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Conserved domains on  [gi|31657132|ref|NP_853557|]
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protein POF1B [Mus musculus]

Protein Classification

Graphical summary

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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 ...
 273-529 1.46e-11

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: 67.79  E-value: 1.46e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657132    273 LLEHLERIGGSKQDFES-TDTSEDIESLIPKGLSEFT--KQQIRYILQMRGMSDKSLRLVLSTFSNIREELGHLQNDLTS 349
Cdd:TIGR02169  676 LQRLRERLEGLKRELSSlQSELRRIENRLDELSQELSdaSRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIEN 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657132    350 LENDKIRLEKDLAFKENQMKEYEELLASVRAnnRQQQQGLQDSSAKCQSLEENNLSLRHTLSDLEYRLKELEYCKRNLEQ 429
Cdd:TIGR02169  756 VKSELKELEARIEELEEDLHKLEEALNDLEA--RLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEK 833

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657132    430 ENKNLRIQVSEtctgptLQAKMDEIGNHYMEMVKNLRlDKDREISKLRSQLNQY-------QKDVSKREGSCSDFQFKLH 502
Cdd:TIGR02169  834 EIQELQEQRID------LKEQIKSIEKEIENLNGKKE-ELEEELEELEAALRDLesrlgdlKKERDELEAQLRELERKIE 906

                          250       260
                   ....*....|....*....|....*..
gi 31657132    503 ELTSLLEEKDSLIKRQSEELSKLRQEI 529
Cdd:TIGR02169  907 ELEAQIEKKRKRLSELKAKLEALEEEL 933
 
Name Accession Description Interval E-value
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 273-529 1.46e-11

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: 67.79  E-value: 1.46e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657132    273 LLEHLERIGGSKQDFES-TDTSEDIESLIPKGLSEFT--KQQIRYILQMRGMSDKSLRLVLSTFSNIREELGHLQNDLTS 349
Cdd:TIGR02169  676 LQRLRERLEGLKRELSSlQSELRRIENRLDELSQELSdaSRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIEN 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657132    350 LENDKIRLEKDLAFKENQMKEYEELLASVRAnnRQQQQGLQDSSAKCQSLEENNLSLRHTLSDLEYRLKELEYCKRNLEQ 429
Cdd:TIGR02169  756 VKSELKELEARIEELEEDLHKLEEALNDLEA--RLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEK 833

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657132    430 ENKNLRIQVSEtctgptLQAKMDEIGNHYMEMVKNLRlDKDREISKLRSQLNQY-------QKDVSKREGSCSDFQFKLH 502
Cdd:TIGR02169  834 EIQELQEQRID------LKEQIKSIEKEIENLNGKKE-ELEEELEELEAALRDLesrlgdlKKERDELEAQLRELERKIE 906

                          250       260
                   ....*....|....*....|....*..
gi 31657132    503 ELTSLLEEKDSLIKRQSEELSKLRQEI 529
Cdd:TIGR02169  907 ELEAQIEKKRKRLSELKAKLEALEEEL 933
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
333-529 1.11e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 51.60  E-value: 1.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657132  333 FSNIREELGHLQNDLTSLENDKIR---LEKDLAFKENQMKEYEELLASVraNNRQQQQG---LQDSSAKCQSLEE---NN 403
Cdd:PRK03918 527 YEKLKEKLIKLKGEIKSLKKELEKleeLKKKLAELEKKLDELEEELAEL--LKELEELGfesVEELEERLKELEPfynEY 604

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657132  404 LSLRHTLSDLEYRLKELEYCKRNLEQENKNLRIQVSETctgPTLQAKMDEIGNHY----MEMVKNLRLDKDREISKLRSQ 479
Cdd:PRK03918 605 LELKDAEKELEREEKELKKLEEELDKAFEELAETEKRL---EELRKELEELEKKYseeeYEELREEYLELSRELAGLRAE 681

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 31657132  480 LNQYQKdvskregscsdfqfKLHELTSLLEEkdslIKRQSEELSKLRQEI 529
Cdd:PRK03918 682 LEELEK--------------RREEIKKTLEK----LKEELEEREKAKKEL 713
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
322-491 1.77e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.20  E-value: 1.77e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657132 322 SDKSLRLVLSTFSNIREELGHLQNDLTSLENDKIRLEKDLAFKENQMKEYEELLasvrannRQQQQGLQDSSAKCQSLEE 401
Cdd:COG4372  29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL-------EELNEQLQAAQAELAQAQE 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657132 402 NNLSLRHTLSDLEYRLKELEYCKRNLEQENKNLRIQVSEtctgptLQAKMDEignhymemvknlrldKDREISKLRSQLN 481
Cdd:COG4372 102 ELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAE------LQSEIAE---------------REEELKELEEQLE 160

                       170
                ....*....|
gi 31657132 482 QYQKDVSKRE 491
Cdd:COG4372 161 SLQEELAALE 170
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 334-518 1.09e-04

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 45.17  E-value: 1.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657132    334 SNIREELGHLQNDLTSLENDKIRLEKDLAFKENQMKEYEELLAsvrannRQQQQGLQDSSaKCQSLEENNLSLRHtlsdl 413
Cdd:pfam01576  436 SKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQ------EETRQKLNLST-RLRQLEDERNSLQE----- 503

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657132    414 eyRLKELEYCKRNLEQENKNLRIQVSETctgptlQAKMDEIgNHYMEMVKNLRLDKDREISKLRSQLNQYQKDVSKREGS 493
Cdd:pfam01576  504 --QLEEEEEAKRNVERQLSTLQAQLSDM------KKKLEED-AGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKT 574

                          170       180
                   ....*....|....*....|....*....
gi 31657132    494 CSDFQFKLHELTSLLEEKDSLI----KRQ 518
Cdd:pfam01576  575 KNRLQQELDDLLVDLDHQRQLVsnleKKQ 603
 
Name Accession Description Interval E-value
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 273-529 1.46e-11

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: 67.79  E-value: 1.46e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657132    273 LLEHLERIGGSKQDFES-TDTSEDIESLIPKGLSEFT--KQQIRYILQMRGMSDKSLRLVLSTFSNIREELGHLQNDLTS 349
Cdd:TIGR02169  676 LQRLRERLEGLKRELSSlQSELRRIENRLDELSQELSdaSRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIEN 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657132    350 LENDKIRLEKDLAFKENQMKEYEELLASVRAnnRQQQQGLQDSSAKCQSLEENNLSLRHTLSDLEYRLKELEYCKRNLEQ 429
Cdd:TIGR02169  756 VKSELKELEARIEELEEDLHKLEEALNDLEA--RLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEK 833

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657132    430 ENKNLRIQVSEtctgptLQAKMDEIGNHYMEMVKNLRlDKDREISKLRSQLNQY-------QKDVSKREGSCSDFQFKLH 502
Cdd:TIGR02169  834 EIQELQEQRID------LKEQIKSIEKEIENLNGKKE-ELEEELEELEAALRDLesrlgdlKKERDELEAQLRELERKIE 906

                          250       260
                   ....*....|....*....|....*..
gi 31657132    503 ELTSLLEEKDSLIKRQSEELSKLRQEI 529
Cdd:TIGR02169  907 ELEAQIEKKRKRLSELKAKLEALEEEL 933
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
333-529 1.11e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 51.60  E-value: 1.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657132  333 FSNIREELGHLQNDLTSLENDKIR---LEKDLAFKENQMKEYEELLASVraNNRQQQQG---LQDSSAKCQSLEE---NN 403
Cdd:PRK03918 527 YEKLKEKLIKLKGEIKSLKKELEKleeLKKKLAELEKKLDELEEELAEL--LKELEELGfesVEELEERLKELEPfynEY 604

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657132  404 LSLRHTLSDLEYRLKELEYCKRNLEQENKNLRIQVSETctgPTLQAKMDEIGNHY----MEMVKNLRLDKDREISKLRSQ 479
Cdd:PRK03918 605 LELKDAEKELEREEKELKKLEEELDKAFEELAETEKRL---EELRKELEELEKKYseeeYEELREEYLELSRELAGLRAE 681

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 31657132  480 LNQYQKdvskregscsdfqfKLHELTSLLEEkdslIKRQSEELSKLRQEI 529
Cdd:PRK03918 682 LEELEK--------------RREEIKKTLEK----LKEELEEREKAKKEL 713
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
277-529 3.56e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 50.06  E-value: 3.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657132  277 LERIGGSKQDFES-TDTSEDIESLIPkgLSEFT-----KQ-QIRYILQMRGMSDKSLRLVLS--TFSNIREELGHLqndL 347
Cdd:PRK03918  97 LKYLDGSEVLEEGdSSVREWVERLIP--YHVFLnaiyiRQgEIDAILESDESREKVVRQILGldDYENAYKNLGEV---I 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657132  348 TSLENDKIRLEKDLAFKEN---QMKEYEELLASVRANNRQQQQGLQDSSAKCQSLEENNLSLRHT---LSDLEYRLKELE 421
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTENieeLIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELkeeIEELEKELESLE 251

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657132  422 YCKRNLEQENKNLRIQVSEtctgptLQAKMDEIGNHYMEmVKNLRLDKD--REISKLRSQLNQYQKDVSKREGSCSDFQF 499
Cdd:PRK03918 252 GSKRKLEEKIRELEERIEE------LKKEIEELEEKVKE-LKELKEKAEeyIKLSEFYEEYLDELREIEKRLSRLEEEIN 324

                        250       260       270
                 ....*....|....*....|....*....|
gi 31657132  500 KLHELTSLLEEKDSLIKRQSEELSKLRQEI 529
Cdd:PRK03918 325 GIEERIKELEEKEERLEELKKKLKELEKRL 354
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 295-535 5.58e-06

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: 49.67  E-value: 5.58e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657132    295 DIESLIpKGLSEFTKQQIRYILQMR------GMSDKSLRLVLSTFSNIREELGHLQNDLTSLENDKIRLEKDLAFK---- 364
Cdd:TIGR02168  233 RLEELR-EELEELQEELKEAEEELEeltaelQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILrerl 311

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657132    365 ---ENQMKEYEELLASVRANNRQQQQGLQDSSAKCQSLEENNLSLRHTLSDLEYRLKELEYCKRNLEQENKNLRIQVSEt 441
Cdd:TIGR02168  312 anlERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ- 390

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657132    442 ctgptLQAKMDEIGNHYMEMVKNL-----RLDK-DREISKLRSQLNQYQKDVSKREgsCSDFQFKLHELTSLLEEKDSLI 515
Cdd:TIGR02168  391 -----LELQIASLNNEIERLEARLerledRRERlQQEIEELLKKLEEAELKELQAE--LEELEEELEELQEELERLEEAL 463

                          250       260
                   ....*....|....*....|
gi 31657132    516 KRQSEELSKLRQEIYSSHNQ 535
Cdd:TIGR02168  464 EELREELEEAEQALDAAERE 483
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 331-529 6.74e-06

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: 49.28  E-value: 6.74e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657132    331 STFSNIREELGHLQNDLTSLENDKIRLEKDLAFKENQMKEYEELLASVRANNRQQQQGLQDSSAKCQSLEENNLSLRHTL 410
Cdd:TIGR02168  691 EKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERL 770

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657132    411 SDLEYRLKELEYCKRNLEQENKNLRIQVSETctgptlqakmdeignhymemvknlrldkDREISKLRSQLNQYQKDVSKR 490
Cdd:TIGR02168  771 EEAEEELAEAEAEIEELEAQIEQLKEELKAL----------------------------REALDELRAELTLLNEEAANL 822

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 31657132    491 EGSCSDFQFKLHELTSLLEEKDSLIKRQSEELSKLRQEI 529
Cdd:TIGR02168  823 RERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEI 861
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 338-529 1.31e-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: 1.31e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657132    338 EELGHLQNDLTSLENDKIRLEKDLAFKENQMKE-------YEELLASVRANNRQQQQGLQDSSAKCQSLEENNLSLRHTL 410
Cdd:TIGR02169  287 EEQLRVKEKIGELEAEIASLERSIAEKERELEDaeerlakLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL 366

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657132    411 SDLEYRLKELEYCKRNLEQENKNLR------------IQVSETCTGPTLQAKMDEIGNHYMEM---------VKNLRLDK 469
Cdd:TIGR02169  367 EDLRAELEEVDKEFAETRDELKDYRekleklkreineLKRELDRLQEELQRLSEELADLNAAIagieakineLEEEKEDK 446

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657132    470 DREISKLRSQLNQYQKDVSKREGSCSDFQFKLHELtslleekdslikrqSEELSKLRQEI 529
Cdd:TIGR02169  447 ALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRV--------------EKELSKLQREL 492
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 257-530 1.49e-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: 48.13  E-value: 1.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657132    257 ELLADLSRKNTDLYHCLLEHLERIGGSKQDF-ESTDTSEDIESLIPKGLSEFtkQQIRYILqmrgmsdKSLRlvlSTFSN 335
Cdd:TIGR02168  747 ERIAQLSKELTELEAEIEELEERLEEAEEELaEAEAEIEELEAQIEQLKEEL--KALREAL-------DELR---AELTL 814

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657132    336 IREELGHLQNDLTSLENDKIRLEKDLAFKENQMKEYEELLASVRANNRQQQQGLQDSSAKCQSL-------EENNLSLRH 408
Cdd:TIGR02168  815 LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALlneraslEEALALLRS 894

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657132    409 TLSDLEYRLKELEYCKRNLEQENKNLRIQVSE--------TCTGPTLQAKMDEIGNHYMEMVKNLRLDKDREISKLRSQL 480
Cdd:TIGR02168  895 ELEELSEELRELESKRSELRRELEELREKLAQlelrleglEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRL 974

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657132    481 NQYQ-----------------KDVSKRegscsdFQFKLHELTSLLEEKDSL---IKRQSEELSKLRQEIY 530
Cdd:TIGR02168  975 KRLEnkikelgpvnlaaieeyEELKER------YDFLTAQKEDLTEAKETLeeaIEEIDREARERFKDTF 1038
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
322-491 1.77e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.20  E-value: 1.77e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657132 322 SDKSLRLVLSTFSNIREELGHLQNDLTSLENDKIRLEKDLAFKENQMKEYEELLasvrannRQQQQGLQDSSAKCQSLEE 401
Cdd:COG4372  29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL-------EELNEQLQAAQAELAQAQE 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657132 402 NNLSLRHTLSDLEYRLKELEYCKRNLEQENKNLRIQVSEtctgptLQAKMDEignhymemvknlrldKDREISKLRSQLN 481
Cdd:COG4372 102 ELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAE------LQSEIAE---------------REEELKELEEQLE 160

                       170
                ....*....|
gi 31657132 482 QYQKDVSKRE 491
Cdd:COG4372 161 SLQEELAALE 170
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 324-529 1.81e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.01  E-value: 1.81e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657132 324 KSLRLVLSTFSNIREELGHLQNDLTSLENDKIRLEKDLAFKENQMKEYEELLASVRANNRQQQQGLQDSSAKCQSLEENN 403
Cdd:COG1196 225 LEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDI 304

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657132 404 LSLRHTLSDLEYRLKELEYCKRNLEQENKNLRIQVSEtctgptLQAKMDEIGNHYMEMVKNL------RLDKDREISKLR 477
Cdd:COG1196 305 ARLEERRRELEERLEELEEELAELEEELEELEEELEE------LEEELEEAEEELEEAEAELaeaeeaLLEAEAELAEAE 378

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 31657132 478 SQLNQYQKDVSKREGSCSDFQFKLHELTSLLEEKDSLIKRQSEELSKLRQEI 529
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 333-535 3.72e-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: 46.97  E-value: 3.72e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657132    333 FSNIREELGHLQndLTSLENDKIRLEKDLAFKENQMKEYEELLASVRANNRQQQQGLQDSSAKCQSLEENNLSLRHTLSD 412
Cdd:TIGR02168  215 YKELKAELRELE--LALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYA 292

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657132    413 LEYRLKELEYCKRNLEQENKNLRIQVSETctgptlqakmdeigNHYMEMVKNLRLDKDREISKLRSQLNQYQKDVSKREG 492
Cdd:TIGR02168  293 LANEISRLEQQKQILRERLANLERQLEEL--------------EAQLEELESKLDELAEELAELEEKLEELKEELESLEA 358

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 31657132    493 SCSDFQFKLHELTSLLEEKDSLIKRQSEELSKLRQEIYSSHNQ 535
Cdd:TIGR02168  359 ELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNE 401
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 334-518 1.09e-04

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 45.17  E-value: 1.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657132    334 SNIREELGHLQNDLTSLENDKIRLEKDLAFKENQMKEYEELLAsvrannRQQQQGLQDSSaKCQSLEENNLSLRHtlsdl 413
Cdd:pfam01576  436 SKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQ------EETRQKLNLST-RLRQLEDERNSLQE----- 503

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657132    414 eyRLKELEYCKRNLEQENKNLRIQVSETctgptlQAKMDEIgNHYMEMVKNLRLDKDREISKLRSQLNQYQKDVSKREGS 493
Cdd:pfam01576  504 --QLEEEEEAKRNVERQLSTLQAQLSDM------KKKLEED-AGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKT 574

                          170       180
                   ....*....|....*....|....*....
gi 31657132    494 CSDFQFKLHELTSLLEEKDSLI----KRQ 518
Cdd:pfam01576  575 KNRLQQELDDLLVDLDHQRQLVsnleKKQ 603
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 278-524 4.69e-04

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 43.29  E-value: 4.69e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657132    278 ERIGGSKQDFESTDTS-EDIESLIPKGLSEFTKQQIRYILQMRgmsdkslRLVlSTFSNIREELGHLQNDLTSLEND-KI 355
Cdd:pfam12128  768 DVIAKLKREIRTLERKiERIAVRRQEVLRYFDWYQETWLQRRP-------RLA-TQLSNIERAISELQQQLARLIADtKL 839

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657132    356 R---LEKDLAFKENQMKEYEELLASVRAnnrqQQQGLQDsSAKCQSLEENNLSLRHTLSDLEYRLKELEYCKRNLEQENK 432
Cdd:pfam12128  840 RrakLEMERKASEKQQVRLSENLRGLRC----EMSKLAT-LKEDANSEQAQGSIGERLAQLEDLKLKRDYLSESVKKYVE 914

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657132    433 NLR-IQVSETCTGP-----TLQAKMDEIGNhymemvKNLRLDKDREISKLRSQLNQY---QKDVSKREGScSDFQFKLHE 503
Cdd:pfam12128  915 HFKnVIADHSGSGLaetweSLREEDHYQND------KGIRLLDYRKLVPYLEQWFDVrvpQSIMVLREQV-SILGVDLTE 987

                          250       260
                   ....*....|....*....|.
gi 31657132    504 LTSLLEEKDSLIKRQSEELSK 524
Cdd:pfam12128  988 FYDVLADFDRRIASFSRELQR 1008
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 325-482 5.00e-04

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 43.40  E-value: 5.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657132  325 SLRLVLSTFSNIREELGHLQNDLTSLENdKIRLEKDLAFKENQMKEYEELLASVRANNRQQQQGLQDSSAKCQsleENNL 404
Cdd:COG3096  506 SQQALAQRLQQLRAQLAELEQRLRQQQN-AERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAV---EQRS 581

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657132  405 SLRHTLSDLEYRLKELEycKR---------NLEQenknLRIQVSETCTgpTLQAKMDeignhYMEMVknlrLDKDREISK 475
Cdd:COG3096  582 ELRQQLEQLRARIKELA--ARapawlaaqdALER----LREQSGEALA--DSQEVTA-----AMQQL----LEREREATV 644


                 ....*..
gi 31657132  476 LRSQLNQ 482
Cdd:COG3096  645 ERDELAA 651
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
324-528 7.29e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 7.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657132  324 KSLRLVLSTFSNIREELGHLQNDLTSLENDKIRLEKDLAFKENQMKEYEELLASVRANN--RQQQQGLQDSSAK--CQSL 399
Cdd:PRK03918 307 DELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEeaKAKKEELERLKKRltGLTP 386

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657132  400 EENN---LSLRHTLSDLEYRLKELEYCKRNLEQENKNLRIQVSE---------TCTGPTLQAKMDEIGNHYMEMVKNLRL 467
Cdd:PRK03918 387 EKLEkelEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEElkkakgkcpVCGRELTEEHRKELLEEYTAELKRIEK 466

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 31657132  468 DK---DREISKLRSQLNQYQKDVSKREGScsdfqFKLHELTSLLEE-KDSL-------IKRQSEELSKLRQE 528
Cdd:PRK03918 467 ELkeiEEKERKLRKELRELEKVLKKESEL-----IKLKELAEQLKElEEKLkkynleeLEKKAEEYEKLKEK 533
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 336-490 8.08e-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: 41.45  E-value: 8.08e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657132 336 IREELGHLQNDLTSLENDKIRLEKDLAFKENQMKEYEELLASVRaNNRQQQQgLQDssakcqslEENNLSLRhtLSDLEY 415
Cdd:COG1579  43 LEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR-NNKEYEA-LQK--------EIESLKRR--ISDLED 110

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 31657132 416 RLKELEYCKRNLEQENKNLRIQVSEtctgptLQAKMDEIGNHYMEMVKNLrldkDREISKLRSQLNQYQKDVSKR 490
Cdd:COG1579 111 EILELMERIEELEEELAELEAELAE------LEAELEEKKAELDEELAEL----EAELEELEAEREELAAKIPPE 175
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 322-530 8.62e-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: 42.36  E-value: 8.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657132    322 SDKSLRLVLSTFSNIREELGHLQNDLTSLENDKIRLEKDLAFKENQMKEYEELLASVR-------ANNRQQQQGLQDSSA 394
Cdd:TIGR02169  796 IQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEkeienlnGKKEELEEELEELEA 875

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657132    395 KCQSLEENNLSLRHTLSDLEYRLKELEYCKRNLEQENKNLRIQVSE-TCTGPTLQAKMDEIGNHYMEM------------ 461
Cdd:TIGR02169  876 ALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSElKAKLEALEEELSEIEDPKGEDeeipeeelsled 955

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 31657132    462 VKNLRLDKDREISKLRS----QLNQYqKDVSKREGscsDFQFKLHELTsllEEKDSLIKRqSEELSKLRQEIY 530
Cdd:TIGR02169  956 VQAELQRVEEEIRALEPvnmlAIQEY-EEVLKRLD---ELKEKRAKLE---EERKAILER-IEEYEKKKREVF 1020
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 310-532 1.45e-03

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 40.95  E-value: 1.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657132   310 QQIRYILQMRGMSDKSLrlvlstfSNIREELGHLQNDLTSLENDKIRLEKDLAFKENQMKEyeellaSVRANNRQQQQGL 389
Cdd:pfam15905  80 KEIRALVQERGEQDKRL-------QALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLE------LTRVNELLKAKFS 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657132   390 QDSSAK-CQSLEENNLSLRHTLS-----------DLEYRLKELEyckRNLEQENKNLriqvsetctgPTLQAKMDEIGNH 457
Cdd:pfam15905 147 EDGTQKkMSSLSMELMKLRNKLEakmkevmakqeGMEGKLQVTQ---KNLEHSKGKV----------AQLEEKLVSTEKE 213

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31657132   458 YMEM---VKNLrLDKDREISKLRSQLNQYQKDVSKREGSCSDFQFKLHELTSLLEEKDSLIKRQSEELSKLRQEIYSS 532
Cdd:pfam15905 214 KIEEkseTEKL-LEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLESE 290
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
356-529 2.31e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 2.31e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657132 356 RLEKDLAFKENQMKEYEELlasvrannrqqQQGLQDSSAKCQSLEENNLSLRHTLSDLEYRLKELEyckrnLEQENKNLR 435
Cdd:COG4717  75 ELEEELKEAEEKEEEYAEL-----------QEELEELEEELEELEAELEELREELEKLEKLLQLLP-----LYQELEALE 138

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657132 436 IQVSEtctgptLQAKMDEIGNHYMEmVKNLRLDKDR---EISKLRSQLNQYQKDVS-KREGSCSDFQFKLHELTSLLEEK 511
Cdd:COG4717 139 AELAE------LPERLEELEERLEE-LRELEEELEEleaELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAEL 211

                       170
                ....*....|....*...
gi 31657132 512 DSLIKRQSEELSKLRQEI 529
Cdd:COG4717 212 EEELEEAQEELEELEEEL 229
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 316-563 4.81e-03

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 40.03  E-value: 4.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657132    316 LQMRGMSDKSlRLVLSTFSNIREELGHLQNDLTSLENDKIRLEKDLAFKENQMKEYEELLASVRANNRQQQQGLQDSSAK 395
Cdd:TIGR00606  398 LVIERQEDEA-KTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILEL 476

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657132    396 CQSL--EENNLSLRHTLSDLEYRLKELEYCKRNLEQENKNLRiqvsetctgpTLQAKMDEIGNH-----YMEMVKNLRLD 468
Cdd:TIGR00606  477 DQELrkAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLR----------KLDQEMEQLNHHtttrtQMEMLTKDKMD 546

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657132    469 KDREISKLRSQ---------------------LNQYQKDVSKREGSCSDFQFKLHELTSLLEEKDSLIKRQSEELSKLRQ 527
Cdd:TIGR00606  547 KDEQIRKIKSRhsdeltsllgyfpnkkqledwLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYED 626

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 31657132    528 EIY---SSHNQPSCGGRTTITTKKYRTQYPILG---LLYDDY 563
Cdd:TIGR00606  627 KLFdvcGSQDEESDLERLKEEIEKSSKQRAMLAgatAVYSQF 668
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
468-531 4.96e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 39.84  E-value: 4.96e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 31657132 468 DKDREISKLRSQLNQYQKDVSkregscsdfqfklhELTSLLEEKDSLIKRQSEELSKLRQEIYS 531
Cdd:COG2433 410 EEEEEIRRLEEQVERLEAEVE--------------ELEAELEEKDERIERLERELSEARSEERR 459
ADIP pfam11559
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ...
 309-482 5.08e-03

Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.


Pssm-ID: 463295 [Multi-domain]  Cd Length: 151  Bit Score: 37.68  E-value: 5.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657132   309 KQQIRYI---LQMRGMSDkslRLVLSTFSNIREE-LGHLQNDLTSLendKIRLEKDLAFKENqmkeYEELLASVRANNRQ 384
Cdd:pfam11559   1 ENAITYInqtLLSRGFLR---SGLLFDTAEGVEEnIARIINVIYEL---LQQRDRDLEFRES----LNETIRTLEAEIER 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657132   385 QQqglqdssAKCQSLEENNLSLRHTLSDLEYRLKELEYCKRNLEQENKNLRIQVSEtctgptLQAKMDEIGNHYMEMVKN 464
Cdd:pfam11559  71 LQ-------SKIERLKTQLEDLERELALLQAKERQLEKKLKTLEQKLKNEKEELQR------LKNALQQIKTQFAHEVKK 137

                         170
                  ....*....|....*...
gi 31657132   465 lrldKDREISKLRSQLNQ 482
Cdd:pfam11559 138 ----RDREIEKLKERLAQ 151
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 352-529 7.76e-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: 38.98  E-value: 7.76e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657132 352 NDKIRLEKDLAFKENQMKEYEELLASVRANNRQQQQGLQDSSAKCQSLEENNLSLRHTLSDLEYRLKELEYCKRNLEQEN 431
Cdd:COG4942  20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657132 432 KNLR---------IQVSETCTGPTL-------------QAKMDEIGNHYMEMVKNLRLDKDrEISKLRSQLNQYQKDVSK 489
Cdd:COG4942 100 EAQKeelaellraLYRLGRQPPLALllspedfldavrrLQYLKYLAPARREQAEELRADLA-ELAALRAELEAERAELEA 178

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 31657132 490 REgscSDFQFKLHELTSLLEEKDSLIKRQSEELSKLRQEI 529
Cdd:COG4942 179 LL---AELEEERAALEALKAERQKLLARLEKELAELAAEL 215
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 310-528 8.24e-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: 8.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657132   310 QQIRYILQMRGMSDKSLRLVLSTFSNIREELGHLQNDLTSLENDKIRLEKDLAFKENQMKEYEELLASVRANNRQQQQGL 389
Cdd:TIGR04523 412 EQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKEL 491

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657132   390 QDSSAKCQSLEENNLSLRHTLSDLEYRLKELEYCKRNLEQENKNLRIQVSEtctgptLQAKMDEIG-NHYMEMVKNLRLD 468
Cdd:TIGR04523 492 KSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISD------LEDELNKDDfELKKENLEKEIDE 565

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 31657132   469 KDREISKLRSQLNQYQKDVSKREGSCSDFQFKLHELTSLLEEKDSLIKRQSEELSKLRQE 528
Cdd:TIGR04523 566 KNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKE 625
 
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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