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Conserved domains on  [gi|205646145|sp|Q8N5R6|]
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RecName: Full=Coiled-coil domain-containing protein 33; AltName: Full=Cancer/testis antigen 61; Short=CT61

Protein Classification

C2 domain-containing protein( domain architecture ID 10033612)

C2 domain-containing protein may be a Ca2+-dependent membrane-targeting protein that binds a wide variety of substances including phospholipids, inositol polyphosphates, and intracellular proteins through its C2 domain

CATH:  2.60.40.150
Gene Ontology:  GO:0005544|GO:0005509
PubMed:  8976547|9632630
SCOP:  3000965

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 240-335 3.65e-06

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: 46.29  E-value: 3.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205646145 240 IMVTLHGATNLPACKDGSEPWPYVVVKSTSEEKnnqsskaVTSVTSEPTRAPIWGDTVNVEIqaEDAGQEDVILKV--VD 317
Cdd:cd00030    1 LRVTVIEARNLPAKDLNGKSDPYVKVSLGGKQK-------FKTKVVKNTLNPVWNETFEFPV--LDPESDTLTVEVwdKD 71

                         90
                 ....*....|....*....
gi 205646145 318 NRKKQELL-SYKIPIKYLR 335
Cdd:cd00030   72 RFSKDDFLgEVEIPLSELL 90
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 630-880 4.53e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 44.28  E-value: 4.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205646145   630 SHDTEMNNYRRAMQKMAEDILSLRRQASILEGENRILRSRLA--QQEEEEGQGKASEAQNTVS--------MKQKLLLSE 699
Cdd:TIGR02168  236 ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSelEEEIEELQKELYALANEISrleqqkqiLRERLANLE 315

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205646145   700 LDMKKLRDRVQHLQNELIRK----NDREKELLLLYQAQQPQAALLKQYQGKLQKMKALEETV--------------RHQE 761
Cdd:TIGR02168  316 RQLEELEAQLEELESKLDELaeelAELEEKLEELKEELESLEAELEELEAELEELESRLEELeeqletlrskvaqlELQI 395

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205646145   762 KVIEKMERVLEDRLQDrskpppLNRQQGKpytgfpmLSASGLPLGSMGENLPVELYSVLLAENAKLRTELDK--NRHQQA 839
Cdd:TIGR02168  396 ASLNNEIERLEARLER------LEDRRER-------LQQEIEELLKKLEEAELKELQAELEELEEELEELQEelERLEEA 462

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 205646145   840 PIILQQQalpdLLSGTSDKFNLLAKLEHAQSRILSLESQLE 880
Cdd:TIGR02168  463 LEELREE----LEEAEQALDAAERELAQLQARLDSLERLQE 499
 
Name Accession Description Interval E-value
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 240-335 3.65e-06

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: 46.29  E-value: 3.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205646145 240 IMVTLHGATNLPACKDGSEPWPYVVVKSTSEEKnnqsskaVTSVTSEPTRAPIWGDTVNVEIqaEDAGQEDVILKV--VD 317
Cdd:cd00030    1 LRVTVIEARNLPAKDLNGKSDPYVKVSLGGKQK-------FKTKVVKNTLNPVWNETFEFPV--LDPESDTLTVEVwdKD 71

                         90
                 ....*....|....*....
gi 205646145 318 NRKKQELL-SYKIPIKYLR 335
Cdd:cd00030   72 RFSKDDFLgEVEIPLSELL 90
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 630-880 4.53e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 44.28  E-value: 4.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205646145   630 SHDTEMNNYRRAMQKMAEDILSLRRQASILEGENRILRSRLA--QQEEEEGQGKASEAQNTVS--------MKQKLLLSE 699
Cdd:TIGR02168  236 ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSelEEEIEELQKELYALANEISrleqqkqiLRERLANLE 315

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205646145   700 LDMKKLRDRVQHLQNELIRK----NDREKELLLLYQAQQPQAALLKQYQGKLQKMKALEETV--------------RHQE 761
Cdd:TIGR02168  316 RQLEELEAQLEELESKLDELaeelAELEEKLEELKEELESLEAELEELEAELEELESRLEELeeqletlrskvaqlELQI 395

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205646145   762 KVIEKMERVLEDRLQDrskpppLNRQQGKpytgfpmLSASGLPLGSMGENLPVELYSVLLAENAKLRTELDK--NRHQQA 839
Cdd:TIGR02168  396 ASLNNEIERLEARLER------LEDRRER-------LQQEIEELLKKLEEAELKELQAELEELEEELEELQEelERLEEA 462

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 205646145   840 PIILQQQalpdLLSGTSDKFNLLAKLEHAQSRILSLESQLE 880
Cdd:TIGR02168  463 LEELREE----LEEAEQALDAAERELAQLQARLDSLERLQE 499
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 639-901 9.46e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 9.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205646145 639 RRAMQKMAEDILSLRRQASILEGENRILRSRLAQQEEEEGQGKASEAQNT---VSMKQKLLLSELDMKKLRDRVQHLQNE 715
Cdd:COG1196  280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEeelEELEEELEELEEELEEAEEELEEAEAE 359

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205646145 716 LIRKNDREKELLLLYQAQqpQAALLKQYQGKLQKMKALEEtvrhQEKVIEKMERVLEDRLQDRSKpppLNRQQGKpytgf 795
Cdd:COG1196  360 LAEAEEALLEAEAELAEA--EEELEELAEELLEALRAAAE----LAAQLEELEEAEEALLERLER---LEEELEE----- 425

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205646145 796 pmLSASGLPLgsmgENLPVELYSVLLAENAKLRTELDKNRHQQAPIILQQQALPDLLSGTSDKFNLLAKLEHAQSRILSL 875
Cdd:COG1196  426 --LEEALAEL----EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA 499

                        250       260
                 ....*....|....*....|....*.
gi 205646145 876 ESQLEDSARRWGREKQDLATRLQEQE 901
Cdd:COG1196  500 EADYEGFLEGVKAALLLAGLRGLAGA 525
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 239-323 9.25e-03

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: 36.70  E-value: 9.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205646145   239 TIMVTLHGATNLPACKDGSEPWPYVVVKSTSEEKNNQSSKAVTSvtsepTRAPIWGDTVNVEIQaeDAGQEDVILKVVDN 318
Cdd:smart00239   1 TLTVKIISARNLPPKDKGGKSDPYVKVSLDGDPKEKKKTKVVKN-----TLNPVWNETFEFEVP--PPELAELEIEVYDK 73


                   ....*
gi 205646145   319 RKKQE 323
Cdd:smart00239  74 DRFGR 78
PRK12704 PRK12704
phosphodiesterase; Provisional
 655-776 9.42e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 39.76  E-value: 9.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205646145 655 QASILEGENRilRSRLAQQEEEEGQGKASEAQNTVSMKQKLLLSELDmKKLRDR---VQHLQNELIRKN---DREKELLl 728
Cdd:PRK12704  30 EAKIKEAEEE--AKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFE-KELRERrneLQKLEKRLLQKEenlDRKLELL- 105

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 205646145 729 lyqaQQPQAALLKQYQGKLQKMKALEEtvrhQEKVIEKMERVLEDRLQ 776
Cdd:PRK12704 106 ----EKREEELEKKEKELEQKQQELEK----KEEELEELIEEQLQELE 145
 
Name Accession Description Interval E-value
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 240-335 3.65e-06

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: 46.29  E-value: 3.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205646145 240 IMVTLHGATNLPACKDGSEPWPYVVVKSTSEEKnnqsskaVTSVTSEPTRAPIWGDTVNVEIqaEDAGQEDVILKV--VD 317
Cdd:cd00030    1 LRVTVIEARNLPAKDLNGKSDPYVKVSLGGKQK-------FKTKVVKNTLNPVWNETFEFPV--LDPESDTLTVEVwdKD 71

                         90
                 ....*....|....*....
gi 205646145 318 NRKKQELL-SYKIPIKYLR 335
Cdd:cd00030   72 RFSKDDFLgEVEIPLSELL 90
C2B_Synaptotagmin-like cd04050
C2 domain second repeat present in Synaptotagmin-like proteins; Synaptotagmin is a ...
 241-334 1.71e-05

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


Pssm-ID: 176015 [Multi-domain]  Cd Length: 105  Bit Score: 44.48  E-value: 1.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205646145 241 MVTLHGATNLPACKDGSEPWPYVVVkstSEEKNNQSSKAVTSvtsepTRAPIWGDTVNVEIQaeDAGQEDVILKVVDNRK 320
Cdd:cd04050    3 FVYLDSAKNLPLAKSTKEPSPYVEL---TVGKTTQKSKVKER-----TNNPVWEEGFTFLVR--NPENQELEIEVKDDKT 72

                         90
                 ....*....|....
gi 205646145 321 KQELLSYKIPIKYL 334
Cdd:cd04050   73 GKSLGSLTLPLSEL 86
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 630-880 4.53e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 44.28  E-value: 4.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205646145   630 SHDTEMNNYRRAMQKMAEDILSLRRQASILEGENRILRSRLA--QQEEEEGQGKASEAQNTVS--------MKQKLLLSE 699
Cdd:TIGR02168  236 ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSelEEEIEELQKELYALANEISrleqqkqiLRERLANLE 315

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205646145   700 LDMKKLRDRVQHLQNELIRK----NDREKELLLLYQAQQPQAALLKQYQGKLQKMKALEETV--------------RHQE 761
Cdd:TIGR02168  316 RQLEELEAQLEELESKLDELaeelAELEEKLEELKEELESLEAELEELEAELEELESRLEELeeqletlrskvaqlELQI 395

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205646145   762 KVIEKMERVLEDRLQDrskpppLNRQQGKpytgfpmLSASGLPLGSMGENLPVELYSVLLAENAKLRTELDK--NRHQQA 839
Cdd:TIGR02168  396 ASLNNEIERLEARLER------LEDRRER-------LQQEIEELLKKLEEAELKELQAELEELEEELEELQEelERLEEA 462

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 205646145   840 PIILQQQalpdLLSGTSDKFNLLAKLEHAQSRILSLESQLE 880
Cdd:TIGR02168  463 LEELREE----LEEAEQALDAAERELAQLQARLDSLERLQE 499
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 639-901 9.46e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 9.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205646145 639 RRAMQKMAEDILSLRRQASILEGENRILRSRLAQQEEEEGQGKASEAQNT---VSMKQKLLLSELDMKKLRDRVQHLQNE 715
Cdd:COG1196  280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEeelEELEEELEELEEELEEAEEELEEAEAE 359

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205646145 716 LIRKNDREKELLLLYQAQqpQAALLKQYQGKLQKMKALEEtvrhQEKVIEKMERVLEDRLQDRSKpppLNRQQGKpytgf 795
Cdd:COG1196  360 LAEAEEALLEAEAELAEA--EEELEELAEELLEALRAAAE----LAAQLEELEEAEEALLERLER---LEEELEE----- 425

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205646145 796 pmLSASGLPLgsmgENLPVELYSVLLAENAKLRTELDKNRHQQAPIILQQQALPDLLSGTSDKFNLLAKLEHAQSRILSL 875
Cdd:COG1196  426 --LEEALAEL----EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA 499

                        250       260
                 ....*....|....*....|....*.
gi 205646145 876 ESQLEDSARRWGREKQDLATRLQEQE 901
Cdd:COG1196  500 EADYEGFLEGVKAALLLAGLRGLAGA 525
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 646-902 1.13e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 1.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205646145 646 AEDILSLRRQASILEGENRILRSRLAQQEEEEGQGKASEAQNtvsmKQKLLLSELDmkKLRDRVQHLQNELIRKNDREKE 725
Cdd:COG1196  212 AERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEA----ELEELEAELA--ELEAELEELRLELEELELELEE 285

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205646145 726 LLL-LYQAQQPQAALLKQYQGKLQKMKALEETVRHQEKVIEKMERVLEDRLQDRSKpppLNRQQgkpytgfpmlsasglp 804
Cdd:COG1196  286 AQAeEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE---LEEEL---------------- 346

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205646145 805 lgsmgENLpVELYSVLLAENAKLRTELDKNRHQQAPIILQQQALpdllsgTSDKFNLLAKLEHAQSRILSLESQLEDSAR 884
Cdd:COG1196  347 -----EEA-EEELEEAEAELAEAEEALLEAEAELAEAEEELEEL------AEELLEALRAAAELAAQLEELEEAEEALLE 414

                        250
                 ....*....|....*...
gi 205646145 885 RWGREKQDLATRLQEQEK 902
Cdd:COG1196  415 RLERLEEELEELEEALAE 432
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
632-902 4.45e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 4.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205646145 632 DTEMNNYRRAMQKMAEDILSLRRQASILEGENRI--LRSRLAQQEEEegqgkaseaqntvsmKQKLLLSELDMKKLRDRV 709
Cdd:COG4717  101 EEELEELEAELEELREELEKLEKLLQLLPLYQELeaLEAELAELPER---------------LEELEERLEELRELEEEL 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205646145 710 QHLQNELIRKNDREKELLLLYQAQQPQAA--LLKQYQGKLQKMKALEETVRHQEKVIEKMERVLEdRLQDRSKPPPLNRQ 787
Cdd:COG4717  166 EELEAELAELQEELEELLEQLSLATEEELqdLAEELEELQQRLAELEEELEEAQEELEELEEELE-QLENELEAAALEER 244

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205646145 788 QGKPYTGFPMLSASGLPLGSMGEN----------------LPVELYSVLLAENAKLRTELDKNRHQQAPIILQQQALPDL 851
Cdd:COG4717  245 LKEARLLLLIAAALLALLGLGGSLlsliltiagvlflvlgLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEEL 324

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 205646145 852 LsgtsDKFNLLAKLEHAQSRILSLE-SQLEDSARRWGREKQDLATRLQEQEK 902
Cdd:COG4717  325 L----AALGLPPDLSPEELLELLDRiEELQELLREAEELEEELQLEELEQEI 372
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 591-776 5.68e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 40.72  E-value: 5.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205646145   591 DKKLRTIQESWSKDTVSSTMDLSTSTPREAEEEPLVPE--MSHDTEMNNYRRAMQKMAEDILSLRRQASILEGENRILRS 668
Cdd:TIGR00618  477 TKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNpaRQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERK 556

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205646145   669 RLAQQEEEEgqgkASEAQNTVSMKQKLLLSELDMKKLRDRVQHLQNELIRKNDREKELLLLYQAQ----QPQAALLK--Q 742
Cdd:TIGR00618  557 QRASLKEQM----QEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALlrklQPEQDLQDvrL 632

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 205646145   743 YQGKLQKMKALEETVRH-------QEKVIEKMERVLEDRLQ 776
Cdd:TIGR00618  633 HLQQCSQELALKLTALHalqltltQERVREHALSIRVLPKE 673
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
634-779 6.98e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.89  E-value: 6.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205646145 634 EMNNYRRAMQKMAEDILSLRRQASILEGENRILRSRLAQQEEE--EGQGKASEAQNTVS-MKQKLLLSELDMKKLRDRVQ 710
Cdd:COG4372   39 ELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEleELNEQLQAAQAELAqAQEELESLQEEAEELQEELE 118

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 205646145 711 HLQNELIRKNDREKELlllyqaQQPQAALLKQYQGKLQKMKALEETVRHQEKVIEKMERVLEDRLQDRS 779
Cdd:COG4372  119 ELQKERQDLEQQRKQL------EAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEA 181
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 239-323 9.25e-03

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: 36.70  E-value: 9.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205646145   239 TIMVTLHGATNLPACKDGSEPWPYVVVKSTSEEKNNQSSKAVTSvtsepTRAPIWGDTVNVEIQaeDAGQEDVILKVVDN 318
Cdd:smart00239   1 TLTVKIISARNLPPKDKGGKSDPYVKVSLDGDPKEKKKTKVVKN-----TLNPVWNETFEFEVP--PPELAELEIEVYDK 73


                   ....*
gi 205646145   319 RKKQE 323
Cdd:smart00239  74 DRFGR 78
PRK12704 PRK12704
phosphodiesterase; Provisional
 655-776 9.42e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 39.76  E-value: 9.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205646145 655 QASILEGENRilRSRLAQQEEEEGQGKASEAQNTVSMKQKLLLSELDmKKLRDR---VQHLQNELIRKN---DREKELLl 728
Cdd:PRK12704  30 EAKIKEAEEE--AKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFE-KELRERrneLQKLEKRLLQKEenlDRKLELL- 105

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 205646145 729 lyqaQQPQAALLKQYQGKLQKMKALEEtvrhQEKVIEKMERVLEDRLQ 776
Cdd:PRK12704 106 ----EKREEELEKKEKELEQKQQELEK----KEEELEELIEEQLQELE 145
 
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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