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Conserved domains on  [gi|1306252169|ref|NP_001345847|]
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intraflagellar transport protein 81 homolog isoform b [Mus musculus]

Protein Classification

IFT81_CH and PTZ00121 superfamily-containing protein( domain architecture ID 1566102)

IFT81_CH and PTZ00121 superfamily-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
IFT81_CH super family cl39721
Intraflagellar transport 81 calponin homology domain; This is the N-terminal domain found in ...
 1-70 4.27e-32

Intraflagellar transport 81 calponin homology domain; This is the N-terminal domain found in IFT81 proteins. Crystal structure analysis revealed that IFT81-N adopts the fold of a calponin homology (CH) domain with structural similarity to the kinetochore complex component NDC80 with microtubule (MT)-binding properties. Functional analysis show that IFT74 and IFT81 form a tubulin-binding module required for ciliogenesis. It is suggested that IFT81-N binds the globular domain of tubulin to provide specificity, and IFT74-N recognizes the beta-tubulin tail to increase affinity.


The actual alignment was detected with superfamily member pfam18383:

Pssm-ID: 465736  Cd Length: 124  Bit Score: 120.43  E-value: 4.27e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169   1 MPEQTAKRMLNLLGILKYKPPGNATDMSTFRQGLVIGSKPVIYPVLHWLLQRSNELKKRAYLARFLIKLE 70
Cdd:pfam18383  55 SPEETAIRILEALRILKYKPPPDIDDPSAFRQGLVRGEKLVIYPILYWLLSNVEELKKRAYLARFLVKVE 124
PTZ00121 super family cl31754
MAEBL; Provisional
 121-617 1.07e-06

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.07  E-value: 1.07e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  121 AMEEEKDQLMKRVERLKKRVETVQNHQRMLKIARQlrvEKEREEFLAQQKQEQKNQLFHAVQRLQRVQNQLK-SMRHAAA 199
Cdd:PTZ00121  1292 ADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEE---AKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEaAEEKAEA 1368

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  200 DAKPESLMKRLEEEIKFNSYMV--TEKFPKELESKKKELHFLQKVVSEPAMGHsdllELETKVNEVNtEINQLIEKKMMR 277
Cdd:PTZ00121  1369 AEKKKEEAKKKADAAKKKAEEKkkADEAKKKAEEDKKKADELKKAAAAKKKAD----EAKKKAEEKK-KADEAKKKAEEA 1443

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  278 NEPIEGKLSLYRQQASIISRKKEAKAEELQETKEKLASLER-EVLVKTNQTREFDGTEVLKGDEFKRYVSKLRSKSTVFK 356
Cdd:PTZ00121  1444 KKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKaDEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKK 1523

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  357 KKHQIIAEFKAEFGLLQRTEELLKQRQETIQHQLRTIEEKKGISGYSYTQEE---LERVSALKSEVDEMKGRTLDDMSEM 433
Cdd:PTZ00121  1524 ADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDknmALRKAEEAKKAEEARIEEVMKLYEE 1603

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  434 VKKLNSLVSEKKSALAPVIKELR---QLRQKCQELTQECDEKKAQYDSCAAGLESNRSKLEQEVRGLREECLQEESKYHY 510
Cdd:PTZ00121  1604 EKKMKAEEAKKAEEAKIKAEELKkaeEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKA 1683

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  511 TNCMIKNLEVELRRATDEMKA--YVSSDQQEKRKA--IREQYTKNITEQENLGKKLREKQKAVRESHGPNMKQAKMWRDL 586
Cdd:PTZ00121  1684 EEDEKKAAEALKKEAEEAKKAeeLKKKEAEEKKKAeeLKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLK 1763

                          490       500       510
                   ....*....|....*....|....*....|.
gi 1306252169  587 EQlmECKKQCFLKQQSPASIGQVIQEGGEDR 617
Cdd:PTZ00121  1764 KE--EEKKAEEIRKEKEAVIEEELDEEDEKR 1792
 
Name Accession Description Interval E-value
IFT81_CH pfam18383
Intraflagellar transport 81 calponin homology domain; This is the N-terminal domain found in ...
 1-70 4.27e-32

Intraflagellar transport 81 calponin homology domain; This is the N-terminal domain found in IFT81 proteins. Crystal structure analysis revealed that IFT81-N adopts the fold of a calponin homology (CH) domain with structural similarity to the kinetochore complex component NDC80 with microtubule (MT)-binding properties. Functional analysis show that IFT74 and IFT81 form a tubulin-binding module required for ciliogenesis. It is suggested that IFT81-N binds the globular domain of tubulin to provide specificity, and IFT74-N recognizes the beta-tubulin tail to increase affinity.


Pssm-ID: 465736  Cd Length: 124  Bit Score: 120.43  E-value: 4.27e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169   1 MPEQTAKRMLNLLGILKYKPPGNATDMSTFRQGLVIGSKPVIYPVLHWLLQRSNELKKRAYLARFLIKLE 70
Cdd:pfam18383  55 SPEETAIRILEALRILKYKPPPDIDDPSAFRQGLVRGEKLVIYPILYWLLSNVEELKKRAYLARFLVKVE 124
PTZ00121 PTZ00121
MAEBL; Provisional
 121-617 1.07e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.07  E-value: 1.07e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  121 AMEEEKDQLMKRVERLKKRVETVQNHQRMLKIARQlrvEKEREEFLAQQKQEQKNQLFHAVQRLQRVQNQLK-SMRHAAA 199
Cdd:PTZ00121  1292 ADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEE---AKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEaAEEKAEA 1368

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  200 DAKPESLMKRLEEEIKFNSYMV--TEKFPKELESKKKELHFLQKVVSEPAMGHsdllELETKVNEVNtEINQLIEKKMMR 277
Cdd:PTZ00121  1369 AEKKKEEAKKKADAAKKKAEEKkkADEAKKKAEEDKKKADELKKAAAAKKKAD----EAKKKAEEKK-KADEAKKKAEEA 1443

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  278 NEPIEGKLSLYRQQASIISRKKEAKAEELQETKEKLASLER-EVLVKTNQTREFDGTEVLKGDEFKRYVSKLRSKSTVFK 356
Cdd:PTZ00121  1444 KKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKaDEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKK 1523

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  357 KKHQIIAEFKAEFGLLQRTEELLKQRQETIQHQLRTIEEKKGISGYSYTQEE---LERVSALKSEVDEMKGRTLDDMSEM 433
Cdd:PTZ00121  1524 ADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDknmALRKAEEAKKAEEARIEEVMKLYEE 1603

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  434 VKKLNSLVSEKKSALAPVIKELR---QLRQKCQELTQECDEKKAQYDSCAAGLESNRSKLEQEVRGLREECLQEESKYHY 510
Cdd:PTZ00121  1604 EKKMKAEEAKKAEEAKIKAEELKkaeEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKA 1683

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  511 TNCMIKNLEVELRRATDEMKA--YVSSDQQEKRKA--IREQYTKNITEQENLGKKLREKQKAVRESHGPNMKQAKMWRDL 586
Cdd:PTZ00121  1684 EEDEKKAAEALKKEAEEAKKAeeLKKKEAEEKKKAeeLKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLK 1763

                          490       500       510
                   ....*....|....*....|....*....|.
gi 1306252169  587 EQlmECKKQCFLKQQSPASIGQVIQEGGEDR 617
Cdd:PTZ00121  1764 KE--EEKKAEEIRKEKEAVIEEELDEEDEKR 1792
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 130-544 5.56e-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: 5.56e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  130 MKRVERLKKRVETVQNHQRMLKIARQLR--VEK-EREEFLAQQKQEQKNQLFHA-----VQRLQRVQNQLKSMRHAAADA 201
Cdd:TIGR02168  172 ERRKETERKLERTRENLDRLEDILNELErqLKSlERQAEKAERYKELKAELRELelallVLRLEELREELEELQEELKEA 251

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  202 kpESLMKRLEEEIKfnsyMVTEKFpKELESKKKELHflqkvvsepamghSDLLELETKVNEVNTEINQLIEKKMMRNEpi 281
Cdd:TIGR02168  252 --EEELEELTAELQ----ELEEKL-EELRLEVSELE-------------EEIEELQKELYALANEISRLEQQKQILRE-- 309

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  282 egKLSLYRQQASIISRKKEAKAEELQETKEKLASLEREVLVKTNQTREFDgtevlkgDEFKRYVSKLRSKSTVFKKKHQI 361
Cdd:TIGR02168  310 --RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLE-------AELEELEAELEELESRLEELEEQ 380

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  362 IAEFKAEFGLLQRTEELLKQRQETIQHQLRTIEEKKgisgysytQEELERVSALKSEVDEMKGRTLDDMSEMVKKLNSLV 441
Cdd:TIGR02168  381 LETLRSKVAQLELQIASLNNEIERLEARLERLEDRR--------ERLQQEIEELLKKLEEAELKELQAELEELEEELEEL 452

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  442 SEKKSALAPVIKELRQLRQKCQELTQECDEKKAQYDSCAAGLESNRSKLEQEVRGLREECLQEESKYHYTNCMIKNLEVE 521
Cdd:TIGR02168  453 QEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVD 532

                          410       420       430
                   ....*....|....*....|....*....|
gi 1306252169  522 --LRRATDE-----MKAYVSSDQQEKRKAI 544
Cdd:TIGR02168  533 egYEAAIEAalggrLQAVVVENLNAAKKAI 562
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
112-326 1.91e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 47.70  E-value: 1.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169 112 TAEIRRDISAMEEEKDQLMKRVERLKKRVETVQNHQRMLKIARQLRVEKEREEFLAQQKQEQKNQLFHAVQRLQRVQNQL 191
Cdd:COG3206   170 REEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQL 249

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169 192 KSMRHAAADAKPESLMKRLEEEIkfnsymvtekfpKELESKKKElhfLQKVVSEpamGHSDLLELETKVNEVNTEINQLI 271
Cdd:COG3206   250 GSGPDALPELLQSPVIQQLRAQL------------AELEAELAE---LSARYTP---NHPDVIALRAQIAALRAQLQQEA 311

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1306252169 272 EKKM--MRNEpiegKLSLYRQQASIISRKKEAKAE--ELQETKEKLASLEREVLVKTNQ 326
Cdd:COG3206   312 QRILasLEAE----LEALQAREASLQAQLAQLEARlaELPELEAELRRLEREVEVAREL 366
Nup88 pfam10168
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ...
 118-268 2.08e-03

Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.


Pssm-ID: 462975 [Multi-domain]  Cd Length: 713  Bit Score: 41.18  E-value: 2.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169 118 DISAMEEEKDQLMKRVERLKKRVETVQNHQ-----RMLKIARQLR------VEKEREEflaqqKQEqknqlfhavqrLQR 186
Cdd:pfam10168 576 ELQSLEEERKSLSERAEKLAEKYEEIKDKQeklmrRCKKVLQRLNsqlpvlSDAEREM-----KKE-----------LET 639

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169 187 VQNQLKSMRHAAADAKpeslMKRLEEEIKFNSYMVTEKfPKELESKKKELHFLQKVVSEpaMGhSDLLELETKVNEVNTE 266
Cdd:pfam10168 640 INEQLKHLANAIKQAK----KKMNYQRYQIAKSQSIRK-KSSLSLSEKQRKTIKEILKQ--LG-SEIDELIKQVKDINKH 711


                  ..
gi 1306252169 267 IN 268
Cdd:pfam10168 712 VG 713
 
Name Accession Description Interval E-value
IFT81_CH pfam18383
Intraflagellar transport 81 calponin homology domain; This is the N-terminal domain found in ...
 1-70 4.27e-32

Intraflagellar transport 81 calponin homology domain; This is the N-terminal domain found in IFT81 proteins. Crystal structure analysis revealed that IFT81-N adopts the fold of a calponin homology (CH) domain with structural similarity to the kinetochore complex component NDC80 with microtubule (MT)-binding properties. Functional analysis show that IFT74 and IFT81 form a tubulin-binding module required for ciliogenesis. It is suggested that IFT81-N binds the globular domain of tubulin to provide specificity, and IFT74-N recognizes the beta-tubulin tail to increase affinity.


Pssm-ID: 465736  Cd Length: 124  Bit Score: 120.43  E-value: 4.27e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169   1 MPEQTAKRMLNLLGILKYKPPGNATDMSTFRQGLVIGSKPVIYPVLHWLLQRSNELKKRAYLARFLIKLE 70
Cdd:pfam18383  55 SPEETAIRILEALRILKYKPPPDIDDPSAFRQGLVRGEKLVIYPILYWLLSNVEELKKRAYLARFLVKVE 124
PTZ00121 PTZ00121
MAEBL; Provisional
 121-617 1.07e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.07  E-value: 1.07e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  121 AMEEEKDQLMKRVERLKKRVETVQNHQRMLKIARQlrvEKEREEFLAQQKQEQKNQLFHAVQRLQRVQNQLK-SMRHAAA 199
Cdd:PTZ00121  1292 ADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEE---AKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEaAEEKAEA 1368

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  200 DAKPESLMKRLEEEIKFNSYMV--TEKFPKELESKKKELHFLQKVVSEPAMGHsdllELETKVNEVNtEINQLIEKKMMR 277
Cdd:PTZ00121  1369 AEKKKEEAKKKADAAKKKAEEKkkADEAKKKAEEDKKKADELKKAAAAKKKAD----EAKKKAEEKK-KADEAKKKAEEA 1443

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  278 NEPIEGKLSLYRQQASIISRKKEAKAEELQETKEKLASLER-EVLVKTNQTREFDGTEVLKGDEFKRYVSKLRSKSTVFK 356
Cdd:PTZ00121  1444 KKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKaDEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKK 1523

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  357 KKHQIIAEFKAEFGLLQRTEELLKQRQETIQHQLRTIEEKKGISGYSYTQEE---LERVSALKSEVDEMKGRTLDDMSEM 433
Cdd:PTZ00121  1524 ADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDknmALRKAEEAKKAEEARIEEVMKLYEE 1603

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  434 VKKLNSLVSEKKSALAPVIKELR---QLRQKCQELTQECDEKKAQYDSCAAGLESNRSKLEQEVRGLREECLQEESKYHY 510
Cdd:PTZ00121  1604 EKKMKAEEAKKAEEAKIKAEELKkaeEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKA 1683

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  511 TNCMIKNLEVELRRATDEMKA--YVSSDQQEKRKA--IREQYTKNITEQENLGKKLREKQKAVRESHGPNMKQAKMWRDL 586
Cdd:PTZ00121  1684 EEDEKKAAEALKKEAEEAKKAeeLKKKEAEEKKKAeeLKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLK 1763

                          490       500       510
                   ....*....|....*....|....*....|.
gi 1306252169  587 EQlmECKKQCFLKQQSPASIGQVIQEGGEDR 617
Cdd:PTZ00121  1764 KE--EEKKAEEIRKEKEAVIEEELDEEDEKR 1792
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 130-544 5.56e-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: 5.56e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  130 MKRVERLKKRVETVQNHQRMLKIARQLR--VEK-EREEFLAQQKQEQKNQLFHA-----VQRLQRVQNQLKSMRHAAADA 201
Cdd:TIGR02168  172 ERRKETERKLERTRENLDRLEDILNELErqLKSlERQAEKAERYKELKAELRELelallVLRLEELREELEELQEELKEA 251

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  202 kpESLMKRLEEEIKfnsyMVTEKFpKELESKKKELHflqkvvsepamghSDLLELETKVNEVNTEINQLIEKKMMRNEpi 281
Cdd:TIGR02168  252 --EEELEELTAELQ----ELEEKL-EELRLEVSELE-------------EEIEELQKELYALANEISRLEQQKQILRE-- 309

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  282 egKLSLYRQQASIISRKKEAKAEELQETKEKLASLEREVLVKTNQTREFDgtevlkgDEFKRYVSKLRSKSTVFKKKHQI 361
Cdd:TIGR02168  310 --RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLE-------AELEELEAELEELESRLEELEEQ 380

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  362 IAEFKAEFGLLQRTEELLKQRQETIQHQLRTIEEKKgisgysytQEELERVSALKSEVDEMKGRTLDDMSEMVKKLNSLV 441
Cdd:TIGR02168  381 LETLRSKVAQLELQIASLNNEIERLEARLERLEDRR--------ERLQQEIEELLKKLEEAELKELQAELEELEEELEEL 452

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  442 SEKKSALAPVIKELRQLRQKCQELTQECDEKKAQYDSCAAGLESNRSKLEQEVRGLREECLQEESKYHYTNCMIKNLEVE 521
Cdd:TIGR02168  453 QEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVD 532

                          410       420       430
                   ....*....|....*....|....*....|
gi 1306252169  522 --LRRATDE-----MKAYVSSDQQEKRKAI 544
Cdd:TIGR02168  533 egYEAAIEAalggrLQAVVVENLNAAKKAI 562
PRK12704 PRK12704
phosphodiesterase; Provisional
 281-436 1.09e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 48.24  E-value: 1.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169 281 IEGKLSLYRQQASIIsrKKEAKAEELQETKEKLASLEREVLvktNQTREFDGTEVLKGDEFKRYVSKLRSKSTVFKKKHQ 360
Cdd:PRK12704   29 AEAKIKEAEEEAKRI--LEEAKKEAEAIKKEALLEAKEEIH---KLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLE 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169 361 IIAEFKAEfglLQRTEELLKQRQETIQHQLRTIEEKkgisgYSYTQEELERVSALKSE------VDEMKGRTLDDMSEMV 434
Cdd:PRK12704  104 LLEKREEE---LEKKEKELEQKQQELEKKEEELEEL-----IEEQLQELERISGLTAEeakeilLEKVEEEARHEAAVLI 175


                  ..
gi 1306252169 435 KK 436
Cdd:PRK12704  176 KE 177
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 85-384 1.78e-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: 1.78e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169   85 NKQYEELMEAFKTLHKECE----QLKTSGFSTAEIRRDISAMEEEKDQLMKRVERLKKRVETVQnhqrmlkiaRQLRVEK 160
Cdd:TIGR02168  238 REELEELQEELKEAEEELEeltaELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLE---------QQKQILR 308

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  161 EREEFLAQQKQEQKNQLFHAVQRLQRVQNQLKSMRHAAADAKPEslMKRLEEEIkfnsymvtekfpKELESKKKELhflq 240
Cdd:TIGR02168  309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEE--LESLEAEL------------EELEAELEEL---- 370

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  241 kvvsepamgHSDLLELETKVNEVNTEINQLIEKKmmrnEPIEGKLSLYRQQASIISRKKEAKAEELQETKEKLASLEREV 320
Cdd:TIGR02168  371 ---------ESRLEELEEQLETLRSKVAQLELQI----ASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKE 437

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1306252169  321 LVKTNQTREFDGTEVLKgdEFKRYVSKLRSKSTVFKKKHQIIAEFKAEFGLLQRTEELLKQRQE 384
Cdd:TIGR02168  438 LQAELEELEEELEELQE--ELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQE 499
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
112-326 1.91e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 47.70  E-value: 1.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169 112 TAEIRRDISAMEEEKDQLMKRVERLKKRVETVQNHQRMLKIARQLRVEKEREEFLAQQKQEQKNQLFHAVQRLQRVQNQL 191
Cdd:COG3206   170 REEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQL 249

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169 192 KSMRHAAADAKPESLMKRLEEEIkfnsymvtekfpKELESKKKElhfLQKVVSEpamGHSDLLELETKVNEVNTEINQLI 271
Cdd:COG3206   250 GSGPDALPELLQSPVIQQLRAQL------------AELEAELAE---LSARYTP---NHPDVIALRAQIAALRAQLQQEA 311

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1306252169 272 EKKM--MRNEpiegKLSLYRQQASIISRKKEAKAE--ELQETKEKLASLEREVLVKTNQ 326
Cdd:COG3206   312 QRILasLEAE----LEALQAREASLQAQLAQLEARlaELPELEAELRRLEREVEVAREL 366
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
83-567 7.28e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.83  E-value: 7.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  83 DTNKQYEELMEAFKTLHKECEQLKTSGFSTAEIRRDISAMEEEKDQLMKRVERLKKRVETVQNHQRMLKiARQLRVEKER 162
Cdd:PRK03918  159 DYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLE-KEVKELEELK 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169 163 EEFLAQQKQEQKNQlfhavQRLQRVQNQLKSMRHAAADAKP-----ESLMKRLEE-EIKFNSYMVTEKFPKELESKKKEL 236
Cdd:PRK03918  238 EEIEELEKELESLE-----GSKRKLEEKIRELEERIEELKKeieelEEKVKELKElKEKAEEYIKLSEFYEEYLDELREI 312

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169 237 HFLQKVVSEPAMGHSDLL-ELETKVNEVNtEINQLIEKKMMRNEPIEGKLSLYRQQASIISR----KKEAKAEELQETKE 311
Cdd:PRK03918  313 EKRLSRLEEEINGIEERIkELEEKEERLE-ELKKKLKELEKRLEELEERHELYEEAKAKKEElerlKKRLTGLTPEKLEK 391

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169 312 KLASLER---EVLVKTNQTREFDGTEVLKGDEFKRYVSKLRSKSTVF---------KKKHQIIAEFKAEFGLLQRTEELL 379
Cdd:PRK03918  392 ELEELEKakeEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCpvcgrelteEHRKELLEEYTAELKRIEKELKEI 471

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169 380 KQRQETIQHQLRTIE-EKKGISGYSYTQEELERVSALKSEVDEMKGRTLDDMSEMVKKLNSLVSEKK---SALAPVIKEL 455
Cdd:PRK03918  472 EEKERKLRKELRELEkVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKgeiKSLKKELEKL 551

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169 456 RQLRQKCQELTQECDEKKAQYDSCAAGLESNRSKLEQEVrglrEECLQEESKYHYTNCMIKNLEVELRRATDEMKayvss 535
Cdd:PRK03918  552 EELKKKLAELEKKLDELEEELAELLKELEELGFESVEEL----EERLKELEPFYNEYLELKDAEKELEREEKELK----- 622

                         490       500       510
                  ....*....|....*....|....*....|..
gi 1306252169 536 DQQEKRKAIREQYTKNITEQENLGKKLREKQK 567
Cdd:PRK03918  623 KLEEELDKAFEELAETEKRLEELRKELEELEK 654
PTZ00121 PTZ00121
MAEBL; Provisional
 114-595 8.62e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.90  E-value: 8.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  114 EIRRdisAMEEEKDQLMKRVERLKK-----RVETVQNHQRMLKIARQLRVE--KEREEFLAQQKQEQKNQLFHAVQRLQR 186
Cdd:PTZ00121  1186 EVRK---AEELRKAEDARKAEAARKaeeerKAEEARKAEDAKKAEAVKKAEeaKKDAEEAKKAEEERNNEEIRKFEEARM 1262

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  187 VQNQLKSMRHAAADAKPESLMKRLEEEIKFNSYMVTEKFPKELESKKKElhflqkvvsepamghsdllELETKVNEVNTE 266
Cdd:PTZ00121  1263 AHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKA-------------------EEAKKADEAKKK 1323

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  267 InqliEKKMMRNEPIEGKLSLYRQQASIISRKKEAKAEELQETKEK--LASLEREVLVKTNQTREFDGTEVLKGDEFKRY 344
Cdd:PTZ00121  1324 A----EEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKaeAAEKKKEEAKKKADAAKKKAEEKKKADEAKKK 1399

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  345 VSKLRSKSTVFKKKHQI---IAEFKAEFGLLQRTEELLKQRQET--IQHQLRTIEEKKGISGYSYTQEELERVSALKSEV 419
Cdd:PTZ00121  1400 AEEDKKKADELKKAAAAkkkADEAKKKAEEKKKADEAKKKAEEAkkADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKA 1479

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  420 DEM-KGRTLDDMSEMVKK----LNSLVSEKKSA----LAPVIKELRQLRqKCQELTQECDEKKAQYDSCAAGL-ESNRSK 489
Cdd:PTZ00121  1480 EEAkKADEAKKKAEEAKKkadeAKKAAEAKKKAdeakKAEEAKKADEAK-KAEEAKKADEAKKAEEKKKADELkKAEELK 1558

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  490 LEQEVRGLREECLQEESKYHYTNCMIKNLEVELRRATDEMKAYVSSDQQEKRKAIREQYTKNITEQENLGKKLREKQKAV 569
Cdd:PTZ00121  1559 KAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQL 1638

                          490       500
                   ....*....|....*....|....*.
gi 1306252169  570 RESHGPNMKQAKMWRDLEQLMECKKQ 595
Cdd:PTZ00121  1639 KKKEAEEKKKAEELKKAEEENKIKAA 1664
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 297-566 1.41e-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: 45.06  E-value: 1.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  297 RKKEAKAEELQETKEKLASLErEVLVKTNQTREFDGTEVLKGDEFK---------RYVSKLRSKSTVFKKKHQIIAEFKA 367
Cdd:TIGR02169  170 RKKEKALEELEEVEENIERLD-LIIDEKRQQLERLRREREKAERYQallkekreyEGYELLKEKEALERQKEAIERQLAS 248

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  368 EFGLLQRTEELLKQRQETIQHQLRTIEE------KKGISGYSYTQEELERVSALKSEVD---EMKGRTLDDMSEMVKKLN 438
Cdd:TIGR02169  249 LEEELEKLTEEISELEKRLEEIEQLLEElnkkikDLGEEEQLRVKEKIGELEAEIASLErsiAEKERELEDAEERLAKLE 328

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  439 SLVSEKKSALAPVIKELRQLRQKCQELTQECDEKKAQYDSCAAGLESnrskLEQEVRGLREECLQEESKYHYTNCMIKNL 518
Cdd:TIGR02169  329 AEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEE----VDKEFAETRDELKDYREKLEKLKREINEL 404

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1306252169  519 EVELRRATDEMKAYVS--SDQQEKRKAIREQYTKNITEQENLGKKLREKQ 566
Cdd:TIGR02169  405 KRELDRLQEELQRLSEelADLNAAIAGIEAKINELEEEKEDKALEIKKQE 454
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 257-507 1.43e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.44  E-value: 1.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169 257 ETKVNEVNTEINQLIEKKmmrnEPIEGKLSLYRQQASIISRKKEAKAEELQETKEKLASLEREvlvktnqtrefdgtevl 336
Cdd:COG3883    15 DPQIQAKQKELSELQAEL----EAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAE----------------- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169 337 kgdefkryvsklrskstvfkkkhqiiaefkaefglLQRTEELLKQRQETIQHQLRTIEEKKGISGY-------SYTQEEL 409
Cdd:COG3883    74 -----------------------------------IAEAEAEIEERREELGERARALYRSGGSVSYldvllgsESFSDFL 118

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169 410 ERVSALKSEVDEMKgRTLDDMSEMVKKLNslvsEKKSALAPVIKELRQLRQKCQELTQECDEKKAQYDSCAAGLESNRSK 489
Cdd:COG3883   119 DRLSALSKIADADA-DLLEELKADKAELE----AKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAA 193

                         250
                  ....*....|....*...
gi 1306252169 490 LEQEVRGLREECLQEESK 507
Cdd:COG3883   194 AEAQLAELEAELAAAEAA 211
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 207-499 1.61e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.05  E-value: 1.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  207 MKRLEEEIKFNSYMVTEKfPKELESKKKELHFLQKVVSEPAmghSDLLELETKVNEVNTEINQL---IEKKMMRNEPIEG 283
Cdd:TIGR02168  679 IEELEEKIEELEEKIAEL-EKALAELRKELEELEEELEQLR---KELEELSRQISALRKDLARLeaeVEQLEERIAQLSK 754

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  284 KLSLYRQQASIISRKKEAKAEELQETKEKLASLEREVlvktnqtrefdgtevlkgDEFKRYVSKLRSKSTVFKKKHQiia 363
Cdd:TIGR02168  755 ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQI------------------EQLKEELKALREALDELRAELT--- 813

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  364 EFKAEFGLLQRTEELLKQRQETIQHQLRTIEEKKGIsgysyTQEELERVSA----LKSEVDEMKgRTLDDMSEMVKKLNS 439
Cdd:TIGR02168  814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEE-----LSEDIESLAAeieeLEELIEELE-SELEALLNERASLEE 887

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  440 LVSEKKSALAPVIKELRQLRQKCQELTQECDEKKAQydscAAGLESNRSKLEQEVRGLRE 499
Cdd:TIGR02168  888 ALALLRSELEELSEELRELESKRSELRRELEELREK----LAQLELRLEGLEVRIDNLQE 943
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 113-503 2.13e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 44.66  E-value: 2.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  113 AEIRRDISAMEEEKDQLMKRVERLKKRVETVQNHqrmlkiARQLRVEKEREEFLAQQKQEQKNQLFHAVQRLQRVQNQLK 192
Cdd:TIGR02168  680 EELEEKIEELEEKIAELEKALAELRKELEELEEE------LEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS 753

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  193 SMRhAAADAKPESLMKRLEEEikfnsymvtEKFPKELESKKKELH-FLQKVVSEPAMGHSDLLELETKVNEVNTEINQLI 271
Cdd:TIGR02168  754 KEL-TELEAEIEELEERLEEA---------EEELAEAEAEIEELEaQIEQLKEELKALREALDELRAELTLLNEEAANLR 823

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  272 EK-KMMRNEPIEGKLSLYR--QQASIISRKKEAKAEELQETKEKLASLEREVLVKTNQTREFDGTEVLKGDEFKRYVSKL 348
Cdd:TIGR02168  824 ERlESLERRIAATERRLEDleEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEEL 903

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  349 RSKSTVFKKKHQIIAEFKAEFGLLQRTEELLKQRQETIQHQLRtieekkgiSGYSYTQEE-LERVSALKSEVDEMKGRtl 427
Cdd:TIGR02168  904 RELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLS--------EEYSLTLEEaEALENKIEDDEEEARRR-- 973

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  428 ddmsemVKKLNslvsEKKSALAPV----IKELRQLRQKCQELTQECDEkkaqydscaagLESNRSKLEQEVRGLREECLQ 503
Cdd:TIGR02168  974 ------LKRLE----NKIKELGPVnlaaIEEYEELKERYDFLTAQKED-----------LTEAKETLEEAIEEIDREARE 1032
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
 86-389 3.02e-04

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 43.89  E-value: 3.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169   86 KQYEELMEAFKTLHKEC-EQLKTSGFSTAEIRRDISAMEEEKdqlmkrverlkkrvETVQNHQRMLKIARQLRVEKEREE 164
Cdd:PRK10929    68 KQYQQVIDNFPKLSAELrQQLNNERDEPRSVPPNMSTDALEQ--------------EILQVSSQLLEKSRQAQQEQDRAR 133

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  165 -------FLAQQKQEQKNQLFHAVQRLQ----------RVQNQLKSMRHAAADAKPESL------------MKRLEEEIK 215
Cdd:PRK10929   134 eisdslsQLPQQQTEARRQLNEIERRLQtlgtpntplaQAQLTALQAESAALKALVDELelaqlsannrqeLARLRSELA 213

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  216 FNSYmvtEKFPKELESKKKELHFLQKVVSEPAMGHSDLLEletkvnEVNTEINQLIEKKMMRNEPIEGKLSLYRQQASII 295
Cdd:PRK10929   214 KKRS---QQLDAYLQALRNQLNSQRQREAERALESTELLA------EQSGDLPKSIVAQFKINRELSQALNQQAQRMDLI 284

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  296 SRKKEAKAEELQETKEKLASLeREvlvktnQTREFDGTEVLkGDEFKRYVSKLRSKStvfkkKHQIIAEFKAEFgLLQRT 375
Cdd:PRK10929   285 ASQQRQAASQTLQVRQALNTL-RE------QSQWLGVSNAL-GEALRAQVARLPEMP-----KPQQLDTEMAQL-RVQRL 350

                          330
                   ....*....|....*..
gi 1306252169  376 --EELL-KQRQETIQHQ 389
Cdd:PRK10929   351 ryEDLLnKQPQLRQIRQ 367
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 77-591 6.28e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.12  E-value: 6.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169   77 QDETVADTNKQYEELMEAFKTLHKECEQLKtSGFSTAE-----IRRDISAMEEEKDQLMKRVERLKKRVE-TVQNHQRML 150
Cdd:TIGR02168  342 LEEKLEELKEELESLEAELEELEAELEELE-SRLEELEeqletLRSKVAQLELQIASLNNEIERLEARLErLEDRRERLQ 420

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  151 KIARQLRVEKEREEFLAQQKQ--EQKNQLFHAVQRLQRVQNQLKSMRHAAADAKPESLMKRLEEEIKFNSYMVTEKFPKE 228
Cdd:TIGR02168  421 QEIEELLKKLEEAELKELQAEleELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQEN 500

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  229 LESKKKELHFLQKVVSEPAMGHSDLLELETKVNEVNTEINQLIEKKMmrNEPIEGKLSLYRQQASIISRKKEAKA---EE 305
Cdd:TIGR02168  501 LEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRL--QAVVVENLNAAKKAIAFLKQNELGRVtflPL 578

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  306 LQETKEKLASLEREVLVKTNQTREFDGTEVLKGDEFKRYVS--------------------KLRSKSTVFKKKHQII--- 362
Cdd:TIGR02168  579 DSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSyllggvlvvddldnalelakKLRPGYRIVTLDGDLVrpg 658

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  363 -----AEFKAEFGLLQRTEELLKQRQETIQHQLRTIEEKKGISGYSYTQEELERVSALKSEVDEMKGRTLDDMSEMVKKL 437
Cdd:TIGR02168  659 gvitgGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARL 738

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  438 ----------NSLVSEKKSALAPVIKELRQLRQKCQELTQECDEKKAQYDSCAAGLESNRSKLEQEVRGLREECLQEESK 507
Cdd:TIGR02168  739 eaeveqleerIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEE 818

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  508 YHYTNCMIKNLEVELRRATDEMKayVSSDQQEKRKAIREQYTKNITEQENLGKKLREKQKAV---RESHGPNMKQAKmwR 584
Cdd:TIGR02168  819 AANLRERLESLERRIAATERRLE--DLEEQIEELSEDIESLAAEIEELEELIEELESELEALlneRASLEEALALLR--S 894


                   ....*..
gi 1306252169  585 DLEQLME 591
Cdd:TIGR02168  895 ELEELSE 901
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 78-319 1.15e-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: 41.98  E-value: 1.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169   78 DETVADTNKQYEELMEAFKTLHKECEQL---------KTSGFSTAEIRRDISAMEEEKDQLMKRVERLKKRVETVQNHQ- 147
Cdd:TIGR02169  257 TEEISELEKRLEEIEQLLEELNKKIKDLgeeeqlrvkEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLa 336

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  148 RMLKIARQLRVEKEREEFLAQQKQEQKNQLFHAVQRLQRVqnqlkSMRHAAADAKPESLMKRLEeeikfnsyMVTEKFPK 227
Cdd:TIGR02169  337 EIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEV-----DKEFAETRDELKDYREKLE--------KLKREINE 403

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  228 ELESKKKELHFLQKVVSEPAMGHSDLLELETKVNEVNTEINQLIEKKmmrnEPIEGKLSLYRQQASIISRKKEAKAEELQ 307
Cdd:TIGR02169  404 LKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEI----KKQEWKLEQLAADLSKYEQELYDLKEEYD 479

                          250
                   ....*....|..
gi 1306252169  308 ETKEKLASLERE 319
Cdd:TIGR02169  480 RVEKELSKLQRE 491
PTZ00121 PTZ00121
MAEBL; Provisional
 123-588 1.63e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 1.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  123 EEEKDQLMKRVERLKkRVETVQNHQRMLKIARQLRVEKEREEFLAQQKQE-QKNQLFHAVQRLQRVQNQLKS--MRHAAA 199
Cdd:PTZ00121  1114 ARKAEEAKKKAEDAR-KAEEARKAEDARKAEEARKAEDAKRVEIARKAEDaRKAEEARKAEDAKKAEAARKAeeVRKAEE 1192

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  200 DAKPESlMKRLEEEIKFNSYMVTEKFPKELESKKKElhflqkVVSEPAMGHSDLLELETKVNEVNTEINQLIEKKMMRNe 279
Cdd:PTZ00121  1193 LRKAED-ARKAEAARKAEEERKAEEARKAEDAKKAE------AVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAH- 1264

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  280 piegklsLYRQQASIISRKKEaKAEELQ--ETKEKLASLEREVLVKTNQTREFDGTEVLKGDEFKRYVSKLRSKSTVFKK 357
Cdd:PTZ00121  1265 -------FARRQAAIKAEEAR-KADELKkaEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKK 1336

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  358 KHQiIAEFKAEFGLLQ---RTEELLKQRQETIQHQLRTIEEKKGISGYSYTQEELERVSALKSEVDEMKGRTLDDMSEMV 434
Cdd:PTZ00121  1337 KAE-EAKKAAEAAKAEaeaAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAA 1415

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  435 KKLNSLVSEKKSALAPVIKELR---QLRQKCQELTQECDEKKAQYDSCAAGLESNRSkleQEVRGLREECLQEESKYHYT 511
Cdd:PTZ00121  1416 AKKKADEAKKKAEEKKKADEAKkkaEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKA---DEAKKKAEEAKKADEAKKKA 1492

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1306252169  512 NCMIKNLEVELRRATDEMKAYVSSDQQEKRKAIREQYTKNITEQENLgKKLREKQKAVRESHGPNMKQAKMWRDLEQ 588
Cdd:PTZ00121  1493 EEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEA-KKAEEKKKADELKKAEELKKAEEKKKAEE 1568
Nup88 pfam10168
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ...
 118-268 2.08e-03

Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.


Pssm-ID: 462975 [Multi-domain]  Cd Length: 713  Bit Score: 41.18  E-value: 2.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169 118 DISAMEEEKDQLMKRVERLKKRVETVQNHQ-----RMLKIARQLR------VEKEREEflaqqKQEqknqlfhavqrLQR 186
Cdd:pfam10168 576 ELQSLEEERKSLSERAEKLAEKYEEIKDKQeklmrRCKKVLQRLNsqlpvlSDAEREM-----KKE-----------LET 639

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169 187 VQNQLKSMRHAAADAKpeslMKRLEEEIKFNSYMVTEKfPKELESKKKELHFLQKVVSEpaMGhSDLLELETKVNEVNTE 266
Cdd:pfam10168 640 INEQLKHLANAIKQAK----KKMNYQRYQIAKSQSIRK-KSSLSLSEKQRKTIKEILKQ--LG-SEIDELIKQVKDINKH 711


                  ..
gi 1306252169 267 IN 268
Cdd:pfam10168 712 VG 713
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
48-215 4.04e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 4.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169   48 WLLQRSNElKKRAYLARFLIKLEvpSEFLQDETVADTNKQYEELMEAFKTLHKECEQLKTSGFSTAEIRRDISAMEEEKD 127
Cdd:COG4913    602 YVLGFDNR-AKLAALEAELAELE--EELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELE 678

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  128 QLM----------KRVERLKKRVETVQNHQRMLKIARQlRVEKEREEFLAQQKQEQKNQLFHAVQRLQRVQNQLKSMRHA 197
Cdd:COG4913    679 RLDassddlaaleEQLEELEAELEELEEELDELKGEIG-RLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAA 757

                          170
                   ....*....|....*....
gi 1306252169  198 AA-DAKPESLMKRLEEEIK 215
Cdd:COG4913    758 ALgDAVERELRENLEERID 776
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
362-568 4.59e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 4.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  362 IAEFKAEFGLLQRTEELLKQRQETIQHQLRTIEEKkgisgysytQEELERVSALKSEvdemkgrtLDDMSEMVKKLNSLV 441
Cdd:COG4913    612 LAALEAELAELEEELAEAEERLEALEAELDALQER---------REALQRLAEYSWD--------EIDVASAEREIAELE 674

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  442 SEKKSALA--PVIKELRQLRQKCQELTQECDEKKAQydscaagLESNRSKLEQEVRGLREECLQEESKYHYtncMIKNLE 519
Cdd:COG4913    675 AELERLDAssDDLAALEEQLEELEAELEELEEELDE-------LKGEIGRLEKELEQAEEELDELQDRLEA---AEDLAR 744

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1306252169  520 VELRRATDEMKAYVSSDQQEK--RKAIREQYTKNITEQENLGKKLREKQKA 568
Cdd:COG4913    745 LELRALLEERFAAALGDAVERelRENLEERIDALRARLNRAEEELERAMRA 795
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
79-500 5.24e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 5.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  79 ETVADTNKQYEELMEAFKTLHKECEQLKTSGfSTAEIRRDISAMEEEKDQLMKRVERLKKRVETVQNHQRMLKIARQ--L 156
Cdd:COG4717    95 EELEELEEELEELEAELEELREELEKLEKLL-QLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAelA 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169 157 RVEKEREEFLAQQKQEQKNQLFHAVQRLQRVQNQLKSMRHAAADAKPEslMKRLEEEIKFNSYMVTEKFPKELESKKKEL 236
Cdd:COG4717   174 ELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEE--LEELEEELEQLENELEAAALEERLKEARLL 251

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169 237 HFLQKVVSEPAMGHSDLLELETKVNEVNTEINQLIekkmmrnepIEGKLSLYRQQASIISRKKEAKAEELQE--TKEKLA 314
Cdd:COG4717   252 LLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLL---------ALLFLLLAREKASLGKEAEELQALPALEelEEEELE 322

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169 315 SLEREVLVKTNQTREFDGTEVLKGDEFKRYVSKLRSK------STVFKKKHQIIAEFKAE-----FGLLQRTEEL--LKQ 381
Cdd:COG4717   323 ELLAALGLPPDLSPEELLELLDRIEELQELLREAEELeeelqlEELEQEIAALLAEAGVEdeeelRAALEQAEEYqeLKE 402

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169 382 RQETIQHQLRTIEEKKGISGYSYTQEEL-ERVSALKSEVDEMKGRtLDDMSEMVKKLNSLVSEKKSAlapviKELRQLRQ 460
Cdd:COG4717   403 ELEELEEQLEELLGELEELLEALDEEELeEELEELEEELEELEEE-LEELREELAELEAELEQLEED-----GELAELLQ 476

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 1306252169 461 KCQELTQECDEKKAQYDSCAAGLEsnrsKLEQEVRGLREE 500
Cdd:COG4717   477 ELEELKAELRELAEEWAALKLALE----LLEEAREEYREE 512
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 265-578 5.76e-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: 5.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  265 TEINQLIEKKMMRNEPIEGKLSLYRQQASIISRKKEAKAEELQETKEKLASLEREVLVKTnqtrefdgtevlkgDEFKRY 344
Cdd:TIGR02169  698 RRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVK--------------SELKEL 763

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  345 VSKLRSKSTVfkkkhqiIAEFKAEFGLLQRteELLKQRQETIQHQLRTIEekkgisgysytqEELERVSALKSEVD-EMK 423
Cdd:TIGR02169  764 EARIEELEED-------LHKLEEALNDLEA--RLSHSRIPEIQAELSKLE------------EEVSRIEARLREIEqKLN 822

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  424 GRTLDD--MSEMVKKLNSLVSEKKSALAPVIKELRQLRQKCQELTQECDEKKA---QYDSCAAGLESNRSKLEQEVRGLR 498
Cdd:TIGR02169  823 RLTLEKeyLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAalrDLESRLGDLKKERDELEAQLRELE 902

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  499 EECLQEESKYHYTNCMIKNLEVELRRATDEMKAYvssdqqEKRKAIREQYTKNITEQENLGKKLREKQKAVRESHGPNMK 578
Cdd:TIGR02169  903 RKIEELEAQIEKKRKRLSELKAKLEALEEELSEI------EDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNML 976
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 78-329 1.00e-02

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.15  E-value: 1.00e-02
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169  78 DETVADTNKQYEELMEAFKTLHKECEQLKTSgfsTAEIRRDISAMEEEKDQLMKRVERLKKRVEtvqnhqrmlKIARQLR 157
Cdd:COG1196   238 EAELEELEAELEELEAELEELEAELAELEAE---LEELRLELEELELELEEAQAEEYELLAELA---------RLEQDIA 305

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169 158 VEKEREEFLAQQKQEQKNQLFHAVQRLQRVQNQLKSMRHAAADAKPESLMKRLEEEIKFNSYMVTEkfpKELESKKKELH 237
Cdd:COG1196   306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE---AELAEAEEELE 382

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306252169 238 FLQKVVSEPAMGHSDLLELETKVNEVNTEINQLIEKKMMRNEPIEGKLSLYRQQASIISRKKEAKAEELQETKEKLASLE 317
Cdd:COG1196   383 ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462

                         250
                  ....*....|..
gi 1306252169 318 REVLVKTNQTRE 329
Cdd:COG1196   463 ELLAELLEEAAL 474
 
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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