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Conserved domains on  [gi|514062053|ref|WP_016528364|]
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SPOR domain-containing protein [Glaesserella parasuis]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ftsN super family cl37078
cell division protein FtsN; FtsN is a poorly conserved protein active in cell division in a ...
1-237 3.09e-24

cell division protein FtsN; FtsN is a poorly conserved protein active in cell division in a number of Proteobacteria. The N-terminal 30 residue region tends to by Lys/Arg-rich, and is followed by a membrane-spanning region. This is followed by an acidic low-complexity region of variable length and a well-conserved C-terminal domain of two tandem regions matched by pfam05036 (Sporulation related repeat), found in several cell division and sporulation proteins. The role of FtsN as a suppressor for other cell division mutations is poorly understood; it may involve cell wall hydrolysis. [Cellular processes, Cell division]


The actual alignment was detected with superfamily member TIGR02223:

Pssm-ID: 274041 [Multi-domain]  Cd Length: 298  Bit Score: 97.84  E-value: 3.09e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062053    1 MPNRDYAVRSKA--KKGGNTALILAVIILLLM-------GSGFVLWFLKESNP--TTPVMPTQMAPSQ-QPKSTLPTPPQ 68
Cdd:TIGR02223   1 MAQRDYVRRGRGapQKKKKNRRLVRATVLIAAilillfiGGSSGLYLLTESKQanEPETLQPKNQTENgETAADLPPKPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062053   69 EVYSYIRDLETREV----PVDKNSKLAQLTKEQELAIQKQKEEQQLSQ-------------TATSDPVANTSTATEQKQE 131
Cdd:TIGR02223  81 ERWSYIEELEAREVlindPEEPSNGGGVEESAQLTAEQRQLLEQMQADmraaekvlatapsEQTVAVEARKQTAEKKPQK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062053  132 QQQ---------------EVSEEKPKQEQLPKTQEQ----AKNITTA----KPALEQPKNVGK----FGLQCGAFKNKAQ 184
Cdd:TIGR02223 161 ARTaeaqktpvetekiasKVKEAKQKQKALPKQTAEtqsnSKPIETApkadKADKTKPKPKEKaeraAALQCGAYANKEQ 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 514062053  185 AENMQARLAMAGYNARINS--NGEWNRVVVGP--AGDRAKAMAALSNARSVAECVII 237
Cdd:TIGR02223 241 AESVRAKLAFLGISSKITTtdGGKWYRVVSGPykNKDDAEKDLNKLKVAGVAGCIIN 297
 
Name Accession Description Interval E-value
ftsN TIGR02223
cell division protein FtsN; FtsN is a poorly conserved protein active in cell division in a ...
1-237 3.09e-24

cell division protein FtsN; FtsN is a poorly conserved protein active in cell division in a number of Proteobacteria. The N-terminal 30 residue region tends to by Lys/Arg-rich, and is followed by a membrane-spanning region. This is followed by an acidic low-complexity region of variable length and a well-conserved C-terminal domain of two tandem regions matched by pfam05036 (Sporulation related repeat), found in several cell division and sporulation proteins. The role of FtsN as a suppressor for other cell division mutations is poorly understood; it may involve cell wall hydrolysis. [Cellular processes, Cell division]


Pssm-ID: 274041 [Multi-domain]  Cd Length: 298  Bit Score: 97.84  E-value: 3.09e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062053    1 MPNRDYAVRSKA--KKGGNTALILAVIILLLM-------GSGFVLWFLKESNP--TTPVMPTQMAPSQ-QPKSTLPTPPQ 68
Cdd:TIGR02223   1 MAQRDYVRRGRGapQKKKKNRRLVRATVLIAAilillfiGGSSGLYLLTESKQanEPETLQPKNQTENgETAADLPPKPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062053   69 EVYSYIRDLETREV----PVDKNSKLAQLTKEQELAIQKQKEEQQLSQ-------------TATSDPVANTSTATEQKQE 131
Cdd:TIGR02223  81 ERWSYIEELEAREVlindPEEPSNGGGVEESAQLTAEQRQLLEQMQADmraaekvlatapsEQTVAVEARKQTAEKKPQK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062053  132 QQQ---------------EVSEEKPKQEQLPKTQEQ----AKNITTA----KPALEQPKNVGK----FGLQCGAFKNKAQ 184
Cdd:TIGR02223 161 ARTaeaqktpvetekiasKVKEAKQKQKALPKQTAEtqsnSKPIETApkadKADKTKPKPKEKaeraAALQCGAYANKEQ 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 514062053  185 AENMQARLAMAGYNARINS--NGEWNRVVVGP--AGDRAKAMAALSNARSVAECVII 237
Cdd:TIGR02223 241 AESVRAKLAFLGISSKITTtdGGKWYRVVSGPykNKDDAEKDLNKLKVAGVAGCIIN 297
PRK12757 PRK12757
cell division protein FtsN; Provisional
36-221 4.29e-22

cell division protein FtsN; Provisional


Pssm-ID: 237191 [Multi-domain]  Cd Length: 256  Bit Score: 91.26  E-value: 4.29e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062053  36 LWFL----KESNPTTPVMptqmapSQQPKSTLPTPPQEVYSYIRDLETREVPVDK----------NSKlAQLTKEQ-ELA 100
Cdd:PRK12757  16 LYFIthnkKEEAPLLPNH------KPRTGNGLPPKPEERWRYIKELENRQIGVPTptepsaggevNSP-TQLTDEQrQLL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062053 101 IQKQKEEQQ----------------------LSQTATSDPVANTSTATEQKQEQQQEVSEEKPKQEQLPKTQEQAKNITT 158
Cdd:PRK12757  89 EQMQADMRQqptqlsevpyneqtpqvprstvQIQQQAQQQQPPATTAQPQPVTPPRQTTAPVQPQTPAPVRTQPAAPVTQ 168
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 514062053 159 AKPALEQP---KNVGKFGLQCGAFKNKAQAENMQARLAMAGYNARINSNGEWNRVVVGPAGDRAKA 221
Cdd:PRK12757 169 AVEAPKVEaekEKEQRWMVQCGSFKGTEQAESVRAQLAFAGIESRITTGGGWNRVVLGPYNSKAAA 234
FtsN COG3087
Cell division protein FtsN [Cell cycle control, cell division, chromosome partitioning];
49-230 2.68e-15

Cell division protein FtsN [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442321 [Multi-domain]  Cd Length: 198  Bit Score: 71.97  E-value: 2.68e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062053  49 MPTQMAPSQQPKSTLPTPPQEVYSYIRDLETREVPVDKNSKLAQLTKEQELAIQKQKEEQQLSQTATSDPVANTSTATEQ 128
Cdd:COG3087    2 ETALAAILLAAAALLLELSAEAAAAASDNLRLAAGSAAAPALAEDALVASAAKAGLAETGAKAGAILAAAALAALNAAAA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062053 129 KQEQQQEVSEEKPKQEQLPKTQEQAKNITTAKPALEQPKNVGKFGLQCGAFKNKAQAENMQARLAMAGYNARINS----N 204
Cdd:COG3087   82 ALAAASAAAAAAAAPAAAAAEAAAAPAGMAKKEAAAAPAAKKPYYVQVGAFRSRANAERLRARLALLGLEARVVEvevgG 161
                        170       180
                 ....*....|....*....|....*.
gi 514062053 205 GEWNRVVVGPAGDRAKAMAALSNARS 230
Cdd:COG3087  162 GTWYRVRVGPFSSRAEAEKAREKLKA 187
SPOR pfam05036
SPOR domain; Bacterial SPOR domains bind peptidoglycan (PG) and target proteins to the cell ...
170-237 1.12e-12

SPOR domain; Bacterial SPOR domains bind peptidoglycan (PG) and target proteins to the cell division site by binding to denuded glycan strands that lack stem peptides. This 70 residue domain is composed of two 35 residue repeats found in proteins involved in sporulation and cell division such as FtsN, DedD, and CwlM. This domain is involved in binding peptidoglycan. Two tandem repeats fold into a pseudo-2-fold symmetric single-domain structure containing numerous contacts between the repeats. FtsN is an essential cell division protein with a simple bitopic topology, a short N-terminal cytoplasmic segment fused to a large carboxy periplasmic domain through a single transmembrane domain. These repeats lay at the periplasmic C-terminus. FtsN localizes to the septum ring complex.


Pssm-ID: 461531 [Multi-domain]  Cd Length: 76  Bit Score: 61.61  E-value: 1.12e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 514062053  170 GKFGLQCGAFKNKAQAENMQARLAMAGYNA---RINSNGEWNRVVVGPAGDRAKAMAALSNARSVA--ECVII 237
Cdd:pfam05036   3 GGYYVQLGAFSNEANAEALAAKLRAKGFAAyvaVTSKGGGLYRVRVGPFASREEARAALKKLKALAglSPFVV 75
 
Name Accession Description Interval E-value
ftsN TIGR02223
cell division protein FtsN; FtsN is a poorly conserved protein active in cell division in a ...
1-237 3.09e-24

cell division protein FtsN; FtsN is a poorly conserved protein active in cell division in a number of Proteobacteria. The N-terminal 30 residue region tends to by Lys/Arg-rich, and is followed by a membrane-spanning region. This is followed by an acidic low-complexity region of variable length and a well-conserved C-terminal domain of two tandem regions matched by pfam05036 (Sporulation related repeat), found in several cell division and sporulation proteins. The role of FtsN as a suppressor for other cell division mutations is poorly understood; it may involve cell wall hydrolysis. [Cellular processes, Cell division]


Pssm-ID: 274041 [Multi-domain]  Cd Length: 298  Bit Score: 97.84  E-value: 3.09e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062053    1 MPNRDYAVRSKA--KKGGNTALILAVIILLLM-------GSGFVLWFLKESNP--TTPVMPTQMAPSQ-QPKSTLPTPPQ 68
Cdd:TIGR02223   1 MAQRDYVRRGRGapQKKKKNRRLVRATVLIAAilillfiGGSSGLYLLTESKQanEPETLQPKNQTENgETAADLPPKPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062053   69 EVYSYIRDLETREV----PVDKNSKLAQLTKEQELAIQKQKEEQQLSQ-------------TATSDPVANTSTATEQKQE 131
Cdd:TIGR02223  81 ERWSYIEELEAREVlindPEEPSNGGGVEESAQLTAEQRQLLEQMQADmraaekvlatapsEQTVAVEARKQTAEKKPQK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062053  132 QQQ---------------EVSEEKPKQEQLPKTQEQ----AKNITTA----KPALEQPKNVGK----FGLQCGAFKNKAQ 184
Cdd:TIGR02223 161 ARTaeaqktpvetekiasKVKEAKQKQKALPKQTAEtqsnSKPIETApkadKADKTKPKPKEKaeraAALQCGAYANKEQ 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 514062053  185 AENMQARLAMAGYNARINS--NGEWNRVVVGP--AGDRAKAMAALSNARSVAECVII 237
Cdd:TIGR02223 241 AESVRAKLAFLGISSKITTtdGGKWYRVVSGPykNKDDAEKDLNKLKVAGVAGCIIN 297
PRK12757 PRK12757
cell division protein FtsN; Provisional
36-221 4.29e-22

cell division protein FtsN; Provisional


Pssm-ID: 237191 [Multi-domain]  Cd Length: 256  Bit Score: 91.26  E-value: 4.29e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062053  36 LWFL----KESNPTTPVMptqmapSQQPKSTLPTPPQEVYSYIRDLETREVPVDK----------NSKlAQLTKEQ-ELA 100
Cdd:PRK12757  16 LYFIthnkKEEAPLLPNH------KPRTGNGLPPKPEERWRYIKELENRQIGVPTptepsaggevNSP-TQLTDEQrQLL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062053 101 IQKQKEEQQ----------------------LSQTATSDPVANTSTATEQKQEQQQEVSEEKPKQEQLPKTQEQAKNITT 158
Cdd:PRK12757  89 EQMQADMRQqptqlsevpyneqtpqvprstvQIQQQAQQQQPPATTAQPQPVTPPRQTTAPVQPQTPAPVRTQPAAPVTQ 168
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 514062053 159 AKPALEQP---KNVGKFGLQCGAFKNKAQAENMQARLAMAGYNARINSNGEWNRVVVGPAGDRAKA 221
Cdd:PRK12757 169 AVEAPKVEaekEKEQRWMVQCGSFKGTEQAESVRAQLAFAGIESRITTGGGWNRVVLGPYNSKAAA 234
FtsN COG3087
Cell division protein FtsN [Cell cycle control, cell division, chromosome partitioning];
49-230 2.68e-15

Cell division protein FtsN [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442321 [Multi-domain]  Cd Length: 198  Bit Score: 71.97  E-value: 2.68e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062053  49 MPTQMAPSQQPKSTLPTPPQEVYSYIRDLETREVPVDKNSKLAQLTKEQELAIQKQKEEQQLSQTATSDPVANTSTATEQ 128
Cdd:COG3087    2 ETALAAILLAAAALLLELSAEAAAAASDNLRLAAGSAAAPALAEDALVASAAKAGLAETGAKAGAILAAAALAALNAAAA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062053 129 KQEQQQEVSEEKPKQEQLPKTQEQAKNITTAKPALEQPKNVGKFGLQCGAFKNKAQAENMQARLAMAGYNARINS----N 204
Cdd:COG3087   82 ALAAASAAAAAAAAPAAAAAEAAAAPAGMAKKEAAAAPAAKKPYYVQVGAFRSRANAERLRARLALLGLEARVVEvevgG 161
                        170       180
                 ....*....|....*....|....*.
gi 514062053 205 GEWNRVVVGPAGDRAKAMAALSNARS 230
Cdd:COG3087  162 GTWYRVRVGPFSSRAEAEKAREKLKA 187
PRK10927 PRK10927
cell division protein FtsN;
63-226 1.86e-14

cell division protein FtsN;


Pssm-ID: 236797 [Multi-domain]  Cd Length: 319  Bit Score: 71.25  E-value: 1.86e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062053  63 LPTPPQEVYSYIRDLETREVPVDKNSKLA---------QLTKEQ-------------------------------ELAIQ 102
Cdd:PRK10927  75 LPPKPEERWRYIKELESRQPGVRAPTEPSaggevktpeQLTPEQrqlleqmqadmrqqptqlvevpwneqtpeqrQQTLQ 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062053 103 KQKEEQQLSQTatsDPVANTSTATEQKQEQQQEVSEEKPKQEQlPKTQEQAKNI------------TTAKPALEQP---- 166
Cdd:PRK10927 155 RQRQAQQLAEQ---QRLAQQSRTTEQSWQQQTRTSQAAPVQAQ-PRQSKPASTQqpyqdllqtpahTTAQSKPQQAapvt 230
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 514062053 167 ------------KNVGKFGLQCGAFKNKAQAENMQARLAMAGYNARINSNGEWNRVVVGPAGDRAKAMAALS 226
Cdd:PRK10927 231 raadapkptaekKDERRWMVQCGSFRGAEQAETVRAQLAFEGFDSKITTNNGWNRVVIGPVKGKENADSTLN 302
SPOR pfam05036
SPOR domain; Bacterial SPOR domains bind peptidoglycan (PG) and target proteins to the cell ...
170-237 1.12e-12

SPOR domain; Bacterial SPOR domains bind peptidoglycan (PG) and target proteins to the cell division site by binding to denuded glycan strands that lack stem peptides. This 70 residue domain is composed of two 35 residue repeats found in proteins involved in sporulation and cell division such as FtsN, DedD, and CwlM. This domain is involved in binding peptidoglycan. Two tandem repeats fold into a pseudo-2-fold symmetric single-domain structure containing numerous contacts between the repeats. FtsN is an essential cell division protein with a simple bitopic topology, a short N-terminal cytoplasmic segment fused to a large carboxy periplasmic domain through a single transmembrane domain. These repeats lay at the periplasmic C-terminus. FtsN localizes to the septum ring complex.


Pssm-ID: 461531 [Multi-domain]  Cd Length: 76  Bit Score: 61.61  E-value: 1.12e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 514062053  170 GKFGLQCGAFKNKAQAENMQARLAMAGYNA---RINSNGEWNRVVVGPAGDRAKAMAALSNARSVA--ECVII 237
Cdd:pfam05036   3 GGYYVQLGAFSNEANAEALAAKLRAKGFAAyvaVTSKGGGLYRVRVGPFASREEARAALKKLKALAglSPFVV 75
DedD COG3147
Cell division protein DedD (periplasmic protein involved in septation) [Cell cycle control, ...
111-230 1.33e-09

Cell division protein DedD (periplasmic protein involved in septation) [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442381 [Multi-domain]  Cd Length: 140  Bit Score: 54.78  E-value: 1.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062053 111 SQTATSDPVANTSTATEQKQEQ---QQEVSEEKPKQEQLPKTQEQAKNITTAKPALEQPKNVGKFGLQCGAFKNKAQAEN 187
Cdd:COG3147    2 AEEAAAAPAAAAAPAAPAAAAApapAAAAAAAAPKPAAKPAAPKPAAAAAAAPAAKAAAPAGGGWVVQLGAFSNEDNAKE 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 514062053 188 MQARLAMAGYNARI----NSNGEWNRVVVGPAGDRAKAMAALSNARS 230
Cdd:COG3147   82 LVAKLRAAGYPAYTepvtTGGGTLYRVRVGPFASRAEAEAALAKLKK 128
PRK11633 PRK11633
cell division protein DedD; Provisional
140-226 2.01e-04

cell division protein DedD; Provisional


Pssm-ID: 236940 [Multi-domain]  Cd Length: 226  Bit Score: 41.14  E-value: 2.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062053 140 KPKQEQLPKTQEQAKNITTAKPALEQPKN-VGK-FGLQCGAFKNKAQAENMQARLAMAGYNARINS----NGEWNRVVVG 213
Cdd:PRK11633 116 KPKPKPQQKVEAPPAPKPEPKPVVEEKAApTGKaYVVQLGALKNADKVNEIVAKLRLSGYRVYTVPstpvQGKITRIYVG 195
                         90
                 ....*....|...
gi 514062053 214 PAGDRAKAMAALS 226
Cdd:PRK11633 196 PDASKDKLKGSLG 208
 
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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