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Conserved domains on  [gi|1958804834|ref|XP_038940456|]
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fer-1-like protein 5 isoform X5 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
C2D_Ferlin cd04017
C2 domain fourth repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and ...
 1117-1252 4.10e-41

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: 148.07  E-value: 4.10e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958804834 1117 YQLFCYIYQARNLMYNQVLTFQESFIQVVFLNHSLCTQTLKSSAAPTWSQTLIFQHLLLFEDPKDTRENPPLVALELWQH 1196
Cdd:cd04017      1 FQLRAYIYQARDLLAADKSGLSDPFARVSFLNQSQETEVIKETLSPTWDQTLIFDEVELYGSPEEIAQNPPLVVVELFDQ 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958804834 1197 DSRGNKILWGRSMWPPVVWLGLQDWVFTPLRWHPLVReLGEEEGEILASCELILET 1252
Cdd:cd04017     81 DSVGKDEFLGRSVAKPLVKLDLEEDFPPKLQWFPIYK-GGQSAGELLAAFELIEVT 135
C2B_Ferlin cd04011
C2 domain second repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and ...
 203-310 5.18e-38

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: 138.09  E-value: 5.18e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958804834  203 PQHFQVRLKVFEARQLLGNNIKPVVKINIAGKQHLTRIQMGNN-PFFNEIFFQNFHEVPAKFFEENILIEVVDSAASRSK 281
Cdd:cd04011      1 PQDFQVRVRVIEARQLVGGNIDPVVKVEVGGQKKYTSVKKGTNcPFYNEYFFFNFHESPDELFDKIIKISVYDSRSLRSD 80

                           90       100
                   ....*....|....*....|....*....
gi 1958804834  282 AEIGRFQIDIGFIYHSPDHTLQRKWLGLC 310
Cdd:cd04011     81 TLIGSFKLDVGTVYDQPDHAFLRKWLLLT 109
FerB pfam08150
FerB (NUC096) domain; This is central domain B in proteins of the Ferlin family.
 731-803 1.17e-31

FerB (NUC096) domain; This is central domain B in proteins of the Ferlin family.


:

Pssm-ID: 462376  Cd Length: 76  Bit Score: 118.85  E-value: 1.17e-31
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958804834  731 PQESLPDVLIWLMSGQKRVAYARIPAHTVLFSTAgPMSSGKFCGKIQNLLLQYPE----GEGQNILPAYLRVCMWLG 803
Cdd:pfam08150    1 PQNSLPDVFIWMLSGGKRVAYARIPAHDILFSPV-EEERGKFCGKVQTLFLKYPGkkakGPAGWEIPAKLRVYLWLG 76
C2 super family cl14603
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 69-170 2.47e-22

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 cd08373:

Pssm-ID: 472691 [Multi-domain]  Cd Length: 127  Bit Score: 93.86  E-value: 2.47e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958804834   69 QEMKKRTRVEEG-NDPIWNETLIWHLWNQPlGNDSFLKVILQDSGSKKKERFIGLATVLLKQLVQRpNEVfyVKNLTLLN 147
Cdd:cd08373     24 RGVKKKTRVLENeLNPVWNETFEWPLAGSP-DPDESLEIVVKDYEKVGRNRLIGSATVSLQDLVSE-GLL--EVTEPLLD 99

                           90       100
                   ....*....|....*....|...
gi 1958804834  148 HSMNPTDCTITLQVAQIDDQGTK 170
Cdd:cd08373    100 SNGRPTGATISLEVSYQPPDGAV 122
C2 super family cl14603
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 385-507 9.43e-20

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 cd04018:

Pssm-ID: 472691 [Multi-domain]  Cd Length: 151  Bit Score: 87.30  E-value: 9.43e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958804834  385 PALEVELIGDKLRTYPKSQSDSPIWNQILTFQIQLPCLSSYIKFRVLDCSKSNCRDEIGSASLCLSQISSTGEEiqgmys 464
Cdd:cd04018     37 PYVEVSFAGQKVKTSVKKNSYNPEWNEQIVFPEMFPPLCERIKIQIRDWDRVGNDDVIGTHFIDLSKISNSGDE------ 110

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1958804834  465 GFLPCFGPSFLTLRGgekPPfrTTEEGTCILDAVNK---DGLAYRG 507
Cdd:cd04018    111 GFLPTFGPSFVNLYG---SP--REYSLLDDHQDLNEglgEGVAYRG 151
FerA super family cl06973
FerA (NUC095) domain; This is central domain A in proteins of the Ferlin family.
 659-705 1.10e-08

FerA (NUC095) domain; This is central domain A in proteins of the Ferlin family.


The actual alignment was detected with superfamily member pfam08165:

Pssm-ID: 462389  Cd Length: 65  Bit Score: 52.97  E-value: 1.10e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1958804834  659 WEKLLKDLQEDCRGPLPCMTDQPRANNLDKNKWKLRSYLLQQLEQRA 705
Cdd:pfam08165   15 WLKLLDQLIEDCSKPLPELEGKPNVTELDRQLRKLRKRALSQIKEAA 61
FerI super family cl06959
FerI (NUC094) domain; This domain is present in proteins of the Ferlin family. It is often ...
 315-348 1.89e-06

FerI (NUC094) domain; This domain is present in proteins of the Ferlin family. It is often located between two C2 domains.


The actual alignment was detected with superfamily member pfam08151:

Pssm-ID: 462377  Cd Length: 52  Bit Score: 46.39  E-value: 1.89e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1958804834  315 TTSGIRGYLKVTICALGVGDEAPVDQKLPYEDDS 348
Cdd:pfam08151    6 ISAGVKGYLKVDISVLGKGDEPPVEPTDKTSDAE 39
C2 super family cl14603
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 1527-1546 8.28e-03

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 cd04037:

Pssm-ID: 472691 [Multi-domain]  Cd Length: 124  Bit Score: 37.91  E-value: 8.28e-03
                           10        20
                   ....*....|....*....|
gi 1958804834 1527 LVRVYLIRAINLQPQDYNGL 1546
Cdd:cd04037      1 LVRVYVVRARNLQPKDPNGK 20
 
Name Accession Description Interval E-value
C2D_Ferlin cd04017
C2 domain fourth repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and ...
 1117-1252 4.10e-41

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: 148.07  E-value: 4.10e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958804834 1117 YQLFCYIYQARNLMYNQVLTFQESFIQVVFLNHSLCTQTLKSSAAPTWSQTLIFQHLLLFEDPKDTRENPPLVALELWQH 1196
Cdd:cd04017      1 FQLRAYIYQARDLLAADKSGLSDPFARVSFLNQSQETEVIKETLSPTWDQTLIFDEVELYGSPEEIAQNPPLVVVELFDQ 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958804834 1197 DSRGNKILWGRSMWPPVVWLGLQDWVFTPLRWHPLVReLGEEEGEILASCELILET 1252
Cdd:cd04017     81 DSVGKDEFLGRSVAKPLVKLDLEEDFPPKLQWFPIYK-GGQSAGELLAAFELIEVT 135
C2B_Ferlin cd04011
C2 domain second repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and ...
 203-310 5.18e-38

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: 138.09  E-value: 5.18e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958804834  203 PQHFQVRLKVFEARQLLGNNIKPVVKINIAGKQHLTRIQMGNN-PFFNEIFFQNFHEVPAKFFEENILIEVVDSAASRSK 281
Cdd:cd04011      1 PQDFQVRVRVIEARQLVGGNIDPVVKVEVGGQKKYTSVKKGTNcPFYNEYFFFNFHESPDELFDKIIKISVYDSRSLRSD 80

                           90       100
                   ....*....|....*....|....*....
gi 1958804834  282 AEIGRFQIDIGFIYHSPDHTLQRKWLGLC 310
Cdd:cd04011     81 TLIGSFKLDVGTVYDQPDHAFLRKWLLLT 109
FerB pfam08150
FerB (NUC096) domain; This is central domain B in proteins of the Ferlin family.
 731-803 1.17e-31

FerB (NUC096) domain; This is central domain B in proteins of the Ferlin family.


Pssm-ID: 462376  Cd Length: 76  Bit Score: 118.85  E-value: 1.17e-31
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958804834  731 PQESLPDVLIWLMSGQKRVAYARIPAHTVLFSTAgPMSSGKFCGKIQNLLLQYPE----GEGQNILPAYLRVCMWLG 803
Cdd:pfam08150    1 PQNSLPDVFIWMLSGGKRVAYARIPAHDILFSPV-EEERGKFCGKVQTLFLKYPGkkakGPAGWEIPAKLRVYLWLG 76
C2A_Ferlin cd08373
C2 domain first repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and ...
 69-170 2.47e-22

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: 93.86  E-value: 2.47e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958804834   69 QEMKKRTRVEEG-NDPIWNETLIWHLWNQPlGNDSFLKVILQDSGSKKKERFIGLATVLLKQLVQRpNEVfyVKNLTLLN 147
Cdd:cd08373     24 RGVKKKTRVLENeLNPVWNETFEWPLAGSP-DPDESLEIVVKDYEKVGRNRLIGSATVSLQDLVSE-GLL--EVTEPLLD 99

                           90       100
                   ....*....|....*....|...
gi 1958804834  148 HSMNPTDCTITLQVAQIDDQGTK 170
Cdd:cd08373    100 SNGRPTGATISLEVSYQPPDGAV 122
C2C_Ferlin cd04018
C2 domain third repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and ...
 385-507 9.43e-20

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: 87.30  E-value: 9.43e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958804834  385 PALEVELIGDKLRTYPKSQSDSPIWNQILTFQIQLPCLSSYIKFRVLDCSKSNCRDEIGSASLCLSQISSTGEEiqgmys 464
Cdd:cd04018     37 PYVEVSFAGQKVKTSVKKNSYNPEWNEQIVFPEMFPPLCERIKIQIRDWDRVGNDDVIGTHFIDLSKISNSGDE------ 110

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1958804834  465 GFLPCFGPSFLTLRGgekPPfrTTEEGTCILDAVNK---DGLAYRG 507
Cdd:cd04018    111 GFLPTFGPSFVNLYG---SP--REYSLLDDHQDLNEglgEGVAYRG 151
FerA pfam08165
FerA (NUC095) domain; This is central domain A in proteins of the Ferlin family.
 659-705 1.10e-08

FerA (NUC095) domain; This is central domain A in proteins of the Ferlin family.


Pssm-ID: 462389  Cd Length: 65  Bit Score: 52.97  E-value: 1.10e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1958804834  659 WEKLLKDLQEDCRGPLPCMTDQPRANNLDKNKWKLRSYLLQQLEQRA 705
Cdd:pfam08165   15 WLKLLDQLIEDCSKPLPELEGKPNVTELDRQLRKLRKRALSQIKEAA 61
FerI pfam08151
FerI (NUC094) domain; This domain is present in proteins of the Ferlin family. It is often ...
 315-348 1.89e-06

FerI (NUC094) domain; This domain is present in proteins of the Ferlin family. It is often located between two C2 domains.


Pssm-ID: 462377  Cd Length: 52  Bit Score: 46.39  E-value: 1.89e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1958804834  315 TTSGIRGYLKVTICALGVGDEAPVDQKLPYEDDS 348
Cdd:pfam08151    6 ISAGVKGYLKVDISVLGKGDEPPVEPTDKTSDAE 39
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 364-452 9.43e-06

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: 45.94  E-value: 9.43e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958804834   364 YLQFFIYCAEDL-HFRNPQSATPALEVELIGD---KLRTYPKSQSDSPIWNQILTFQIQLPCLSSyIKFRVLDCSKSNCR 439
Cdd:smart00239    1 TLTVKIISARNLpPKDKGGKSDPYVKVSLDGDpkeKKKTKVVKNTLNPVWNETFEFEVPPPELAE-LEIEVYDKDRFGRD 79

                            90
                    ....*....|...
gi 1958804834   440 DEIGSASLCLSQI 452
Cdd:smart00239   80 DFIGQVTIPLSDL 92
C2 pfam00168
C2 domain;
364-460 2.63e-05

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 44.62  E-value: 2.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958804834  364 YLQFFIYCAEDLHFRNPQSAT-PALEVELIGD--KLRTYPKSQSDSPIWNQILTFQIQLPcLSSYIKFRVLDCSKSNCRD 440
Cdd:pfam00168    2 RLTVTVIEAKNLPPKDGNGTSdPYVKVYLLDGkqKKKTKVVKNTLNPVWNETFTFSVPDP-ENAVLEIEVYDYDRFGRDD 80

                           90       100
                   ....*....|....*....|
gi 1958804834  441 EIGSASLCLSQISSTGEEIQ 460
Cdd:pfam00168   81 FIGEVRIPLSELDSGEGLDG 100
C2 pfam00168
C2 domain;
68-133 1.39e-04

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 42.69  E-value: 1.39e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958804834   68 RQEMKKRTRVEEGN-DPIWNETLIWHLwnqPLGNDSFLKVILQDSGSKKKERFIGLATVLLKQLVQR 133
Cdd:pfam00168   32 DGKQKKKTKVVKNTlNPVWNETFTFSV---PDPENAVLEIEVYDYDRFGRDDFIGEVRIPLSELDSG 95
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 72-134 1.59e-04

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: 42.47  E-value: 1.59e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958804834    72 KKRTRVEEGN-DPIWNETLIWHLwnqPLGNDSFLKVILQDSGSKKKERFIGLATVLLKQLVQRP 134
Cdd:smart00239   36 KKKTKVVKNTlNPVWNETFEFEV---PPPELAELEIEVYDKDRFGRDDFIGQVTIPLSDLLLGG 96
C2 pfam00168
C2 domain;
207-292 1.61e-04

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 42.31  E-value: 1.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958804834  207 QVRLKVFEARQLLGNNIK----PVVKINIAGKQHL--TRIQMGN-NPFFNEIFFqnFhEVPAkFFEENILIEVVDSAASR 279
Cdd:pfam00168    2 RLTVTVIEAKNLPPKDGNgtsdPYVKVYLLDGKQKkkTKVVKNTlNPVWNETFT--F-SVPD-PENAVLEIEVYDYDRFG 77

                           90
                   ....*....|...
gi 1958804834  280 SKAEIGRFQIDIG 292
Cdd:pfam00168   78 RDDFIGEVRIPLS 90
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 207-291 4.04e-04

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: 41.32  E-value: 4.04e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958804834   207 QVRLKVFEARQLLGNNIK----PVVKINIAGKQHL---TRIQMGN-NPFFNEIFFqnFHEVPakFFEENILIEVVDSAAS 278
Cdd:smart00239    1 TLTVKIISARNLPPKDKGgksdPYVKVSLDGDPKEkkkTKVVKNTlNPVWNETFE--FEVPP--PELAELEIEVYDKDRF 76

                            90
                    ....*....|...
gi 1958804834   279 RSKAEIGRFQIDI 291
Cdd:smart00239   77 GRDDFIGQVTIPL 89
C2E_Ferlin cd04037
C2 domain fifth repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and ...
 1527-1546 8.28e-03

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: 37.91  E-value: 8.28e-03
                           10        20
                   ....*....|....*....|
gi 1958804834 1527 LVRVYLIRAINLQPQDYNGL 1546
Cdd:cd04037      1 LVRVYVVRARNLQPKDPNGK 20
 
Name Accession Description Interval E-value
C2D_Ferlin cd04017
C2 domain fourth repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and ...
 1117-1252 4.10e-41

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: 148.07  E-value: 4.10e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958804834 1117 YQLFCYIYQARNLMYNQVLTFQESFIQVVFLNHSLCTQTLKSSAAPTWSQTLIFQHLLLFEDPKDTRENPPLVALELWQH 1196
Cdd:cd04017      1 FQLRAYIYQARDLLAADKSGLSDPFARVSFLNQSQETEVIKETLSPTWDQTLIFDEVELYGSPEEIAQNPPLVVVELFDQ 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958804834 1197 DSRGNKILWGRSMWPPVVWLGLQDWVFTPLRWHPLVReLGEEEGEILASCELILET 1252
Cdd:cd04017     81 DSVGKDEFLGRSVAKPLVKLDLEEDFPPKLQWFPIYK-GGQSAGELLAAFELIEVT 135
C2B_Ferlin cd04011
C2 domain second repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and ...
 203-310 5.18e-38

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: 138.09  E-value: 5.18e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958804834  203 PQHFQVRLKVFEARQLLGNNIKPVVKINIAGKQHLTRIQMGNN-PFFNEIFFQNFHEVPAKFFEENILIEVVDSAASRSK 281
Cdd:cd04011      1 PQDFQVRVRVIEARQLVGGNIDPVVKVEVGGQKKYTSVKKGTNcPFYNEYFFFNFHESPDELFDKIIKISVYDSRSLRSD 80

                           90       100
                   ....*....|....*....|....*....
gi 1958804834  282 AEIGRFQIDIGFIYHSPDHTLQRKWLGLC 310
Cdd:cd04011     81 TLIGSFKLDVGTVYDQPDHAFLRKWLLLT 109
FerB pfam08150
FerB (NUC096) domain; This is central domain B in proteins of the Ferlin family.
 731-803 1.17e-31

FerB (NUC096) domain; This is central domain B in proteins of the Ferlin family.


Pssm-ID: 462376  Cd Length: 76  Bit Score: 118.85  E-value: 1.17e-31
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958804834  731 PQESLPDVLIWLMSGQKRVAYARIPAHTVLFSTAgPMSSGKFCGKIQNLLLQYPE----GEGQNILPAYLRVCMWLG 803
Cdd:pfam08150    1 PQNSLPDVFIWMLSGGKRVAYARIPAHDILFSPV-EEERGKFCGKVQTLFLKYPGkkakGPAGWEIPAKLRVYLWLG 76
C2A_Ferlin cd08373
C2 domain first repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and ...
 69-170 2.47e-22

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: 93.86  E-value: 2.47e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958804834   69 QEMKKRTRVEEG-NDPIWNETLIWHLWNQPlGNDSFLKVILQDSGSKKKERFIGLATVLLKQLVQRpNEVfyVKNLTLLN 147
Cdd:cd08373     24 RGVKKKTRVLENeLNPVWNETFEWPLAGSP-DPDESLEIVVKDYEKVGRNRLIGSATVSLQDLVSE-GLL--EVTEPLLD 99

                           90       100
                   ....*....|....*....|...
gi 1958804834  148 HSMNPTDCTITLQVAQIDDQGTK 170
Cdd:cd08373    100 SNGRPTGATISLEVSYQPPDGAV 122
C2C_Ferlin cd04018
C2 domain third repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and ...
 385-507 9.43e-20

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: 87.30  E-value: 9.43e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958804834  385 PALEVELIGDKLRTYPKSQSDSPIWNQILTFQIQLPCLSSYIKFRVLDCSKSNCRDEIGSASLCLSQISSTGEEiqgmys 464
Cdd:cd04018     37 PYVEVSFAGQKVKTSVKKNSYNPEWNEQIVFPEMFPPLCERIKIQIRDWDRVGNDDVIGTHFIDLSKISNSGDE------ 110

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1958804834  465 GFLPCFGPSFLTLRGgekPPfrTTEEGTCILDAVNK---DGLAYRG 507
Cdd:cd04018    111 GFLPTFGPSFVNLYG---SP--REYSLLDDHQDLNEglgEGVAYRG 151
FerA pfam08165
FerA (NUC095) domain; This is central domain A in proteins of the Ferlin family.
 659-705 1.10e-08

FerA (NUC095) domain; This is central domain A in proteins of the Ferlin family.


Pssm-ID: 462389  Cd Length: 65  Bit Score: 52.97  E-value: 1.10e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1958804834  659 WEKLLKDLQEDCRGPLPCMTDQPRANNLDKNKWKLRSYLLQQLEQRA 705
Cdd:pfam08165   15 WLKLLDQLIEDCSKPLPELEGKPNVTELDRQLRKLRKRALSQIKEAA 61
FerI pfam08151
FerI (NUC094) domain; This domain is present in proteins of the Ferlin family. It is often ...
 315-348 1.89e-06

FerI (NUC094) domain; This domain is present in proteins of the Ferlin family. It is often located between two C2 domains.


Pssm-ID: 462377  Cd Length: 52  Bit Score: 46.39  E-value: 1.89e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1958804834  315 TTSGIRGYLKVTICALGVGDEAPVDQKLPYEDDS 348
Cdd:pfam08151    6 ISAGVKGYLKVDISVLGKGDEPPVEPTDKTSDAE 39
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 364-452 9.43e-06

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: 45.94  E-value: 9.43e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958804834   364 YLQFFIYCAEDL-HFRNPQSATPALEVELIGD---KLRTYPKSQSDSPIWNQILTFQIQLPCLSSyIKFRVLDCSKSNCR 439
Cdd:smart00239    1 TLTVKIISARNLpPKDKGGKSDPYVKVSLDGDpkeKKKTKVVKNTLNPVWNETFEFEVPPPELAE-LEIEVYDKDRFGRD 79

                            90
                    ....*....|...
gi 1958804834   440 DEIGSASLCLSQI 452
Cdd:smart00239   80 DFIGQVTIPLSDL 92
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 365-459 2.20e-05

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: 44.75  E-value: 2.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958804834  365 LQFFIYCAEDLHFRNPQSAT-PALEVELIGD-KLRTYPKSQSDSPIWNQILTFQIqLPCLSSYIKFRVLDCSKSNCRDEI 442
Cdd:cd00030      1 LRVTVIEARNLPAKDLNGKSdPYVKVSLGGKqKFKTKVVKNTLNPVWNETFEFPV-LDPESDTLTVEVWDKDRFSKDDFL 79

                           90
                   ....*....|....*..
gi 1958804834  443 GSASLCLSQISSTGEEI 459
Cdd:cd00030     80 GEVEIPLSELLDSGKEG 96
C2 pfam00168
C2 domain;
364-460 2.63e-05

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 44.62  E-value: 2.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958804834  364 YLQFFIYCAEDLHFRNPQSAT-PALEVELIGD--KLRTYPKSQSDSPIWNQILTFQIQLPcLSSYIKFRVLDCSKSNCRD 440
Cdd:pfam00168    2 RLTVTVIEAKNLPPKDGNGTSdPYVKVYLLDGkqKKKTKVVKNTLNPVWNETFTFSVPDP-ENAVLEIEVYDYDRFGRDD 80

                           90       100
                   ....*....|....*....|
gi 1958804834  441 EIGSASLCLSQISSTGEEIQ 460
Cdd:pfam00168   81 FIGEVRIPLSELDSGEGLDG 100
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 208-309 2.72e-05

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: 44.37  E-value: 2.72e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958804834  208 VRLKVFEARQLLGNNIK----PVVKINIAGKQHL-TRIQMGN-NPFFNEIFfqNFHEVPAKffEENILIEVVDSAASRSK 281
Cdd:cd00030      1 LRVTVIEARNLPAKDLNgksdPYVKVSLGGKQKFkTKVVKNTlNPVWNETF--EFPVLDPE--SDTLTVEVWDKDRFSKD 76

                           90       100
                   ....*....|....*....|....*...
gi 1958804834  282 AEIGRFQIDIGFIYHSPDHTLQrkWLGL 309
Cdd:cd00030     77 DFLGEVEIPLSELLDSGKEGEL--WLPL 102
C2 pfam00168
C2 domain;
68-133 1.39e-04

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 42.69  E-value: 1.39e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958804834   68 RQEMKKRTRVEEGN-DPIWNETLIWHLwnqPLGNDSFLKVILQDSGSKKKERFIGLATVLLKQLVQR 133
Cdd:pfam00168   32 DGKQKKKTKVVKNTlNPVWNETFTFSV---PDPENAVLEIEVYDYDRFGRDDFIGEVRIPLSELDSG 95
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 72-134 1.59e-04

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: 42.47  E-value: 1.59e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958804834    72 KKRTRVEEGN-DPIWNETLIWHLwnqPLGNDSFLKVILQDSGSKKKERFIGLATVLLKQLVQRP 134
Cdd:smart00239   36 KKKTKVVKNTlNPVWNETFEFEV---PPPELAELEIEVYDKDRFGRDDFIGQVTIPLSDLLLGG 96
C2 pfam00168
C2 domain;
207-292 1.61e-04

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 42.31  E-value: 1.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958804834  207 QVRLKVFEARQLLGNNIK----PVVKINIAGKQHL--TRIQMGN-NPFFNEIFFqnFhEVPAkFFEENILIEVVDSAASR 279
Cdd:pfam00168    2 RLTVTVIEAKNLPPKDGNgtsdPYVKVYLLDGKQKkkTKVVKNTlNPVWNETFT--F-SVPD-PENAVLEIEVYDYDRFG 77

                           90
                   ....*....|...
gi 1958804834  280 SKAEIGRFQIDIG 292
Cdd:pfam00168   78 RDDFIGEVRIPLS 90
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 207-291 4.04e-04

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: 41.32  E-value: 4.04e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958804834   207 QVRLKVFEARQLLGNNIK----PVVKINIAGKQHL---TRIQMGN-NPFFNEIFFqnFHEVPakFFEENILIEVVDSAAS 278
Cdd:smart00239    1 TLTVKIISARNLPPKDKGgksdPYVKVSLDGDPKEkkkTKVVKNTlNPVWNETFE--FEVPP--PELAELEIEVYDKDRF 76

                            90
                    ....*....|...
gi 1958804834   279 RSKAEIGRFQIDI 291
Cdd:smart00239   77 GRDDFIGQVTIPL 89
C2_E3_ubiquitin_ligase cd04021
C2 domain present in E3 ubiquitin ligase; E3 ubiquitin ligase is part of the ubiquitylation ...
 385-452 4.88e-04

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: 41.49  E-value: 4.88e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958804834  385 PALEVELIGDKL---RTYPKSQSDSPIWNQILTFQIQlPclSSYIKFRVLDCSKSNcRDE-IGSASLCLSQI 452
Cdd:cd04021     22 PDPYVEVTVDGQppkKTEVSKKTSNPKWNEHFTVLVT-P--QSTLEFKVWSHHTLK-ADVlLGEASLDLSDI 89
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 72-136 8.38e-04

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: 40.13  E-value: 8.38e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958804834   72 KKRTRVEEGN-DPIWNETLIWHLwnqPLGNDSFLKVILQDSGSKKKERFIGLATVLLKQLVQRPNE 136
Cdd:cd00030     33 KFKTKVVKNTlNPVWNETFEFPV---LDPESDTLTVEVWDKDRFSKDDFLGEVEIPLSELLDSGKE 95
C2C_Ferlin cd04018
C2 domain third repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and ...
 1139-1171 4.05e-03

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: 39.54  E-value: 4.05e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1958804834 1139 ESFIQVVFLNHSLCTQTLKSSAAPTWSQTLIFQ 1171
Cdd:cd04018     36 DPYVEVSFAGQKVKTSVKKNSYNPEWNEQIVFP 68
C2_SRC2_like cd04051
C2 domain present in Soybean genes Regulated by Cold 2 (SRC2)-like proteins; SRC2 production ...
 70-134 6.98e-03

C2 domain present in Soybean genes Regulated by Cold 2 (SRC2)-like proteins; SRC2 production is a response to pathogen infiltration. The initial response of increased Ca2+ concentrations are coupled to downstream signal transduction pathways via calcium binding proteins. SRC2 contains a single C2 domain which localizes to the plasma membrane and is involved in Ca2+ dependent protein binding. 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: 176016 [Multi-domain]  Cd Length: 125  Bit Score: 38.37  E-value: 6.98e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958804834   70 EMKKRTRVEE--GNDPIWNETLIWHLWNQPL-GNDSFLKVILQDSGSKKKERFIGLATVLLKQLVQRP 134
Cdd:cd04051     32 SHKQSTPVDRdgGTNPTWNETLRFPLDERLLqQGRLALTIEVYCERPSLGDKLIGEVRVPLKDLLDGA 99
C2D_Tricalbin-like cd04040
C2 domain fourth repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are ...
 372-452 7.14e-03

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: 37.93  E-value: 7.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958804834  372 AEDL--HFRNPQSaTPALEVELIGDKL-RTYPKSQSDSPIWNQilTFQIQLPCLS-SYIKFRVLDCSKSNCRDEIGSASL 447
Cdd:cd04040      8 AENLpsADRNGKS-DPFVKFYLNGEKVfKTKTIKKTLNPVWNE--SFEVPVPSRVrAVLKVEVYDWDRGGKDDLLGSAYI 84


                   ....*
gi 1958804834  448 CLSQI 452
Cdd:cd04040     85 DLSDL 89
C2E_Ferlin cd04037
C2 domain fifth repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and ...
 1527-1546 8.28e-03

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: 37.91  E-value: 8.28e-03
                           10        20
                   ....*....|....*....|
gi 1958804834 1527 LVRVYLIRAINLQPQDYNGL 1546
Cdd:cd04037      1 LVRVYVVRARNLQPKDPNGK 20
C2_putative_Elicitor-responsive_gene cd04049
C2 domain present in the putative elicitor-responsive gene; In plants elicitor-responsive ...
 401-458 9.65e-03

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: 37.70  E-value: 9.65e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958804834  401 KSQSDSPIWNQILTFQIQLPCLS--SYIKFRVLDCSKSNCRDEIGSASLCLSQISSTGEE 458
Cdd:cd04049     41 KGDGRNPEWNEKFKFTVEYPGWGgdTKLILRIMDKDNFSDDDFIGEATIHLKGLFEEGVE 100
 
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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