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Conserved domains on  [gi|1958797847|ref|XP_038938030|]
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angiomotin-like protein 2 isoform X2 [Rattus norvegicus]

Protein Classification

Smc and Angiomotin_C domain-containing protein( domain architecture ID 10573751)

Smc and Angiomotin_C domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Angiomotin_C pfam12240
Angiomotin C terminal; This domain family is found in eukaryotes, and is typically between 197 ...
 477-679 5.10e-96

Angiomotin C terminal; This domain family is found in eukaryotes, and is typically between 197 and 211 amino acids in length. This family is the C terminal region of angiomotin. Angiomotin regulates the action of angiogenesis inhibitor angiostatin. The C terminal region of angiomotin appears to be involved in directing the protein chemotactically.


:

Pssm-ID: 463503 [Multi-domain]  Cd Length: 200  Bit Score: 296.68  E-value: 5.10e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847 477 YVEKVERLQQALGQLQAACEKREQLELRLRTRLEQELKALRAQQRQTGTLTGGGGshtgstELSALRLSEQLREKEEQIL 556
Cdd:pfam12240   1 YVEKVERLQQALAQLQAACEKREQLELRLRTRLEQELKSLRAQQRQGGSQGSGPS------EYSAPALMELLREKEERIL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847 557 ALEADMTKWEQKYLEERAMRQFAMDAAATAAAQRDTTLIRHSPQPSPSSSFNEGLLAGNHRHQEMESRLKVLHAQILEKD 636
Cdd:pfam12240  75 ALEADMTKWEQKYLEESTMRQFAMDAAATAAAQRDTTIINHSPRHSYDSSFNEELLLANRRCQEMENRIKNLHAQILEKD 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1958797847 637 AVIKVLQQRSRKDPGKATQGTLRPAKSVPSIFAAAVGTQGWQG 679
Cdd:pfam12240 155 AMIKVLQQRSRKDPGKTDQQSLRPARSVPSISAAATGLHSRQT 197
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 307-577 9.31e-12

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 68.81  E-value: 9.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847 307 AQMESVLRENARLQRDNERLQRELESTSEKascIEKLENEIQRLSEAHESLmrtsSKREALEKTMRNKMDSEMRRLQDFN 386
Cdd:COG1196   239 AELEELEAELEELEAELEELEAELAELEAE---LEELRLELEELELELEEA----QAEEYELLAELARLEQDIARLEERR 311

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847 387 RDLRERLESANRHLASKTQEAQAGSQDMVAKLLAQSYEQQQEQEKLEREMALLRGAIEDQRRRAELLEQALgNAQSRAAR 466
Cdd:COG1196   312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE-ELAEELLE 390

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847 467 AEEELRKKQAYVEKVERLQQALGQLQAACEKREQLELRLRTRLEQELKALRAQQRQTGTLTGGGGSHTGSTELSALRLSE 546
Cdd:COG1196   391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1958797847 547 QLREKEEQILALEADMTKWEQKYLEERAMRQ 577
Cdd:COG1196   471 EAALLEAALAELLEELAEAAARLLLLLEAEA 501
 
Name Accession Description Interval E-value
Angiomotin_C pfam12240
Angiomotin C terminal; This domain family is found in eukaryotes, and is typically between 197 ...
 477-679 5.10e-96

Angiomotin C terminal; This domain family is found in eukaryotes, and is typically between 197 and 211 amino acids in length. This family is the C terminal region of angiomotin. Angiomotin regulates the action of angiogenesis inhibitor angiostatin. The C terminal region of angiomotin appears to be involved in directing the protein chemotactically.


Pssm-ID: 463503 [Multi-domain]  Cd Length: 200  Bit Score: 296.68  E-value: 5.10e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847 477 YVEKVERLQQALGQLQAACEKREQLELRLRTRLEQELKALRAQQRQTGTLTGGGGshtgstELSALRLSEQLREKEEQIL 556
Cdd:pfam12240   1 YVEKVERLQQALAQLQAACEKREQLELRLRTRLEQELKSLRAQQRQGGSQGSGPS------EYSAPALMELLREKEERIL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847 557 ALEADMTKWEQKYLEERAMRQFAMDAAATAAAQRDTTLIRHSPQPSPSSSFNEGLLAGNHRHQEMESRLKVLHAQILEKD 636
Cdd:pfam12240  75 ALEADMTKWEQKYLEESTMRQFAMDAAATAAAQRDTTIINHSPRHSYDSSFNEELLLANRRCQEMENRIKNLHAQILEKD 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1958797847 637 AVIKVLQQRSRKDPGKATQGTLRPAKSVPSIFAAAVGTQGWQG 679
Cdd:pfam12240 155 AMIKVLQQRSRKDPGKTDQQSLRPARSVPSISAAATGLHSRQT 197
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 307-577 9.31e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 68.81  E-value: 9.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847 307 AQMESVLRENARLQRDNERLQRELESTSEKascIEKLENEIQRLSEAHESLmrtsSKREALEKTMRNKMDSEMRRLQDFN 386
Cdd:COG1196   239 AELEELEAELEELEAELEELEAELAELEAE---LEELRLELEELELELEEA----QAEEYELLAELARLEQDIARLEERR 311

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847 387 RDLRERLESANRHLASKTQEAQAGSQDMVAKLLAQSYEQQQEQEKLEREMALLRGAIEDQRRRAELLEQALgNAQSRAAR 466
Cdd:COG1196   312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE-ELAEELLE 390

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847 467 AEEELRKKQAYVEKVERLQQALGQLQAACEKREQLELRLRTRLEQELKALRAQQRQTGTLTGGGGSHTGSTELSALRLSE 546
Cdd:COG1196   391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1958797847 547 QLREKEEQILALEADMTKWEQKYLEERAMRQ 577
Cdd:COG1196   471 EAALLEAALAELLEELAEAAARLLLLLEAEA 501
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 307-574 4.86e-08

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: 57.00  E-value: 4.86e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847  307 AQMESVLRENARLQRDNERLQRELESTSEKascIEKLENEIQRLSEAHESLMRTSSK-REALEKTMRN-------KMDSE 378
Cdd:TIGR02169  723 KEIEQLEQEEEKLKERLEELEEDLSSLEQE---IENVKSELKELEARIEELEEDLHKlEEALNDLEARlshsripEIQAE 799

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847  379 MRRLQDFNRDLRERLESANRHLASKTQEAQAgSQDMVAKLLAQSYEQQQEQEKLEREMALLRGAIEDQRRRAELLEQALG 458
Cdd:TIGR02169  800 LSKLEEEVSRIEARLREIEQKLNRLTLEKEY-LEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALR 878

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847  459 NAQSRAARAEEELRKKQAyveKVERLQQALGQLQAACEKREQLELRLRTRLE---QELKALRAQQRQTGTLTGGggshtg 535
Cdd:TIGR02169  879 DLESRLGDLKKERDELEA---QLRELERKIEELEAQIEKKRKRLSELKAKLEaleEELSEIEDPKGEDEEIPEE------ 949

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1958797847  536 stELSALRLSEQLREKEEQILALEADMTKWEQKYLEERA 574
Cdd:TIGR02169  950 --ELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLK 986
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 442-645 1.78e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.94  E-value: 1.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847 442 AIEDQRRRAELLEQALGNAQSRAARAEEELRKKQAYVEKVERLQQALGQLQAACEKREQLELRLRTRLEQELKALRAQQR 521
Cdd:COG1196   233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847 522 QTGTLTGGGGSHTGSTELSALRLSEQLREKEEQILALEADMTKWEQKYLEERAMRQFAMDAAATAAAQRDTTLIRHSPQP 601
Cdd:COG1196   313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1958797847 602 SPSSSFNEGLLAGNHRHQEMESRLKVLHAQILEKDAVIKVLQQR 645
Cdd:COG1196   393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE 436
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 440-648 2.82e-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: 47.74  E-value: 2.82e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847  440 RGAIEDQRRRAELLEQALGNAQSRAARAEEELRKKQAYVEKVERLQQALGQLQAACEKREQLELRLRTRLEQELKALRAQ 519
Cdd:TIGR02168  683 EEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE 762

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847  520 QRQTGTLTGGGGSHTGSTELSALRLSEQLREKEEQILALEADMTKWEQKYLEERAMRQFAMDAAATAAAQRDTTLIRHSP 599
Cdd:TIGR02168  763 IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLED 842

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1958797847  600 QPSPSSSFNEGLLAGNHRHQEMESRLKVLHAQILEKDAVIKVLQQRSRK 648
Cdd:TIGR02168  843 LEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALAL 891
PTZ00121 PTZ00121
MAEBL; Provisional
 304-572 2.99e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 2.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847  304 AHLAQMESVLRENARLQRDNERLQRELESTSEKASCIEKL-ENEIQRLSEAheslmrtSSKREALEKTMRNKMDSEMRRL 382
Cdd:PTZ00121  1064 AHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAkKTETGKAEEA-------RKAEEAKKKAEDARKAEEARKA 1136

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847  383 QDFNR--DLRERLESANRHLASKTQEAQAGSQDMVAKllaqsyeqqqeqekLEREMALLRGAIEdqRRRAELLEQALGNA 460
Cdd:PTZ00121  1137 EDARKaeEARKAEDAKRVEIARKAEDARKAEEARKAE--------------DAKKAEAARKAEE--VRKAEELRKAEDAR 1200

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847  461 QSRAARAEEELRK--------KQAYVEKVERLQQALGQLQAAcEKREQLELRLRTRLEQELKALRAQQRQTGTLTGGGGS 532
Cdd:PTZ00121  1201 KAEAARKAEEERKaeearkaeDAKKAEAVKKAEEAKKDAEEA-KKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARK 1279

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1958797847  533 HTGSTELSALRLSEQLREKEEQILALEADMTKWEQKYLEE 572
Cdd:PTZ00121  1280 ADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADE 1319
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 306-508 8.11e-04

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 42.80  E-value: 8.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847 306 LAQMESVLRENARLQ----RDNERLQRELEStsekASCIEKLENEIQRLSEAHESLMRT--SSKREALEKTMRNKMDSEM 379
Cdd:pfam17380 370 IAMEISRMRELERLQmerqQKNERVRQELEA----ARKVKILEEERQRKIQQQKVEMEQirAEQEEARQREVRRLEEERA 445

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847 380 RRLQDFNRDLRERLESANRhLASKTQEAQAGSQDMVAKLLAQSYEQQQEQEKLEREMALLRGAIEDQRRRAELLEQALGN 459
Cdd:pfam17380 446 REMERVRLEEQERQQQVER-LRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEE 524

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958797847 460 AQSRAA-----RAEEELRKKQAYVEKVERLQQalgQLQAACEKREQLELRLRTR 508
Cdd:pfam17380 525 RQKAIYeeerrREAEEERRKQQEMEERRRIQE---QMRKATEERSRLEAMERER 575
 
Name Accession Description Interval E-value
Angiomotin_C pfam12240
Angiomotin C terminal; This domain family is found in eukaryotes, and is typically between 197 ...
 477-679 5.10e-96

Angiomotin C terminal; This domain family is found in eukaryotes, and is typically between 197 and 211 amino acids in length. This family is the C terminal region of angiomotin. Angiomotin regulates the action of angiogenesis inhibitor angiostatin. The C terminal region of angiomotin appears to be involved in directing the protein chemotactically.


Pssm-ID: 463503 [Multi-domain]  Cd Length: 200  Bit Score: 296.68  E-value: 5.10e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847 477 YVEKVERLQQALGQLQAACEKREQLELRLRTRLEQELKALRAQQRQTGTLTGGGGshtgstELSALRLSEQLREKEEQIL 556
Cdd:pfam12240   1 YVEKVERLQQALAQLQAACEKREQLELRLRTRLEQELKSLRAQQRQGGSQGSGPS------EYSAPALMELLREKEERIL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847 557 ALEADMTKWEQKYLEERAMRQFAMDAAATAAAQRDTTLIRHSPQPSPSSSFNEGLLAGNHRHQEMESRLKVLHAQILEKD 636
Cdd:pfam12240  75 ALEADMTKWEQKYLEESTMRQFAMDAAATAAAQRDTTIINHSPRHSYDSSFNEELLLANRRCQEMENRIKNLHAQILEKD 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1958797847 637 AVIKVLQQRSRKDPGKATQGTLRPAKSVPSIFAAAVGTQGWQG 679
Cdd:pfam12240 155 AMIKVLQQRSRKDPGKTDQQSLRPARSVPSISAAATGLHSRQT 197
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 307-577 9.31e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 68.81  E-value: 9.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847 307 AQMESVLRENARLQRDNERLQRELESTSEKascIEKLENEIQRLSEAHESLmrtsSKREALEKTMRNKMDSEMRRLQDFN 386
Cdd:COG1196   239 AELEELEAELEELEAELEELEAELAELEAE---LEELRLELEELELELEEA----QAEEYELLAELARLEQDIARLEERR 311

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847 387 RDLRERLESANRHLASKTQEAQAGSQDMVAKLLAQSYEQQQEQEKLEREMALLRGAIEDQRRRAELLEQALgNAQSRAAR 466
Cdd:COG1196   312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE-ELAEELLE 390

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847 467 AEEELRKKQAYVEKVERLQQALGQLQAACEKREQLELRLRTRLEQELKALRAQQRQTGTLTGGGGSHTGSTELSALRLSE 546
Cdd:COG1196   391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1958797847 547 QLREKEEQILALEADMTKWEQKYLEERAMRQ 577
Cdd:COG1196   471 EAALLEAALAELLEELAEAAARLLLLLEAEA 501
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 313-577 3.49e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 60.34  E-value: 3.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847 313 LRENARlQRDNERLQRELESTSEKascIEKLENEIQRLSEAHESLMRTSSKREALEKTMRNKMDSEMRRLQDFNRDLRER 392
Cdd:COG1196   218 LKEELK-ELEAELLLLKLRELEAE---LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL 293

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847 393 LESANRHLASKTQEAQagsqdmvakllaqsyeqqqeqekleREMALLRGAIEDQRRRAELLEQALGNAQSRAARAEEELR 472
Cdd:COG1196   294 LAELARLEQDIARLEE-------------------------RRRELEERLEELEEELAELEEELEELEEELEELEEELEE 348

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847 473 KKQAYVEKVERLQQALGQLQAACEKREQLELRLRTRLEQELKALRAQQRQTGTLTGGGGSHTGSTELSAlRLSEQLREKE 552
Cdd:COG1196   349 AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE-RLEEELEELE 427

                         250       260
                  ....*....|....*....|....*
gi 1958797847 553 EQILALEADMTKWEQKYLEERAMRQ 577
Cdd:COG1196   428 EALAELEEEEEEEEEALEEAAEEEA 452
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 307-574 4.86e-08

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: 57.00  E-value: 4.86e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847  307 AQMESVLRENARLQRDNERLQRELESTSEKascIEKLENEIQRLSEAHESLMRTSSK-REALEKTMRN-------KMDSE 378
Cdd:TIGR02169  723 KEIEQLEQEEEKLKERLEELEEDLSSLEQE---IENVKSELKELEARIEELEEDLHKlEEALNDLEARlshsripEIQAE 799

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847  379 MRRLQDFNRDLRERLESANRHLASKTQEAQAgSQDMVAKLLAQSYEQQQEQEKLEREMALLRGAIEDQRRRAELLEQALG 458
Cdd:TIGR02169  800 LSKLEEEVSRIEARLREIEQKLNRLTLEKEY-LEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALR 878

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847  459 NAQSRAARAEEELRKKQAyveKVERLQQALGQLQAACEKREQLELRLRTRLE---QELKALRAQQRQTGTLTGGggshtg 535
Cdd:TIGR02169  879 DLESRLGDLKKERDELEA---QLRELERKIEELEAQIEKKRKRLSELKAKLEaleEELSEIEDPKGEDEEIPEE------ 949

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1958797847  536 stELSALRLSEQLREKEEQILALEADMTKWEQKYLEERA 574
Cdd:TIGR02169  950 --ELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLK 986
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 307-568 6.45e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 56.60  E-value: 6.45e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847  307 AQMESVLRENARLQRDNERLQRELESTSEKASCIEKLENEIQR-LSEAHESLMRTSSKREALEKTMRNkMDSEMRRLQDF 385
Cdd:TIGR02168  684 EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRqISALRKDLARLEAEVEQLEERIAQ-LSKELTELEAE 762

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847  386 NRDLRERLESANRHLASKTQEAQAGSQDmVAKLLAQSYEQQQEQEKLEREMALLRGAIEDQRRRAELLEQALGNAQSRAA 465
Cdd:TIGR02168  763 IEELEERLEEAEEELAEAEAEIEELEAQ-IEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE 841

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847  466 RAEEELRKKQayvEKVERLQQALGQLQAACEK-REQLE--LRLRTRLEQELKALRAQQRQtgtltggGGSHTGSTELSAL 542
Cdd:TIGR02168  842 DLEEQIEELS---EDIESLAAEIEELEELIEElESELEalLNERASLEEALALLRSELEE-------LSEELRELESKRS 911

                          250       260
                   ....*....|....*....|....*.
gi 1958797847  543 RLSEQLREKEEQILALEADMTKWEQK 568
Cdd:TIGR02168  912 ELRRELEELREKLAQLELRLEGLEVR 937
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 442-645 1.78e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.94  E-value: 1.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847 442 AIEDQRRRAELLEQALGNAQSRAARAEEELRKKQAYVEKVERLQQALGQLQAACEKREQLELRLRTRLEQELKALRAQQR 521
Cdd:COG1196   233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847 522 QTGTLTGGGGSHTGSTELSALRLSEQLREKEEQILALEADMTKWEQKYLEERAMRQFAMDAAATAAAQRDTTLIRHSPQP 601
Cdd:COG1196   313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1958797847 602 SPSSSFNEGLLAGNHRHQEMESRLKVLHAQILEKDAVIKVLQQR 645
Cdd:COG1196   393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE 436
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 315-560 2.31e-07

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: 54.69  E-value: 2.31e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847  315 ENARLQRDNERLQRELESTSEKASCIEKLENEI-QRLSEAHESLMRTSSKREALEKTmRNKMDSEMRRLQDFNRDLRERL 393
Cdd:TIGR02169  675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELsQELSDASRKIGEIEKEIEQLEQE-EEKLKERLEELEEDLSSLEQEI 753

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847  394 ESANRHLASKTQEAQAGSQDMVAKLLAQSYEQQQEQEKLEREMALLRGAIEDQRRRAEL----LEQALGNAQSRAARAEE 469
Cdd:TIGR02169  754 ENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEArlreIEQKLNRLTLEKEYLEK 833

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847  470 ELRKKQAYV-----------EKVERLQQALGQLQAACEKREQLELRLRTR---LEQELKALRAQQRQTGTLTGGGGSHTG 535
Cdd:TIGR02169  834 EIQELQEQRidlkeqiksieKEIENLNGKKEELEEELEELEAALRDLESRlgdLKKERDELEAQLRELERKIEELEAQIE 913

                          250       260
                   ....*....|....*....|....*
gi 1958797847  536 STELSALRLSEQLREKEEQILALEA 560
Cdd:TIGR02169  914 KKRKRLSELKAKLEALEEELSEIED 938
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 302-522 4.27e-06

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: 49.76  E-value: 4.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847 302 GSAHLAQMESVLRENARLQRDNERLQRELESTSEKASCIEKLENEIQRLSEAhesLMRTSSKREALEKTMrNKMDSEMRR 381
Cdd:COG4942    12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR---IAALARRIRALEQEL-AALEAELAE 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847 382 LQDFNRDLRERLESANRHLASKTQEAQAGSQDMVAKLLAqsyeQQQEQEKLEREMALLRGAIEDQRRRAELLEQALGNAQ 461
Cdd:COG4942    88 LEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLL----SPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELA 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958797847 462 SRAARAEEELRKKQAYVEKVERLQQALGQLQAaceKREQLELRLRTRLEQELKALRAQQRQ 522
Cdd:COG4942   164 ALRAELEAERAELEALLAELEEERAALEALKA---ERQKLLARLEKELAELAAELAELQQE 221
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 311-575 4.69e-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: 50.44  E-value: 4.69e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847  311 SVLRENARLQRDNErlqrelestsekascIEKLENEIQRL-SEAHESLMRTSSKREALEkTMRNKMDSEMRRLQDFNRDL 389
Cdd:TIGR02168  665 SAKTNSSILERRRE---------------IEELEEKIEELeEKIAELEKALAELRKELE-ELEEELEQLRKELEELSRQI 728

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847  390 RERLESANRHLASKTQEAQAGSQ--DMVAKLLAQSYEQQQEQEKLEREMALLRGAIEDQRRRAELLEQALGNAQSRAARA 467
Cdd:TIGR02168  729 SALRKDLARLEAEVEQLEERIAQlsKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL 808

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847  468 EEELRK-KQAYVEKVERLQQALGQLQAACEKREQLELRLR------TRLEQELKALRAQQRQTGTLTGGGGSHTGSTELS 540
Cdd:TIGR02168  809 RAELTLlNEEAANLRERLESLERRIAATERRLEDLEEQIEelsediESLAAEIEELEELIEELESELEALLNERASLEEA 888

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1958797847  541 ALRLSEQLREKEEQILALEADMTKWEQKYLEERAM 575
Cdd:TIGR02168  889 LALLRSELEELSEELRELESKRSELRRELEELREK 923
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 440-648 2.82e-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: 47.74  E-value: 2.82e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847  440 RGAIEDQRRRAELLEQALGNAQSRAARAEEELRKKQAYVEKVERLQQALGQLQAACEKREQLELRLRTRLEQELKALRAQ 519
Cdd:TIGR02168  683 EEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE 762

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847  520 QRQTGTLTGGGGSHTGSTELSALRLSEQLREKEEQILALEADMTKWEQKYLEERAMRQFAMDAAATAAAQRDTTLIRHSP 599
Cdd:TIGR02168  763 IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLED 842

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1958797847  600 QPSPSSSFNEGLLAGNHRHQEMESRLKVLHAQILEKDAVIKVLQQRSRK 648
Cdd:TIGR02168  843 LEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALAL 891
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
445-573 3.89e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.22  E-value: 3.89e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847  445 DQRRRAELLEQALGNAQSRAARAEEELRKKQAYVEKVERLQQALGQLQ----------AACEKREQLELRLR-------- 506
Cdd:COG4913    607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAeyswdeidvaSAEREIAELEAELErldassdd 686

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958797847  507 -TRLEQELKALRAQQRQTGTLTGGGGSHTGSTELSALRLSEQLREKEEQILALEADMTKWEQKYLEER 573
Cdd:COG4913    687 lAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEER 754
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
287-401 1.60e-04

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 45.23  E-value: 1.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847 287 SPPALEGPPGAQATSGSAHLAQMESVLREN----ARLQRDNERLQRELEstsEKASCIEKLENEIqrlseaheSLMRTSS 362
Cdd:COG2433   389 ELPEEEPEAEREKEHEERELTEEEEEIRRLeeqvERLEAEVEELEAELE---EKDERIERLEREL--------SEARSEE 457

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1958797847 363 KREALEKTMRNKMDSEMRRLQDFNRDLRERLESANRHLA 401
Cdd:COG2433   458 RREIRKDREISRLDREIERLERELEEERERIEELKRKLE 496
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 306-576 1.62e-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: 45.44  E-value: 1.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847  306 LAQMESVLRE-NARLQRDNE----RLQRELES-TSEKASCIEKLENEIQRLSEAHESLMRTSSKREALEKTMRNkMDSEM 379
Cdd:TIGR02169  267 LEEIEQLLEElNKKIKDLGEeeqlRVKEKIGElEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEE-LEREI 345

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847  380 RRLQDFNRDLRERLESANRHLASKTQEAQAGSQDMvAKLLAQSYEQQQEQEKLEREMALLRGAIEDQRRRAELLEQALGN 459
Cdd:TIGR02169  346 EEERKRRDKLTEEYAELKEELEDLRAELEEVDKEF-AETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELAD 424

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847  460 AQSRAARAEEELRKKQAYVE-KVERLQQALGQLQAACEKREqlelrlrtRLEQELKALRAQQRqtgtltggggshtgste 538
Cdd:TIGR02169  425 LNAAIAGIEAKINELEEEKEdKALEIKKQEWKLEQLAADLS--------KYEQELYDLKEEYD----------------- 479

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1958797847  539 lsalRLSEQLREKEEQILALEADMTKWEQKYLEERAMR 576
Cdd:TIGR02169  480 ----RVEKELSKLQRELAEAEAQARASEERVRGGRAVE 513
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 297-632 2.13e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.93  E-value: 2.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847 297 AQATSGSAHLAQMESVLRENARLQRDNERLQRELES-TSEKASCIEKLENEIQRLSEAHESLMRTSSKREALEKTMRNKM 375
Cdd:COG1196   390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEElEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847 376 DSEMRRLQDFNRDLRERLESANRHLASKTQEAQAGSQDMVAKLLAQSYEQQQEQEKLEREM----------------ALL 439
Cdd:COG1196   470 EEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIgveaayeaaleaalaaALQ 549

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847 440 RGAIEDQRRRAELLEQALGNAQSRAAR-AEEELRKKQAYVEKVERLQQALGQLQAACEKREQLE---------------- 502
Cdd:COG1196   550 NIVVEDDEVAAAAIEYLKAAKAGRATFlPLDKIRARAALAAALARGAIGAAVDLVASDLREADAryyvlgdtllgrtlva 629

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847 503 ------LRLRTRLEQELKALRAQ-----------QRQTGTLTGGGGSHTGSTELSALRLSEQLREKEEQILALEADMTKW 565
Cdd:COG1196   630 arleaaLRRAVTLAGRLREVTLEgeggsaggsltGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEEREL 709

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958797847 566 EQKYLEERAMRQFAMDAAATAAAQRDTTLIRHSPQPSPSSSFNEGLLAGNHRHQEMESRLKVLHAQI 632
Cdd:COG1196   710 AEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREI 776
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
340-522 2.44e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.91  E-value: 2.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847  340 IEKLENEIQRLSEAHESLMRTSSKREALEKTMRNKmDSEMRRLQDFNRDLRErLESANRHLASKTQEAQA--GSQDMVAK 417
Cdd:COG4913    612 LAALEAELAELEEELAEAEERLEALEAELDALQER-REALQRLAEYSWDEID-VASAEREIAELEAELERldASSDDLAA 689

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847  418 LlaqsyeqqqeqeklEREMALLRGAIEDQRRRAELLEQALGNAQSRAARAEEELRKKQAYVEKVERLQQAlgQLQAACEK 497
Cdd:COG4913    690 L--------------EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL--ELRALLEE 753

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1958797847  498 R------EQLELRLRTRLEQELKALRAQQRQ 522
Cdd:COG4913    754 RfaaalgDAVERELRENLEERIDALRARLNR 784
PTZ00121 PTZ00121
MAEBL; Provisional
 304-572 2.99e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 2.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847  304 AHLAQMESVLRENARLQRDNERLQRELESTSEKASCIEKL-ENEIQRLSEAheslmrtSSKREALEKTMRNKMDSEMRRL 382
Cdd:PTZ00121  1064 AHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAkKTETGKAEEA-------RKAEEAKKKAEDARKAEEARKA 1136

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847  383 QDFNR--DLRERLESANRHLASKTQEAQAGSQDMVAKllaqsyeqqqeqekLEREMALLRGAIEdqRRRAELLEQALGNA 460
Cdd:PTZ00121  1137 EDARKaeEARKAEDAKRVEIARKAEDARKAEEARKAE--------------DAKKAEAARKAEE--VRKAEELRKAEDAR 1200

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847  461 QSRAARAEEELRK--------KQAYVEKVERLQQALGQLQAAcEKREQLELRLRTRLEQELKALRAQQRQTGTLTGGGGS 532
Cdd:PTZ00121  1201 KAEAARKAEEERKaeearkaeDAKKAEAVKKAEEAKKDAEEA-KKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARK 1279

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1958797847  533 HTGSTELSALRLSEQLREKEEQILALEADMTKWEQKYLEE 572
Cdd:PTZ00121  1280 ADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADE 1319
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 304-644 3.27e-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: 44.28  E-value: 3.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847  304 AHLAQMESVLREnarLQRDNERLQRElestSEKASCIEKLENEIQRLsEAHESLMRTSSKREALEKTmRNKMDSEMRRLQ 383
Cdd:TIGR02168  186 ENLDRLEDILNE---LERQLKSLERQ----AEKAERYKELKAELREL-ELALLVLRLEELREELEEL-QEELKEAEEELE 256

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847  384 DFNRDLRERLESANRhLASKTQEAQAGSQDMVAKLLAqsyeqqqeqekleremalLRGAIEDQRRRAELLEQALGNAQSR 463
Cdd:TIGR02168  257 ELTAELQELEEKLEE-LRLEVSELEEEIEELQKELYA------------------LANEISRLEQQKQILRERLANLERQ 317

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847  464 AARAEEEL----RKKQAYVEKVERLQQALGQLQaacEKREQLELRLrTRLEQELKALRAQQRQTGTLTGGGGSHTGSTEL 539
Cdd:TIGR02168  318 LEELEAQLeeleSKLDELAEELAELEEKLEELK---EELESLEAEL-EELEAELEELESRLEELEEQLETLRSKVAQLEL 393

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847  540 SALRLSEQLREKEEQILALEADMTKWEQKYLEERamRQFAMDAAATAAAQRDTTLIRHSPQPSPSSSFNEGLLAGNHRHQ 619
Cdd:TIGR02168  394 QIASLNNEIERLEARLERLEDRRERLQQEIEELL--KKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELE 471

                          330       340
                   ....*....|....*....|....*
gi 1958797847  620 EMESRLKVLHAQILEKDAVIKVLQQ 644
Cdd:TIGR02168  472 EAEQALDAAERELAQLQARLDSLER 496
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
340-573 6.67e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 6.67e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847  340 IEKLENEIQRLSEAHESLMRTSSKREALE--KTMRNKMDSEMRRLQDfNRDLRERLESANRHLAsktqeaqagsqdmvak 417
Cdd:COG4913    227 ADALVEHFDDLERAHEALEDAREQIELLEpiRELAERYAAARERLAE-LEYLRAALRLWFAQRR---------------- 289

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847  418 llaqsyeqqqeqeklereMALLRGAIEDQRRRAELLEQALGNAQSRAARAEEELR------------KKQAYVEKVERLQ 485
Cdd:COG4913    290 ------------------LELLEAELEELRAELARLEAELERLEARLDALREELDeleaqirgnggdRLEQLEREIERLE 351

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847  486 QALGQLQAACEKREQLELRLRTRLEQELKALRAQQRQTGTLTGGGGSHTGSTELSALRLSEQLREKEEQILALEAdmtkw 565
Cdd:COG4913    352 RELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEA----- 426


                   ....*...
gi 1958797847  566 EQKYLEER 573
Cdd:COG4913    427 EIASLERR 434
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 306-508 8.11e-04

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 42.80  E-value: 8.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847 306 LAQMESVLRENARLQ----RDNERLQRELEStsekASCIEKLENEIQRLSEAHESLMRT--SSKREALEKTMRNKMDSEM 379
Cdd:pfam17380 370 IAMEISRMRELERLQmerqQKNERVRQELEA----ARKVKILEEERQRKIQQQKVEMEQirAEQEEARQREVRRLEEERA 445

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847 380 RRLQDFNRDLRERLESANRhLASKTQEAQAGSQDMVAKLLAQSYEQQQEQEKLEREMALLRGAIEDQRRRAELLEQALGN 459
Cdd:pfam17380 446 REMERVRLEEQERQQQVER-LRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEE 524

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958797847 460 AQSRAA-----RAEEELRKKQAYVEKVERLQQalgQLQAACEKREQLELRLRTR 508
Cdd:pfam17380 525 RQKAIYeeerrREAEEERRKQQEMEERRRIQE---QMRKATEERSRLEAMERER 575
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 307-564 9.99e-04

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 42.37  E-value: 9.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847 307 AQMESVLRENARL--QRDNerlqreLESTSEKASCIEKLENEiqrLSEAHESLMRTSSKREALEKTMrnkMDSEMR---- 380
Cdd:pfam05622 218 EKLEALQKEKERLiiERDT------LRETNEELRCAQLQQAE---LSQADALLSPSSDPGDNLAAEI---MPAEIRekli 285

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847 381 RLQDFNRDLRERLESANRHLASKTQEAQAGSQDMVAKLLAQSYEQQQEQEKLEREMALLRGAIEDQRRRAE---LLEQAL 457
Cdd:pfam05622 286 RLQHENKMLRLGQEGSYRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQGSKAEdssLLKQKL 365

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847 458 GNAQSRAARAEEELRKKQAYVEKVE-----RLQQALGQLQAACEKREQ----LELRLRTRLEQE---LKALRAQQRQtgt 525
Cdd:pfam05622 366 EEHLEKLHEAQSELQKKKEQIEELEpkqdsNLAQKIDELQEALRKKDEdmkaMEERYKKYVEKAksvIKTLDPKQNP--- 442

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1958797847 526 ltggggshTGSTELSALRlsEQLREKEEQILALEADMTK 564
Cdd:pfam05622 443 --------ASPPEIQALK--NQLLEKDKKIEHLERDFEK 471
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
290-478 1.06e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847 290 ALEGPPGAQATSGSAHLAQMESVLRENARLQRDNERLQRELESTSEKascIEKLENEIQRLSEAHESLMRTSSKREALE- 368
Cdd:COG4717    57 ELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEE---LEELEAELEELREELEKLEKLLQLLPLYQe 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847 369 -KTMRNKMDSEMRRLQDFN------RDLRERLESANRHLASKTQEAQAGSQDMVAKLLAQSYEQQQEQEKLEREMALLRG 441
Cdd:COG4717   134 lEALEAELAELPERLEELEerleelRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEE 213

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1958797847 442 AIEDQRRRAELLEQALGNAQSRAARAEEELRKKQAYV 478
Cdd:COG4717   214 ELEEAQEELEELEEELEQLENELEAAALEERLKEARL 250
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
307-476 1.11e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.59  E-value: 1.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847  307 AQMESVLRENARLQRDNERLQRELESTSEKASCIEKLEN---EIQRLSEAHESLMRTSSKREALEKTmrnkmDSEMRRLQ 383
Cdd:COG4913    617 AELAELEEELAEAEERLEALEAELDALQERREALQRLAEyswDEIDVASAEREIAELEAELERLDAS-----SDDLAALE 691

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847  384 DFNRDLRERLESANRHLA------SKTQEAQAGSQDMVAKLLAQSYEQQQEQEKLEREM--ALLRGAIEDQRRR--AELL 453
Cdd:COG4913    692 EQLEELEAELEELEEELDelkgeiGRLEKELEQAEEELDELQDRLEAAEDLARLELRALleERFAAALGDAVERelRENL 771

                          170       180
                   ....*....|....*....|...
gi 1958797847  454 EQALGNAQSRAARAEEELRKKQA 476
Cdd:COG4913    772 EERIDALRARLNRAEEELERAMR 794
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
442-568 1.67e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 1.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847 442 AIEDQRRRAELLEQALGNAQSRAARAEEELRKKQAYVEKVERLQQALGQLQAACEKREQLELRLRTR--LEQELKALRAQ 519
Cdd:COG4717    92 ELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELreLEEELEELEAE 171

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958797847 520 QRQTGTLTGGGGSHTGSTELSAL-RLSEQLREKEEQILALEADMTKWEQK 568
Cdd:COG4717   172 LAELQEELEELLEQLSLATEEELqDLAEELEELQQRLAELEEELEEAQEE 221
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
324-522 2.93e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 2.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847  324 ERLQRELESTSEKASCIEKLENEIQRLSEAHESLMRTSSKREALEKTMRNKMDSEMRRLQDFNRDLRERLESANRHLASK 403
Cdd:COG4913    238 ERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEAR 317

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847  404 TQEAQAGSQDMVAKLLAqsyeqqqeqeKLEREMALLRGAIEDQRRRAELLEQALGNAQSRAARAEEELRK-KQAYVEKVE 482
Cdd:COG4913    318 LDALREELDELEAQIRG----------NGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPAsAEEFAALRA 387

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1958797847  483 RLQQALGQLQAAcekREQLELRlRTRLEQELKALRAQQRQ 522
Cdd:COG4913    388 EAAALLEALEEE---LEALEEA-LAEAEAALRDLRRELRE 423
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 304-522 4.34e-03

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: 40.59  E-value: 4.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847  304 AHLAQMESVLRenARLQRDNERLQRELESTSEKASCIEKLENEIQRLSEAHESLMRTSSKREALEKTMRNKMDSEMRRLQ 383
Cdd:pfam12128  322 SELEALEDQHG--AFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKL 399

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847  384 DFNRDLRERLESANRHlASKTQEAQAGSQdmvakllaqsyeqqqeqekleremalLRGAIEDQRRRAELLEQALGNAQSR 463
Cdd:pfam12128  400 AKIREARDRQLAVAED-DLQALESELREQ--------------------------LEAGKLEFNEEEYRLKSRLGELKLR 452

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958797847  464 AARA---EEELRKKQAYVEKVERLQQALGQLQAACEKREQLELRLRTRLEQELKAL-----RAQQRQ 522
Cdd:pfam12128  453 LNQAtatPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALrqasrRLEERQ 519
PTZ00121 PTZ00121
MAEBL; Provisional
 313-568 4.62e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 4.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847  313 LRENARLQRDNERLQRELESTSEKASCIEKLENEIQRLSEAHESLMRTSSKREALEKTMRNKMDSEMRRLQDFNR----- 387
Cdd:PTZ00121  1383 AKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKkaeea 1462

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847  388 -----------DLRERLESANR--HLASKTQEAQAGSQDMVAKLLAQSYEQQQEQEKLEREMALLRGAIE----DQRRRA 450
Cdd:PTZ00121  1463 kkkaeeakkadEAKKKAEEAKKadEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEakkaDEAKKA 1542

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847  451 ELLEQALGNAQSRAARAEEELRKKQAYVEKVERLQQALGQLQAA--CEKREQLELRLRTRLEQELKA----------LRA 518
Cdd:PTZ00121  1543 EEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAkkAEEARIEEVMKLYEEEKKMKAeeakkaeeakIKA 1622

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958797847  519 QQRQTGTLTGGGGSHTGSTELSALRLSEQLREKEEQILALEADMTKWEQK 568
Cdd:PTZ00121  1623 EELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEE 1672
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
314-521 5.06e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.41  E-value: 5.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847 314 RENARLQRDNerLQRELESTSEKASCIEKLENEIQRLSEAHESlmrTSSKREALEKTMRNKmDSEMRRLQDFNRDLRER- 392
Cdd:PRK02224  229 REQARETRDE--ADEVLEEHEERREELETLEAEIEDLRETIAE---TEREREELAEEVRDL-RERLEELEEERDDLLAEa 302

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847 393 -LESANRHLASKTQEAQAGSQDMVAKLLAQSYEQQQEQEKLEREmalLRGAIEDQRRRAELLEQALGNAQSRAARAEEEL 471
Cdd:PRK02224  303 gLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAES---LREDADDLEERAEELREEAAELESELEEAREAV 379

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958797847 472 RKKQAYVEKVE-RLQQALGQLQAACEKREQLELRL------RTRLEQELKALRAQQR 521
Cdd:PRK02224  380 EDRREEIEELEeEIEELRERFGDAPVDLGNAEDFLeelreeRDELREREAELEATLR 436
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
318-517 6.42e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.05  E-value: 6.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847 318 RLQRDNERLQRELESTSEKASCIEKLENEIQRLSEAHESLMRTSSKREALEKTMRnKMDSEMRRLQDFNRDLRERLESAN 397
Cdd:PRK03918  194 LIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELE-SLEGSKRKLEEKIRELEERIEELK 272

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797847 398 RHLasKTQEAQAGSQDMVAKLLAQSYEQQQEQEKLEREMALLRGAIEDQRRRAELLEQALGNAQSRAARAEEELRKKQAY 477
Cdd:PRK03918  273 KEI--EELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKEL 350

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1958797847 478 VEKVERLQQALGQLQAACEKREQLElRLRTR--------LEQELKALR 517
Cdd:PRK03918  351 EKRLEELEERHELYEEAKAKKEELE-RLKKRltgltpekLEKELEELE 397
 
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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