NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1032018943|ref|XP_016767111|]
View 

centrosomal protein of 89 kDa [Apis mellifera]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
252-612 3.73e-06

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: 50.45  E-value: 3.73e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032018943  252 HALGPLLNAYQENLLEKQELIYMYEQEMADFSNRCKQILTENEIMHKEVEELKSECDRYTKEIQKMVENTAllkkqndvl 331
Cdd:TIGR02169  705 DELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLH--------- 775
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032018943  332 kketlNIKRETNDIRSSY-ESKIEVILKCNEALKKEHTITVSELSNLRGKYEILSKEFE----EMRNKEQQtvpttvhvt 406
Cdd:TIGR02169  776 -----KLEEALNDLEARLsHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEylekEIQELQEQ--------- 841
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032018943  407 aIEECKILLDELKYQYENEKRDlcnhIKHIEEIQPENEKKLIMVIAERNHLKGLVNNLETTLKRTQRKSEQMQSLVYSTR 486
Cdd:TIGR02169  842 -RIDLKEQIKSIEKEIENLNGK----KEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKR 916
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032018943  487 VSRNSLKEKLSKVtaycEELFSEYERIVSEREKLLSFLRETEKENANMDRLGKSITSrveglknqLEIVRKGTKQQVDSV 566
Cdd:TIGR02169  917 KRLSELKAKLEAL----EEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRA--------LEPVNMLAIQEYEEV 984
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 1032018943  567 EKRIKlqelhvrrmkhDYQRKIQHLNDIIKEQEDVIKKLQKEKYSS 612
Cdd:TIGR02169  985 LKRLD-----------ELKEKRAKLEEERKAILERIEEYEKKKREV 1019
 
Name Accession Description Interval E-value
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
252-612 3.73e-06

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: 50.45  E-value: 3.73e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032018943  252 HALGPLLNAYQENLLEKQELIYMYEQEMADFSNRCKQILTENEIMHKEVEELKSECDRYTKEIQKMVENTAllkkqndvl 331
Cdd:TIGR02169  705 DELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLH--------- 775
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032018943  332 kketlNIKRETNDIRSSY-ESKIEVILKCNEALKKEHTITVSELSNLRGKYEILSKEFE----EMRNKEQQtvpttvhvt 406
Cdd:TIGR02169  776 -----KLEEALNDLEARLsHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEylekEIQELQEQ--------- 841
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032018943  407 aIEECKILLDELKYQYENEKRDlcnhIKHIEEIQPENEKKLIMVIAERNHLKGLVNNLETTLKRTQRKSEQMQSLVYSTR 486
Cdd:TIGR02169  842 -RIDLKEQIKSIEKEIENLNGK----KEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKR 916
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032018943  487 VSRNSLKEKLSKVtaycEELFSEYERIVSEREKLLSFLRETEKENANMDRLGKSITSrveglknqLEIVRKGTKQQVDSV 566
Cdd:TIGR02169  917 KRLSELKAKLEAL----EEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRA--------LEPVNMLAIQEYEEV 984
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 1032018943  567 EKRIKlqelhvrrmkhDYQRKIQHLNDIIKEQEDVIKKLQKEKYSS 612
Cdd:TIGR02169  985 LKRLD-----------ELKEKRAKLEEERKAILERIEEYEKKKREV 1019
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
83-622 3.07e-04

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 43.95  E-value: 3.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032018943   83 HERSKKLTEENNSQKILFDKDDADSgIILSRLKDKYVSKETlkvvnEYHKLEKCYKNIQEECQKL-----------NNIL 151
Cdd:pfam15921  387 HKREKELSLEKEQNKRLWDRDTGNS-ITIDHLRRELDDRNM-----EVQRLEALLKAMKSECQGQmerqmaaiqgkNESL 460
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032018943  152 EQRELEYKKLCLHYEALIQMVQELEGAKINLLKQNKQLE--TEKIQSNEditllkTIVYQLNAELERYQDKLGDRKHENI 229
Cdd:pfam15921  461 EKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSdlTASLQEKE------RAIEATNAEITKLRSRVDLKLQELQ 534
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032018943  230 SASNNGNNEKKYDSRIwgninfhalgpllNAYQENLLEKQELIYMYEQEMADFSNRCKQ-------ILTENEIMHKEVEE 302
Cdd:pfam15921  535 HLKNEGDHLRNVQTEC-------------EALKLQMAEKDKVIEILRQQIENMTQLVGQhgrtagaMQVEKAQLEKEIND 601
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032018943  303 ----------LKSECDRYTKEIQKMVENTALLKKQNDVLKKETLnikRETNDIRSSYESKIEVILKCNealkkehtitvS 372
Cdd:pfam15921  602 rrlelqefkiLKDKKDAKIRELEARVSDLELEKVKLVNAGSERL---RAVKDIKQERDQLLNEVKTSR-----------N 667
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032018943  373 ELSNLRGKYEILSKEFeemRNKEQQTVPTTvhvtaieeckillDELKYQYENEKRDL---CNHIKHIEEIQPENEKKLIM 449
Cdd:pfam15921  668 ELNSLSEDYEVLKRNF---RNKSEEMETTT-------------NKLKMQLKSAQSELeqtRNTLKSMEGSDGHAMKVAMG 731
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032018943  450 VIAERNHLKGLVNNLettlkrtQRKSEQMQSLVYSTRVSRNSLKEKLSKVTAYCEELFSEYERIVSEREKLLSFLRETEK 529
Cdd:pfam15921  732 MQKQITAKRGQIDAL-------QSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKE 804
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032018943  530 ENANMdrlgksitsrveglknqlEIVRKGTKQQVDSVEKRIKLQELHVRRMkhdyqrKIQHLNDiikeqedvIKKLQKEK 609
Cdd:pfam15921  805 KVANM------------------EVALDKASLQFAECQDIIQRQEQESVRL------KLQHTLD--------VKELQGPG 852
                          570
                   ....*....|...
gi 1032018943  610 YSSQDTLTRRILQ 622
Cdd:pfam15921  853 YTSNSSMKPRLLQ 865
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
258-620 8.43e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 8.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032018943 258 LNAYQENLLEKQELIYMYEQEMADFSNRCKQILTENEIMHKEVEELKSECDRyTKEIQKMVENTALLKKqndvLKKETLN 337
Cdd:PRK03918  233 LEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKE-LKELKEKAEEYIKLSE----FYEEYLD 307
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032018943 338 IKRETNDIRSSYESKIEVILKcnealkkehtiTVSELSNLRGKYEILSKEFEEMRNKEQQTVPttvHVTAIEECKILLDE 417
Cdd:PRK03918  308 ELREIEKRLSRLEEEINGIEE-----------RIKELEEKEERLEELKKKLKELEKRLEELEE---RHELYEEAKAKKEE 373
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032018943 418 L----KYQYENEKRDLCNHIKHIEEIQPENEKKLIMVIAERNHLKGLVNNLETTLKRTqrKSEQMQSLVYSTRVSRNSLK 493
Cdd:PRK03918  374 LerlkKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEEL--KKAKGKCPVCGRELTEEHRK 451
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032018943 494 EKLSKVTAYCEELFSEYERIVSEREKLLSFLRETEKENANMDRLGK--SITSRVEGLKNQLEIVRK-----------GTK 560
Cdd:PRK03918  452 ELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKlkELAEQLKELEEKLKKYNLeelekkaeeyeKLK 531
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1032018943 561 QQVDSVEKRIKLQELHVRRMKHDYQRKI---QHLNDIIKEQEDVIKKLQKEKYSSQDTLTRRI 620
Cdd:PRK03918  532 EKLIKLKGEIKSLKKELEKLEELKKKLAeleKKLDELEEELAELLKELEELGFESVEELEERL 594
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
421-625 2.26e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.90  E-value: 2.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032018943 421 QYENEKRDLCNHIKHIEEIQPENEKKLIMVIAERNHLKGLVNNLETTLKRTQRKSEQMQSLVYSTRVSRNSLKEKLSKVT 500
Cdd:COG4942    24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032018943 501 AYCEELFSEYERIVSEREKLLSFLRETEKENANMDRLGKSITsrvEGLKNQLEIVRKgTKQQVDSVEKRIKLQELHVRRM 580
Cdd:COG4942   104 EELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLA---PARREQAEELRA-DLAELAALRAELEAERAELEAL 179
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1032018943 581 KHDYQRKIQHLNDIIKEQEDVIKKLQKEKYSSQDTLTRRILQATN 625
Cdd:COG4942   180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
 
Name Accession Description Interval E-value
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
252-612 3.73e-06

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: 50.45  E-value: 3.73e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032018943  252 HALGPLLNAYQENLLEKQELIYMYEQEMADFSNRCKQILTENEIMHKEVEELKSECDRYTKEIQKMVENTAllkkqndvl 331
Cdd:TIGR02169  705 DELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLH--------- 775
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032018943  332 kketlNIKRETNDIRSSY-ESKIEVILKCNEALKKEHTITVSELSNLRGKYEILSKEFE----EMRNKEQQtvpttvhvt 406
Cdd:TIGR02169  776 -----KLEEALNDLEARLsHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEylekEIQELQEQ--------- 841
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032018943  407 aIEECKILLDELKYQYENEKRDlcnhIKHIEEIQPENEKKLIMVIAERNHLKGLVNNLETTLKRTQRKSEQMQSLVYSTR 486
Cdd:TIGR02169  842 -RIDLKEQIKSIEKEIENLNGK----KEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKR 916
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032018943  487 VSRNSLKEKLSKVtaycEELFSEYERIVSEREKLLSFLRETEKENANMDRLGKSITSrveglknqLEIVRKGTKQQVDSV 566
Cdd:TIGR02169  917 KRLSELKAKLEAL----EEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRA--------LEPVNMLAIQEYEEV 984
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 1032018943  567 EKRIKlqelhvrrmkhDYQRKIQHLNDIIKEQEDVIKKLQKEKYSS 612
Cdd:TIGR02169  985 LKRLD-----------ELKEKRAKLEEERKAILERIEEYEKKKREV 1019
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
300-608 4.17e-06

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: 50.07  E-value: 4.17e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032018943  300 VEELKSECDRYTKEIQKMVENTALLKKQNDVLKKETLNIKRETNDIRSSYESKIEVILKCNEALKKEHTITVSELSNLRG 379
Cdd:TIGR02169  193 IDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQ 272
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032018943  380 KYEILSKEFEEMRNKEQQTVPTTVH-VTA-IEECKILLDELKYQYENEKRDLCNHIKHIEEIQPENE---KKLIMVIAER 454
Cdd:TIGR02169  273 LLEELNKKIKDLGEEEQLRVKEKIGeLEAeIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEeleREIEEERKRR 352
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032018943  455 NHLKGLVNNLETTLKRTQRKSEQMQSLVYSTRVSRNSLKEKLSKVTayceelfSEYERIVSEREKLLSFLRETEKENANM 534
Cdd:TIGR02169  353 DKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLK-------REINELKRELDRLQEELQRLSEELADL 425
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1032018943  535 DRLGKSITSRVEGLKNQLEIVRKGTKQQvdsvekRIKLQELhvRRMKHDYQRKIQHLNDIIKEQEDVIKKLQKE 608
Cdd:TIGR02169  426 NAAIAGIEAKINELEEEKEDKALEIKKQ------EWKLEQL--AADLSKYEQELYDLKEEYDRVEKELSKLQRE 491
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
83-622 3.07e-04

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 43.95  E-value: 3.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032018943   83 HERSKKLTEENNSQKILFDKDDADSgIILSRLKDKYVSKETlkvvnEYHKLEKCYKNIQEECQKL-----------NNIL 151
Cdd:pfam15921  387 HKREKELSLEKEQNKRLWDRDTGNS-ITIDHLRRELDDRNM-----EVQRLEALLKAMKSECQGQmerqmaaiqgkNESL 460
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032018943  152 EQRELEYKKLCLHYEALIQMVQELEGAKINLLKQNKQLE--TEKIQSNEditllkTIVYQLNAELERYQDKLGDRKHENI 229
Cdd:pfam15921  461 EKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSdlTASLQEKE------RAIEATNAEITKLRSRVDLKLQELQ 534
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032018943  230 SASNNGNNEKKYDSRIwgninfhalgpllNAYQENLLEKQELIYMYEQEMADFSNRCKQ-------ILTENEIMHKEVEE 302
Cdd:pfam15921  535 HLKNEGDHLRNVQTEC-------------EALKLQMAEKDKVIEILRQQIENMTQLVGQhgrtagaMQVEKAQLEKEIND 601
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032018943  303 ----------LKSECDRYTKEIQKMVENTALLKKQNDVLKKETLnikRETNDIRSSYESKIEVILKCNealkkehtitvS 372
Cdd:pfam15921  602 rrlelqefkiLKDKKDAKIRELEARVSDLELEKVKLVNAGSERL---RAVKDIKQERDQLLNEVKTSR-----------N 667
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032018943  373 ELSNLRGKYEILSKEFeemRNKEQQTVPTTvhvtaieeckillDELKYQYENEKRDL---CNHIKHIEEIQPENEKKLIM 449
Cdd:pfam15921  668 ELNSLSEDYEVLKRNF---RNKSEEMETTT-------------NKLKMQLKSAQSELeqtRNTLKSMEGSDGHAMKVAMG 731
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032018943  450 VIAERNHLKGLVNNLettlkrtQRKSEQMQSLVYSTRVSRNSLKEKLSKVTAYCEELFSEYERIVSEREKLLSFLRETEK 529
Cdd:pfam15921  732 MQKQITAKRGQIDAL-------QSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKE 804
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032018943  530 ENANMdrlgksitsrveglknqlEIVRKGTKQQVDSVEKRIKLQELHVRRMkhdyqrKIQHLNDiikeqedvIKKLQKEK 609
Cdd:pfam15921  805 KVANM------------------EVALDKASLQFAECQDIIQRQEQESVRL------KLQHTLD--------VKELQGPG 852
                          570
                   ....*....|...
gi 1032018943  610 YSSQDTLTRRILQ 622
Cdd:pfam15921  853 YTSNSSMKPRLLQ 865
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
258-620 8.43e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 8.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032018943 258 LNAYQENLLEKQELIYMYEQEMADFSNRCKQILTENEIMHKEVEELKSECDRyTKEIQKMVENTALLKKqndvLKKETLN 337
Cdd:PRK03918  233 LEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKE-LKELKEKAEEYIKLSE----FYEEYLD 307
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032018943 338 IKRETNDIRSSYESKIEVILKcnealkkehtiTVSELSNLRGKYEILSKEFEEMRNKEQQTVPttvHVTAIEECKILLDE 417
Cdd:PRK03918  308 ELREIEKRLSRLEEEINGIEE-----------RIKELEEKEERLEELKKKLKELEKRLEELEE---RHELYEEAKAKKEE 373
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032018943 418 L----KYQYENEKRDLCNHIKHIEEIQPENEKKLIMVIAERNHLKGLVNNLETTLKRTqrKSEQMQSLVYSTRVSRNSLK 493
Cdd:PRK03918  374 LerlkKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEEL--KKAKGKCPVCGRELTEEHRK 451
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032018943 494 EKLSKVTAYCEELFSEYERIVSEREKLLSFLRETEKENANMDRLGK--SITSRVEGLKNQLEIVRK-----------GTK 560
Cdd:PRK03918  452 ELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKlkELAEQLKELEEKLKKYNLeelekkaeeyeKLK 531
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1032018943 561 QQVDSVEKRIKLQELHVRRMKHDYQRKI---QHLNDIIKEQEDVIKKLQKEKYSSQDTLTRRI 620
Cdd:PRK03918  532 EKLIKLKGEIKSLKKELEKLEELKKKLAeleKKLDELEEELAELLKELEELGFESVEELEERL 594
FPP pfam05911
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ...
283-447 1.13e-03

Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.


Pssm-ID: 461778 [Multi-domain]  Cd Length: 859  Bit Score: 41.97  E-value: 1.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032018943 283 SNRCKQILTENEIMHKEVEELKSECDRYTKEIQKMVENTALLKKQNDVLKKETLNIKRETNDIRSSyESKIEVILKC--- 359
Cdd:pfam05911 673 SGSNDLKTEENKRLKEEFEQLKSEKENLEVELASCTENLESTKSQLQESEQLIAELRSELASLKES-NSLAETQLKCmae 751
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032018943 360 -NEALKKEHTITVSELSNLRGKYEILSKEFEEMRNKEQQTVPTtvhvtaieeCKilldELKYQYE-NEKRDLCNHIKHIE 437
Cdd:pfam05911 752 sYEDLETRLTELEAELNELRQKFEALEVELEEEKNCHEELEAK---------CL----ELQEQLErNEKKESSNCDADQE 818
                         170
                  ....*....|
gi 1032018943 438 EIQPENEKKL 447
Cdd:pfam05911 819 DKKLQQEKEI 828
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
421-625 2.26e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.90  E-value: 2.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032018943 421 QYENEKRDLCNHIKHIEEIQPENEKKLIMVIAERNHLKGLVNNLETTLKRTQRKSEQMQSLVYSTRVSRNSLKEKLSKVT 500
Cdd:COG4942    24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032018943 501 AYCEELFSEYERIVSEREKLLSFLRETEKENANMDRLGKSITsrvEGLKNQLEIVRKgTKQQVDSVEKRIKLQELHVRRM 580
Cdd:COG4942   104 EELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLA---PARREQAEELRA-DLAELAALRAELEAERAELEAL 179
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1032018943 581 KHDYQRKIQHLNDIIKEQEDVIKKLQKEKYSSQDTLTRRILQATN 625
Cdd:COG4942   180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
PLN02939 PLN02939
transferase, transferring glycosyl groups
343-608 2.33e-03

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 41.04  E-value: 2.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032018943 343 NDIRSSYESKIEVILKCNEALKKEHTITVSELSNLRGKY----------EILSKEFEEMRNKEQQTVPTT---VHVTAIE 409
Cdd:PLN02939  148 NQARLQALEDLEKILTEKEALQGKINILEMRLSETDARIklaaqekihvEILEEQLEKLRNELLIRGATEglcVHSLSKE 227
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032018943 410 eckilLDELKYQYENEKRDLCNHIKHIEEIQpENEKKLIMVIAERNHLKGLVNNLETTLKRTQRKSEQMQSLVYstrvsr 489
Cdd:PLN02939  228 -----LDVLKEENMLLKDDIQFLKAELIEVA-ETEERVFKLEKERSLLDASLRELESKFIVAQEDVSKLSPLQY------ 295
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032018943 490 NSLKEKLskvtaycEELFSEYERIVSEREKLLSFLRETEKENANMDRLGKSITSRVeglknqleiVRKGTKQQVDSVEKR 569
Cdd:PLN02939  296 DCWWEKV-------ENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKLEASLKEAN---------VSKFSSYKVELLQQK 359
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1032018943 570 IKLQELHVRRMKHDYQRKIQHLNDIIKEQEDVIKKLQKE 608
Cdd:PLN02939  360 LKLLEERLQASDHEIHSYIQLYQESIKEFQDTLSKLKEE 398
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
275-570 4.59e-03

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: 40.43  E-value: 4.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032018943  275 YEQEMADFSNRCKQILTENEIMHKEVEELKSECDRYTKEIQKMVENTALLKKQNDVLKKETLNIKRETNdirsSYESKIE 354
Cdd:TIGR02168  675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE----QLEERIA 750
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032018943  355 VILKCNEALKKEHTITVSELSNLRGKyeilSKEFEEMRNKEQQTVPTtvhvtAIEECKIL---LDELKYQYENEKRDLCN 431
Cdd:TIGR02168  751 QLSKELTELEAEIEELEERLEEAEEE----LAEAEAEIEELEAQIEQ-----LKEELKALreaLDELRAELTLLNEEAAN 821
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032018943  432 HIKHIEEIQPENEKKLIMviaernhlkglvnnLETTLKRTQRKSEQMQSL---VYSTRVSRNSLKEKLSKVTAYCEELFS 508
Cdd:TIGR02168  822 LRERLESLERRIAATERR--------------LEDLEEQIEELSEDIESLaaeIEELEELIEELESELEALLNERASLEE 887
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1032018943  509 EYERIVSEREKLLSFLRETEKENANMDRLGKSITSRVEGLKNQLEivrkGTKQQVDSVEKRI 570
Cdd:TIGR02168  888 ALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLE----GLEVRIDNLQERL 945
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
294-553 5.17e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 39.91  E-value: 5.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032018943 294 EIMHK----EVEELK--SECDRYTKEIQKMVENTALLKKQNDVLKKETLNIKR-------ETNDIRSSYESKIEVILKcn 360
Cdd:PRK05771   23 EALHElgvvHIEDLKeeLSNERLRKLRSLLTKLSEALDKLRSYLPKLNPLREEkkkvsvkSLEELIKDVEEELEKIEK-- 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032018943 361 EALKKEHTITV--SELSNLRGKYEILSK------EFEEMRNKEQQTVPT-TVHVTAIEECKILLDelkyqyenekrdlcn 431
Cdd:PRK05771  101 EIKELEEEISEleNEIKELEQEIERLEPwgnfdlDLSLLLGFKYVSVFVgTVPEDKLEELKLESD--------------- 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032018943 432 hIKHIEEIQPENEKKLIMVIAERNHLKglvnNLETTLKRTQRKSEQMQSLVYSTRVsRNSLKEKLSKVTAYCEELFSEYE 511
Cdd:PRK05771  166 -VENVEYISTDKGYVYVVVVVLKELSD----EVEEELKKLGFERLELEEEGTPSEL-IREIKEELEEIEKERESLLEELK 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1032018943 512 RIVSEREKLLSFLRE---TEKENANM-DRLGKS----------ITSRVEGLKNQLE 553
Cdd:PRK05771  240 ELAKKYLEELLALYEyleIELERAEAlSKFLKTdktfaiegwvPEDRVKKLKELID 295
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
132-381 5.93e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.36  E-value: 5.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032018943 132 KLEKCYKNIQEECQKLNNILEQRELEYKklclhyeALIQMVQELEGAKINLLKQNKQLETEKIQSNEDITLLKTIVYQLN 211
Cdd:COG4942    24 EAEAELEQLQQEIAELEKELAALKKEEK-------ALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032018943 212 AELERYQDKLGDRkheNISASNNGNNEkkYDSRIWGNINFHALGPLLNAYQENLLEKQELIYMYEQEMADFSNRCKQILT 291
Cdd:COG4942    97 AELEAQKEELAEL---LRALYRLGRQP--PLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEA 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032018943 292 ENEIMHKEVEELKSECDRYTKEIQKMVENTALLKKQNDVLKKETLNIKRETNDIRSSYESKIEvilkcnEALKKEHTITV 371
Cdd:COG4942   172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA------EAAAAAERTPA 245
                         250
                  ....*....|
gi 1032018943 372 SELSNLRGKY 381
Cdd:COG4942   246 AGFAALKGKL 255
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH