQGKPEEQRGLAKHPSQQQSPkLVQQQGPVKPTPQQTESSKPVPQQQQPGEPKQI--------QKPGP 248
Cdd:pfam09770  200 EAAMRAQAKKPAQQPAPAPAQPPAAPPAQQAQQ-QQQFPPQIQQQQQPQQQPQQPQQHPGQGHPVTIlqrpqspqPDPAQ 278

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1201829585  249 SHQGDSKVEQPKQPPqPRGPQKSQLQQ-----SEPTKPVQQQTSAKPSVGPTKPLPQQPDSAktSSQASPPTKPSS 319
Cdd:pfam09770  279 PSIQPQAQQFHQQPP-PVPVQPTQILQnpnrlSAARVGYPQNPQPGVQPAPAHQAHRQQGSF--GRQAPIITHPQQ 351
PHA03269 PHA03269
envelope glycoprotein C; Provisional
 258-366 2.23e-04

envelope glycoprotein C; Provisional


Pssm-ID: 165527 [Multi-domain]  Cd Length: 566  Bit Score: 47.42  E-value: 2.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  258 QPKQPPQPRGPQKSQLQQSEPTKPVQQQTSAKP--SVGPTKPLPQQPDSAKTssqaspPTKPSSQQSGPVKQPSQQPARQ 335
Cdd:PHA03269    22 LNTNIPIPELHTSAATQKPDPAPAPHQAASRAPdpAVAPTSAASRKPDLAQA------PTPAASEKFDPAPAPHQAASRA 95

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1201829585  336 GGP-VKPSAQQAgpPKQQPGSEKPSAQQTGPA 366
Cdd:PHA03269    96 PDPaVAPQLAAA--PKPDAAEAFTSAAQAHEA 125
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
 205-302 2.32e-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: 45.17  E-value: 2.32e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585   205 QQQSPKLVQQQGPVKPTPQQteSSKPVPQQQQPGEPKQIQKPGPSHQG--DSKVEQPKQPPQPRGPQKSQ-LQQSEPTKP 281
Cdd:smart00818   36 HHQIIPVSQQHPPTHTLQPH--HHIPVLPAQQPVVPQQPLMPVPGQHSmtPTQHHQPNLPQPAQQPFQPQpLQPPQPQQP 113

                            90       100
                    ....*....|....*....|.
gi 1201829585   282 VQQQtsakPSVGPTKPLPQQP 302
Cdd:smart00818  114 MQPQ----PPVHPIPPLPPQP 130
C2A_Synaptotagmin-14_16 cd08389
C2A domain first repeat present in Synaptotagmins 14 and 16; Synaptotagmin 14 and 16 are ...
 5041-5141 2.33e-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: 44.15  E-value: 2.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 5041 EQLIVEILQCRNITYKFKSPdhlpdlyvklyvvNISTQKRV----IKK---KTRVcRHDREPSFNETFRFS-LSP---AG 5109
Cdd:cd08389     16 RKLTVTVIRAQDIPTKDRGG-------------ASSWQVHLvllpSKKqraKTKV-QRGPNPVFNETFTFSrVEPeelNN 81

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1201829585 5110 HSLQILLVSNgGKFMKKTLIGEAYVWLDKVDL 5141
Cdd:cd08389     82 MALRFRLYGV-ERMRKERLIGEKVVPLSQLNL 112
PDZ_GOPC-like cd06800
PDZ domain of Golgi-associated PDZ and coiled-coil motif-containing protein (GOPC), and ...
 4539-4613 2.61e-04

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: 42.74  E-value: 2.61e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1201829585 4539 GLGIRVVGGKE--IPgssgeigAYIAKVLPGGSAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQNIIIQQCGEAEICV 4613
Cdd:cd06800     12 GLGISITGGKEhgVP-------ILISEIHEGQPADRCGGLYVGDAILSVNGIDLRDAKHKEAVTILSQQRGEITLEV 81
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
 301-438 2.78e-04

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


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 45.03  E-value: 2.78e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  301 QPDSAKTSSQASPPTKPSSQQSGP-VKQPSQQPARQGGPVKPSAQQAGPPKQQPGSEKPSAQQTGPAKQ---PLQTGPGK 376
Cdd:pfam15240   17 QSSSEDVSQEDSPSLISEEEGQSQqGGQGPQGPPPGGFPPQPPASDDPPGPPPPGGPQQPPPQGGKQKPqgpPPQGGPRP 96

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1201829585  377 PPLQQTGPvkqvPPQAGPTKPSSQTAGATKSVAQQPGLTKP-PGPQSGPEKPSQQKQASAAQP 438
Cdd:pfam15240   97 PPGKPQGP----PPQGGNQQQGPPPPGKPQGPPPQGGGPPPqGGNQQGPPPPPPGNPQGPPQR 155
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
197-438 3.05e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 47.18  E-value: 3.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  197 RGLAKHPSQQQSpklvqQQGPvkPTPQQTESSKPVPQQQQPGEPKQIQKPGPSHQGDSKVEQPKQPPQPRGPqksqlqqs 276
Cdd:PRK12323   359 RMLAFRPGQSGG-----GAGP--ATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAP-------- 423

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  277 eptkpvqqqTSAKPSVGPTKPLPQQPDSAKTSSQASPPTKPssqqsgPVKQPSQQPARQGGPVKPSAQQAGPPKQQPGSE 356
Cdd:PRK12323   424 ---------ARRSPAPEALAAARQASARGPGGAPAPAPAPA------AAPAAAARPAAAGPRPVAAAAAAAPARAAPAAA 488

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  357 KPSAQQTGPakqPLQTGPGKPPlqQTGPVKQVPPQAGPTKPSSQTAGATKSVAQQPGLTKPPGPQSGPEKPSQQKQASAA 436
Cdd:PRK12323   489 PAPADDDPP---PWEELPPEFA--SPAPAQPDAAPAGWVAESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAP 563


                   ..
gi 1201829585  437 QP 438
Cdd:PRK12323   564 RP 565
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 183-361 3.40e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 47.29  E-value: 3.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  183 QKVTQKDQGKPEEQRGLAKHPSQQQSPKLVQQQGPVKPTPQQTESSKPVP-QQQQPGEPKQIQKPGPSHQGDSKVEQPKQ 261
Cdd:PRK07764   623 APAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKaGGAAPAAPPPAPAPAAPAAPAGAAPAQPA 702

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  262 PPQPRGPQKSQLQQSEPTKPVQQQTSAKPSVGPTK--PLPQQPDsaktsSQASPPTKPSSQQSGPVKQPSQQPARQGGPV 339
Cdd:PRK07764   703 PAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDpvPLPPEPD-----DPPDPAGAPAQPPPPPAPAPAAAPAAAPPPS 777

                          170       180
                   ....*....|....*....|..
gi 1201829585  340 KPSAQQAGPPKQQPGSEKPSAQ 361
Cdd:PRK07764   778 PPSEEEEMAEDDAPSMDDEDRR 799
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
 299-445 3.46e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 47.17  E-value: 3.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  299 PQQPDSAKTSSQASPPTKPSSQQSGpvkQPSQQPARQGGPVKPSAQQAGPPKQQPGSEKPSAQQTGPAKQPLQtgpgkPP 378
Cdd:PRK07994   361 PAAPLPEPEVPPQSAAPAASAQATA---APTAAVAPPQAPAVPPPPASAPQQAPAVPLPETTSQLLAARQQLQ-----RA 432

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1201829585  379 LQQTGPVKQVPPQAGPTKP--SSQTAGATKSVAQQPGLTKPPGPQSGPEKPSQqkQASAAQPVESTPKK 445
Cdd:PRK07994   433 QGATKAKKSEPAAASRARPvnSALERLASVRPAPSALEKAPAKKEAYRWKATN--PVEVKKEPVATPKA 499
PDZ3_FL-whirlin-like cd06742
PDZ domain 3 of the full-length isoform of whirlin, PDZ domain 1 of the short isoform of ...
 4540-4602 3.53e-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: 42.73  E-value: 3.53e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1201829585 4540 LGIRVVGGkeipGSSGEIGAYIAKVLPGGSAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQNII 4602
Cdd:cd06742     13 LGIAIEGG----ANTKQPLPRVINIQRGGSAHNCGGLKVGHVILEVNGTSLRGLEHREAARLI 71
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
201-333 3.81e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 46.69  E-value: 3.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  201 KHPSQQQSPKLVQqqgpvkPTPQQTESSKPVPQQQQPGEPKQIQKPGPshqgdskveQPKQPPQPRGPQKSqLQQSEPTk 280
Cdd:PRK14971   373 RGPKQHIKPVFTQ------PAAAPQPSAAAAASPSPSQSSAAAQPSAP---------QSATQPAGTPPTVS-VDPPAAV- 435

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1201829585  281 PVQQQTSAKPSVGPTKPLPQQPDSAKTSSQASPPTKpssqqsGPVKQPSQQPA 333
Cdd:PRK14971   436 PVNPPSTAPQAVRPAQFKEEKKIPVSKVSSLGPSTL------RPIQEKAEQAT 482
PHA03247 PHA03247
large tegument protein UL36; Provisional
 195-444 3.84e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.24  E-value: 3.84e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  195 EQRGLAKHP----SQQQSPKLVQQQGPVKPtPQQTESSKPVPQQQQPGEPKQIQKPGPSHQGDSKVEQP--KQPPQPRGP 268
Cdd:PHA03247   239 ERRVVISHPlrgdIAAPAPPPVVGEGADRA-PETARGATGPPPPPEAAAPNGAAAPPDGVWGAALAGAPlaLPAPPDPPP 317

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  269 QKSqlqqSEPTKPVQQQTSAKPSVGPTkPLPQQPDSAKTSSQASPP-TKPSSQQ---SGPVKQPSQQPARQggpVKPSAQ 344
Cdd:PHA03247   318 PAP----AGDAEEEDDEDGAMEVVSPL-PRPRQHYPLGFPKRRRPTwTPPSSLEdlsAGRHHPKRASLPTR---KRRSAR 389

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  345 QAGPP--KQQPGSEKPSAQQTGPAKQPLqtgPGKPPlqqtGPVKQVPPQAGPTkPSSQtagatksvaqqPGLTKPPGPQS 422
Cdd:PHA03247   390 HAATPfaRGPGGDDQTRPAAPVPASVPT---PAPTP----VPASAPPPPATPL-PSAE-----------PGSDDGPAPPP 450

                          250       260
                   ....*....|....*....|..
gi 1201829585  423 GPEKPSQQKQASAAQPVESTPK 444
Cdd:PHA03247   451 ERQPPAPATEPAPDDPDDATRK 472
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 263-395 3.88e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 47.02  E-value: 3.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  263 PQPRGPQKSQLQQSEPTKPVQQQTSAKP-SVGPTKPLPQQPDSAKTSSQASPPTKPssqQSGPVKQPsqqPARQGGPVKP 341
Cdd:PRK14951   366 PAAAAEAAAPAEKKTPARPEAAAPAAAPvAQAAAAPAPAAAPAAAASAPAAPPAAA---PPAPVAAP---AAAAPAAAPA 439

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1201829585  342 SAQQAGPPKQQPgsekPSAQQTGPAKQPLQTGPGKPPLQQTGPVKQVPPQAGPT 395
Cdd:PRK14951   440 AAPAAVALAPAP----PAQAAPETVAIPVRVAPEPAVASAAPAPAAAPAAARLT 489
C2B_Synaptotagmin-15 cd08409
C2 domain second repeat present in Synaptotagmin 15; Synaptotagmin is a membrane-trafficking ...
 5026-5151 4.66e-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: 43.48  E-value: 4.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 5026 GEIKIALKKEMKTDgeQLIVEILQCRNItyKFKSPDHLpDLYVKLYVVNISTQkrVIKKKTRVCRHDREPSFNETFRFSL 5105
Cdd:cd08409      2 GDIQISLTYNPTLN--RLTVVVLRARGL--RQLDHAHT-SVYVKVSLMIHNKV--VKTKKTEVVDGAASPSFNESFSFKV 74

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1201829585 5106 SPAGHSLQILLVS--NGGKFMKKTLIGEAYV-------------WLDKV-DLRKRIVNWHKL 5151
Cdd:cd08409     75 TSRQLDTASLSLSvmQSGGVRKSKLLGRVVLgpfmyargkelehWNDMLsKPKELIKRWHAL 136
C2_cPLA2 cd04036
C2 domain present in cytosolic PhosphoLipase A2 (cPLA2); A single copy of the C2 domain is ...
 5042-5108 4.73e-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: 4.73e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1201829585 5042 QLIVEILQCRNIT-YKFKSPdhlPDLYVKLYVVNISTQKrvikKKTRVCRHDREPSFNETFRFSLSPA 5108
Cdd:cd04036      1 LLTVRVLRATNITkGDLLST---PDCYVELWLPTASDEK----KRTKTIKNSINPVWNETFEFRIQSQ 61
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 536-900 5.11e-04

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: 46.68  E-value: 5.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  536 SPQSQPGQKKDASPKPDpsQQADSKKPVPQKKQPSMPGSPPVKSKQTDAEPSDTFQQIDPTPKSDQAKPTQAEEKQNQPS 615
Cdd:pfam03154  112 SPSEGEGESSDGRSVND--EGSSDPKDIDQDNRSTSPSIPSPQDNESDSDSSAQQQILQTQPPVLQAQSGAASPPSPPPP 189

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  616 VQKPTTDTVPTSAAPGVKQDLADPRPPLTQQKVTDSPKPETTKPPADTHPAGDKPDSKPLPQVSRQKSDPKLASQSGSKS 695
Cdd:pfam03154  190 GTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPLPQP 269

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  696 DAKTQKAVEPAQVRDDPKKLQTKSAPKPDTKPaPKGPQAGTGPKPMSAQPAPQPQQPQKTPEQSRRFSLNLGGITDVP-- 773
Cdd:pfam03154  270 SLHGQMPPMPHSLQTGPSHMQHPVPPQPFPLT-PQSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPpa 348

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  774 -------KPQPTTPQETVTGKL------FGFGASIFSQASSL-ISTAGQPGSQTSGPAPPAAKQPQPPSQPTASQAPPKE 839
Cdd:pfam03154  349 plsmphiKPPPTTPIPQLPNPQshkhppHLSGPSPFQMNSNLpPPPALKPLSSLSTHHPPSAHPPPLQLMPQSQQLPPPP 428

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1201829585  840 A-----TQAQPLPKAAPTKKETKPLASEKLEPMAADSTLTTKGSDLEKKPSLAKDSKPQAAEAKKP 900
Cdd:pfam03154  429 AqppvlTQSQSLPPPAASHPPTSGLHQVPSQSPFPQHPFVPGGPPPITPPSGPPTSTSSAMPGIQP 494
Pneumo_att_G pfam05539
Pneumovirinae attachment membrane glycoprotein G;
259-442 5.14e-04

Pneumovirinae attachment membrane glycoprotein G;


Pssm-ID: 114270 [Multi-domain]  Cd Length: 408  Bit Score: 46.19  E-value: 5.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  259 PKQPPQPRGPQKSQLQQ-SEPTKPVQQQTSAKPSVGPTKPLPQQPDSAKTSSQASPPTKPSSQQSGPVKQPSQQPARQGG 337
Cdd:pfam05539  195 PQSQPATQGHQTATANQrLSSTEPVGTQGTTTSSNPEPQTEPPPSQRGPSGSPQHPPSTTSQDQSTTGDGQEHTQRRKTP 274

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  338 PVKPSAQQagppkqqpgsekPSAQQTGPAKQPLQTGpGKPPLQQTGPVkQVPPQAGPTKPSSQTAGATKSVAQQPGLTKP 417
Cdd:pfam05539  275 PATSNRRS------------PHSTATPPPTTKRQET-GRPTPRPTATT-QSGSSPPHSSPPGVQANPTTQNLVDCKELDP 340

                          170       180       190
                   ....*....|....*....|....*....|
gi 1201829585  418 PGPQS-----GPEKPSQQKQASAAQPVEST 442
Cdd:pfam05539  341 PKPNSicygvGIYNEALPRGCDIVVPLCST 370
PDZ4_INAD-like cd23065
PDZ domain 4 of inactivation-no-after-potential D (INAD), and related domains; PDZ (PSD-95 ...
 4535-4613 5.20e-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: 41.73  E-value: 5.20e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1201829585 4535 VSGNGLGIRVVGGKEipgsSGEIGAYIAKVLPGGSAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQNIIIQQCGEAEICV 4613
Cdd:cd23065      6 TDKSPLGVSVVGGKN----HVTTGCIITHIYPNSIVAADKRLKVFDQILDINGTKVHVMTTLKVHQLFHKTYEKAVTLV 80
PDZ1_harmonin cd06737
PDZ domain 1 of harmonin isoforms a, b, and c, and related domains; PDZ (PSD-95 (Postsynaptic ...
 4523-4602 5.30e-04

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: 41.86  E-value: 5.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4523 RLKLLRDPKDHtvsGNGLGIRVVGGKEIpgssgEIGAYIAKVLPGGSAEQTGkLIEGMQVLEWNGIPLTGKTYEEVQNII 4602
Cdd:cd06737      1 KLRLVRLDRRG---PESLGFSVRGGLEH-----GCGLFVSHVSPGSQADNKG-LRVGDEIVRINGYSISQCTHEEVINLI 71
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
 171-398 5.41e-04

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 46.46  E-value: 5.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  171 DSDAAHEEAGRKQKVTQKDQGKPEEQRGLAKHPSQQQSP-----KLVQQQGPVKPTPQQT----ESSKPVPQQQQPGEPK 241
Cdd:PLN03209   332 ESDAADGPKPVPTKPVTPEAPSPPIEEEPPQPKAVVPRPlspytAYEDLKPPTSPIPTPPssspASSKSVDAVAKPAEPD 411

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  242 QIQKPG-PSHQGDSKVEQ-PKQPPQPRGPQKSQLQQSEPTKPV-QQQTSAKPSVGPTKPLPQQPDSA---KTSSQASPPT 315
Cdd:PLN03209   412 VVPSPGsASNVPEVEPAQvEAKKTRPLSPYARYEDLKPPTSPSpTAPTGVSPSVSSTSSVPAVPDTApatAATDAAAPPP 491

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  316 KPSSQQSGPVKQPSQQPARQGGPVKPSAQQAGPPKQQPGSEKPSAQQTGPAKQPLQTGPGKPPLQQTGPVKQVPPQAGPT 395
Cdd:PLN03209   492 ANMRPLSPYAVYDDLKPPTSPSPAAPVGKVAPSSTNEVVKVGNSAPPTALADEQHHAQPKPRPLSPYTMYEDLKPPTSPT 571


                   ...
gi 1201829585  396 kPS 398
Cdd:PLN03209   572 -PS 573
C2B_Synaptotagmin-14_16 cd08408
C2 domain second repeat present in Synaptotagmins 14 and 16; Synaptotagmin 14 and 16 are ...
 4723-4850 6.13e-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: 43.13  E-value: 6.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4723 EIQLQINYDKHLGNLIIHILQARNLAPRDNNGYSDPFVKVYLLPGRGAEYKR-RTKYVQKSLNPEWNQTVIYKnISTEQL 4801
Cdd:cd08408      3 ELLLGLEYNALTGRLSVEVIKGSNFKNLAMNKAPDTYVKLTLLNSDGQEISKsKTSIRRGQPDPEFKETFVFQ-VALFQL 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1201829585 4802 KKKTLEVTVWDYDRFSSNDFLGEVLIDLSSVSQlDNTPRWYPLKEQSEN 4850
Cdd:cd08408     82 SEVTLMFSVYNKRKMKRKEMIGWFSLGLNSSGE-EEEEHWNEMKESKGQ 129
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
 1410-1663 6.30e-04

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 46.58  E-value: 6.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 1410 EKDLTRESSKKDTISQESPPSPSDLAKLESTVLSILEAQASTLADEKSVKRKELHEAYSDQTKDQHKTKPLPV--TPESY 1487
Cdd:PTZ00108  1142 EEQEEVEEKEIAKEQRLKSKTKGKASKLRKPKLKKKEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDnkKSNSS 1221

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 1488 SSDEED-------LESIQEGERTIAADGKGGSSSRTDYKEEGGGDDTPARRQRYDSVEDSSESENSPVPRRKRRASVGSS 1560
Cdd:PTZ00108  1222 GSDQEDdeeqktkPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPDGESNGGSK 1301

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 1561 SSDEYKQDDsqgsgdeEDFIRKQIIEMSADEDASgseddefirnqLKEISVTESQKKEEVKSKAKGTAGKHRRMARKSSA 1640
Cdd:PTZ00108  1302 PSSPTKKKV-------KKRLEGSLAALKKKKKSE-----------KKTARKKKSKTRVKQASASQSSRLLRRPRKKKSDS 1363

                          250       260
                   ....*....|....*....|...
gi 1201829585 1641 GYDEDAGRRHSWHDDDDETFDES 1663
Cdd:PTZ00108  1364 SSEDDDDSEVDDSEDEDDEDDED 1386
PDZ3_LNX1_2-like cd06679
PDZ domain 3 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ ...
 4540-4614 6.33e-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: 41.85  E-value: 6.33e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1201829585 4540 LGIRVVGGKEIPgsSGEIGAYIAKVLPGGSAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQNIIIQQCGEAEICVR 4614
Cdd:cd06679     13 LGISVAGGRGSR--RGDLPIYVTNVQPDGCLGRDGRIKKGDVLLSINGISLTNLSHSEAVAVLKASAASSSIVLK 85
C2B_SLP_1-2-3-4 cd04020
C2 domain second repeat present in Synaptotagmin-like proteins 1-4; All Slp members basically ...
 5026-5104 6.60e-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: 6.60e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 5026 GEIKIALK----------KEMKTDGEQLIVEILQCRNITYKfKSPDHLpDLYVKLYVvnISTQKRVIKKKTRVCRHDREP 5095
Cdd:cd04020      2 GELKVALKyvppesegalKSKKPSTGELHVWVKEAKNLPAL-KSGGTS-DSFVKCYL--LPDKSKKSKQKTPVVKKSVNP 77


                   ....*....
gi 1201829585 5096 SFNETFRFS 5104
Cdd:cd04020     78 VWNHTFVYD 86
PBP1 COG5180
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ...
 253-437 6.87e-04

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


Pssm-ID: 444064 [Multi-domain]  Cd Length: 548  Bit Score: 45.82  E-value: 6.87e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  253 DSKVEQPKQPPQPRGPQKSQlQQSEPTKPVQQQTSAKPSVGPTKPLPQQPDSAKTSSQASPPTKPSSQQSGPVKQPSQQP 332
Cdd:COG5180    190 DALKDSPEKLDRPKVEVKDE-AQEEPPDLTGGADHPRPEAASSPKVDPPSTSEARSRPATVDAQPEMRPPADAKERRRAA 268

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  333 ARQGGPVKPSAQQAGPPKQQPGSEKPSA------QQTGPAKQPLQTGPGKPPLQQTGPVKQVPPQAGPTKPSSQTAGATk 406
Cdd:COG5180    269 IGDTPAAEPPGLPVLEAGSEPQSDAPEAetarpiDVKGVASAPPATRPVRPPGGARDPGTPRPGQPTERPAGVPEAASD- 347

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1201829585  407 svAQQPGLTKPPGPQSGPEKPSQQKQASAAQ 437
Cdd:COG5180    348 --AGQPPSAYPPAEEAVPGKPLEQGAPRPGS 376
PDZ2_GRIP1-2-like cd06681
PDZ domain 2 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
 4564-4607 7.18e-04

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: 41.45  E-value: 7.18e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1201829585 4564 VLPGGSAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQNiIIQQCG 4607
Cdd:cd06681     37 VRPGGPADREGTIKPGDRLLSVDGISLHGATHAEAMS-ILKQCG 79
PDZ3_DLG5-like cd06767
PDZ domain 3 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density ...
 4529-4607 7.21e-04

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: 41.54  E-value: 7.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4529 DPKDHTV--SGNGLGIRVVGGKeipgsSGeiGAYIAKVLPGGSAEQTGkLIEGMQVLEWNGIPLTGKTYEEVQNIIIQQC 4606
Cdd:cd06767      2 EPRHVSIekGSEPLGISIVSGE-----NG--GIFVSSVTEGSLAHQAG-LEYGDQLLEVNGINLRNATEQQAALILRQCG 73


                   .
gi 1201829585 4607 G 4607
Cdd:cd06767     74 D 74
dnaA PRK14086
chromosomal replication initiator protein DnaA;
268-446 7.21e-04

chromosomal replication initiator protein DnaA;


Pssm-ID: 237605 [Multi-domain]  Cd Length: 617  Bit Score: 45.97  E-value: 7.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  268 PQKSQLQQSEPTKPVQQQTSAKPSVGPTKPLPQQPDSAKTSSQASPPTKPSSQQSGPVKQPSQQPARQgGPVKPSAQQAG 347
Cdd:PRK14086    68 PIISETLSRELGRPIRIAITVDPSAGEPAPPPPHARRTSEPELPRPGRRPYEGYGGPRADDRPPGLPR-QDQLPTARPAY 146

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  348 PPKQQ---PGSEKPSAQQTGPAKQPLQTGPGKPPlqqTGPVKQVPPQAGPTKPSSQTAGATKSVAQQPGLTKP------- 417
Cdd:PRK14086   147 PAYQQrpePGAWPRAADDYGWQQQRLGFPPRAPY---ASPASYAPEQERDREPYDAGRPEYDQRRRDYDHPRPdwdrprr 223

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1201829585  418 -----PGPQSGPEKPSQQKQASAAQPVESTPKKT 446
Cdd:PRK14086   224 drtdrPEPPPGAGHVHRGGPGPPERDDAPVVPIR 257
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 534-918 7.41e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 46.32  E-value: 7.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  534 KPSPQSQPGQKKDASPKPDPSQQADSKKPVPQKKQPSMPGSPPvkskqtdaepsdtfqqidPTPKSDQAKPTQAEekqnQ 613
Cdd:PHA03307    85 RSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPP------------------PSPAPDLSEMLRPV----G 142

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  614 PSVQKPTTDTVPTSAAPGVKQdlADPRPPLTQQKVTDSPKPETTKPPADTHPAGDKPDSKPLPQVSRQKSDPKLASQSGS 693
Cdd:PHA03307   143 SPGPPPAASPPAAGASPAAVA--SDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSP 220

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  694 KS-DAKTQKAVEPAQVRDDPKKLQTKSAPKPDTKPAPKGPQAGTGPKPMSAQPAPQPQQPQKTPEQSRRfslnlGGITDV 772
Cdd:PHA03307   221 APaPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSS-----SPRERS 295

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  773 PKPQPTTPQetvtgklfgfGASIFSQASSLISTAGQPGSQTSGPAPPAAKQPQPPSQPTASQA-PPKEATQAQPLPKAAP 851
Cdd:PHA03307   296 PSPSPSSPG----------SGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSrSPSPSRPPPPADPSSP 365

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1201829585  852 TKKETKPLASEKLEPMAADSTLTTKGSDLEKKPSLAKDSKPQAAEAKKPAELSEQEKASQPKVSCPL 918
Cdd:PHA03307   366 RKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATGRFPAGRPRPSPLDAGAASGAFYARYPL 432
C2B_Synaptotagmin-13 cd08407
C2 domain second repeat present in Synaptotagmin 13; Synaptotagmin is a membrane-trafficking ...
 4721-4844 7.71e-04

C2 domain second repeat present in Synaptotagmin 13; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Synaptotagmin 13, a member of class 6 synaptotagmins, is located in the brain. It functions are unknown. It, like synaptotagmins 8 and 12, does 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: 176052 [Multi-domain]  Cd Length: 138  Bit Score: 43.05  E-value: 7.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4721 TGEIQLQINYDKHLGNLIIHILQARNLAPR-----DNNGYSdpfVKVYLLPGRGAEYKRRTKYVQKSLNPEWNQTVIYKn 4795
Cdd:cd08407      1 TGEVLLSISYLPAANRLLVVVIKAKNLHSDqlkllLGIDVS---VKVTLKHQNAKLKKKQTKRAKHKINPVWNEMIMFE- 76

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1201829585 4796 ISTEQLKKKTLEVTVWDYDRFSSNDFLGEVLIDLSSV--------SQLDNtPR-----WYPL 4844
Cdd:cd08407     77 LPSELLAASSVELEVLNQDSPGQSLPLGRCSLGLHTSgterqhweEMLDN-PRrqiamWHQL 137
PDZ1_FL-whirlin cd06740
PDZ domain 1 of the full-length isoform of whirlin and related domains; PDZ (PSD-95 ...
 4523-4602 8.97e-04

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: 41.20  E-value: 8.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4523 RLKLLRDPKDHTvsgnGLGIRVVGGKEipgsSGeIGAYIAKVLPGGSAEQTGkLIEGMQVLEWNGIPLTGKTYEEVQNII 4602
Cdd:cd06740      2 RQVTLKRSKSHE----GLGFSIRGGAE----HG-VGIYVSLVEPGSLAEKEG-LRVGDQILRVNDVSFEKVTHAEAVKIL 71
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
 200-307 9.22e-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: 43.24  E-value: 9.22e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585   200 AKHPSQQQSPkLVQQQGPVKPTPQQTESSKPVPQQQQPGEPKQIQKPGPshqgdskvEQPKQPPQPRGPQKSQLQQS--E 277
Cdd:smart00818   63 AQQPVVPQQP-LMPVPGQHSMTPTQHHQPNLPQPAQQPFQPQPLQPPQP--------QQPMQPQPPVHPIPPLPPQPplP 133

                            90       100       110
                    ....*....|....*....|....*....|
gi 1201829585   278 PTKPVQQQtsakPSVGPTKPLPQQPDSAKT 307
Cdd:smart00818  134 PMFPMQPL----PPLLPDLPLEAWPATDKT 159
PHA03377 PHA03377
EBNA-3C; Provisional
 217-443 9.26e-04

EBNA-3C; Provisional


Pssm-ID: 177614 [Multi-domain]  Cd Length: 1000  Bit Score: 45.81  E-value: 9.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  217 PVKPTPQQTESSKPVPQQQQpGEPKQiqkPGPSHQGDSKVEQPKQPPQPRG-------PQKSQLQQSEPTKP-------- 281
Cdd:PHA03377   428 PVKRTLVKTSGRSDEAEQAQ-STPER---PGPSDQPSVPVEPAHLTPVEHTtvilhqpPQSPPTVAIKPAPPpsrrrrga 503

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  282 -------------VQQQTSAKPSVGPTKPLPQQPDSAKTSSQ-----ASPPTKPSSQQSGPVKQPSQQPARQGGPVKpSA 343
Cdd:PHA03377   504 cvvydddiievidVETTEEEESVTQPAKPHRKVQDGFQRSGRrqkraTPPKVSPSDRGPPKASPPVMAPPSTGPRVM-AT 582

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  344 QQAGPPKQQPGSEKPSAQQTGPAKQPlQTGPGKPPLQQTGPVKQVPPQ----------AGPTKPSSQTAGATKSVAQQPG 413
Cdd:PHA03377   583 PSTGPRDMAPPSTGPRQQAKCKDGPP-ASGPHEKQPPSSAPRDMAPSVvrmflrerllEQSTGPKPKSFWEMRAGRDGSG 661

                          250       260       270
                   ....*....|....*....|....*....|
gi 1201829585  414 LTKPPGPQSGPEKPSQQKQASAAQPVESTP 443
Cdd:PHA03377   662 IQQEPSSRRQPATQSTPPRPSWLPSVFVLP 691
C2A_RasGAP cd08383
C2 domain (first repeat) of Ras GTPase activating proteins (GAPs); RasGAPs suppress Ras ...
 4737-4844 9.53e-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: 42.25  E-value: 9.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4737 LIIHILQARNLAPRdnnGYSDPFVKVYLlpgrGAEYKRRTKYVQKsLNPEWNQTVIYKNISTEqLKKKTLEVTVWDYDRF 4816
Cdd:cd08383      2 LRLRILEAKNLPSK---GTRDPYCTVSL----DQVEVARTKTVEK-LNPFWGEEFVFDDPPPD-VTFFTLSFYNKDKRSK 72

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1201829585 4817 SSNDFLGEVlidlsSVSQLDN---TPRWYPL 4844
Cdd:cd08383     73 DRDIVIGKV-----ALSKLDLgqgKDEWFPL 98
PDZ3_MUPP1-like cd06791
PDZ domain 3 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ...
 4537-4598 1.01e-03

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: 41.06  E-value: 1.01e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1201829585 4537 GNGLGIRVVGGKEIPGSSGEIGAYIAKVLPGGSAEQTGKLIEGMQVLEWNGIPLTGKTYEEV 4598
Cdd:cd06791     11 EQGLGITIAGYVGEKASGELSGIFVKSIIPGSAADQDGRIQVNDQIIAVDGVNLQGFTNQEA 72
C2A_Synaptotagmin-4-11 cd08388
C2A domain first repeat present in Synaptotagmins 4 and 11; Synaptotagmin is a ...
 5043-5141 1.04e-03

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: 42.34  E-value: 1.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 5043 LIVEILQCRNITYKfKSPDHLPDLYVKLYVVNiSTQKRVikkKTRVCRHDREPSFNETFRFSLSPAGH----SLQILLVS 5118
Cdd:cd08388     18 LLVNIIECRDLPAM-DEQSGTSDPYVKLQLLP-EKEHKV---KTRVLRKTRNPVYDETFTFYGIPYNQlqdlSLHFAVLS 92

                           90       100
                   ....*....|....*....|...
gi 1201829585 5119 NgGKFMKKTLIGEAYVWLDKVDL 5141
Cdd:cd08388     93 F-DRYSRDDVIGEVVCPLAGADL 114
PBP1 COG5180
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ...
 264-438 1.07e-03

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


Pssm-ID: 444064 [Multi-domain]  Cd Length: 548  Bit Score: 45.44  E-value: 1.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  264 QPRGPQKSQLQQSEPTKPVQQQTSAKPSvgpTKPLPQQPDSAKTSSQASPPTK----PSSQQSGPVKQPSQQPARQGGPV 339
Cdd:COG5180    172 STLPPPAEKLDKVLTEPRDALKDSPEKL---DRPKVEVKDEAQEEPPDLTGGAdhprPEAASSPKVDPPSTSEARSRPAT 248

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  340 KPSAQQAGPPKqqpgsEKPSAQQTGPAKQPLQTGPGKPPLQQTGPVKQVPPQAGPTKPSSQTAGATKSVAQQPGLTKPPG 419
Cdd:COG5180    249 VDAQPEMRPPA-----DAKERRRAAIGDTPAAEPPGLPVLEAGSEPQSDAPEAETARPIDVKGVASAPPATRPVRPPGGA 323

                          170
                   ....*....|....*....
gi 1201829585  420 PQSGPEKPSQQKQASAAQP 438
Cdd:COG5180    324 RDPGTPRPGQPTERPAGVP 342
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 279-695 1.08e-03

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: 45.38  E-value: 1.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  279 TKPVQQQTSAKPSVGPTKPLPQQpdsaktssQASPPTKPSSQQSGPVKQPSQQPARQGGPVKPSAQQAGPPKQ----QPG 354
Cdd:pfam09606   55 KKAAQQQQPQGGQGNGGMGGGQQ--------GMPDPINALQNLAGQGTRPQMMGPMGPGPGGPMGQQMGGPGTasnlLAS 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  355 SEKPSAQQT--GPAKQPLQTGPGKPPLQQTGPVKQVPPQAGPTKPSSQTAGatksvaQQPGLTKPPGPQSGPEKPSQQKQ 432
Cdd:pfam09606  127 LGRPQMPMGgaGFPSQMSRVGRMQPGGQAGGMMQPSSGQPGSGTPNQMGPN------GGPGQGQAGGMNGGQQGPMGGQM 200

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  433 ASA----AQPVESTPKKtfcplctttelllHVPEKANYNTCTQCHTVV-----CSLCGFNPNPHITEIKEWLCLNCQMQR 503
Cdd:pfam09606  201 PPQmgvpGMPGPADAGA-------------QMGQQAQANGGMNPQQMGgapnqVAMQQQQPQQQGQQSQLGMGINQMQQM 267

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  504 ALGGDLASGHGpGPQLPPPKQKTPTPTSTAKPSPQSQPgqKKDASPKPDPSQQADSKKPVPQKKQPSMPGSPpvkSKQTD 583
Cdd:pfam09606  268 PQGVGGGAGQG-GPGQPMGPPGQQPGAMPNVMSIGDQN--NYQQQQTRQQQQQQGGNHPAAHQQQMNQSVGQ---GGQVV 341

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  584 AEPsdtFQQIDPTPKSDQAKPTQAEEKQNQPSVQKPTTDTVPTSAAPGVKQDLADPRPPltqQKVTDSPKPETTKPPAdT 663
Cdd:pfam09606  342 ALG---GLNHLETWNPGNFGGLGANPMQRGQPGMMSSPSPVPGQQVRQVTPNQFMRQSP---QPSVPSPQGPGSQPPQ-S 414

                          410       420       430
                   ....*....|....*....|....*....|....*..
gi 1201829585  664 HPAGDKPD----SKPLPQVSRQKSDPK-LASQSGSKS 695
Cdd:pfam09606  415 HPGGMIPSpaliPSPSPQMSQQPAQQRtIGQDSPGGS 451
DUF4045 pfam13254
Domain of unknown function (DUF4045); This presumed domain is functionally uncharacterized. ...
 536-710 1.25e-03

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: 44.77  E-value: 1.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  536 SPQSQPGQKKDASPKpDPSQQADSKKPVPQKKQPSMPGSPPVKSKQTDAEPSDTFQqiDPTPKSDQAKPTQAEEKQNQPS 615
Cdd:pfam13254  219 KSPSVSGISADSSPT-KEEPSEEADTLSTDKEQSPAPTSASEPPPKTKELPKDSEE--PAAPSKSAEASTEKKEPDTESS 295

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  616 VQKPTTDTVPTSAAPGVKQDLADPRPPLTQQKVTDSPKPETtkPPADTHpAGDKpdSKPLPQVSRQKSDPKLASQSGSKS 695
Cdd:pfam13254  296 PETSSEKSAPSLLSPVSKASIDKPLSSPDRDPLSPKPKPQS--PPKDFR-ANLR--SREVPKDKSKKDEPEFKNVFGKLR 370

                          170
                   ....*....|....*
gi 1201829585  696 DAKTQKAVEPAQVRD 710
Cdd:pfam13254  371 KAETKNYVAPDELKD 385
PDZ11_MUPP1-PDZ9_PATJ-like cd06674
PDZ domain 11 of MUPP1 of multi-PDZ-domain protein 1 (MUPP1), domain 9 of PATJ ...
 4536-4598 1.32e-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: 40.73  E-value: 1.32e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1201829585 4536 SGNGLGIRVVGGKEipgssgEIGAYIAKVLPGGSAEQTGKLIEGMQVLEWNGIPLTGKTYEEV 4598
Cdd:cd06674     12 PGRGLGLSIVGKRN------DTGVFVSDIVKGGAADADGRLMQGDQILSVNGEDVRNASQEAA 68
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
269-394 1.38e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 45.15  E-value: 1.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  269 QKSQLQQS--EPTKPVQQQTSAKPSVgpTKPLPQQPDSAKTSSQASPP-TKPSSQQSGPVKQPSQQPARQGGPVKPSAQ- 344
Cdd:PRK14971   358 QLAQLTQKgdDASGGRGPKQHIKPVF--TQPAAAPQPSAAAAASPSPSqSSAAAQPSAPQSATQPAGTPPTVSVDPPAAv 435

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1201829585  345 ----QAGPPKQQPGSEKPSAQQTGPAKQ----PLQTGPGKPPLQQ-TGPVKQVPPQAGP 394
Cdd:PRK14971   436 pvnpPSTAPQAVRPAQFKEEKKIPVSKVsslgPSTLRPIQEKAEQaTGNIKEAPTGTQK 494
PDZ1_PTPN13-like cd23072
PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), and related ...
 4524-4608 1.40e-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: 1.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4524 LKLLRDPKdhtvsgNGLGIRVVGGkEIPGSSgEIGAYIAKVLPGGSAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQNiII 4603
Cdd:cd23072      5 VNLKKDAK------YGLGFQIVGG-EKSGRL-DLGIFISSITPGGPADLDGRLKPGDRLISVNDVSLEGLSHDAAVE-IL 75


                   ....*
gi 1201829585 4604 QQCGE 4608
Cdd:cd23072     76 QNAPE 80
PHA03269 PHA03269
envelope glycoprotein C; Provisional
 829-958 1.54e-03

envelope glycoprotein C; Provisional


Pssm-ID: 165527 [Multi-domain]  Cd Length: 566  Bit Score: 44.72  E-value: 1.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  829 QPT--ASQAP-----PKEATQAQPLPKAAPTkketkPLASEKLEPMAADSTLTTKGSDLEKKPSLAKDSKPQAAEAKKPA 901
Cdd:PHA03269    45 APHqaASRAPdpavaPTSAASRKPDLAQAPT-----PAASEKFDPAPAPHQAASRAPDPAVAPQLAAAPKPDAAEAFTSA 119

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1201829585  902 ELSEQEKASQP-----KVSCPLCKTglnigSKDPPNFNTCTECKKVVCNLCGFNPMPHIAEV 958
Cdd:PHA03269   120 AQAHEAPADAGtsaasKKPDPAAHT-----QHSPPPFAYTRSMEHIACTHGGIQFIPYFHKF 176
C2B_Tricalbin-like cd04052
C2 domain second repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are ...
 4758-4855 1.62e-03

C2 domain second 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 second C2 repeat, C2B, and has a type-II topology.


Pssm-ID: 176017 [Multi-domain]  Cd Length: 111  Bit Score: 41.05  E-value: 1.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4758 PFVKVYLlpgrGAEYKRRTKYVQKSLNPEWNQtviykniSTEQL----KKKTLEVTVWDyDRFSSNDFLGEV------LI 4827
Cdd:cd04052     15 PYAELYL----NGKLVYTTRVKKKTNNPSWNA-------STEFLvtdrRKSRVTVVVKD-DRDRHDPVLGSVsislndLI 82

                           90       100
                   ....*....|....*....|....*...
gi 1201829585 4828 DLSSVSQldntpRWYPLKeqseNIDHGK 4855
Cdd:cd04052     83 DATSVGQ-----QWFPLS----GNGQGR 101
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 1363-1677 1.66e-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: 44.90  E-value: 1.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 1363 KMEKEDDKSDTSSSQQQKSPQGLSDTGYSSDGISSSLGEIPSHIPSDEKDLTRESSKKDTISQESPPSPSDLAKLESTVL 1442
Cdd:NF033609   553 EIEPIPEDSDSDPGSDSGSDSSNSDSGSDSGSDSTSDSGSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSAS 632

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 1443 SILEAQASTLADEKSVKRKELHEAYSDQTKDQHKTKPLPVTPESYSSDEEDLESIQEGERTIAADGKGGSSSRTDYKEEG 1522
Cdd:NF033609   633 DSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 712

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 1523 GGDDTPARRQRYDSVEDSSESENSPVPRRKRRASVGSSSSDEYKQDDSQGSGDEEDfirKQIIEMSADEDA-SGSEDDEF 1601
Cdd:NF033609   713 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS---DSDSDSDSDSDSdSDSDSDSD 789

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1201829585 1602 IRNQLKEISVTESQKKEEVKSKAKGTAGKHRRMARKSSAGYDEDAGRRHSWHDDDDETFDESPEPKYRETKSQDGE 1677
Cdd:NF033609   790 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSESDSNSDSE 865
PRK12757 PRK12757
cell division protein FtsN; Provisional
 260-359 1.70e-03

cell division protein FtsN; Provisional


Pssm-ID: 237191 [Multi-domain]  Cd Length: 256  Bit Score: 43.88  E-value: 1.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  260 KQPPQPRGPQKSQLQQSE------PTK----PVQQQTSAKPSVGPTKPLPQQPDSAKTSSQASPPTKPSSQQSGPVKQPS 329
Cdd:PRK12757    75 NSPTQLTDEQRQLLEQMQadmrqqPTQlsevPYNEQTPQVPRSTVQIQQQAQQQQPPATTAQPQPVTPPRQTTAPVQPQT 154

                           90       100       110
                   ....*....|....*....|....*....|
gi 1201829585  330 QQPARQGGPvKPSAQQAGPPKQQPGSEKPS 359
Cdd:PRK12757   155 PAPVRTQPA-APVTQAVEAPKVEAEKEKEQ 183
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
 203-352 1.77e-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: 44.80  E-value: 1.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  203 PSQQQSPKLVQQQGPVKPTPQQTESSKPVPQQQQPGEPKQIQKPGPShqgdskveQPKQPPQPRGpqksqlqqsePTKPV 282
Cdd:TIGR01628  380 PRMRQLPMGSPMGGAMGQPPYYGQGPQQQFNGQPLGWPRMSMMPTPM--------GPGGPLRPNG----------LAPMN 441

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1201829585  283 QQQTSAKPSVGPTKPLPQQPDSAktssqaspptkPSSQQSGPVKQPSQQPAR---QGGPVKPSAQ--QAGPPKQQ 352
Cdd:TIGR01628  442 AVRAPSRNAQNAAQKPPMQPVMY-----------PPNYQSLPLSQDLPQPQStasQGGQNKKLAQvlASATPQMQ 505
PHA03418 PHA03418
hypothetical E4 protein; Provisional
 246-409 1.98e-03

hypothetical E4 protein; Provisional


Pssm-ID: 177646 [Multi-domain]  Cd Length: 230  Bit Score: 43.19  E-value: 1.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  246 PGPSHQG--DSKVEQPKQPPQPRGPQKSQLQQSEPTKPVQQQTSAKPSVGPTKPLPQQPDS------AKTSSQASPPTKP 317
Cdd:PHA03418    37 PAPHHPNpqEDPDKNPSPPPDPPLTPRPPAQPNGHNKPPVTKQPGGEGTEEDHQAPLAADAdddprpGKRSKADEHGPAP 116

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  318 SSQQSGPVKQPSQQPARQGGPVKPSAQQAGppkqqPGSEKPsaqQTGPAKQPlqtgpgkPPLQQTGPVKQVPPQAGPT-- 395
Cdd:PHA03418   117 GRAALAPFKLDLDQDPLHGDPDPPPGATGG-----QGEEPP---EGGEESQP-------PLGEGEGAVEGHPPPLPPApe 181

                          170
                   ....*....|....*..
gi 1201829585  396 -KPSS--QTAGATKSVA 409
Cdd:PHA03418   182 pKPHNgdATHGLLGTVA 198
Treacle pfam03546
Treacher Collins syndrome protein Treacle;
221-444 2.07e-03

Treacher Collins syndrome protein Treacle;


Pssm-ID: 460967 [Multi-domain]  Cd Length: 531  Bit Score: 44.29  E-value: 2.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  221 TPQQTESSKPVPQQQQPGEPKQIQKPGPSHQGDSKVEQP--KQPPQPRGPQKSQLQQSEPTKPVQQQTSAKPSVGPTKPL 298
Cdd:pfam03546    1 TPATPGKAGPAATQAKAGKPEEDSESSSEEESDSEEETPaaKTPLQAKPSGKTPQVRAASAPAKESPRKGAPPVPPGKTG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  299 PqqpdsAKTSSQASPPTKPSSQQSGPVKQPSQQPArqGGPVKPSAQQAGPPKQQPGSEKPSAQQTGPA-KQPLQTGPGKP 377
Cdd:pfam03546   81 P-----AAAQAQAGKPEEDSESSSEESDSDGETPA--AATLTTSPAQVKPLGKNSQVRPASTVGKGPSgKGANPAPPGKA 153

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1201829585  378 ----PLQQTGPVKQVPPQAGPTKPSSQTAGATKSVAQQPGLTKPPGPQSGPEKPSQQKQASAAQPVESTPK 444
Cdd:pfam03546  154 gsaaPLVQVGKKEEDSESSSEESDSEGEAPPAATQAKPSGKILQVRPASGPAKGAAPAPPQKAGPVATQVK 224
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
 310-429 2.43e-03

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


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 41.95  E-value: 2.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  310 QASPPTKPSSQQSGPVKQPSQQPARQGGPVKPsaqQAGPPKQQPGSEKPSAQQTGPAKQPLQTGPGKP--PLQQTGPVKQ 387
Cdd:pfam15240   37 GQSQQGGQGPQGPPPGGFPPQPPASDDPPGPP---PPGGPQQPPPQGGKQKPQGPPPQGGPRPPPGKPqgPPPQGGNQQQ 113

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1201829585  388 VPPQAGPTKPSSQTAGATKSV---AQQPGLTKPPGPQSGPEKPSQ 429
Cdd:pfam15240  114 GPPPPGKPQGPPPQGGGPPPQggnQQGPPPPPPGNPQGPPQRPPQ 158
Not5 COG5665
CCR4-NOT transcriptional regulation complex, NOT5 subunit [Transcription];
532-732 2.44e-03

CCR4-NOT transcriptional regulation complex, NOT5 subunit [Transcription];


Pssm-ID: 444384 [Multi-domain]  Cd Length: 874  Bit Score: 44.27  E-value: 2.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  532 TAKPSPQSQPGQKKDASPKPDpsqqADSKKPVPQ-KKQPSmpgsPPVKSKQTDAEPSDTF-------------------- 590
Cdd:COG5665    259 QPKSQPTSPSGGTTPPSTNQL----TTSNTPTSTaKAQPQ----PPTKKQPAKEPPSDTAsgnpsapsvlinsdsptsed 330

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  591 --QQIDPTPKSDQAKPTQAEEKQNQPSVQKPTTDTV----PTSAAPGVKQDLADPRPPLTQQKVTDSPKPETTKPPADTH 664
Cdd:COG5665    331 paTASVPTTEETTAFTTPSSVPSTPAEKDTPATDLAtpvsPTPPETSVDKKVSPDSATSSTKSEKEGGTASSPMPPNIAI 410

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1201829585  665 PAGDKPD-SKPLPQVSRQKSDPKLASQSGSKSDAKTQKAVEPAQVRDDPKKLQTKSAPKPDTKPAPKGP 732
Cdd:COG5665    411 GAKDDVDaTDPSQEAKEYTKNAPMTPEADSAPESSVRTEASPSAGSDLEPENTTLRDPAPNAIPPPEDP 479
motB PRK05996
MotB family protein;
240-440 2.46e-03

MotB family protein;


Pssm-ID: 235665 [Multi-domain]  Cd Length: 423  Bit Score: 43.92  E-value: 2.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  240 PKQIQKPGPSHQGDSKveqpkqppqprgPQKSQLQQSEPTKPvqqqTSAKpsvgptkplpqqpDSAKTSSQASPPTKPS- 318
Cdd:PRK05996    80 EKGLKDPVDGAEGEQK------------PGKSKFEEDQRVEG----SSAV-------------TGDDTTRTSGDQTNYSe 130

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  319 --------------SQQSGPVKQPSQQpaRQGGpvkpsAQQAGPP-------------------KQQPGSEKPSAQQTGP 365
Cdd:PRK05996   131 adlfrnpyavlaeiAQEVGQQANVSAK--GDGG-----AAQSGPAtgadggeayrdpfdpdfwsKQVEVTTAGDLLPPGQ 203

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1201829585  366 AKQPLQTGPGKPPLQQTGPVKQVPPQAGPTKPSSQT---AGATKSVAQQPGLTKPPGPQsgPEKPSQQKQASAAQPVE 440
Cdd:PRK05996   204 AREQAQGAKSATAAPATVPQAAPLPQAQPKKAATEEeliADAKKAATGEPAANAAKAAK--PEPMPDDQQKEAEQLQA 279
Treacle pfam03546
Treacher Collins syndrome protein Treacle;
223-443 2.54e-03

Treacher Collins syndrome protein Treacle;


Pssm-ID: 460967 [Multi-domain]  Cd Length: 531  Bit Score: 44.29  E-value: 2.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  223 QQTESSKPVPQQQQPGEPKQIQKPGPSHQGDSKVEQPKQPPQPRGPQKSQLQQSEPTKPVQQQTSAKPSVGPT---KPLP 299
Cdd:pfam03546   36 EETPAAKTPLQAKPSGKTPQVRAASAPAKESPRKGAPPVPPGKTGPAAAQAQAGKPEEDSESSSEESDSDGETpaaATLT 115

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  300 QQPDSAKTSSQASPPTKPSSQQSGPVKQPSQQPArqGGPVKPSAQQAGPPKQQPGSEKPSAQQTGPAKQPLQTGPGKPPl 379
Cdd:pfam03546  116 TSPAQVKPLGKNSQVRPASTVGKGPSGKGANPAP--PGKAGSAAPLVQVGKKEEDSESSSEESDSEGEAPPAATQAKPS- 192

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  380 qqtGPVKQVPPQAGPTK------PSSQTAGATKSVAQQPgltKPPGPQSGPEKPSQQKQASAAQPVESTP 443
Cdd:pfam03546  193 ---GKILQVRPASGPAKgaapapPQKAGPVATQVKAERS---KEDSESSEESSDSEEEAPAAATPAQAKP 256
DUF4045 pfam13254
Domain of unknown function (DUF4045); This presumed domain is functionally uncharacterized. ...
 182-359 2.61e-03

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: 44.00  E-value: 2.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  182 KQKVTQKDQGKPEEQRGLAKHPSQQQS--------PKLVQQQGPVKPTPQQTESSKPVPQQQQPGEPKQiqKPGPSHQGD 253
Cdd:pfam13254  165 KPKAQPSQPAQPAWMKELNKIRQSRASvdlgrpnsFKEVTPVGLMRSPAPGGHSKSPSVSGISADSSPT--KEEPSEEAD 242

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  254 SKVEQPKQPPQPRGPQKSQLQQSEPTKPVQQQT--SAKPSVGPTKPLPQQPDSAKTSSQASPPTKPSSQQSGPVKQPSQQ 331
Cdd:pfam13254  243 TLSTDKEQSPAPTSASEPPPKTKELPKDSEEPAapSKSAEASTEKKEPDTESSPETSSEKSAPSLLSPVSKASIDKPLSS 322

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1201829585  332 PARQGGPVKPSAQ------QAGPPKQQPGSEKPS 359
Cdd:pfam13254  323 PDRDPLSPKPKPQsppkdfRANLRSREVPKDKSK 356
C2_E3_ubiquitin_ligase cd04021
C2 domain present in E3 ubiquitin ligase; E3 ubiquitin ligase is part of the ubiquitylation ...
 4771-4837 2.88e-03

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


Pssm-ID: 175988 [Multi-domain]  Cd Length: 125  Bit Score: 40.72  E-value: 2.88e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1201829585 4771 EYKRRTKYVQKSLNPEWNQ--TViyknISTEQlkkKTLEVTVWDYDRFSSNDFLGEVLIDLSSVSQLDN 4837
Cdd:cd04021     33 QPPKKTEVSKKTSNPKWNEhfTV----LVTPQ---STLEFKVWSHHTLKADVLLGEASLDLSDILKNHN 94
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 535-1016 2.88e-03

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: 44.37  E-value: 2.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  535 PSP-QSQPGQKKDASPKPDPSQQADSKKPVPQkkQPSMPGSPP------VKSKQTDAEPSDTFQQID----------PTP 597
Cdd:pfam03154   74 PSPlKSAKRQREKGASDTEEPERATAKKSKTQ--EISRPNSPSegegesSDGRSVNDEGSSDPKDIDqdnrstspsiPSP 151

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  598 K---SDQAKPTQAEEKQNQPSV-QKPTTDTVPTSAAPGVKQDLADPRPPLTQQKVTDSPKPETTKPPADTHPagdkpdsk 673
Cdd:pfam03154  152 QdneSDSDSSAQQQILQTQPPVlQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQS-------- 223

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  674 PLPQVSRQKSDPKLASQSGSKSDAKTQKAVEPAqvrddpkklqtksaPKPDTKPAPKGPQAGTGPKPmsaqpapqpqqPQ 753
Cdd:pfam03154  224 TAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPP--------------PPSQVSPQPLPQPSLHGQMP-----------PM 278

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  754 KTPEQSrrfslnlgGITDVPKPQPTTPqetvtgklfgfgasiFSQASSLISTAGQPGSQTSGPAPPAAKQPQPPSQPTA- 832
Cdd:pfam03154  279 PHSLQT--------GPSHMQHPVPPQP---------------FPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLq 335

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  833 SQAPPKEatqaQPLPKAAPTKKETKPLASEKLEPMAAD------------------------------STLTTKGSDLEK 882
Cdd:pfam03154  336 SQQPPRE----QPLPPAPLSMPHIKPPPTTPIPQLPNPqshkhpphlsgpspfqmnsnlppppalkplSSLSTHHPPSAH 411

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  883 KP--SLAKDSKPQAAEAKKPAELSEQEKASQPKVSCPlCKTGLNIGSKDPPNFNTCTECKKVVCNLCGFNPMPHIAEVQE 960
Cdd:pfam03154  412 PPplQLMPQSQQLPPPPAQPPVLTQSQSLPPPAASHP-PTSGLHQVPSQSPFPQHPFVPGGPPPITPPSGPPTSTSSAMP 490

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1201829585  961 WLCLNCQTQRAMSGQLGDMGKVPLPKLG--------PSQPVSKPPATPQKQPVPAVSHSPQKTS 1016
Cdd:pfam03154  491 GIQPPSSASVSSSGPVPAAVSCPLPPVQikeealdeAEEPESPPPPPRSPSPEPTVVNTPSHAS 554
PRK10927 PRK10927
cell division protein FtsN;
314-446 3.16e-03

cell division protein FtsN;


Pssm-ID: 236797 [Multi-domain]  Cd Length: 319  Bit Score: 43.13  E-value: 3.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  314 PTKPSSqqSGPVKQPSQQPARQGGPVkpsAQQAGPPKQQPG--SEKPSAQQTgPAK--QPLQTGPGKPPLQQTGPVKQvp 389
Cdd:PRK10927    99 PTEPSA--GGEVKTPEQLTPEQRQLL---EQMQADMRQQPTqlVEVPWNEQT-PEQrqQTLQRQRQAQQLAEQQRLAQ-- 170

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  390 PQAGPTKPSSQTagaTKSVAQQPgltkppgpqsGPEKPSQQKQASAAQPVE---STPKKT 446
Cdd:PRK10927   171 QSRTTEQSWQQQ---TRTSQAAP----------VQAQPRQSKPASTQQPYQdllQTPAHT 217
C2A_RasA2_RasA3 cd08401
C2 domain first repeat present in RasA2 and RasA3; RasA2 and RasA3 are GAP1s (GTPase ...
 4737-4857 3.17e-03

C2 domain first repeat present in RasA2 and RasA3; RasA2 and RasA3 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. RasA2 and RasA3 are both inositol 1,3,4,5-tetrakisphosphate-binding proteins and contain an N-terminal C2 domain, a Ras-GAP domain, a pleckstrin-homology (PH) domain which localizes it to the plasma membrane, and Bruton's Tyrosine Kinase (BTK) a 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 first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 176046 [Multi-domain]  Cd Length: 121  Bit Score: 40.88  E-value: 3.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4737 LIIHILQARNLAPRDN-NGYSDPFVKVYLlpgrGAEYKRRTKYVQKSLNPEWNQTVIYKNISTEQlkkkTLEVTVWDYDR 4815
Cdd:cd08401      2 LKIKIGEAKNLPPRSGpNKMRDCYCTVNL----DQEEVFRTKTVEKSLCPFFGEDFYFEIPRTFR----HLSFYIYDRDV 73

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1201829585 4816 FSSNDFLGEVLI---DLSSVSQLDNtprWYPLKEQSENID-HGKSH 4857
Cdd:cd08401     74 LRRDSVIGKVAIkkeDLHKYYGKDT---WFPLQPVDADSEvQGKVH 116
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
280-450 3.27e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 43.71  E-value: 3.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  280 KPVQQQTSAKPSVGPTKPLPQQPDSAKTSSQASPPTKP---SSQQSGPVKQPSQQPARQGGPVKPSAQQAGPPKQQPGSE 356
Cdd:PRK12323   364 RPGQSGGGAGPATAAAAPVAQPAPAAAAPAAAAPAPAAppaAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARG 443

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  357 KPSAQQTGPAKQPLQTGPGKPPLQQTGPV----KQVPPQAGPTKPSSQTAGATKSVAQQPGLTKPPGPQSGPEKPSQQKQ 432
Cdd:PRK12323   444 PGGAPAPAPAPAAAPAAAARPAAAGPRPVaaaaAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPAGWVA 523

                          170
                   ....*....|....*...
gi 1201829585  433 ASAAQPVESTPKKTFCPL 450
Cdd:PRK12323   524 ESIPDPATADPDDAFETL 541
Amelin smart00817
Ameloblastin precursor (Amelin); This family consists of several mammalian Ameloblastin ...
 287-392 3.51e-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: 43.34  E-value: 3.51e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585   287 SAKPSVGPTKPLPQQPDSAKTSSQASPPTKPSSQQSGPVKQPSQQ----PARQGGPVKPSAQ---QAGPPKQQPGSEKPS 359
Cdd:smart00817   74 SSFPWLRPREHETQQYEYSLPVHPPPLPSQPSLQPQQPGLKPFLQptalPTNQATPQKNGPQppmHLGQPPLQQAELPMI 153

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*..
gi 1201829585   360 AQQTGPAKQPLQT--------GPGKPPLQQT------GPVKQVPPQA 392
Cdd:smart00817  154 PPQVAPSDKPPQTelplydfaDPQNPLLFQIahlmsrGPMPQNKQQH 200
Amelin smart00817
Ameloblastin precursor (Amelin); This family consists of several mammalian Ameloblastin ...
 267-393 3.54e-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: 43.34  E-value: 3.54e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585   267 GPQKSQLQQSEPTKPVQ-----QQTSAKPSVGPTKPLPQQPdsAKTSSQASpPTKPSSQqsgPVKQPSQQPARQGGPvKP 341
Cdd:smart00817   80 RPREHETQQYEYSLPVHppplpSQPSLQPQQPGLKPFLQPT--ALPTNQAT-PQKNGPQ---PPMHLGQPPLQQAEL-PM 152

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1201829585   342 SAQQAGPPKQQPGSEKPSAQQTGPAKQPLQTGPGKPPLQQTGPVKQVPPQAG 393
Cdd:smart00817  153 IPPQVAPSDKPPQTELPLYDFADPQNPLLFQIAHLMSRGPMPQNKQQHLYPG 204
AF-4 pfam05110
AF-4 proto-oncoprotein N-terminal region; This family consists of AF4 (Proto-oncogene AF4) and ...
 222-431 3.55e-03

AF-4 proto-oncoprotein N-terminal region; This family consists of AF4 (Proto-oncogene AF4) and FMR2 (Fragile X E mental retardation syndrome) nuclear proteins. These proteins have been linked to human diseases such as acute lymphoblastic leukaemia and mental retardation. The family also contains a Drosophila AF4 protein homolog Lilliputian which contains an AT-hook domain. Lilliputian represents a novel pair-rule gene that acts in cytoskeleton regulation, segmentation and morphogenesis in Drosophila.


Pssm-ID: 461550 [Multi-domain]  Cd Length: 514  Bit Score: 43.57  E-value: 3.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  222 PQQTESSKPVPQQQQPGEPKQIQKPGPSHQGDSKvEQPKQPPQPRGPQKSQLQQSEPTKPVQQQTSA--KPSVGPTKPLP 299
Cdd:pfam05110   76 PKNSVPQTPQEKPDQPFFPDKTSGLPPSFHTSSH-SQPMGPPSSSSPSVSSSQSQKKSQARTEPAHGghSSSGSQSSQRS 154

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  300 QQPDSAKTSSQASPPTKPSSQQSGPVKQPSQQPARQGGPVKPSAQQAGPPKQqPGSEKPSAQQTGPAKQPLQTGPGKPPL 379
Cdd:pfam05110  155 QGQSRSKGGQESHSSSHHKRQERREDLFSCASLSHSLEELSPLLSSLSSPVK-PLSPSHSRQHTGSKAQNSSDHHGKEYS 233

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1201829585  380 QQTGPVKQVppqAGPTKPSSQTAGATKSVAQQPGLTKPPGPQSgpeKPS--QQK 431
Cdd:pfam05110  234 HSKSPRDSE---AGSHGPESPSTSLLASSSQLSSQTFPPSLPS---KTSamQQK 281
PHA03269 PHA03269
envelope glycoprotein C; Provisional
 532-700 3.63e-03

envelope glycoprotein C; Provisional


Pssm-ID: 165527 [Multi-domain]  Cd Length: 566  Bit Score: 43.56  E-value: 3.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  532 TAKPSPQ---SQPGQKKDasPKPDPSQQAdSKKPVPQKKQPSMPGSPPvksKQTDAEPSDTFQQIDPTPKSDQAkptqae 608
Cdd:PHA03269    24 TNIPIPElhtSAATQKPD--PAPAPHQAA-SRAPDPAVAPTSAASRKP---DLAQAPTPAASEKFDPAPAPHQA------ 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  609 ekqnqpSVQKPTTDTVPTSAApgvkqdladprppltqqkvtdSPKPETTKPPADTHPAGDKPDSKPLPQVSRqKSDPKLA 688
Cdd:PHA03269    92 ------ASRAPDPAVAPQLAA---------------------APKPDAAEAFTSAAQAHEAPADAGTSAASK-KPDPAAH 143

                          170
                   ....*....|..
gi 1201829585  689 SQSGSKSDAKTQ 700
Cdd:PHA03269   144 TQHSPPPFAYTR 155
C2B_Munc13-like cd04009
C2 domain second repeat in Munc13 (mammalian uncoordinated)-like proteins; C2-like domains are ...
 5041-5139 3.95e-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: 3.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 5041 EQLIVEILQCRNItykfKSPD--HLPDLYVKLYVVNISTQKRVIKKKTRVCRHDREPSFNETFRFSLSPAGHSLQ----- 5113
Cdd:cd04009     16 QSLRVEILNARNL----LPLDsnGSSDPFVKVELLPRHLFPDVPTPKTQVKKKTLFPLFDESFEFNVPPEQCSVEgalll 91

                           90       100
                   ....*....|....*....|....*..
gi 1201829585 5114 -ILLVSNggKFMKKTLIGEAYVWLDKV 5139
Cdd:cd04009     92 fTVKDYD--LLGSNDFEGEAFLPLNDI 116
PDZ1_Dlg1-2-4-like cd06723
PDZ domain 1 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg) ...
 4537-4576 4.35e-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: 4.35e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1201829585 4537 GNGLGIRVVGGKEIPGSSGEIGAYIAKVLPGGSAEQTGKL 4576
Cdd:cd06723     10 NSGLGFSIAGGTDNPHIGDDPSIYITKIIPGGAAAADGRL 49
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 270-424 4.44e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 43.62  E-value: 4.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  270 KSQLQQSEPTKPVQQQTSAKPSVGPTKPLPQQPDSAKTSSQASPPTKPSSQQSGpvkqpSQQPARQGGPVKPSAqqagPP 349
Cdd:PHA03307   778 AEPQRGAGSSPPVRAEAAFRRPGRLRRSGPAADAASRTASKRKSRSHTPDGGSE-----SSGPARPPGAAARPP----PA 848

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1201829585  350 KQQPGSEKPSAQQTGPAKQPLQTGPGKPPLQQTGPVKQVPPQAGPTKPSSQTAGATKSVAQQPGLTkpPGPQSGP 424
Cdd:PHA03307   849 RSSESSKSKPAAAGGRARGKNGRRRPRPPEPRARPGAAAPPKAAAAAPPAGAPAPRPRPAPRVKLG--PMPPGGP 921
C2C_MCTP_PRT_plant cd04019
C2 domain third repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); ...
 4739-4855 4.44e-03

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: 41.12  E-value: 4.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4739 IHILQARNLAPRDNNGYSDPFVKVYLLPgrgaeYKRRTKYVQ-KSLNPEWNQTVIYknISTEQLkKKTLEVTVwdYDRFS 4817
Cdd:cd04019      4 VTVIEAQDLVPSDKNRVPEVFVKAQLGN-----QVLRTRPSQtRNGNPSWNEELMF--VAAEPF-EDHLILSV--EDRVG 73

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1201829585 4818 SN--DFLGEVLIDLSSVSQ-LDNTP---RWYPLkEQSENIDHGK 4855
Cdd:cd04019     74 PNkdEPLGRAVIPLNDIERrVDDRPvpsRWFSL-ERPGGAMEQK 116
PDZ5_MAGI-1_3-like cd06735
PDZ domain 5 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ...
 4526-4602 4.61e-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: 39.10  E-value: 4.61e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1201829585 4526 LLRDPKdhtvsGNGLGIRvvGGKEipgsSGEIGAYIAKVLPGGSAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQNII 4602
Cdd:cd06735      6 LERGPK-----GFGFSIR--GGRE----YNNMPLYVLRLAEDGPAQRDGRLRVGDQILEINGESTQGMTHAQAIELI 71
PDZ6_PDZD2-PDZ3_hPro-IL-16-like cd06762
PDZ domain 6 of PDZ domain containing 2 (PDZD2), PDZ domain 3 of human pro-interleukin-16 ...
 4533-4604 4.72e-03

PDZ domain 6 of PDZ domain containing 2 (PDZD2), PDZ domain 3 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 6 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 third PDZ domain (PDZ3) 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 PDZ6 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: 467243 [Multi-domain]  Cd Length: 86  Bit Score: 39.16  E-value: 4.72e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1201829585 4533 HTVSGNGLGIRVVGG-----KEIPgssgeigayIAKVLPGGSAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQNIIIQ 4604
Cdd:cd06762      7 HKEEGSGLGFSLAGGsdlenKSIT---------VHRVFPSGLAAQEGTIQKGDRILSINGKSLKGVTHGDALSVLKQ 74
CCDC47 pfam07946
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ...
 3776-3839 4.77e-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: 4.77e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1201829585 3776 ARAKILQDIDRELDLVERESAKLRKKQAELDEEEKEIDaklrylEMGINRRKEALLKEREKRER 3839
Cdd:pfam07946  265 TREEEIEKIKKAAEEERAEEAQEKKEEAKKKEREEKLA------KLSPEEQRKYEEKERKKEQR 322
C2A_RIM1alpha cd04031
C2 domain first repeat contained in Rab3-interacting molecule (RIM) proteins; RIMs are ...
 5024-5104 5.28e-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: 5.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 5024 VMGEIKIALKKEMKTdgEQLIVEILQCRNItykfKSPDH--LPDLYVKLYVVNISTQKRviKKKTRVCRHDREPSFNETF 5101
Cdd:cd04031      1 ITGRIQIQLWYDKVT--SQLIVTVLQARDL----PPRDDgsLRNPYVKVYLLPDRSEKS--KRRTKTVKKTLNPEWNQTF 72


                   ...
gi 1201829585 5102 RFS 5104
Cdd:cd04031     73 EYS 75
PDZ2_PDZD7-like cd10834
PDZ domain 2 of the canonical isoform 1 of PDZ domain containing 7 (PDZD7), and related ...
 4534-4588 5.28e-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: 38.91  E-value: 5.28e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1201829585 4534 TVSGNGLGIRVVGGKEIPgssgeIGAYIAKVLPGGSAEQTGkLIEGMQVLEWNGI 4588
Cdd:cd10834      9 TSDDYCLGFNIRGGSEYG-----LGIYVSKVDPGGLAEQNG-IKVGDQILAVNGV 57
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
 309-435 5.49e-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: 42.87  E-value: 5.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  309 SQASPPTKPSSQQSGPVKQPSQQPARQGGPvkpsAQQAGPPKQQPGSEKPSAQQTGPAKQPLQTGPGKPPLQQTGPVKQv 388
Cdd:TIGR01628  376 MQLQPRMRQLPMGSPMGGAMGQPPYYGQGP----QQQFNGQPLGWPRMSMMPTPMGPGGPLRPNGLAPMNAVRAPSRNA- 450

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1201829585  389 ppQAGPTKPSSQTAGATKSVAQQPGLTKPPGPQS-----GPEKPSQQKQASA 435
Cdd:TIGR01628  451 --QNAAQKPPMQPVMYPPNYQSLPLSQDLPQPQStasqgGQNKKLAQVLASA 500
FimV COG3170
Type IV pilus assembly protein FimV [Cell motility, Extracellular structures];
192-442 5.56e-03

Type IV pilus assembly protein FimV [Cell motility, Extracellular structures];


Pssm-ID: 442403 [Multi-domain]  Cd Length: 508  Bit Score: 42.86  E-value: 5.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  192 KPEEQRGLAKHPSQQQSPKLVQQQGPVKPTPQQTESSKPVPQQQQPGEPKQ----IQKPGPSHQGDSKVEQPKQPPQPRG 267
Cdd:COG3170    126 APAAAAAAADQPAAEAAPAASGEYYPVRPGDTLWSIAARPVRPSSGVSLDQmmvaLYRANPDAFIDGNINRLKAGAVLRV 205

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  268 PQKSQLQ---QSEPTKPVQQQTSAKPSVGPTKPLPQQPdsaktssqaSPPTKPSSQQSGPVKQPSQQPARQGGPVKPSAQ 344
Cdd:COG3170    206 PAAEEVAalsPAEARQEVQAQSADWAAYRARLAAAVEP---------APAAAAPAAPPAAAAAAGPVPAAAEDTLSPEVT 276

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  345 QAGPPKQQPGSEKPSAQQTGPAKQpLQTGPGKppLQQTGPVKQVPPQAGPTKPSSQTAGATksvaqqpgltkppgpqSGP 424
Cdd:COG3170    277 AAAAAEEADALPEAAAELAERLAA-LEAQLAE--LQRLLALKNPAPAAAVSAPAAAAAAAT----------------VEA 337

                          250
                   ....*....|....*...
gi 1201829585  425 EKPSQQKQASAAQPVEST 442
Cdd:COG3170    338 AAPAAAAQPAAAAPAPAL 355
valS PRK14900
valyl-tRNA synthetase; Provisional
 316-433 5.58e-03

valyl-tRNA synthetase; Provisional


Pssm-ID: 237855 [Multi-domain]  Cd Length: 1052  Bit Score: 43.44  E-value: 5.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  316 KPSSQQSGPVKQPSQQPARQGGPVKPSAQQAGPPKQ-----QPGSEKPSAQQTGPAKQPLQTGPGKPPLQQTGPVKQVPP 390
Cdd:PRK14900   923 KPTQDGPAAEAQPAQENTVVESAEKAVAAVSEAAQQaatavASGIEKVAEAVRKTVRRSVKKAAATRAAMKKKVAKKAPA 1002

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1201829585  391 QAGPT-KPSSQTAGATKSVAQQP---GLTKPPGPQSGPEKPSQQKQA 433
Cdd:PRK14900  1003 KKAAAkKAAAKKAAAKKKVAKKApakKVARKPAAKKAAKKPARKAAG 1049
SP2_N cd22540
N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins ...
 203-444 5.60e-03

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: 42.99  E-value: 5.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  203 PSQQQSPKLVQQQGPVKPTPQQTESSKPVPQQQQpgePKQIQKPGPshqGDSKVEQPKQPPQPRGPQKSQLQQSEPTKPV 282
Cdd:cd22540    158 VQVLQQPQQAHKPVPIKPAPLQTSNTNSASLQVP---GNVIKLQSG---GNVALTLPVNNLVGTQDGATQLQLAAAPSKP 231

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  283 QQQTSAKPSVGPTKPLPQQpdsAKTSSQASPPTKPSSQQSGPVKQPSQQPArQGGPVKPSAQQAGPPKQQPGSekpsaQQ 362
Cdd:cd22540    232 SKKIRKKSAQAAQPAVTVA---EQVETVLIETTADNIIQAGNNLLIVQSPG-TGQPAVLQQVQVLQPKQEQQV-----VQ 302

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  363 TGPakQPLQ----TGPGKPPLQQ--TGPVKQVPPQAGPTKPSSQTA-GATKSVAQQPGLTKPPGPQSGpEKPSQQKQASA 435
Cdd:cd22540    303 IPQ--QALRvvqaASATLPTVPQkpLQNIQIQNSEPTPTQVYIKTPsGEVQTVLLQEAPAATATPSSS-TSTVQQQVTAN 379


                   ....*....
gi 1201829585  436 AQPVESTPK 444
Cdd:cd22540    380 NGTGTSKPN 388
PDZ2_FL-whirlin cd06741
PDZ domain 2 of the full-length isoform of whirlin and related domains; PDZ (PSD-95 ...
 4536-4602 6.83e-03

PDZ domain 2 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 2 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 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: 467223 [Multi-domain]  Cd Length: 84  Bit Score: 38.78  E-value: 6.83e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1201829585 4536 SGNGLGIRVVGGKEIpgssgEIGAYIAKVLPGGSAEQTGkLIEGMQVLEWNGIPLTGKTYEEVQNII 4602
Cdd:cd06741     10 DGQSLGLMIRGGAEY-----GLGIYVTGVDPGSVAENAG-LKVGDQILEVNGRSFLDITHDEAVKIL 70
KLF11_N cd21584
N-terminal domain of Kruppel-like factor 11; Kruppel-like factor 11 (KLF11; also known as ...
 299-424 6.83e-03

N-terminal domain of Kruppel-like factor 11; Kruppel-like factor 11 (KLF11; also known as Krueppel-like factor 11; Fetal Kruppel-like factor-1/FKLF-1; maturity-onset diabetes of the young 7/MODY7; TGFbeta Inducible Early Growth Response 2/TIEG2) is a protein that in humans is encoded by the KLF11 gene. KLF11 is involved in cell growth, apoptosis, cellular inflammation and differentiation, endometriosis, and cholesterol, prostaglandin, neurotransmitter, fat, and sugar metabolism. KLF9, KLF10, KLF11, KLF13, KLF14, and KLF16 share a conserved a-helical motif AA/VXXL that mediates their binding to Sin3A and their activities as transcriptional repressors. KLF11 belongs 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. 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 N-terminal domain of KLF11.


Pssm-ID: 409242 [Multi-domain]  Cd Length: 217  Bit Score: 41.52  E-value: 6.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  299 PQQPDSAKTSSQASPP---------TKPSSQQSGPVKQPSQQPARQGGPVkpsAQQAG-------PPKQQPGSEKPSAQQ 362
Cdd:cd21584     67 PHSPSFAEPSTTAPPPpcramatsvIRHTADSSPPVPVPSPPVLCQMIPV---SGQSGmisaflqPPALSAGTVKPILPQ 143

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1201829585  363 TGPAKQPLQTGPGKPPlqqtGPVKQVPPQAgptkPSSQTAGATKSVaQQPGLTK-----------PPGPQSGP 424
Cdd:cd21584    144 TAPASQPLLVGSPVPQ----GTVMLVLPQA----SVPQPPQCPQTV-MTLGNTKllplapapvfiPSGQSCAP 207
PRK10927 PRK10927
cell division protein FtsN;
202-395 6.94e-03

cell division protein FtsN;


Pssm-ID: 236797 [Multi-domain]  Cd Length: 319  Bit Score: 42.36  E-value: 6.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  202 HPSQQQSPKLVQQQ---GPVKPTPQQTESSKPVPQQQQPGepkqIQKPG-PSHQGDskVEQPKQPPQPRGPQKSQLQ--- 274
Cdd:PRK10927    56 HHKKEESETLQSQKvtgNGLPPKPEERWRYIKELESRQPG----VRAPTePSAGGE--VKTPEQLTPEQRQLLEQMQadm 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  275 QSEPTK----PVQQQTSAKPsvgptkplpQQPDSAKTSSQASPPTKPSSQQSGPVKQPSQQPARqggpvkpsAQQAGPPK 350
Cdd:PRK10927   130 RQQPTQlvevPWNEQTPEQR---------QQTLQRQRQAQQLAEQQRLAQQSRTTEQSWQQQTR--------TSQAAPVQ 192

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1201829585  351 QQPGSEKPSAQQTgPAKQPLQT---GPGKPPLQQTGPVKQVPPQAGPT 395
Cdd:PRK10927   193 AQPRQSKPASTQQ-PYQDLLQTpahTTAQSKPQQAAPVTRAADAPKPT 239
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 253-852 7.21e-03

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: 42.83  E-value: 7.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  253 DSKVEQPKQP--------PQPRGPQKSQLQQSEPTKPVQQQTSAKPSvgPTKPLpQQPDSAKTSSQASPPTKPSSQQSGP 324
Cdd:pfam03154   56 DSKAESMKKSskkikeeaPSPLKSAKRQREKGASDTEEPERATAKKS--KTQEI-SRPNSPSEGEGESSDGRSVNDEGSS 132

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  325 VKQPSQQPARQGGPVKPSaqqagpPKQQPGSEKPSAQQtgpakQPLQTGPgkPPLQ-QTGPVkqVPPQAGPTKPSSQTAG 403
Cdd:pfam03154  133 DPKDIDQDNRSTSPSIPS------PQDNESDSDSSAQQ-----QILQTQP--PVLQaQSGAA--SPPSPPPPGTTQAATA 197

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  404 ATKSVAqqPGLTKPPGPQSGPEKPSQQKQASAAQPVESTPKktfcplctttellLHVPEKANYNTCTQCHTVVCSLCGFN 483
Cdd:pfam03154  198 GPTPSA--PSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPT-------------LHPQRLPSPHPPLQPMTQPPPPSQVS 262

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  484 PNPHITeikewlclncqmqralggdlASGHGPGPQLPPPKQktptptstAKPSPQSQPGqkkdaSPKPDPSQQADSKKPV 563
Cdd:pfam03154  263 PQPLPQ--------------------PSLHGQMPPMPHSLQ--------TGPSHMQHPV-----PPQPFPLTPQSSQSQV 309

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  564 PQKKQPSMPGsppvKSKQTDAEPSDTFQQIDPTPKSDQAKPTQAeekQNQPSVQKPTTDTVPTSAAPGVKQDLADPRPPL 643
Cdd:pfam03154  310 PPGPSPAAPG----QSQQRIHTPPSQSQLQSQQPPREQPLPPAP---LSMPHIKPPPTTPIPQLPNPQSHKHPPHLSGPS 382

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  644 TQQKVTDSPKPETTKPPAD--TH--PAGDKPDSKPLPQVSRQKSDPklasqsgSKSDAKTQKAVEPAQVRDDPKklQTKS 719
Cdd:pfam03154  383 PFQMNSNLPPPPALKPLSSlsTHhpPSAHPPPLQLMPQSQQLPPPP-------AQPPVLTQSQSLPPPAASHPP--TSGL 453

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  720 APKPDTKPAPKGPQAGTGPKPmsaqpapqpqqpqktpeqsrrfslnlggITDVPKPQPTTPQEtvtgklfgfGASIFSQA 799
Cdd:pfam03154  454 HQVPSQSPFPQHPFVPGGPPP----------------------------ITPPSGPPTSTSSA---------MPGIQPPS 496

                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1201829585  800 SSLISTAGQPGSQTSGPAPPAAKQPQPPSQPTASQAPPKEATQAQPLPKAAPT 852
Cdd:pfam03154  497 SASVSSSGPVPAAVSCPLPPVQIKEEALDEAEEPESPPPPPRSPSPEPTVVNT 549
PDZ1_Par3-like cd06691
PDZ domain 1 of partitioning defective 3 (Par3), and related domains; PDZ (PSD-95 ...
 4534-4615 7.29e-03

PDZ domain 1 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 1 of Par3 (or PAR3 or Par-3, also known as Atypical PKC isotype-specific-interacting protein, ASIP) and related domains; Drosophila bazooka PDZ1 belongs to a different PDZ family. 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: Par-3 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 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: 467178 [Multi-domain]  Cd Length: 98  Bit Score: 39.14  E-value: 7.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4534 TVSGNG--LGIRVVggkeiP----GSSGEIGAYIAKVLPGGSAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQNIIIQQCG 4607
Cdd:cd06691      9 ELSNDGgpLGIHVV-----PfsssLSGRTLGLLIRGIEEGSRAERDGRFQENDCIVEINGVDLIDKSFEQAQDIFRQAMR 83


                   ....*...
gi 1201829585 4608 EAEICVRL 4615
Cdd:cd06691     84 SPEVKLHV 91
PRK12757 PRK12757
cell division protein FtsN; Provisional
 314-428 8.29e-03

cell division protein FtsN; Provisional


Pssm-ID: 237191 [Multi-domain]  Cd Length: 256  Bit Score: 41.57  E-value: 8.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  314 PTKPSSqqSGPVKQPSQ-----------------QPARQGGPVkPSAQQAGPPKQQPGSEKPSAQQTGPAKQPLQTGPGK 376
Cdd:PRK12757    65 PTEPSA--GGEVNSPTQltdeqrqlleqmqadmrQQPTQLSEV-PYNEQTPQVPRSTVQIQQQAQQQQPPATTAQPQPVT 141

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1201829585  377 PPLQQTGPVKQVPPQagPTKPsSQTAGATKSVaqqpgltKPPGPQSGPEKPS 428
Cdd:PRK12757   142 PPRQTTAPVQPQTPA--PVRT-QPAAPVTQAV-------EAPKVEAEKEKEQ 183
PDZ4_GRIP1-2-like cd06686
PDZ domain 4 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
 4538-4602 8.54e-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: 8.54e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1201829585 4538 NGLGIRVVGG---KEIPGSSGEIGaYIAkvlPGGSAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQNII 4602
Cdd:cd06686     18 KGFGIQLQGGvfaTETLSSPPLIS-FIE---PDSPAERCGVLQVGDRVLSINGIPTEDRTLEEANQLL 81
PDZ3_PDZD7-like cd06751
PDZ domain 3 of the canonical isoform 1 of PDZ domain containing 7 (PDZD7), and related ...
 4540-4602 8.74e-03

PDZ domain 3 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 3 of the long isoform 1 of PDZD7, and related domains. PDZD7 is critical for the organization of the 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 and can also form homodimers through its PDZ2 domain. Various isoforms of PDZD7 produced by alternative splicing have been identified; this subgroup includes the third 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 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: 467233 [Multi-domain]  Cd Length: 89  Bit Score: 38.57  E-value: 8.74e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1201829585 4540 LGIRVVGGKEipgSSGEIGAYIAKVLPGGSAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQNII 4602
Cdd:cd06751     13 LGISISGGIE---SKVQPVVKIEKIFPGGAAALSGNLKAGYELVSVDGESLQQVTHQQAVDII 72
C2_Ras_p21A1 cd08400
C2 domain present in RAS p21 protein activator 1 (RasA1); RasA1 is a GAP1 (GTPase activating ...
 4732-4844 9.08e-03

C2 domain present in RAS p21 protein activator 1 (RasA1); RasA1 is a GAP1 (GTPase activating protein 1), a Ras-specific GAP member, 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. RasA1 contains a C2 domain, a Ras-GAP domain, a pleckstrin homology (PH)-like domain, a SH3 domain, and 2 SH2 domains. 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: 176045 [Multi-domain]  Cd Length: 126  Bit Score: 39.66  E-value: 9.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585 4732 KHLGNLIIHILQARNLAPRDnngYSDPFVKVYLLPGRGAeykrRTKyVQKSLNPEWNQTVIYKNISTEQLkkkTLEVTVW 4811
Cdd:cd08400      1 RQVRSLQLNVLEAHKLPVKH---VPHPYCVISLNEVKVA----RTK-VREGPNPVWSEEFVFDDLPPDVN---SFTISLS 69

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1201829585 4812 DYDRFSSNDFLGEVLIDLSSVSQLDNTPRWYPL 4844
Cdd:cd08400     70 NKAKRSKDSEIAEVTVQLSKLQNGQETDEWYPL 102
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
 531-711 9.37e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 42.55  E-value: 9.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  531 STAKPSPQSQPGQKKDASPKPDPSQQADSKKPVPQKKQPSMPGSPPVKSKQTDAEPSDTFQQIDPTPKSDQAKPTQAEek 610
Cdd:PRK07994   367 EPEVPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPASAPQQAPAVPLPETTSQLLAARQQLQRAQGATKAKKSEPA-- 444

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  611 qnQPSVQKPTTDTVPTSAAPGVKQDLADPRPPLTQQKVTDSPKPETTKPPADTHPagdkpdsKPLPQVSRQKSDPKLAsq 690
Cdd:PRK07994   445 --AASRARPVNSALERLASVRPAPSALEKAPAKKEAYRWKATNPVEVKKEPVATP-------KALKKALEHEKTPELA-- 513

                          170       180
                   ....*....|....*....|.
gi 1201829585  691 sgsksdaktQKAVEPAQVRDD 711
Cdd:PRK07994   514 ---------AKLAAEAIERDP 525
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
510-642 9.42e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 42.56  E-value: 9.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201829585  510 ASGHGPGPQLPPPKQKTPTPTSTAKPSPQSQPGQKKDASPKPDPSQQADSKKPVPQKKQP--SMPGSPPVKS-KQTDAEP 586
Cdd:PRK12323   439 ASARGPGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPweELPPEFASPApAQPDAAP 518

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1201829585  587 SDTFQQIDPTPKSDQAKPTQAEEKQNQPSVQKPTTDTVPTSAAPGVKQDLADPRPP 642
Cdd:PRK12323   519 AGWVAESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRASASGLP 574
PDZ_PDZD11-like cd06752
PDZ domain of PDZ domain-containing protein 11, and related domains; PDZ (PSD-95 (Postsynaptic ...
 4523-4597 9.80e-03

PDZ domain of PDZ domain-containing protein 11, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of PDZD11, and related domains. PDZD11 (also known as ATPase-interacting PDZ protein, plasma membrane calcium ATPase-interacting single-PDZ protein, PMCA-interacting single-PDZ protein, PISP) is involved in the dynamic assembly of apical junctions (AJs). It is recruited by PLEKHA7 to AJs to promote the efficient junctional recruitment and stabilization of nectins, and the efficient early phases of assembly of AJs in epithelial cells. The PDZD11 PDZ domain binds nectin-1 and nectin-3. PDZD11 also binds to a PDZ binding motif located in the C-terminal tail of the human sodium-dependent multivitamin transporter, to the cytoplasmic tail of the Menkes copper ATPase ATP7A, and to the cytoplasmic tail of all plasma membrane Ca2+-ATPase b-splice variants. 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 PDZD11-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: 467234 [Multi-domain]  Cd Length: 83  Bit Score: 38.06  E-value: 9.80e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1201829585 4523 RLKLLRDPKDHTvsgngLGIRVVGGKEipgssGEIGAYIAKVLPGGSAEQTGkLIEGMQVLEWNGIPLTGKTYEE 4597
Cdd:cd06752      1 RTVVLKRPPGEQ-----LGFNIRGGKA-----SGLGIFISKVIPDSDAHRLG-LKEGDQILSVNGVDFEDIEHSE 64
 
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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