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Conserved domains on  [gi|1039793614|ref|XP_017168935|]
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coiled-coil domain-containing protein 33 isoform X4 [Mus musculus]

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 ...
 283-365 5.85e-07

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: 48.60  E-value: 5.85e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793614  283 ITVTLYGATNLPAGKDGSEPWPYVVVKTTSEKANKhspqamtSVTSEPTRAPVWGDTVNVEIqaEDTGREDLILKVMDNK 362
Cdd:cd00030      1 LRVTVIEARNLPAKDLNGKSDPYVKVSLGGKQKFK-------TKVVKNTLNPVWNETFEFPV--LDPESDTLTVEVWDKD 71


                   ...
gi 1039793614  363 RKK 365
Cdd:cd00030     72 RFS 74
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 649-832 1.42e-05

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


The actual alignment was detected with superfamily member TIGR02169:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1164  Bit Score: 49.30  E-value: 1.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793614  649 TQEMEELQPRDVEMNNYRRAMQKMAEDILALKKQANILEEENGMLRSHLSQQSIE---------EQSRAEEENLAVSMKQ 719
Cdd:TIGR02169  740 EELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPeiqaelsklEEEVSRIEARLREIEQ 819

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793614  720 KLLLNELDMKRLRDRVQHLQNELI----RKNDREKELLLLYQAQQPQAAQLRRY-------------------------- 769
Cdd:TIGR02169  820 KLNRLTLEKEYLEKEIQELQEQRIdlkeQIKSIEKEIENLNGKKEELEEELEELeaalrdlesrlgdlkkerdeleaqlr 899

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039793614  770 --QDKLQKMKALEDTVRHQEKVIEKMEQILEERLCERKEPIpsnrPQGKPIMASGIPLGPVGETL 832
Cdd:TIGR02169  900 elERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPK----GEDEEIPEEELSLEDVQAEL 960
 
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 ...
 283-365 5.85e-07

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: 48.60  E-value: 5.85e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793614  283 ITVTLYGATNLPAGKDGSEPWPYVVVKTTSEKANKhspqamtSVTSEPTRAPVWGDTVNVEIqaEDTGREDLILKVMDNK 362
Cdd:cd00030      1 LRVTVIEARNLPAKDLNGKSDPYVKVSLGGKQKFK-------TKVVKNTLNPVWNETFEFPV--LDPESDTLTVEVWDKD 71


                   ...
gi 1039793614  363 RKK 365
Cdd:cd00030     72 RFS 74
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 649-832 1.42e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 49.30  E-value: 1.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793614  649 TQEMEELQPRDVEMNNYRRAMQKMAEDILALKKQANILEEENGMLRSHLSQQSIE---------EQSRAEEENLAVSMKQ 719
Cdd:TIGR02169  740 EELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPeiqaelsklEEEVSRIEARLREIEQ 819

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793614  720 KLLLNELDMKRLRDRVQHLQNELI----RKNDREKELLLLYQAQQPQAAQLRRY-------------------------- 769
Cdd:TIGR02169  820 KLNRLTLEKEYLEKEIQELQEQRIdlkeQIKSIEKEIENLNGKKEELEEELEELeaalrdlesrlgdlkkerdeleaqlr 899

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039793614  770 --QDKLQKMKALEDTVRHQEKVIEKMEQILEERLCERKEPIpsnrPQGKPIMASGIPLGPVGETL 832
Cdd:TIGR02169  900 elERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPK----GEDEEIPEEELSLEDVQAEL 960
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 282-366 1.11e-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: 42.09  E-value: 1.11e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793614   282 TITVTLYGATNLPAGKDGSEPWPYVVVKTTSEKANKHSpqamTSVTSEpTRAPVWGDTVNVEIQaeDTGREDLILKVMDN 361
Cdd:smart00239    1 TLTVKIISARNLPPKDKGGKSDPYVKVSLDGDPKEKKK----TKVVKN-TLNPVWNETFEFEVP--PPELAELEIEVYDK 73


                    ....*
gi 1039793614   362 KRKKE 366
Cdd:smart00239   74 DRFGR 78
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
650-1007 1.70e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.53  E-value: 1.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793614  650 QEMEELQPRDVEMNNYRRAMQKMAEDILALKKQANILEEENGMLRSHLSQQSIEEQSRAEEENLAVSMKQ--KLLLNELD 727
Cdd:COG4717     78 EELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERleELEERLEE 157

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793614  728 MKRLRDRVQHLQNELIRKNDREKELL--LLYQAQQPQAAQLRRYQDKLQKMKALEDTVRHQEKVIEKMEQILEERLCERK 805
Cdd:COG4717    158 LRELEEELEELEAELAELQEELEELLeqLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELE 237

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793614  806 EPIPSNRPQ------------------GKPIMASGIPLGPVG---ETLAVDLYSMLLAENTRLRTELEKNRQQSAPIILQ 864
Cdd:COG4717    238 AAALEERLKearlllliaaallallglGGSLLSLILTIAGVLflvLGLLALLFLLLAREKASLGKEAEELQALPALEELE 317

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793614  865 QQALPvdprelgaggDLAERLqdtngpGHPKSTETLPAQDFLGGTSDKFNLLAKLEQAQSRIL--SLENQL--------- 933
Cdd:COG4717    318 EEELE----------ELLAAL------GLPPDLSPEELLELLDRIEELQELLREAEELEEELQleELEQEIaallaeagv 381

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039793614  934 --EESARHWA---REKQNLAIRLQEQQHGFGQPPNSIIIDQPNAGASKNRQQLSKLETSLPSSDKKLNRPSDSQIEISN 1007
Cdd:COG4717    382 edEEELRAALeqaEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEA 460
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 649-945 9.32e-04

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 43.24  E-value: 9.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793614  649 TQEMEELQPRDVEMNNYRRAMQKMAEDILALKKQANILEEENGMLRSHLsQQSIEEQSRAEE--ENLAvSMKQKL--LLN 724
Cdd:pfam01576    1 TRQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQL-QAETELCAEAEEmrARLA-ARKQELeeILH 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793614  725 ELDmKRL---RDRVQHLQNElirKNDREKELLLLYQAQQPQAAQLRRYQ-DKLQ---KMKALED---TVRHQEKVIEKME 794
Cdd:pfam01576   79 ELE-SRLeeeEERSQQLQNE---KKKMQQHIQDLEEQLDEEEAARQKLQlEKVTteaKIKKLEEdilLLEDQNSKLSKER 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793614  795 QILEERLCErkepIPSNRPQGKPIMASGIPLGPVGETLAVDLYSMLLAENtRLRTELEKNRQQSapiilqqQALPVDPRE 874
Cdd:pfam01576  155 KLLEERISE----FTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEE-KGRQELEKAKRKL-------EGESTDLQE 222

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039793614  875 LGAggDLAERLQDTNGPGHPKSTETLPAQDFLGG-TSDKFNLLAKLEQAQSRILSLENQL--EESARHWArEKQ 945
Cdd:pfam01576  223 QIA--ELQAQIAELRAQLAKKEEELQAALARLEEeTAQKNNALKKIRELEAQISELQEDLesERAARNKA-EKQ 293
C2 pfam00168
C2 domain;
282-363 1.90e-03

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 38.84  E-value: 1.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793614  282 TITVTLYGATNLPAGKDGSEPWPYVVVKTTSEKaNKHSpqamTSVTSEpTRAPVWGDTVNVEIQAEDTgrEDLILKVMDN 361
Cdd:pfam00168    2 RLTVTVIEAKNLPPKDGNGTSDPYVKVYLLDGK-QKKK----TKVVKN-TLNPVWNETFTFSVPDPEN--AVLEIEVYDY 73


                   ..
gi 1039793614  362 KR 363
Cdd:pfam00168   74 DR 75
 
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 ...
 283-365 5.85e-07

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: 48.60  E-value: 5.85e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793614  283 ITVTLYGATNLPAGKDGSEPWPYVVVKTTSEKANKhspqamtSVTSEPTRAPVWGDTVNVEIqaEDTGREDLILKVMDNK 362
Cdd:cd00030      1 LRVTVIEARNLPAKDLNGKSDPYVKVSLGGKQKFK-------TKVVKNTLNPVWNETFEFPV--LDPESDTLTVEVWDKD 71


                   ...
gi 1039793614  363 RKK 365
Cdd:cd00030     72 RFS 74
C2B_Synaptotagmin-like cd04050
C2 domain second repeat present in Synaptotagmin-like proteins; Synaptotagmin is a ...
 284-391 1.04e-06

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: 47.94  E-value: 1.04e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793614  284 TVTLYGATNLPAGKDGSEPWPYVVVKT--TSEKankhspqamtSVTSEPTRAPVWGDTVNVEIQaeDTGREDLILKVMDN 361
Cdd:cd04050      3 FVYLDSAKNLPLAKSTKEPSPYVELTVgkTTQK----------SKVKERTNNPVWEEGFTFLVR--NPENQELEIEVKDD 70

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1039793614  362 KRKKELVSYDIPIKYL-----RIFHPyQFKLEKSE 391
Cdd:cd04050     71 KTGKSLGSLTLPLSELlkepdLTLDQ-PFPLDNSG 104
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 649-832 1.42e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 49.30  E-value: 1.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793614  649 TQEMEELQPRDVEMNNYRRAMQKMAEDILALKKQANILEEENGMLRSHLSQQSIE---------EQSRAEEENLAVSMKQ 719
Cdd:TIGR02169  740 EELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPeiqaelsklEEEVSRIEARLREIEQ 819

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793614  720 KLLLNELDMKRLRDRVQHLQNELI----RKNDREKELLLLYQAQQPQAAQLRRY-------------------------- 769
Cdd:TIGR02169  820 KLNRLTLEKEYLEKEIQELQEQRIdlkeQIKSIEKEIENLNGKKEELEEELEELeaalrdlesrlgdlkkerdeleaqlr 899

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039793614  770 --QDKLQKMKALEDTVRHQEKVIEKMEQILEERLCERKEPIpsnrPQGKPIMASGIPLGPVGETL 832
Cdd:TIGR02169  900 elERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPK----GEDEEIPEEELSLEDVQAEL 960
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 282-366 1.11e-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: 42.09  E-value: 1.11e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793614   282 TITVTLYGATNLPAGKDGSEPWPYVVVKTTSEKANKHSpqamTSVTSEpTRAPVWGDTVNVEIQaeDTGREDLILKVMDN 361
Cdd:smart00239    1 TLTVKIISARNLPPKDKGGKSDPYVKVSLDGDPKEKKK----TKVVKN-TLNPVWNETFEFEVP--PPELAELEIEVYDK 73


                    ....*
gi 1039793614   362 KRKKE 366
Cdd:smart00239   74 DRFGR 78
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
650-1007 1.70e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.53  E-value: 1.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793614  650 QEMEELQPRDVEMNNYRRAMQKMAEDILALKKQANILEEENGMLRSHLSQQSIEEQSRAEEENLAVSMKQ--KLLLNELD 727
Cdd:COG4717     78 EELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERleELEERLEE 157

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793614  728 MKRLRDRVQHLQNELIRKNDREKELL--LLYQAQQPQAAQLRRYQDKLQKMKALEDTVRHQEKVIEKMEQILEERLCERK 805
Cdd:COG4717    158 LRELEEELEELEAELAELQEELEELLeqLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELE 237

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793614  806 EPIPSNRPQ------------------GKPIMASGIPLGPVG---ETLAVDLYSMLLAENTRLRTELEKNRQQSAPIILQ 864
Cdd:COG4717    238 AAALEERLKearlllliaaallallglGGSLLSLILTIAGVLflvLGLLALLFLLLAREKASLGKEAEELQALPALEELE 317

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793614  865 QQALPvdprelgaggDLAERLqdtngpGHPKSTETLPAQDFLGGTSDKFNLLAKLEQAQSRIL--SLENQL--------- 933
Cdd:COG4717    318 EEELE----------ELLAAL------GLPPDLSPEELLELLDRIEELQELLREAEELEEELQleELEQEIaallaeagv 381

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039793614  934 --EESARHWA---REKQNLAIRLQEQQHGFGQPPNSIIIDQPNAGASKNRQQLSKLETSLPSSDKKLNRPSDSQIEISN 1007
Cdd:COG4717    382 edEEELRAALeqaEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEA 460
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 630-953 7.64e-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: 43.51  E-value: 7.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793614  630 LDENLGAIRESWSMSSLDSTQEMEELQPRDVEMNNYRRAMQKMAEDI-------LALKKQANILEEENGMLRSHL--SQQ 700
Cdd:TIGR02168  237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIeelqkelYALANEISRLEQQKQILRERLanLER 316

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793614  701 SIEEQSRAEEENLAVSMKQKLLLNELDMK--RLRDRVQHLQNELIRKNDREKELLLLYQAQQPQAAQLRR-YQDKLQKMK 777
Cdd:TIGR02168  317 QLEELEAQLEELESKLDELAEELAELEEKleELKEELESLEAELEELEAELEELESRLEELEEQLETLRSkVAQLELQIA 396

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793614  778 ALEDTVRHQEKVIEKMEQILEERLCERKEPIPsnRPQGKPIMASGIPLGPVGETLAvdlysMLLAENTRLRTELEKNRQQ 857
Cdd:TIGR02168  397 SLNNEIERLEARLERLEDRRERLQQEIEELLK--KLEEAELKELQAELEELEEELE-----ELQEELERLEEALEELREE 469

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793614  858 SAPIILQQQALPVDPRELGAGGDLAERLQDTN-GPGHPKSTETLPAQDFLGGT---SDKFNLLAKLEQAqsrilsLENQL 933
Cdd:TIGR02168  470 LEEAEQALDAAERELAQLQARLDSLERLQENLeGFSEGVKALLKNQSGLSGILgvlSELISVDEGYEAA------IEAAL 543

                          330       340
                   ....*....|....*....|
gi 1039793614  934 EESARHWAREKQNLAIRLQE 953
Cdd:TIGR02168  544 GGRLQAVVVENLNAAKKAIA 563
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 649-945 9.32e-04

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 43.24  E-value: 9.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793614  649 TQEMEELQPRDVEMNNYRRAMQKMAEDILALKKQANILEEENGMLRSHLsQQSIEEQSRAEE--ENLAvSMKQKL--LLN 724
Cdd:pfam01576    1 TRQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQL-QAETELCAEAEEmrARLA-ARKQELeeILH 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793614  725 ELDmKRL---RDRVQHLQNElirKNDREKELLLLYQAQQPQAAQLRRYQ-DKLQ---KMKALED---TVRHQEKVIEKME 794
Cdd:pfam01576   79 ELE-SRLeeeEERSQQLQNE---KKKMQQHIQDLEEQLDEEEAARQKLQlEKVTteaKIKKLEEdilLLEDQNSKLSKER 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793614  795 QILEERLCErkepIPSNRPQGKPIMASGIPLGPVGETLAVDLYSMLLAENtRLRTELEKNRQQSapiilqqQALPVDPRE 874
Cdd:pfam01576  155 KLLEERISE----FTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEE-KGRQELEKAKRKL-------EGESTDLQE 222

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039793614  875 LGAggDLAERLQDTNGPGHPKSTETLPAQDFLGG-TSDKFNLLAKLEQAQSRILSLENQL--EESARHWArEKQ 945
Cdd:pfam01576  223 QIA--ELQAQIAELRAQLAKKEEELQAALARLEEeTAQKNNALKKIRELEAQISELQEDLesERAARNKA-EKQ 293
C2 pfam00168
C2 domain;
282-363 1.90e-03

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 38.84  E-value: 1.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793614  282 TITVTLYGATNLPAGKDGSEPWPYVVVKTTSEKaNKHSpqamTSVTSEpTRAPVWGDTVNVEIQAEDTgrEDLILKVMDN 361
Cdd:pfam00168    2 RLTVTVIEAKNLPPKDGNGTSDPYVKVYLLDGK-QKKK----TKVVKN-TLNPVWNETFTFSVPDPEN--AVLEIEVYDY 73


                   ..
gi 1039793614  362 KR 363
Cdd:pfam00168   74 DR 75
 
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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