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Conserved domains on  [gi|2076993129|ref|NP_001119742|]
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kinetochore protein NDC80 homolog [Rattus norvegicus]

Protein Classification

Ndc80_HEC and PRK00409 domain-containing protein( domain architecture ID 13422162)

Ndc80_HEC and PRK00409 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ndc80_HEC pfam03801
HEC/Ndc80p family; Members of this family are components of the mitotic spindle. It has been ...
 51-206 4.77e-67

HEC/Ndc80p family; Members of this family are components of the mitotic spindle. It has been shown that Ndc80/HEC from yeast is part of a complex called the Ndc80p complex. This complex is thought to bind to the microtubules of the spindle.


:

Pssm-ID: 461058  Cd Length: 159  Bit Score: 216.39  E-value: 4.77e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129  51 ERKVSIFGKRTseHGSRNSQLGIFSSSEKI----KDPRPLNDKAFIQQCIRQLYEFLTENGYVYSVSMKSLQAPSTKDFL 126
Cdd:pfam03801   1 QRRSSVYGGRG--GGPRSSHQSFFSSSPMPasvpRDPRPLRDKSFQQQCIQELLEYLTENNFEHPLSPKLLKSPTQKDFN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129 127 KIFAFLYGFLCPSYELPDtKCEEEVPRIFKELGYPFA--LSKSSMYTVGAPHTWPHIVAALVWLTDCIKIHDAMKQSSPL 204
Cdd:pfam03801  79 SIFKFLYHRLDPSYEFQK-KIEEEVPMILKQLRYPFLdsISKSQLSAVGGPHTWPTFLGLLHWLVELAKFLEALEQNLYD 157


                  ..
gi 2076993129 205 FD 206
Cdd:pfam03801 158 DD 159
DUF5595 pfam18077
Domain of unknown function (DUF5595); This domain is found in Nude C 80 (Ndc80) proteins which ...
 213-285 2.85e-28

Domain of unknown function (DUF5595); This domain is found in Nude C 80 (Ndc80) proteins which can be found in species such as Homo sapiens. Ndc80 protein complexes are a core component of the end-on attachment sites for kinetochore microtubules. Ndc80 is also known as Hec1, for highly expressed in cancer 1.


:

Pssm-ID: 465636 [Multi-domain]  Cd Length: 73  Bit Score: 107.79  E-value: 2.85e-28
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2076993129 213 EETEDGIKHNKLFLDYTKKCYEKFMTGADTFEDVDAELQAKLKDLYKVDASKLESLVEENKALNEQIARLEQE 285
Cdd:pfam18077   1 EEIEDGIEYNKLFLDYTVKCYNKFMQGEDTFEEEDAELLSKLKELYNVDEALIESLEEEHKRLNEEIERLEKE 73
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 249-575 4.02e-08

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: 56.60  E-value: 4.02e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129  249 ELQAKLKDLykvdasKLESLVEENKALNEQIARLEQEREKEPNRLISLRKLKASLQADVQNYKAYMSNLESHSSILEQKL 328
Cdd:TIGR02168  217 ELKAELREL------ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKEL 290

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129  329 SSLDEEIGRLELECETVKQentRLQSVVDNQKYSIADIERI-------NHEKNELQQTINKLTKDLEAEQQQMWNEELKY 401
Cdd:TIGR02168  291 YALANEISRLEQQKQILRE---RLANLERQLEELEAQLEELeskldelAEELAELEEKLEELKEELESLEAELEELEAEL 367

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129  402 ARGKEAIEAQLAEYHKLARKLKLIPKGAENSKGydfEIKFNpEAGANCLVKYRTQVYAPLKELLNEIEEEINKALnkKMG 481
Cdd:TIGR02168  368 EELESRLEELEEQLETLRSKVAQLELQIASLNN---EIERL-EARLERLEDRRERLQQEIEELLKKLEEAELKEL--QAE 441

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129  482 LEDTLEQLNTVKTESKRAVRMLkEEVQKLDDLYQQKVKEAEEEDKKCASELDSLEKHKHLLESAvNEGLSEAM------- 554
Cdd:TIGR02168  442 LEELEEELEELQEELERLEEAL-EELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGF-SEGVKALLknqsgls 519

                          330       340
                   ....*....|....*....|....*..
gi 2076993129  555 ------GELDAVQREYQLAVQTTTEER 575
Cdd:TIGR02168  520 gilgvlSELISVDEGYEAAIEAALGGR 546
 
Name Accession Description Interval E-value
Ndc80_HEC pfam03801
HEC/Ndc80p family; Members of this family are components of the mitotic spindle. It has been ...
 51-206 4.77e-67

HEC/Ndc80p family; Members of this family are components of the mitotic spindle. It has been shown that Ndc80/HEC from yeast is part of a complex called the Ndc80p complex. This complex is thought to bind to the microtubules of the spindle.


Pssm-ID: 461058  Cd Length: 159  Bit Score: 216.39  E-value: 4.77e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129  51 ERKVSIFGKRTseHGSRNSQLGIFSSSEKI----KDPRPLNDKAFIQQCIRQLYEFLTENGYVYSVSMKSLQAPSTKDFL 126
Cdd:pfam03801   1 QRRSSVYGGRG--GGPRSSHQSFFSSSPMPasvpRDPRPLRDKSFQQQCIQELLEYLTENNFEHPLSPKLLKSPTQKDFN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129 127 KIFAFLYGFLCPSYELPDtKCEEEVPRIFKELGYPFA--LSKSSMYTVGAPHTWPHIVAALVWLTDCIKIHDAMKQSSPL 204
Cdd:pfam03801  79 SIFKFLYHRLDPSYEFQK-KIEEEVPMILKQLRYPFLdsISKSQLSAVGGPHTWPTFLGLLHWLVELAKFLEALEQNLYD 157


                  ..
gi 2076993129 205 FD 206
Cdd:pfam03801 158 DD 159
DUF5595 pfam18077
Domain of unknown function (DUF5595); This domain is found in Nude C 80 (Ndc80) proteins which ...
 213-285 2.85e-28

Domain of unknown function (DUF5595); This domain is found in Nude C 80 (Ndc80) proteins which can be found in species such as Homo sapiens. Ndc80 protein complexes are a core component of the end-on attachment sites for kinetochore microtubules. Ndc80 is also known as Hec1, for highly expressed in cancer 1.


Pssm-ID: 465636 [Multi-domain]  Cd Length: 73  Bit Score: 107.79  E-value: 2.85e-28
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2076993129 213 EETEDGIKHNKLFLDYTKKCYEKFMTGADTFEDVDAELQAKLKDLYKVDASKLESLVEENKALNEQIARLEQE 285
Cdd:pfam18077   1 EEIEDGIEYNKLFLDYTVKCYNKFMQGEDTFEEEDAELLSKLKELYNVDEALIESLEEEHKRLNEEIERLEKE 73
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 249-575 4.02e-08

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: 56.60  E-value: 4.02e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129  249 ELQAKLKDLykvdasKLESLVEENKALNEQIARLEQEREKEPNRLISLRKLKASLQADVQNYKAYMSNLESHSSILEQKL 328
Cdd:TIGR02168  217 ELKAELREL------ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKEL 290

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129  329 SSLDEEIGRLELECETVKQentRLQSVVDNQKYSIADIERI-------NHEKNELQQTINKLTKDLEAEQQQMWNEELKY 401
Cdd:TIGR02168  291 YALANEISRLEQQKQILRE---RLANLERQLEELEAQLEELeskldelAEELAELEEKLEELKEELESLEAELEELEAEL 367

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129  402 ARGKEAIEAQLAEYHKLARKLKLIPKGAENSKGydfEIKFNpEAGANCLVKYRTQVYAPLKELLNEIEEEINKALnkKMG 481
Cdd:TIGR02168  368 EELESRLEELEEQLETLRSKVAQLELQIASLNN---EIERL-EARLERLEDRRERLQQEIEELLKKLEEAELKEL--QAE 441

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129  482 LEDTLEQLNTVKTESKRAVRMLkEEVQKLDDLYQQKVKEAEEEDKKCASELDSLEKHKHLLESAvNEGLSEAM------- 554
Cdd:TIGR02168  442 LEELEEELEELQEELERLEEAL-EELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGF-SEGVKALLknqsgls 519

                          330       340
                   ....*....|....*....|....*..
gi 2076993129  555 ------GELDAVQREYQLAVQTTTEER 575
Cdd:TIGR02168  520 gilgvlSELISVDEGYEAAIEAALGGR 546
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
248-628 6.91e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 52.46  E-value: 6.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129 248 AELQAKLKDLYKVDASKLESLVEENKALNEQIARLEQERE---KEPNRLISLRKLKASLQADVQNYKAYMSNLESHSSIL 324
Cdd:COG4717    49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEeyaELQEELEELEEELEELEAELEELREELEKLEKLLQLL 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129 325 E--QKLSSLDEEIGRLELECETVKQENTRLQSVVDNQKYSIADIERINHEKNEL--------QQTINKLTKDLEAEQQQM 394
Cdd:COG4717   129 PlyQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELleqlslatEEELQDLAEELEELQQRL 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129 395 WNEELKYARGKEAIEAQLAEYHKLARKLKLIPKGAENSK-----------------GYDFEIKFNPEAGANCLV------ 451
Cdd:COG4717   209 AELEEELEEAQEELEELEEELEQLENELEAAALEERLKEarlllliaaallallglGGSLLSLILTIAGVLFLVlgllal 288

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129 452 --KYRTQVYAPLKELLNEIEEEINKALNKKMGLEDTLEQLNTVKTESKRAVRMLKEEVQKLDDLYQQKVKEAEEedkkca 529
Cdd:COG4717   289 lfLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEE------ 362

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129 530 SELDSLEKHKHLLESAVNEGLSEAMGELDAVQREYqlavQTTTEERRKVGNNLQRLL-EMVATHVGSLEKHLEEQIVKAD 608
Cdd:COG4717   363 LQLEELEQEIAALLAEAGVEDEEELRAALEQAEEY----QELKEELEELEEQLEELLgELEELLEALDEEELEEELEELE 438

                         410       420
                  ....*....|....*....|
gi 2076993129 609 REYEECtSEDLLENIRRIAE 628
Cdd:COG4717   439 EELEEL-EEELEELREELAE 457
46 PHA02562
endonuclease subunit; Provisional
 231-409 1.92e-06

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 50.78  E-value: 1.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129 231 KCYEKFMtgaDTFEDVDAELQAKLKDLYKVDASKLESLVEENKALNEQIARLEQEREKEPNRLISLRKLKASLQADVQNY 310
Cdd:PHA02562  198 KTYNKNI---EEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQF 274

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129 311 KAYMSNLESHSS--ILEQKLSSLDEEIgrlelecETVKQENTRLQSVVDNQKYSIADIERINHEKNELQQTINKLTKDLE 388
Cdd:PHA02562  275 QKVIKMYEKGGVcpTCTQQISEGPDRI-------TKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKIS 347

                         170       180
                  ....*....|....*....|.
gi 2076993129 389 AEQQQMWNEELKYARGKEAIE 409
Cdd:PHA02562  348 TNKQSLITLVDKAKKVKAAIE 368
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 248-614 2.72e-03

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: 40.87  E-value: 2.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129  248 AELQAKLKDLYKVDA--SKLESLVEENKALNEQIARLEQEREKEpNRLISlrKLKASLQAD---VQNYKAYMSNLESHSS 322
Cdd:pfam15921  451 AAIQGKNESLEKVSSltAQLESTKEMLRKVVEELTAKKMTLESS-ERTVS--DLTASLQEKeraIEATNAEITKLRSRVD 527

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129  323 ILEQKLSSLDEE---IGRLELECETVKQENTRLQSVVDNQKYSIADIERI--NHEKNELQQTINKLTKDLEAEQQQMWNE 397
Cdd:pfam15921  528 LKLQELQHLKNEgdhLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLvgQHGRTAGAMQVEKAQLEKEINDRRLELQ 607

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129  398 ELKYARGKE-----AIEAQLAEYHklARKLKLIPKGAENSKGYDfEIKfnpeaganclvkyrtqvyaplkellneieEEI 472
Cdd:pfam15921  608 EFKILKDKKdakirELEARVSDLE--LEKVKLVNAGSERLRAVK-DIK-----------------------------QER 655

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129  473 NKALNKKMGLEDTLEQLNTVKTESKRAVRMLKEEVQKLDDLYQQKVKEAEEEDKKCASELDSLE-KHKHLLESAV--NEG 549
Cdd:pfam15921  656 DQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEgSDGHAMKVAMgmQKQ 735

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129  550 LSEAMGELDAVQREYQL---AVQTTTEER---RKVGNNLQRLLEMVATH----------VGSLEKHLEEQIV-------K 606
Cdd:pfam15921  736 ITAKRGQIDALQSKIQFleeAMTNANKEKhflKEEKNKLSQELSTVATEknkmagelevLRSQERRLKEKVAnmevaldK 815


                   ....*...
gi 2076993129  607 ADREYEEC 614
Cdd:pfam15921  816 ASLQFAEC 823
 
Name Accession Description Interval E-value
Ndc80_HEC pfam03801
HEC/Ndc80p family; Members of this family are components of the mitotic spindle. It has been ...
 51-206 4.77e-67

HEC/Ndc80p family; Members of this family are components of the mitotic spindle. It has been shown that Ndc80/HEC from yeast is part of a complex called the Ndc80p complex. This complex is thought to bind to the microtubules of the spindle.


Pssm-ID: 461058  Cd Length: 159  Bit Score: 216.39  E-value: 4.77e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129  51 ERKVSIFGKRTseHGSRNSQLGIFSSSEKI----KDPRPLNDKAFIQQCIRQLYEFLTENGYVYSVSMKSLQAPSTKDFL 126
Cdd:pfam03801   1 QRRSSVYGGRG--GGPRSSHQSFFSSSPMPasvpRDPRPLRDKSFQQQCIQELLEYLTENNFEHPLSPKLLKSPTQKDFN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129 127 KIFAFLYGFLCPSYELPDtKCEEEVPRIFKELGYPFA--LSKSSMYTVGAPHTWPHIVAALVWLTDCIKIHDAMKQSSPL 204
Cdd:pfam03801  79 SIFKFLYHRLDPSYEFQK-KIEEEVPMILKQLRYPFLdsISKSQLSAVGGPHTWPTFLGLLHWLVELAKFLEALEQNLYD 157


                  ..
gi 2076993129 205 FD 206
Cdd:pfam03801 158 DD 159
DUF5595 pfam18077
Domain of unknown function (DUF5595); This domain is found in Nude C 80 (Ndc80) proteins which ...
 213-285 2.85e-28

Domain of unknown function (DUF5595); This domain is found in Nude C 80 (Ndc80) proteins which can be found in species such as Homo sapiens. Ndc80 protein complexes are a core component of the end-on attachment sites for kinetochore microtubules. Ndc80 is also known as Hec1, for highly expressed in cancer 1.


Pssm-ID: 465636 [Multi-domain]  Cd Length: 73  Bit Score: 107.79  E-value: 2.85e-28
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2076993129 213 EETEDGIKHNKLFLDYTKKCYEKFMTGADTFEDVDAELQAKLKDLYKVDASKLESLVEENKALNEQIARLEQE 285
Cdd:pfam18077   1 EEIEDGIEYNKLFLDYTVKCYNKFMQGEDTFEEEDAELLSKLKELYNVDEALIESLEEEHKRLNEEIERLEKE 73
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 249-575 4.02e-08

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: 56.60  E-value: 4.02e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129  249 ELQAKLKDLykvdasKLESLVEENKALNEQIARLEQEREKEPNRLISLRKLKASLQADVQNYKAYMSNLESHSSILEQKL 328
Cdd:TIGR02168  217 ELKAELREL------ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKEL 290

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129  329 SSLDEEIGRLELECETVKQentRLQSVVDNQKYSIADIERI-------NHEKNELQQTINKLTKDLEAEQQQMWNEELKY 401
Cdd:TIGR02168  291 YALANEISRLEQQKQILRE---RLANLERQLEELEAQLEELeskldelAEELAELEEKLEELKEELESLEAELEELEAEL 367

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129  402 ARGKEAIEAQLAEYHKLARKLKLIPKGAENSKGydfEIKFNpEAGANCLVKYRTQVYAPLKELLNEIEEEINKALnkKMG 481
Cdd:TIGR02168  368 EELESRLEELEEQLETLRSKVAQLELQIASLNN---EIERL-EARLERLEDRRERLQQEIEELLKKLEEAELKEL--QAE 441

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129  482 LEDTLEQLNTVKTESKRAVRMLkEEVQKLDDLYQQKVKEAEEEDKKCASELDSLEKHKHLLESAvNEGLSEAM------- 554
Cdd:TIGR02168  442 LEELEEELEELQEELERLEEAL-EELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGF-SEGVKALLknqsgls 519

                          330       340
                   ....*....|....*....|....*..
gi 2076993129  555 ------GELDAVQREYQLAVQTTTEER 575
Cdd:TIGR02168  520 gilgvlSELISVDEGYEAAIEAALGGR 546
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 279-603 4.25e-07

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: 53.52  E-value: 4.25e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129  279 IARLEQEREKEPNRLISLRKLKASLQADVQNYKAYMSNLESHSSILEQKLSSLDEEIGRLELECETVKQENTRLQsvvdn 358
Cdd:TIGR02168  679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS----- 753

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129  359 qkysiADIERINHEKNELQQTINKLTKDLEAEQQQMWNEELKYARGKEAIEAQLAEYHKLARKLKLIPKGAENskgydfe 438
Cdd:TIGR02168  754 -----KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAAN------- 821

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129  439 ikfnpeaganclvkyRTQVYAPLKELLNEIEEEINKALNKKMGLEDTLEQLNTVKTESKRAVRMLKEEVQKLDDLY---Q 515
Cdd:TIGR02168  822 ---------------LRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERaslE 886

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129  516 QKVKEAEEEDKKCASELDSLEKHKHLLEsavnEGLSEAMGELDAVQREYQLAVQTTTEERRKVGNNLQRLLEMVATHVGS 595
Cdd:TIGR02168  887 EALALLRSELEELSEELRELESKRSELR----RELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENK 962


                   ....*...
gi 2076993129  596 LEKHLEEQ 603
Cdd:TIGR02168  963 IEDDEEEA 970
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
248-628 6.91e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 52.46  E-value: 6.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129 248 AELQAKLKDLYKVDASKLESLVEENKALNEQIARLEQERE---KEPNRLISLRKLKASLQADVQNYKAYMSNLESHSSIL 324
Cdd:COG4717    49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEeyaELQEELEELEEELEELEAELEELREELEKLEKLLQLL 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129 325 E--QKLSSLDEEIGRLELECETVKQENTRLQSVVDNQKYSIADIERINHEKNEL--------QQTINKLTKDLEAEQQQM 394
Cdd:COG4717   129 PlyQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELleqlslatEEELQDLAEELEELQQRL 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129 395 WNEELKYARGKEAIEAQLAEYHKLARKLKLIPKGAENSK-----------------GYDFEIKFNPEAGANCLV------ 451
Cdd:COG4717   209 AELEEELEEAQEELEELEEELEQLENELEAAALEERLKEarlllliaaallallglGGSLLSLILTIAGVLFLVlgllal 288

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129 452 --KYRTQVYAPLKELLNEIEEEINKALNKKMGLEDTLEQLNTVKTESKRAVRMLKEEVQKLDDLYQQKVKEAEEedkkca 529
Cdd:COG4717   289 lfLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEE------ 362

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129 530 SELDSLEKHKHLLESAVNEGLSEAMGELDAVQREYqlavQTTTEERRKVGNNLQRLL-EMVATHVGSLEKHLEEQIVKAD 608
Cdd:COG4717   363 LQLEELEQEIAALLAEAGVEDEEELRAALEQAEEY----QELKEELEELEEQLEELLgELEELLEALDEEELEEELEELE 438

                         410       420
                  ....*....|....*....|
gi 2076993129 609 REYEECtSEDLLENIRRIAE 628
Cdd:COG4717   439 EELEEL-EEELEELREELAE 457
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 247-422 1.14e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.86  E-value: 1.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129 247 DAELQAKLKDLykvdASKLESLVEENKALNEQIARLEQEREKEPNRLISLRKLKASLQADVQNYKAYMSNLESHSSILEQ 326
Cdd:COG1196   234 LRELEAELEEL----EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE 309

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129 327 KLSSLDEEIGRLELECETVKQENTRLQSVVDNQKYSIADIERINHEKNELQQTINKLTKDLEAEQQQMWNEELKYARGKE 406
Cdd:COG1196   310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389

                         170
                  ....*....|....*.
gi 2076993129 407 AIEAQLAEYHKLARKL 422
Cdd:COG1196   390 EALRAAAELAAQLEEL 405
46 PHA02562
endonuclease subunit; Provisional
 231-409 1.92e-06

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 50.78  E-value: 1.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129 231 KCYEKFMtgaDTFEDVDAELQAKLKDLYKVDASKLESLVEENKALNEQIARLEQEREKEPNRLISLRKLKASLQADVQNY 310
Cdd:PHA02562  198 KTYNKNI---EEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQF 274

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129 311 KAYMSNLESHSS--ILEQKLSSLDEEIgrlelecETVKQENTRLQSVVDNQKYSIADIERINHEKNELQQTINKLTKDLE 388
Cdd:PHA02562  275 QKVIKMYEKGGVcpTCTQQISEGPDRI-------TKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKIS 347

                         170       180
                  ....*....|....*....|.
gi 2076993129 389 AEQQQMWNEELKYARGKEAIE 409
Cdd:PHA02562  348 TNKQSLITLVDKAKKVKAAIE 368
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 248-430 3.13e-06

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 49.83  E-value: 3.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129 248 AELQAKLKDLYKvdasKLESLVEENKALNEQIARLEQEREKEPNRLISLRKLKASLQADVQNYKAYMSNLESHSSILEQK 327
Cdd:COG3883    33 EAAQAELDALQA----ELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYLDVL 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129 328 LSS--LDEEIGRLELecetVKQENTRLQSVVDNQKYSIADIERINHEKNELQQTINKLTKDLEAEQQQMWNEELKYARGK 405
Cdd:COG3883   109 LGSesFSDFLDRLSA----LSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALL 184

                         170       180
                  ....*....|....*....|....*
gi 2076993129 406 EAIEAQLAEYHKLARKLKLIPKGAE 430
Cdd:COG3883   185 AQLSAEEAAAEAQLAELEAELAAAE 209
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 241-423 3.50e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.32  E-value: 3.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129 241 DTFEDVDAELQAKLKDLYKVDAS------KLESLVEENKALNEQIARLEQEREKEPNRLISLRKLKASLQADVQNYKAYM 314
Cdd:COG1196   274 LELEELELELEEAQAEEYELLAElarleqDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129 315 SNLESHSSILEQKLSSLDEEIGRLELECETVKQENTRLQS----VVDNQKYSIADIERINHEKNELQQTINKLTKDLEAE 390
Cdd:COG1196   354 EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRaaaeLAAQLEELEEAEEALLERLERLEEELEELEEALAEL 433

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2076993129 391 QQQMWNEELKYARGKEAIEAQLAEYHKLARKLK 423
Cdd:COG1196   434 EEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 249-609 1.10e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.78  E-value: 1.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129 249 ELQAKLKDLykvdasKLESLVEENKALNEQIARLEQEREKEPNRLISLRKLKASLQADVQNYKAYMSNLESHSSILEQKL 328
Cdd:COG1196   217 ELKEELKEL------EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE 290

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129 329 SSLDEEIGRLELECETVKQENTRLQSvvdnqkysiadierinhEKNELQQTINKLTKDLEAEQQQMWNEELKYARGKEAI 408
Cdd:COG1196   291 YELLAELARLEQDIARLEERRRELEE-----------------RLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129 409 EAQLAEYHKLARKLKLIpkgaenskgydfeikfnpeaganclvkyrTQVYAPLKELLNEIEEEINKALNKKMGLEDTLEQ 488
Cdd:COG1196   354 EEAEAELAEAEEALLEA-----------------------------EAELAEAEEELEELAEELLEALRAAAELAAQLEE 404

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129 489 LNTVKTESKRAVRMLKEEVQKLDDLYQQKVKEAEEEdkkcaSELDSLEKHKHLLESAVNEGLSEAMGELDAVQREYQLAV 568
Cdd:COG1196   405 LEEAEEALLERLERLEEELEELEEALAELEEEEEEE-----EEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAAL 479

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 2076993129 569 QTTTEERRKVGNNLQRLLEMVATHVGSLEKHLEEQIVKADR 609
Cdd:COG1196   480 AELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLR 520
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 229-423 1.46e-05

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: 48.51  E-value: 1.46e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129  229 TKKCYEKFMTGADTFEDVDAELQAKLKDLYK---VDASKLESLVEENKALNEQIARLEQEREKEPNRLISLRKLKASLQA 305
Cdd:TIGR02168  731 LRKDLARLEAEVEQLEERIAQLSKELTELEAeieELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA 810

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129  306 DVQnykaymsNLESHSSILEQKLSSLDEEIGRLELECETVKQENTRLQsvvdnqkysiADIERINHEKNELQQTINKLTK 385
Cdd:TIGR02168  811 ELT-------LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELS----------EDIESLAAEIEELEELIEELES 873

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 2076993129  386 DLEAEQQQmwneelkYARGKEAIEAQLAEYHKLARKLK 423
Cdd:TIGR02168  874 ELEALLNE-------RASLEEALALLRSELEELSEELR 904
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 244-402 1.47e-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: 48.53  E-value: 1.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129  244 EDVDAELQAKLKDLYKVDAsKLESLVEENKALNEQIARLEQEREKEPNRLISLRKLKASLQADVQNYKAYMSNLESHSS- 322
Cdd:TIGR02169  712 SDASRKIGEIEKEIEQLEQ-EEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSh 790

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129  323 ----ILEQKLSSLDEEIGRLELECETVKQENTRLQSVVDNQKYSIADIERINHE----KNELQQTINKLTKDLEAEQQQM 394
Cdd:TIGR02169  791 sripEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDlkeqIKSIEKEIENLNGKKEELEEEL 870


                   ....*...
gi 2076993129  395 wnEELKYA 402
Cdd:TIGR02169  871 --EELEAA 876
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
240-400 2.01e-05

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 47.55  E-value: 2.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129 240 ADTFEDVDAELQAKLkDLYKVDASKLESL-VEEnkALNEQIARLEQEREKEPNRL-ISLRKLKASLQADVQNYKAYMSNL 317
Cdd:COG2433   349 KNKFERVEKKVPPDV-DRDEVKARVIRGLsIEE--ALEELIEKELPEEEPEAEREkEHEERELTEEEEEIRRLEEQVERL 425

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129 318 ESHSSILEQKLSSLDEEIGRLELECETVKQEntRLQSVVDNQKYSI--ADIERINHEKNELQQTINKLTKDLEaEQQQMW 395
Cdd:COG2433   426 EAEVEELEAELEEKDERIERLERELSEARSE--ERREIRKDREISRldREIERLERELEEERERIEELKRKLE-RLKELW 502


                  ....*
gi 2076993129 396 NEELK 400
Cdd:COG2433   503 KLEHS 507
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 244-639 4.15e-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: 46.98  E-value: 4.15e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129  244 EDVDAELQAKLKDLYKVDAS--KLESLVEEnkaLNEQIARLEQEREK-EPNRLISLRKLKASLQADVQNYKAY---MSNL 317
Cdd:TIGR02169  166 AEFDRKKEKALEELEEVEENieRLDLIIDE---KRQQLERLRREREKaERYQALLKEKREYEGYELLKEKEALerqKEAI 242

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129  318 ESHSSILEQKLSSLDEEIGRLELECE----TVKQENTRLQSVVDNQkysiadIERINHEKNELQQTINKLTKDLEAEQQQ 393
Cdd:TIGR02169  243 ERQLASLEEELEKLTEEISELEKRLEeieqLLEELNKKIKDLGEEE------QLRVKEKIGELEAEIASLERSIAEKERE 316

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129  394 MWNEELKYARGKEAIEAQLAEYHKLARKLklipkgaenskgydfeikfnpeaganclvkyrtqvyaplkellneieeein 473
Cdd:TIGR02169  317 LEDAEERLAKLEAEIDKLLAEIEELEREI--------------------------------------------------- 345

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129  474 kalnkkmgledtleqlntvkTESKRAVRMLKEEVQKLDDLYQQKVKEAEEEDKKCASELDSLEKHKHLLesavnEGLSEA 553
Cdd:TIGR02169  346 --------------------EEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKL-----EKLKRE 400

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129  554 MGELDAVQREYQLAVQTTTEERRKVGNNLQRLlemvathvgsLEKHLEEQIVKADREYEECTSEDLLENIRRIAEKYKSN 633
Cdd:TIGR02169  401 INELKRELDRLQEELQRLSEELADLNAAIAGI----------EAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQE 470


                   ....*.
gi 2076993129  634 AAQLKA 639
Cdd:TIGR02169  471 LYDLKE 476
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
248-422 6.40e-05

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 46.16  E-value: 6.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129 248 AELQAKLKDlYKVDaSKLESLVEENKALNEQIARLEQEREKEPNRLISLRKLKASLQADVQNYKAYMSNLESHSSIleqk 327
Cdd:COG3206   192 EEAEAALEE-FRQK-NGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVI---- 265

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129 328 lSSLDEEIGRLELECETVKQENTRLQSVVDNQKYSIADIERinheknELQQTINKLTKDLEAEQQQMWNEELKYARGKEA 407
Cdd:COG3206   266 -QQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRA------QLQQEAQRILASLEAELEALQAREASLQAQLAQ 338

                         170
                  ....*....|....*
gi 2076993129 408 IEAQLAEYHKLARKL 422
Cdd:COG3206   339 LEARLAELPELEAEL 353
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
226-548 7.45e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.83  E-value: 7.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129 226 LDYTKKCYEKFMTGADTFED----VDAELQAKLKDLYKVDaSKLESLVEENKALNEQIARLEQEREKepnrLISLRKLKA 301
Cdd:PRK03918  174 IKRRIERLEKFIKRTENIEElikeKEKELEEVLREINEIS-SELPELREELEKLEKEVKELEELKEE----IEELEKELE 248

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129 302 SLQADVQNYKAYMSNLESHSSILEQKLSSLDEEIGRLElECETVKQENTRLQSVVDNQKYSIADIE----RINHEKNELQ 377
Cdd:PRK03918  249 SLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIEkrlsRLEEEINGIE 327

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129 378 QTINKLTKDlEAEQQQMWNEELKYARGKEAIEAQLAEYHKLARKLKLIPKGAENSKGYDFEiKFNPEaganclvkyrtqv 457
Cdd:PRK03918  328 ERIKELEEK-EERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPE-KLEKE------------- 392

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129 458 YAPLKELLNEIEEEINKALNKKMGLEDTLEQLNTVKTESKRAV-------RMLKEEVQK-LDDLYQQKVKEAEEEDKKCA 529
Cdd:PRK03918  393 LEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKgkcpvcgRELTEEHRKeLLEEYTAELKRIEKELKEIE 472

                         330
                  ....*....|....*....
gi 2076993129 530 SELDSLEKHKHLLESAVNE 548
Cdd:PRK03918  473 EKERKLRKELRELEKVLKK 491
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 244-422 8.72e-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: 45.83  E-value: 8.72e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129  244 EDVDAElQAKLKDLYKVDASKLESLVEENKALNEQIARLEQEREKEPNRLISLRKLKASLQADVQNYKAYMSNLESH--- 320
Cdd:TIGR02169  297 GELEAE-IASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAElee 375

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129  321 ----SSILEQKLSSLDEEIGRLELECETVKQENTRLQSVVDNQKYSIAD----IERINHEKNELQQT-------INKLTK 385
Cdd:TIGR02169  376 vdkeFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADlnaaIAGIEAKINELEEEkedkaleIKKQEW 455

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 2076993129  386 DLEAEQQQMWNEELKYARGKEAIEAQLAEYHKLARKL 422
Cdd:TIGR02169  456 KLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQREL 492
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 262-414 1.09e-04

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: 44.75  E-value: 1.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129 262 ASKLESLVEENKALNEQIARLEQEREKEPNRLISLRKLKASLQADVQNYKAYMSNLESHSSILEQKLSSLDEEIGRLELE 341
Cdd:COG4942    19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129 342 CETVKQE--------------------------------NTRLQSVVDNQKYSIADIERINHEKNELQQTINKLTKDLEA 389
Cdd:COG4942    99 LEAQKEElaellralyrlgrqpplalllspedfldavrrLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178

                         170       180
                  ....*....|....*....|....*
gi 2076993129 390 EQQQMWNEELKYARGKEAIEAQLAE 414
Cdd:COG4942   179 LLAELEEERAALEALKAERQKLLAR 203
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 249-576 1.18e-04

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: 45.44  E-value: 1.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129  249 ELQAKLKDL-YKVDASKLESLVEENKALNEQIARLEQEREkepnrlislrKLKASLQADVQNYKAymsnleshssiLEQK 327
Cdd:TIGR02169  215 ALLKEKREYeGYELLKEKEALERQKEAIERQLASLEEELE----------KLTEEISELEKRLEE-----------IEQL 273

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129  328 LSSLDEEIGRLELEcetvkqENTRLQSVVDNQKYSIADIERINHEKNELQQtinkltkDLEAEQQQMWNEELKYARGKEA 407
Cdd:TIGR02169  274 LEELNKKIKDLGEE------EQLRVKEKIGELEAEIASLERSIAEKERELE-------DAEERLAKLEAEIDKLLAEIEE 340

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129  408 IEAQLAEYHKLARKLKLIpkgaenskgydfeikfnpeaganclVKYRTQVYAPLKELLNEIEEEINKALNKKMGLEDTLE 487
Cdd:TIGR02169  341 LEREIEEERKRRDKLTEE-------------------------YAELKEELEDLRAELEEVDKEFAETRDELKDYREKLE 395

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129  488 QLNTVKTESKRAVRMLKEEVQKLD------------------------DLYQQKVKEAEEEDKKCASELDSLEKHKHLLE 543
Cdd:TIGR02169  396 KLKREINELKRELDRLQEELQRLSeeladlnaaiagieakineleeekEDKALEIKKQEWKLEQLAADLSKYEQELYDLK 475

                          330       340       350
                   ....*....|....*....|....*....|....*.
gi 2076993129  544 S---AVNEGLSEAMGELDAVQREYQLAVQTTTEERR 576
Cdd:TIGR02169  476 EeydRVEKELSKLQRELAEAEAQARASEERVRGGRA 511
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 247-414 1.72e-04

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 43.37  E-value: 1.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129 247 DAELQAKLKDLYKVDAskleslveenkalneQIARLEQEREKEPNRLISLRKLKASLQADVQNYKAYMSNLESHSSILEQ 326
Cdd:COG1579     2 MPEDLRALLDLQELDS---------------ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLEL 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129 327 KLSSLDEEIGRLELECETVK--QENTRLQSVVDNQKYSIADIE----RINHEKNELQQTINKLTKDLEAEQQQMWNEELK 400
Cdd:COG1579    67 EIEEVEARIKKYEEQLGNVRnnKEYEALQKEIESLKRRISDLEdeilELMERIEELEEELAELEAELAELEAELEEKKAE 146

                         170
                  ....*....|....
gi 2076993129 401 YARGKEAIEAQLAE 414
Cdd:COG1579   147 LDEELAELEAELEE 160
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 248-419 1.93e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 1.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129 248 AELQAKLKDLYKVDASKLESLVEENKALNEQIARLEQEREKEPNRLISLRKLKASLQADVQNYKAYMS---NLESHSSIL 324
Cdd:COG1196   326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRaaaELAAQLEEL 405

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129 325 EQKLSSLDEEIGRLELECETVKQENTRLQSVVDNQKysiADIERINHEKNELQQTINKLTKDLEAEQQQMWNEELKYARG 404
Cdd:COG1196   406 EEAEEALLERLERLEEELEELEEALAELEEEEEEEE---EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482

                         170
                  ....*....|....*
gi 2076993129 405 KEAIEAQLAEYHKLA 419
Cdd:COG1196   483 LEELAEAAARLLLLL 497
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 324-537 3.38e-04

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: 43.21  E-value: 3.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129 324 LEQKLSSLDEEIGRLELECETVKQENTRLQSVVDNQKYSIADIERinhEKNELQQTINKLTKDLEAEQQQMWNEELKYAR 403
Cdd:COG4942    25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALAR---RIRALEQELAALEAELAELEKEIAELRAELEA 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129 404 GKEAIEAQLAEYHKLAR--KLKLIPKGAENSKGYDFEIKFnpeagaNCLVKYRTQVYAPLKELLNEIEEEINKALNKKmg 481
Cdd:COG4942   102 QKEELAELLRALYRLGRqpPLALLLSPEDFLDAVRRLQYL------KYLAPARREQAEELRADLAELAALRAELEAER-- 173

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2076993129 482 leDTLEQLNTVKTESKRAVRMLKEEVQKLDDLYQQKVKEAEEEDKKCASELDSLEK 537
Cdd:COG4942   174 --AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 244-423 3.53e-04

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: 43.21  E-value: 3.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129 244 EDVDAELQAKLKDLYKVDASK------LESLVEENKALNEQIARLEQEREKEPNRLISLRKLKASLQADVQNYKAYMSNL 317
Cdd:COG4942    30 EQLQQEIAELEKELAALKKEEkallkqLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEL 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129 318 ------ESHSSILEQKLSSldEEIGRLELECETVKQENTRLQSVVDNQKYSIADIERINHEKNELQQTINKLTKDLEAEQ 391
Cdd:COG4942   110 lralyrLGRQPPLALLLSP--EDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEER 187

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2076993129 392 QQMWNEELKYARGKEAIEAQLAEYHKLARKLK 423
Cdd:COG4942   188 AALEALKAERQKLLARLEKELAELAAELAELQ 219
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
241-424 7.36e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.98  E-value: 7.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129  241 DTFEDVDAeLQAKLKDLykvdaSKLESLVEEnkaLNEQIARLEQEREKEpNRLISLRKLKASLQADVQNYKAYmsnlesh 320
Cdd:COG4913    222 DTFEAADA-LVEHFDDL-----ERAHEALED---AREQIELLEPIRELA-ERYAAARERLAELEYLRAALRLW------- 284

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129  321 ssILEQKLSSLDEEIGRLELECETVKQENTRLQSVVDNQKYSIADIERiNHEKNELQQtINKLTKDLEAEQQQmwneelk 400
Cdd:COG4913    285 --FAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEA-QIRGNGGDR-LEQLEREIERLERE------- 353

                          170       180
                   ....*....|....*....|....
gi 2076993129  401 yargKEAIEAQLAEYHKLARKLKL 424
Cdd:COG4913    354 ----LEERERRRARLEALLAALGL 373
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 233-339 1.21e-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: 41.67  E-value: 1.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129 233 YEKFMTGADTFEDVDAELQAkLKDLYKVDASKLESLVEENKALNEQIARLEQEREKEPNRLISLRKLKASLQADVQNYKA 312
Cdd:COG4942   121 PLALLLSPEDFLDAVRRLQY-LKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQK 199

                          90       100
                  ....*....|....*....|....*..
gi 2076993129 313 YMSNLESHSSILEQKLSSLDEEIGRLE 339
Cdd:COG4942   200 LLARLEKELAELAAELAELQQEAEELE 226
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
251-422 1.21e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 1.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129  251 QAKLKDLykvdASKLESLVEENKALNEQIARLEQEREKEPNRLISLRKLK---------ASLQADVQNYKAYMSNLESHS 321
Cdd:COG4913    609 RAKLAAL----EAELAELEEELAEAEERLEALEAELDALQERREALQRLAeyswdeidvASAEREIAELEAELERLDASS 684

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129  322 SIL----------EQKLSSLDEEIGRLELECETVKQENTRLQsvvdnqkysiadiERINHEKNELQQTINKLTKDLEAEQ 391
Cdd:COG4913    685 DDLaaleeqleelEAELEELEEELDELKGEIGRLEKELEQAE-------------EELDELQDRLEAAEDLARLELRALL 751

                          170       180       190
                   ....*....|....*....|....*....|.
gi 2076993129  392 QQMWNEELKYARGKEAIEAQLAEYHKLARKL 422
Cdd:COG4913    752 EERFAAALGDAVERELRENLEERIDALRARL 782
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
238-639 2.27e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 2.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129 238 TGADTFEDVDAELQAKLKDLyKVDASKLESLVEENKALNEQIARLEQEREKEPNRLISLRKLKASLQADVQNYKAYMSNL 317
Cdd:PRK03918  155 LGLDDYENAYKNLGEVIKEI-KRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKEL 233

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129 318 ESHSSILEQK---LSSLDEEIGRLELECETVKQENTRLQSVVDNQKYSIADIERINhEKNELQQTINKLTKDLEAEQQQM 394
Cdd:PRK03918  234 EELKEEIEELekeLESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELK-EKAEEYIKLSEFYEEYLDELREI 312

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129 395 WNEELKYARGKEAIEAQLAEYHKLARKLKLIPKGAENSKGYDFEIKfnpeaganclvkyrtqvyaplkellneieeEINK 474
Cdd:PRK03918  313 EKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELE------------------------------ERHE 362

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129 475 ALNKKMGLEDTLEQLntvktESKRAVRMLKEEVQKLDDLYQQKvKEAEEEDKKCASELDSLEKHKHLLESAVNEgLSEAM 554
Cdd:PRK03918  363 LYEEAKAKKEELERL-----KKRLTGLTPEKLEKELEELEKAK-EEIEEEISKITARIGELKKEIKELKKAIEE-LKKAK 435

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129 555 GELDAVQREyqlavqtTTEERRKvgnnlqRLLEMVATHVGSLEKHL---EEQIVKADREYEECtsEDLLENIRRIAeKYK 631
Cdd:PRK03918  436 GKCPVCGRE-------LTEEHRK------ELLEEYTAELKRIEKELkeiEEKERKLRKELREL--EKVLKKESELI-KLK 499


                  ....*...
gi 2076993129 632 SNAAQLKA 639
Cdd:PRK03918  500 ELAEQLKE 507
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 239-339 2.54e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.58  E-value: 2.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129 239 GADTFEDVDAELQAkLKDLYKVDASKLESLVEENKALNEQIARLEQEREKEPNRLISLRKLKASLQADVQNYKAYMSNLE 318
Cdd:COG3883   110 GSESFSDFLDRLSA-LSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLS 188

                          90       100
                  ....*....|....*....|.
gi 2076993129 319 SHSSILEQKLSSLDEEIGRLE 339
Cdd:COG3883   189 AEEAAAEAQLAELEAELAAAE 209
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 248-614 2.72e-03

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: 40.87  E-value: 2.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129  248 AELQAKLKDLYKVDA--SKLESLVEENKALNEQIARLEQEREKEpNRLISlrKLKASLQAD---VQNYKAYMSNLESHSS 322
Cdd:pfam15921  451 AAIQGKNESLEKVSSltAQLESTKEMLRKVVEELTAKKMTLESS-ERTVS--DLTASLQEKeraIEATNAEITKLRSRVD 527

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129  323 ILEQKLSSLDEE---IGRLELECETVKQENTRLQSVVDNQKYSIADIERI--NHEKNELQQTINKLTKDLEAEQQQMWNE 397
Cdd:pfam15921  528 LKLQELQHLKNEgdhLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLvgQHGRTAGAMQVEKAQLEKEINDRRLELQ 607

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129  398 ELKYARGKE-----AIEAQLAEYHklARKLKLIPKGAENSKGYDfEIKfnpeaganclvkyrtqvyaplkellneieEEI 472
Cdd:pfam15921  608 EFKILKDKKdakirELEARVSDLE--LEKVKLVNAGSERLRAVK-DIK-----------------------------QER 655

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129  473 NKALNKKMGLEDTLEQLNTVKTESKRAVRMLKEEVQKLDDLYQQKVKEAEEEDKKCASELDSLE-KHKHLLESAV--NEG 549
Cdd:pfam15921  656 DQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEgSDGHAMKVAMgmQKQ 735

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129  550 LSEAMGELDAVQREYQL---AVQTTTEER---RKVGNNLQRLLEMVATH----------VGSLEKHLEEQIV-------K 606
Cdd:pfam15921  736 ITAKRGQIDALQSKIQFleeAMTNANKEKhflKEEKNKLSQELSTVATEknkmagelevLRSQERRLKEKVAnmevaldK 815


                   ....*...
gi 2076993129  607 ADREYEEC 614
Cdd:pfam15921  816 ASLQFAEC 823
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 226-414 2.82e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 40.68  E-value: 2.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129 226 LDYTKKCYEKFMTGADTFEDVDAElqaKLKDLYKVDASKLESLVEENKALNEQIARLEQEREKEPNRLISLRKLKaSLQA 305
Cdd:PRK05771   59 LDKLRSYLPKLNPLREEKKKVSVK---SLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLEPWG-NFDL 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129 306 DVQNYKAYmSNLESHS-SILEQKLSSLDEEIGRLELECETVKQENTRLQSVVDN---------------QKYSIAD---- 365
Cdd:PRK05771  135 DLSLLLGF-KYVSVFVgTVPEDKLEELKLESDVENVEYISTDKGYVYVVVVVLKelsdeveeelkklgfERLELEEegtp 213

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2076993129 366 ---IERINHEKNELQQTINKLTKDLEAEQQQmWNEELKYARGKEAIEAQLAE 414
Cdd:PRK05771  214 selIREIKEELEEIEKERESLLEELKELAKK-YLEELLALYEYLEIELERAE 264
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
249-425 2.83e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.27  E-value: 2.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129 249 ELQAKLKDLykvdASKLESLVEENKALNEQIARLEQEREKEPNRLISLRKLKASLQADVQNYKAYMSNLESHSSILEQKL 328
Cdd:COG4372    42 KLQEELEQL----REELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEEL 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129 329 SSLDEEIGRLELECETVKQENTRLQSVVDNQKYSIADIE-RINHEKNELQQTINKLTKDLEAEQQQMWNEELKYARGKEA 407
Cdd:COG4372   118 EELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEeQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAE 197

                         170
                  ....*....|....*...
gi 2076993129 408 IEAQLAEYHKLARKLKLI 425
Cdd:COG4372   198 KEEELAEAEKLIESLPRE 215
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
482-617 2.88e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 2.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129  482 LEDTLEQLntvkTESKRAVRMLKEEVQKLddlyQQKVKEAEEEDKKCASELDSLEKHKHLLEsavnEGLSEAMGELDAVQ 561
Cdd:COG4913    673 LEAELERL----DASSDDLAALEEQLEEL----EAELEELEEELDELKGEIGRLEKELEQAE----EELDELQDRLEAAE 740

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2076993129  562 REYQLAVQTTTEER----------RKVGNNLQRLLEMVATHVGSLEKHLEEQIVKADREYEECTSE 617
Cdd:COG4913    741 DLARLELRALLEERfaaalgdaveRELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETAD 806
COG5022 COG5022
Myosin heavy chain [General function prediction only];
266-411 3.07e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 40.83  E-value: 3.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129  266 ESLVEENKALNEQIARLEQEREKepNRLISLRKLKASLQADVQNYKAYMSNLESHSSILEQKLSSLDEEIGRLELECETV 345
Cdd:COG5022    917 SDLIENLEFKTELIARLKKLLNN--IDLEEGPSIEYVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSEL 994

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2076993129  346 KQENTRLQSVVDNQK---YSIADIERINHEKNELQQTINKLTKDLEAEQQQMWNEELKYARGKEAIEAQ 411
Cdd:COG5022    995 KNFKKELAELSKQYGalqESTKQLKELPVEVAELQSASKIISSESTELSILKPLQKLKGLLLLENNQLQ 1063
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 243-616 3.62e-03

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 40.48  E-value: 3.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129 243 FEDVDAELQAKLKDLYkvDASKLESLVEENKALNEQIARLEQEREKEPNRL-ISLRKLKASLQADVQNYKAYMSNLESHs 321
Cdd:pfam05483 407 LEELKKILAEDEKLLD--EKKQFEKIAEELKGKEQELIFLLQAREKEIHDLeIQLTAIKTSEEHYLKEVEDLKTELEKE- 483

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129 322 silEQKLSSLDEEIGRLELECETVKQENTRLQSVVDNQKYSIADI----ERINHEKNELQQTINKLTKDLEAEQQQMWN- 396
Cdd:pfam05483 484 ---KLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCkkqeERMLKQIENLEEKEMNLRDELESVREEFIQk 560

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129 397 -EELKYARGKEAIEAQLAEYHKLARKLKL---------IPKGAENSKGYDFEIKFNPEAgancLVKYRTQVYAPLKELLN 466
Cdd:pfam05483 561 gDEVKCKLDKSEENARSIEYEVLKKEKQMkilenkcnnLKKQIENKNKNIEELHQENKA----LKKKGSAENKQLNAYEI 636

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129 467 EIEEEINKALNKKMGLEDTLEQLNTVKTESKRAVRMLKEEVQKLDDLYQQKVKEAEEEDKKC----ASELDSLEKHKHLL 542
Cdd:pfam05483 637 KVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCqhkiAEMVALMEKHKHQY 716

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2076993129 543 ESAVNEglseamgeldavqREYQLAVQTTTE-ERRKVGNNLQRLLEMVATHVGSLEKHLE---EQIVKADREYEECTS 616
Cdd:pfam05483 717 DKIIEE-------------RDSELGLYKNKEqEQSSAKAALEIELSNIKAELLSLKKQLEiekEEKEKLKMEAKENTA 781
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 240-423 4.96e-03

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: 40.05  E-value: 4.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129  240 ADTFEDVDAELQAKLKDLYKVDASKLESLVEENKALNEQIARLEQEREKEPNRLislrklkASLQADVQNYKAYMSNLES 319
Cdd:TIGR02169  271 EQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERL-------AKLEAEIDKLLAEIEELER 343

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129  320 HSSILEQKLSSLDEEIGRLELECET----VKQENTRLQSVVDNQKYSIADIERINHEKNELQQTINKLTKDLEAEQQQMW 395
Cdd:TIGR02169  344 EIEEERKRRDKLTEEYAELKEELEDlraeLEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELA 423

                          170       180
                   ....*....|....*....|....*...
gi 2076993129  396 NEELKYARGKEAIEAQLAEYHKLARKLK 423
Cdd:TIGR02169  424 DLNAAIAGIEAKINELEEEKEDKALEIK 451
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 364-639 7.50e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.53  E-value: 7.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129 364 ADIERINHEKNELQQTINKLTKDLEAEQQQMWNEELKYARGKEAIEAQLAEYHKLARKLklipkgAENSKGYDFEIKfnp 443
Cdd:COG1196   239 AELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL------ARLEQDIARLEE--- 309

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129 444 eaganclvkyrtqvyaplkellneieeeinkalnKKMGLEDTLEQLNTVKTESKRAVRMLKEEVQKLddlyQQKVKEAEE 523
Cdd:COG1196   310 ----------------------------------RRRELEERLEELEEELAELEEELEELEEELEEL----EEELEEAEE 351

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129 524 EDKKCASELDSLEKhkhlLESAVNEGLSEAMGELDAVQREYQLAVQTTTEERrkvgNNLQRLLEMVATHVGSLEKHLEEQ 603
Cdd:COG1196   352 ELEEAEAELAEAEE----ALLEAEAELAEAEEELEELAEELLEALRAAAELA----AQLEELEEAEEALLERLERLEEEL 423

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 2076993129 604 IVKADREYEECTSEDLLENIRRIAEKYKSNAAQLKA 639
Cdd:COG1196   424 EELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 240-431 7.73e-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: 39.65  E-value: 7.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129  240 ADTFEDVDAELQAK------LKDLYKVDASKLESLVEENKALNEQIARLEQErekepnrlisLRKLKASLQADVQNYKAY 313
Cdd:TIGR02168  252 EEELEELTAELQELeekleeLRLEVSELEEEIEELQKELYALANEISRLEQQ----------KQILRERLANLERQLEEL 321

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129  314 msnleshSSILEQKLSSLDE----------EIGRLELECETVKQENTRLQSVVDNQKYSIAD----IERINHEKNELQQT 379
Cdd:TIGR02168  322 -------EAQLEELESKLDElaeelaeleeKLEELKEELESLEAELEELEAELEELESRLEEleeqLETLRSKVAQLELQ 394

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2076993129  380 INKLTKDLE-----AEQQQMWNEELKYARGKEAIEAQLAEYHKLARKLKLIPKGAEN 431
Cdd:TIGR02168  395 IASLNNEIErlearLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEE 451
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 275-588 9.42e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 39.23  E-value: 9.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129 275 LNEQIARLEQER--------------EKEPNRLISLRKLKASLQADVQNYKAYMSNLESHSSILEQKLSSLDEEIGRLEL 340
Cdd:TIGR04523 340 LNEQISQLKKELtnsesensekqrelEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQ 419

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129 341 ECETVKQENTRLQSVVDNQKYSIADIERinhEKNELQQTINKLTKDLEAEQQQMWNEELKYARGKEAIEAQLAEYHKLAR 420
Cdd:TIGR04523 420 EKELLEKEIERLKETIIKNNSEIKDLTN---QDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEK 496

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129 421 KLKLIPKGAENSKGYdfeikfnpeaganclVKYRTQVYAPLKELLNEIEEEINKALNKKMGLEDTLEQLNTVKTESKrav 500
Cdd:TIGR04523 497 ELKKLNEEKKELEEK---------------VKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKEN--- 558

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076993129 501 rmLKEEVQKLDDLYQQkVKEAEEEDKKCASELDSLEKHKHLLESAVNEGLSEAMGELDAVQREyqlaVQTTTEERRKVGN 580
Cdd:TIGR04523 559 --LEKEIDEKNKEIEE-LKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKE----LEKAKKENEKLSS 631


                  ....*...
gi 2076993129 581 NLQRLLEM 588
Cdd:TIGR04523 632 IIKNIKSK 639
 
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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