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Conserved domains on  [gi|2505756949|ref|NP_001408230|]
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angiomotin-like protein 2 [Mus musculus]

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 ...
478-680 1.11e-97

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: 300.92  E-value: 1.11e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949 478 YVEKVERLQQALGQLQAACEKREQLELRLRTRLEQELKALRAQQRQTGTLAGGGgshggsAELSALRLSEQLREKEEQIL 557
Cdd:pfam12240   1 YVEKVERLQQALAQLQAACEKREQLELRLRTRLEQELKSLRAQQRQGGSQGSGP------SEYSAPALMELLREKEERIL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949 558 ALEADMTKWEQKYLEERAMRQFAMDAAATAAAQRDTTLIRHSPQPSPSSSFNEGLLPGNHRHQEMESRLKVLHAQILEKD 637
Cdd:pfam12240  75 ALEADMTKWEQKYLEESTMRQFAMDAAATAAAQRDTTIINHSPRHSYDSSFNEELLLANRRCQEMENRIKNLHAQILEKD 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2505756949 638 AVIKVLQQRSRKDPGKATQGTLRPAKSVPSIFAAAVGTQGWQG 680
Cdd:pfam12240 155 AMIKVLQQRSRKDPGKTDQQSLRPARSVPSISAAATGLHSRQT 197
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
308-562 3.36e-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: 70.35  E-value: 3.36e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949 308 AQMETVLRENARLQRDNERLQRELESTSEKAGRIE-KLENEIQRLSEAHESLMRTSSKREALEKTMRNKMDGEMRRLQDF 386
Cdd:COG1196   239 AELEELEAELEELEAELEELEAELAELEAELEELRlELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERL 318
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949 387 NRDLRERLESANRHLASKTQEAQAGSQDMVA--KLLAQSYEQQQEQEKLEREMALLRGAIEDQRRHAELLEQALGNAQSR 464
Cdd:COG1196   319 EELEEELAELEEELEELEEELEELEEELEEAeeELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL 398
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949 465 AARAEEELRKKQAYVEKVERLQQALGQLQAACEKREQLELRLRTRLEQELKALRAQQRQTGTLAGGGGSHGGSAELSALR 544
Cdd:COG1196   399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
                         250
                  ....*....|....*...
gi 2505756949 545 LSEQLREKEEQILALEAD 562
Cdd:COG1196   479 LAELLEELAEAAARLLLL 496
 
Name Accession Description Interval E-value
Angiomotin_C pfam12240
Angiomotin C terminal; This domain family is found in eukaryotes, and is typically between 197 ...
478-680 1.11e-97

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: 300.92  E-value: 1.11e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949 478 YVEKVERLQQALGQLQAACEKREQLELRLRTRLEQELKALRAQQRQTGTLAGGGgshggsAELSALRLSEQLREKEEQIL 557
Cdd:pfam12240   1 YVEKVERLQQALAQLQAACEKREQLELRLRTRLEQELKSLRAQQRQGGSQGSGP------SEYSAPALMELLREKEERIL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949 558 ALEADMTKWEQKYLEERAMRQFAMDAAATAAAQRDTTLIRHSPQPSPSSSFNEGLLPGNHRHQEMESRLKVLHAQILEKD 637
Cdd:pfam12240  75 ALEADMTKWEQKYLEESTMRQFAMDAAATAAAQRDTTIINHSPRHSYDSSFNEELLLANRRCQEMENRIKNLHAQILEKD 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2505756949 638 AVIKVLQQRSRKDPGKATQGTLRPAKSVPSIFAAAVGTQGWQG 680
Cdd:pfam12240 155 AMIKVLQQRSRKDPGKTDQQSLRPARSVPSISAAATGLHSRQT 197
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
308-562 3.36e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 70.35  E-value: 3.36e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949 308 AQMETVLRENARLQRDNERLQRELESTSEKAGRIE-KLENEIQRLSEAHESLMRTSSKREALEKTMRNKMDGEMRRLQDF 386
Cdd:COG1196   239 AELEELEAELEELEAELEELEAELAELEAELEELRlELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERL 318
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949 387 NRDLRERLESANRHLASKTQEAQAGSQDMVA--KLLAQSYEQQQEQEKLEREMALLRGAIEDQRRHAELLEQALGNAQSR 464
Cdd:COG1196   319 EELEEELAELEEELEELEEELEELEEELEEAeeELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL 398
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949 465 AARAEEELRKKQAYVEKVERLQQALGQLQAACEKREQLELRLRTRLEQELKALRAQQRQTGTLAGGGGSHGGSAELSALR 544
Cdd:COG1196   399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
                         250
                  ....*....|....*...
gi 2505756949 545 LSEQLREKEEQILALEAD 562
Cdd:COG1196   479 LAELLEELAEAAARLLLL 496
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
308-575 2.72e-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: 57.77  E-value: 2.72e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949  308 AQMETVLRENARLQRDNERLQRELESTSEKagrIEKLENEIQRLSEAHESLMRTSSK-REALEKTMRN-------KMDGE 379
Cdd:TIGR02169  723 KEIEQLEQEEEKLKERLEELEEDLSSLEQE---IENVKSELKELEARIEELEEDLHKlEEALNDLEARlshsripEIQAE 799
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949  380 MRRLQDFNRDLRERLESANRHLASKTQEAQAgSQDMVAKLLAQSYEQQQEQEKLEREMALLRGAIEDQRRHAELLEQALG 459
Cdd:TIGR02169  800 LSKLEEEVSRIEARLREIEQKLNRLTLEKEY-LEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALR 878
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949  460 NAQSRAARAEEELRKKQAyveKVERLQQALGQLQAACEKREQLELRLRTRLE---QELKALRAQQRQtgtlagggGSHGG 536
Cdd:TIGR02169  879 DLESRLGDLKKERDELEA---QLRELERKIEELEAQIEKKRKRLSELKAKLEaleEELSEIEDPKGE--------DEEIP 947
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 2505756949  537 SAELSALRLSEQLREKEEQILALEADMTKWEQKYLEERA 575
Cdd:TIGR02169  948 EEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLK 986
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
328-682 1.32e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.33  E-value: 1.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949 328 QRELESTSEKAGRIEKLENEI-QRLseahESLmrtssKREAlEKTMR--------NKMDGEMRRLQDfnRDLRERLESAN 398
Cdd:COG1196   178 ERKLEATEENLERLEDILGELeRQL----EPL-----ERQA-EKAERyrelkeelKELEAELLLLKL--RELEAELEELE 245
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949 399 RHLASKTQEAQAGSQDM------VAKLLAQSYEQQQEQEKLEREMALLRGAIEDQRRHAELLEQALGNAQSRAARAEEEL 472
Cdd:COG1196   246 AELEELEAELEELEAELaeleaeLEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEEL 325
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949 473 RKKQA-YVEKVERLQQALGQLQAACEKREQLELRLRtRLEQELKALRAQQRQTGTLAGGGGSHGGSAELSALRLSEQLRE 551
Cdd:COG1196   326 AELEEeLEELEEELEELEEELEEAEEELEEAEAELA-EAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949 552 KEEQILALEADMTKWEQKYLEERAMRQFAMDAAATAAAQRDTTLIRHSPQPSPSSSFNEGLLPGNHRHQEMESRLKVLHA 631
Cdd:COG1196   405 LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE 484
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2505756949 632 QILEKDAVIKVLQQRSRKDPGKATQGTLRPAKSVPSIFAAAVGTQGWQGLV 682
Cdd:COG1196   485 ELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAA 535
PTZ00121 PTZ00121
MAEBL; Provisional
314-578 4.79e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.06  E-value: 4.79e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949  314 LRENARLQRDNERLQRELESTSEKAGRIEKLENEIQRLSEAHESLMRTSSKREALEKTMRNKMDGEMRRLQDFNR---DL 390
Cdd:PTZ00121  1383 AKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKkaeEA 1462
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949  391 RERLESANR--HLASKTQEA-QAGSQDMVAKLLAQSYEQQQEQEKLEREMALLRGAieDQRRHAELLEQALGNAQSRAAR 467
Cdd:PTZ00121  1463 KKKAEEAKKadEAKKKAEEAkKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKA--EEAKKADEAKKAEEAKKADEAK 1540
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949  468 AEEELRKKQAyVEKVERLQQALGQLQAACEKREQLELRLRTRLEQELKALRaQQRQTGTLAGGGGSHGGSAElsALRLSE 547
Cdd:PTZ00121  1541 KAEEKKKADE-LKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAE-EARIEEVMKLYEEEKKMKAE--EAKKAE 1616
                          250       260       270
                   ....*....|....*....|....*....|..
gi 2505756949  548 QLREKEEQILALEADMTKWEQ-KYLEERAMRQ 578
Cdd:PTZ00121  1617 EAKIKAEELKKAEEEKKKVEQlKKKEAEEKKK 1648
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
440-649 1.57e-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: 45.43  E-value: 1.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949  440 LRGAIEDQRRHAELLEQALGNAQSRAARAEEELRKKQAYVEKVERLQQALGQLQAACEKREQLELRLRTRLEQELKALRA 519
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA 761
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949  520 QQRQTGTLAGGGGSHGGSAELSALRLSEQLREKEEQILALEADMTKWEQKYLEERAMRQFAMDAAATAAAQRDTTLIRHS 599
Cdd:TIGR02168  762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE 841
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 2505756949  600 PQPSPSSSFNEGLLPGNHRHQEMESRLKVLHAQILEKDAVIKVLQQRSRK 649
Cdd:TIGR02168  842 DLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALAL 891
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
308-565 7.64e-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: 42.75  E-value: 7.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949 308 AQMETVLRENARL--QRDNER-LQRELESTSEKAGRIEKLENEIQRLSEAHESLMRTSSKREALEKTMRnkmdgemrrLQ 384
Cdd:pfam05622 218 EKLEALQKEKERLiiERDTLReTNEELRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIR---------LQ 288
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949 385 DFNRDLRERLESANRHLASKTQEAQAGSQDMVAKLLAQSYEQQQEQEKLEREMALLRGAIEDQRRHAE---LLEQALGNA 461
Cdd:pfam05622 289 HENKMLRLGQEGSYRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQGSKAEdssLLKQKLEEH 368
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949 462 QSRAARAEEELRKKQAYVEKVE-----RLQQALGQLQAACEKREQ----LELRLRTRLEQE---LKALRAQQRQtgtlag 529
Cdd:pfam05622 369 LEKLHEAQSELQKKKEQIEELEpkqdsNLAQKIDELQEALRKKDEdmkaMEERYKKYVEKAksvIKTLDPKQNP------ 442
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 2505756949 530 gggshGGSAELSALRlsEQLREKEEQILALEADMTK 565
Cdd:pfam05622 443 -----ASPPEIQALK--NQLLEKDKKIEHLERDFEK 471
 
Name Accession Description Interval E-value
Angiomotin_C pfam12240
Angiomotin C terminal; This domain family is found in eukaryotes, and is typically between 197 ...
478-680 1.11e-97

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: 300.92  E-value: 1.11e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949 478 YVEKVERLQQALGQLQAACEKREQLELRLRTRLEQELKALRAQQRQTGTLAGGGgshggsAELSALRLSEQLREKEEQIL 557
Cdd:pfam12240   1 YVEKVERLQQALAQLQAACEKREQLELRLRTRLEQELKSLRAQQRQGGSQGSGP------SEYSAPALMELLREKEERIL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949 558 ALEADMTKWEQKYLEERAMRQFAMDAAATAAAQRDTTLIRHSPQPSPSSSFNEGLLPGNHRHQEMESRLKVLHAQILEKD 637
Cdd:pfam12240  75 ALEADMTKWEQKYLEESTMRQFAMDAAATAAAQRDTTIINHSPRHSYDSSFNEELLLANRRCQEMENRIKNLHAQILEKD 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2505756949 638 AVIKVLQQRSRKDPGKATQGTLRPAKSVPSIFAAAVGTQGWQG 680
Cdd:pfam12240 155 AMIKVLQQRSRKDPGKTDQQSLRPARSVPSISAAATGLHSRQT 197
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
308-562 3.36e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 70.35  E-value: 3.36e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949 308 AQMETVLRENARLQRDNERLQRELESTSEKAGRIE-KLENEIQRLSEAHESLMRTSSKREALEKTMRNKMDGEMRRLQDF 386
Cdd:COG1196   239 AELEELEAELEELEAELEELEAELAELEAELEELRlELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERL 318
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949 387 NRDLRERLESANRHLASKTQEAQAGSQDMVA--KLLAQSYEQQQEQEKLEREMALLRGAIEDQRRHAELLEQALGNAQSR 464
Cdd:COG1196   319 EELEEELAELEEELEELEEELEELEEELEEAeeELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL 398
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949 465 AARAEEELRKKQAYVEKVERLQQALGQLQAACEKREQLELRLRTRLEQELKALRAQQRQTGTLAGGGGSHGGSAELSALR 544
Cdd:COG1196   399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
                         250
                  ....*....|....*...
gi 2505756949 545 LSEQLREKEEQILALEAD 562
Cdd:COG1196   479 LAELLEELAEAAARLLLL 496
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
340-578 2.94e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 60.72  E-value: 2.94e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949 340 RIEKLENEIQRLSEAHESLmrtSSKREALEKTMRnKMDGEMRRLQDFNRDLRERLESANRHLASKTQEaqagsqdmVAKL 419
Cdd:COG1196   233 KLRELEAELEELEAELEEL---EAELEELEAELA-ELEAELEELRLELEELELELEEAQAEEYELLAE--------LARL 300
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949 420 LAQSYEQQQEQEKLEREMALLRGAIEDQRRHAELLEQALGNAQSRAARAEEELRKKQayvekvERLQQALGQLQAACEKR 499
Cdd:COG1196   301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE------AELAEAEEALLEAEAEL 374
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2505756949 500 EQLELRLRTRLEQELKALRAQQRQTGTLAGGGGSHGGSAELSAlRLSEQLREKEEQILALEADMTKWEQKYLEERAMRQ 578
Cdd:COG1196   375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE-RLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
308-575 2.72e-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: 57.77  E-value: 2.72e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949  308 AQMETVLRENARLQRDNERLQRELESTSEKagrIEKLENEIQRLSEAHESLMRTSSK-REALEKTMRN-------KMDGE 379
Cdd:TIGR02169  723 KEIEQLEQEEEKLKERLEELEEDLSSLEQE---IENVKSELKELEARIEELEEDLHKlEEALNDLEARlshsripEIQAE 799
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949  380 MRRLQDFNRDLRERLESANRHLASKTQEAQAgSQDMVAKLLAQSYEQQQEQEKLEREMALLRGAIEDQRRHAELLEQALG 459
Cdd:TIGR02169  800 LSKLEEEVSRIEARLREIEQKLNRLTLEKEY-LEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALR 878
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949  460 NAQSRAARAEEELRKKQAyveKVERLQQALGQLQAACEKREQLELRLRTRLE---QELKALRAQQRQtgtlagggGSHGG 536
Cdd:TIGR02169  879 DLESRLGDLKKERDELEA---QLRELERKIEELEAQIEKKRKRLSELKAKLEaleEELSEIEDPKGE--------DEEIP 947
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 2505756949  537 SAELSALRLSEQLREKEEQILALEADMTKWEQKYLEERA 575
Cdd:TIGR02169  948 EEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLK 986
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
316-544 9.38e-08

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: 55.16  E-value: 9.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949 316 ENARLQRDNERLQRELESTSEKAGRIEKLENEIQRLSEAHESLMRTSSKREALEKTMRNKMDGEMRRLQDFNRDLRERLE 395
Cdd:COG4942    21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949 396 SANRHLASKTQEAQAGSQDMVAKLLAqsyeQQQEQEKLEREMALLRGAIEDQRRHAELLEQALGNAQSRAARAEEELRKK 475
Cdd:COG4942   101 AQKEELAELLRALYRLGRQPPLALLL----SPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2505756949 476 QAYVEKVERLQQALGQLQAaceKREQLELRLRTRLEQELKALRAQQRQTGTLAGGGGSHGGSAELSALR 544
Cdd:COG4942   177 EALLAELEEERAALEALKA---ERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
308-569 1.21e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 55.45  E-value: 1.21e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949  308 AQMETVLRENARLQRDNERLQRELESTSEKAGRIEKLENEIQR-LSEAHESLMRTSSKREALEKTMRNkMDGEMRRLQDF 386
Cdd:TIGR02168  684 EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRqISALRKDLARLEAEVEQLEERIAQ-LSKELTELEAE 762
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949  387 NRDLRERLESANRHLASKTQEAQAGSQDmVAKLLAQSYEQQQEQEKLEREMALLRGAIEDQRRHAELLEQALGNAQSRAA 466
Cdd:TIGR02168  763 IEELEERLEEAEEELAEAEAEIEELEAQ-IEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE 841
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949  467 RAEEELRKKQayvEKVERLQQALGQLQAACEK-REQLE--LRLRTRLEQELKALRAQQRQTGTlaggggsHGGSAELSAL 543
Cdd:TIGR02168  842 DLEEQIEELS---EDIESLAAEIEELEELIEElESELEalLNERASLEEALALLRSELEELSE-------ELRELESKRS 911
                          250       260
                   ....*....|....*....|....*.
gi 2505756949  544 RLSEQLREKEEQILALEADMTKWEQK 569
Cdd:TIGR02168  912 ELRRELEELREKLAQLELRLEGLEVR 937
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
328-682 1.32e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.33  E-value: 1.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949 328 QRELESTSEKAGRIEKLENEI-QRLseahESLmrtssKREAlEKTMR--------NKMDGEMRRLQDfnRDLRERLESAN 398
Cdd:COG1196   178 ERKLEATEENLERLEDILGELeRQL----EPL-----ERQA-EKAERyrelkeelKELEAELLLLKL--RELEAELEELE 245
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949 399 RHLASKTQEAQAGSQDM------VAKLLAQSYEQQQEQEKLEREMALLRGAIEDQRRHAELLEQALGNAQSRAARAEEEL 472
Cdd:COG1196   246 AELEELEAELEELEAELaeleaeLEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEEL 325
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949 473 RKKQA-YVEKVERLQQALGQLQAACEKREQLELRLRtRLEQELKALRAQQRQTGTLAGGGGSHGGSAELSALRLSEQLRE 551
Cdd:COG1196   326 AELEEeLEELEEELEELEEELEEAEEELEEAEAELA-EAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949 552 KEEQILALEADMTKWEQKYLEERAMRQFAMDAAATAAAQRDTTLIRHSPQPSPSSSFNEGLLPGNHRHQEMESRLKVLHA 631
Cdd:COG1196   405 LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE 484
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2505756949 632 QILEKDAVIKVLQQRSRKDPGKATQGTLRPAKSVPSIFAAAVGTQGWQGLV 682
Cdd:COG1196   485 ELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAA 535
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
311-570 1.93e-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: 1.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949 311 ETVLRENARLQRDNERLQRELESTSEKAGRIEKLENEIQRLSEAHESLMRTSSKREALEKTMRNKMDGEMRRLQDFNRDL 390
Cdd:COG1196   295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949 391 RERLESANRHLAsktQEAQAGSQDMVAKLLAQSYEQQQEQEkleremallrgaiedQRRHAELLEQALGNAQSRAARAEE 470
Cdd:COG1196   375 AEAEEELEELAE---ELLEALRAAAELAAQLEELEEAEEAL---------------LERLERLEEELEELEEALAELEEE 436
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949 471 ELRKKQAYVEKVERLQQALGQLQAACEKREQLELRLRTRLEQELKALRAQQRQTGTLAGGGGSHGGSAELSALRLSEQLR 550
Cdd:COG1196   437 EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLL 516
                         250       260
                  ....*....|....*....|
gi 2505756949 551 EKEEQILALEADMTKWEQKY 570
Cdd:COG1196   517 AGLRGLAGAVAVLIGVEAAY 536
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
316-572 4.70e-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: 53.53  E-value: 4.70e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949  316 ENARLQRDNERLQRELESTSEKAGRIEKLENEI-QRLSEAHESLMRTSSKREALEKtmrnkmdgEMRRLQDFNRDLRERL 394
Cdd:TIGR02169  675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELsQELSDASRKIGEIEKEIEQLEQ--------EEEKLKERLEELEEDL 746
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949  395 ESANRHLASKTQEaqagsQDMVAKLLAqsyeqqqeqeKLEREMALLRGAIEDQRRHaeLLEQALGNAQSRAARAEEELRK 474
Cdd:TIGR02169  747 SSLEQEIENVKSE-----LKELEARIE----------ELEEDLHKLEEALNDLEAR--LSHSRIPEIQAELSKLEEEVSR 809
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949  475 KQAYVEKVERLQQALGQLQAACEKREQLELRLRTRLEQELKALRAQQRQTGTLAGGGGSHGGSAELSALRLSEQLREKEE 554
Cdd:TIGR02169  810 IEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKK 889
                          250
                   ....*....|....*...
gi 2505756949  555 QILALEADMTKWEQKYLE 572
Cdd:TIGR02169  890 ERDELEAQLRELERKIEE 907
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
340-574 1.71e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 51.84  E-value: 1.71e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949  340 RIEKLENEIQRLSEAHESLMRTSSKREALEKTmrnkmdgemrrlqdfnRDLRERLESAnrhlasktQEAQAGSQDMVAKL 419
Cdd:COG4913    226 AADALVEHFDDLERAHEALEDAREQIELLEPI----------------RELAERYAAA--------RERLAELEYLRAAL 281
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949  420 laqsyeqqqEQEKLEREMALLRGAIEDQRRHAELLEQALGNAQSRAARAEEELRK-KQAY----VEKVERLQQALGQLQA 494
Cdd:COG4913    282 ---------RLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDElEAQIrgngGDRLEQLEREIERLER 352
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949  495 ACEKREQLELRLRTRLEQ-------ELKALRAQQRQTGTLAGGGGSHGGSAELSALRLSEQLREKEEQILALEAdmtkwE 567
Cdd:COG4913    353 ELEERERRRARLEALLAAlglplpaSAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEA-----E 427

                   ....*..
gi 2505756949  568 QKYLEER 574
Cdd:COG4913    428 IASLERR 434
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
333-592 5.80e-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: 50.06  E-value: 5.80e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949  333 STSEKAGRIEKLENEIQRLSEAHESLmrtSSKREALEKtmrnkmdgEMRRLQDFNRDLRERLESANRHLASKTQEAQAGS 412
Cdd:TIGR02168  671 SILERRREIEELEEKIEELEEKIAEL---EKALAELRK--------ELEELEEELEQLRKELEELSRQISALRKDLARLE 739
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949  413 QdmvakllaqsyeqqqEQEKLEREMALLRGAIEDQRRHAELLEQALGNAQSRAARAEEELRKKQAYVEKVERLQQALGQL 492
Cdd:TIGR02168  740 A---------------EVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREA 804
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949  493 QAACEKREQLELRLRTRLEQELKALRAQQRQTGTLAGGGGSHGGSAELSALRLSEQLREKEEQILALEADMTKW-EQKYL 571
Cdd:TIGR02168  805 LDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALlNERAS 884
                          250       260
                   ....*....|....*....|.
gi 2505756949  572 EERAMRQFAMDAAATAAAQRD 592
Cdd:TIGR02168  885 LEEALALLRSELEELSEELRE 905
PTZ00121 PTZ00121
MAEBL; Provisional
314-578 4.79e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.06  E-value: 4.79e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949  314 LRENARLQRDNERLQRELESTSEKAGRIEKLENEIQRLSEAHESLMRTSSKREALEKTMRNKMDGEMRRLQDFNR---DL 390
Cdd:PTZ00121  1383 AKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKkaeEA 1462
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949  391 RERLESANR--HLASKTQEA-QAGSQDMVAKLLAQSYEQQQEQEKLEREMALLRGAieDQRRHAELLEQALGNAQSRAAR 467
Cdd:PTZ00121  1463 KKKAEEAKKadEAKKKAEEAkKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKA--EEAKKADEAKKAEEAKKADEAK 1540
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949  468 AEEELRKKQAyVEKVERLQQALGQLQAACEKREQLELRLRTRLEQELKALRaQQRQTGTLAGGGGSHGGSAElsALRLSE 547
Cdd:PTZ00121  1541 KAEEKKKADE-LKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAE-EARIEEVMKLYEEEKKMKAE--EAKKAE 1616
                          250       260       270
                   ....*....|....*....|....*....|..
gi 2505756949  548 QLREKEEQILALEADMTKWEQ-KYLEERAMRQ 578
Cdd:PTZ00121  1617 EAKIKAEELKKAEEEKKKVEQlKKKEAEEKKK 1648
PTZ00121 PTZ00121
MAEBL; Provisional
305-573 8.39e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.29  E-value: 8.39e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949  305 AHLAQMETVLRENARLQRDNERLQRELESTSEKAGRIEKL-ENEIQRLSEAheslmrtSSKREALEKTMRNKMDGEMRRL 383
Cdd:PTZ00121  1064 AHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAkKTETGKAEEA-------RKAEEAKKKAEDARKAEEARKA 1136
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949  384 QDFNR--DLRERLESANRHLASKTQEAQAGSQDMVAKllAQSYEQQQEQEKLEREMALLRGAiEDQRRhAELLEQALGNA 461
Cdd:PTZ00121  1137 EDARKaeEARKAEDAKRVEIARKAEDARKAEEARKAE--DAKKAEAARKAEEVRKAEELRKA-EDARK-AEAARKAEEER 1212
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949  462 QSRAARAEEELRKKQAyVEKVERLQQALGQLQAACEKREQLELrlrtRLEQELKALRAQQRQTGTLAGGGGSHGGSAELS 541
Cdd:PTZ00121  1213 KAEEARKAEDAKKAEA-VKKAEEAKKDAEEAKKAEEERNNEEI----RKFEEARMAHFARRQAAIKAEEARKADELKKAE 1287
                          250       260       270
                   ....*....|....*....|....*....|..
gi 2505756949  542 ALRLSEQLREKEEQILALEADMTKWEQKYLEE 573
Cdd:PTZ00121  1288 EKKKADEAKKAEEKKKADEAKKKAEEAKKADE 1319
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
315-633 1.03e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.08  E-value: 1.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949 315 RENARLQRDNERLQRELESTSEKAGRIEKLENEIQRLSEAHESLMRTSSKREALEKTMRNKMDGEMRRLQDFNRDLRERL 394
Cdd:COG1196   408 AEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELA 487
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949 395 ESANRHLASKTQEAQAGSQDMVAKLLAQSYEQQQEQEKLEREM----------------ALLRGAIEDQRRHAELLEQAL 458
Cdd:COG1196   488 EAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIgveaayeaaleaalaaALQNIVVEDDEVAAAAIEYLK 567
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949 459 GNAQSRAAR-AEEELRKKQAYVEKVERLQQALGQLQAACEKREQLE----------------------LRLRTRLEQELK 515
Cdd:COG1196   568 AAKAGRATFlPLDKIRARAALAAALARGAIGAAVDLVASDLREADAryyvlgdtllgrtlvaarleaaLRRAVTLAGRLR 647
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949 516 ALRAQ-----------QRQTGTLAGGGGSHGGSAELSALRLSEQLREKEEQILALEADMTKWEQKYLEERAMRQFAMDAA 584
Cdd:COG1196   648 EVTLEgeggsaggsltGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALE 727
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 2505756949 585 ATAAAQRDTTLIRHSPQPSPSSSFNEGLLPGNHRHQEMESRLKVLHAQI 633
Cdd:COG1196   728 EQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREI 776
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
440-649 1.57e-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: 45.43  E-value: 1.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949  440 LRGAIEDQRRHAELLEQALGNAQSRAARAEEELRKKQAYVEKVERLQQALGQLQAACEKREQLELRLRTRLEQELKALRA 519
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA 761
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949  520 QQRQTGTLAGGGGSHGGSAELSALRLSEQLREKEEQILALEADMTKWEQKYLEERAMRQFAMDAAATAAAQRDTTLIRHS 599
Cdd:TIGR02168  762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE 841
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 2505756949  600 PQPSPSSSFNEGLLPGNHRHQEMESRLKVLHAQILEKDAVIKVLQQRSRK 649
Cdd:TIGR02168  842 DLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALAL 891
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
305-578 1.60e-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: 45.43  E-value: 1.60e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949  305 AHLAQMETVLREnarLQRDNERLQRElestSEKAGRIEKLENEIQRLsEAHESLMRTSSKREALE--KTMRNKMDGEMRR 382
Cdd:TIGR02168  186 ENLDRLEDILNE---LERQLKSLERQ----AEKAERYKELKAELREL-ELALLVLRLEELREELEelQEELKEAEEELEE 257
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949  383 LQdfnRDLRERLESANRhLASKTQEAQAGSQDMVAKLLAqsyeqqqeqekleremalLRGAIEDQRRHAELLEQALGNAQ 462
Cdd:TIGR02168  258 LT---AELQELEEKLEE-LRLEVSELEEEIEELQKELYA------------------LANEISRLEQQKQILRERLANLE 315
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949  463 SRAARAEEEL----RKKQAYVEKVERLQQALGQLQaacEKREQLELRLrTRLEQELKALRAQQRQTGTLAGGGGSHGGSA 538
Cdd:TIGR02168  316 RQLEELEAQLeeleSKLDELAEELAELEEKLEELK---EELESLEAEL-EELEAELEELESRLEELEEQLETLRSKVAQL 391
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 2505756949  539 ELSALRLSEQLREKEEQILALEADMTKWEQKYLEERAMRQ 578
Cdd:TIGR02168  392 ELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE 431
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
340-526 2.42e-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: 2.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949  340 RIEKLENEIQRLSEAHESLMRTSSKREALEKTMRNKMDgEMRRLQDFNRDLRErLESANRHLASKTQEAQA--GSQDMVA 417
Cdd:COG4913    611 KLAALEAELAELEEELAEAEERLEALEAELDALQERRE-ALQRLAEYSWDEID-VASAEREIAELEAELERldASSDDLA 688
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949  418 KLlaqsyeqqqeqeklEREMALLRGAIEDQRRHAELLEQALGNAQSRAARAEEELRKKQAYVEKVERLQQAlgQLQAACE 497
Cdd:COG4913    689 AL--------------EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL--ELRALLE 752
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 2505756949  498 KR------EQLELRLRTRLEQELKALRAQQRQTGT 526
Cdd:COG4913    753 ERfaaalgDAVERELRENLEERIDALRARLNRAEE 787
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
452-574 2.66e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.52  E-value: 2.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949  452 ELLEQALGNAQSRAARAEEELRKKQAYVEKVERLQQALGQLQ----------AACEKREQLELRLR---------TRLEQ 512
Cdd:COG4913    613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAeyswdeidvaSAEREIAELEAELErldassddlAALEE 692
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2505756949  513 ELKALRAQQRQTGTLAGGGGSHGGSAELSALRLSEQLREKEEQILALEADMTKWEQKYLEER 574
Cdd:COG4913    693 QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEER 754
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
307-477 4.43e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.75  E-value: 4.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949  307 LAQMETVLRENARLQRDNERLQRELESTSEKAGRIEKLENEIQRLSEAHESLMRTSSKREALEKTmrnkmDGEMRRLQDF 386
Cdd:COG4913    619 LAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDAS-----SDDLAALEEQ 693
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949  387 NRDLRERLESANRHLA------SKTQEAQAGSQDMVAKLLAQSYEQQQEQEKLEREM--ALLRGAIEDQ--RRHAELLEQ 456
Cdd:COG4913    694 LEELEAELEELEEELDelkgeiGRLEKELEQAEEELDELQDRLEAAEDLARLELRALleERFAAALGDAveRELRENLEE 773
                          170       180
                   ....*....|....*....|.
gi 2505756949  457 ALGNAQSRAARAEEELRKKQA 477
Cdd:COG4913    774 RIDALRARLNRAEEELERAMR 794
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
308-565 7.64e-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: 42.75  E-value: 7.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949 308 AQMETVLRENARL--QRDNER-LQRELESTSEKAGRIEKLENEIQRLSEAHESLMRTSSKREALEKTMRnkmdgemrrLQ 384
Cdd:pfam05622 218 EKLEALQKEKERLiiERDTLReTNEELRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIR---------LQ 288
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949 385 DFNRDLRERLESANRHLASKTQEAQAGSQDMVAKLLAQSYEQQQEQEKLEREMALLRGAIEDQRRHAE---LLEQALGNA 461
Cdd:pfam05622 289 HENKMLRLGQEGSYRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQGSKAEdssLLKQKLEEH 368
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949 462 QSRAARAEEELRKKQAYVEKVE-----RLQQALGQLQAACEKREQ----LELRLRTRLEQE---LKALRAQQRQtgtlag 529
Cdd:pfam05622 369 LEKLHEAQSELQKKKEQIEELEpkqdsNLAQKIDELQEALRKKDEdmkaMEERYKKYVEKAksvIKTLDPKQNP------ 442
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 2505756949 530 gggshGGSAELSALRlsEQLREKEEQILALEADMTK 565
Cdd:pfam05622 443 -----ASPPEIQALK--NQLLEKDKKIEHLERDFEK 471
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
307-577 7.75e-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: 43.13  E-value: 7.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949  307 LAQMETVLRE-NARLQRDNE----RLQRELESTSekaGRIEKLENEI----QRLSEAHESLMRTSSKREALEKTMRNkMD 377
Cdd:TIGR02169  267 LEEIEQLLEElNKKIKDLGEeeqlRVKEKIGELE---AEIASLERSIaekeRELEDAEERLAKLEAEIDKLLAEIEE-LE 342
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949  378 GEMRRLQDFNRDLRERLESANRHLASKTQEAQAGSQDMvAKLLAQSYEQQQEQEKLEREMALLRGAIEDQRRHAELLEQA 457
Cdd:TIGR02169  343 REIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEF-AETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEE 421
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949  458 LGNAQSRAARAEEELRKKQAYVE-KVERLQQALGQLQAACEKREqlelrlrtRLEQELKALRAQQRqtgtlaggggshgg 536
Cdd:TIGR02169  422 LADLNAAIAGIEAKINELEEEKEdKALEIKKQEWKLEQLAADLS--------KYEQELYDLKEEYD-------------- 479
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 2505756949  537 saelsalRLSEQLREKEEQILALEADMTKWEQKYLEERAMR 577
Cdd:TIGR02169  480 -------RVEKELSKLQRELAEAEAQARASEERVRGGRAVE 513
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
297-524 9.48e-04

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


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 42.90  E-value: 9.48e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949  297 SAQATLGSAHLAQMETVLRENARLQRDNERLQRELESTSEKAGRIEKLENEI-QRLSEAHESLMRTSSKREALEKTMRNK 375
Cdd:pfam12128  255 SAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELnGELSAADAAVAKDRSELEALEDQHGAF 334
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949  376 MD-------GEMRRLQDFNRDLRER------LESANRHLASKTQE-AQAGSQDMVAKLLAQSYEQQQEQEKLEREMALLR 441
Cdd:pfam12128  335 LDadietaaADQEQLPSWQSELENLeerlkaLTGKHQDVTAKYNRrRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAE 414
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949  442 G---AIEDQRRH------------AELLEQALGNAQSRAARA---EEELRKKQAYVEKVERLQQALGQLQAACEKREQLE 503
Cdd:pfam12128  415 DdlqALESELREqleagklefneeEYRLKSRLGELKLRLNQAtatPELLLQLENFDERIERAREEQEAANAEVERLQSEL 494
                          250       260
                   ....*....|....*....|....*.
gi 2505756949  504 LRLRTRLEQELKAL-----RAQQRQT 524
Cdd:pfam12128  495 RQARKRRDQASEALrqasrRLEERQS 520
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
307-509 1.34e-03

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: 42.03  E-value: 1.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949 307 LAQMETVLRENARLQRDNERLQRELEStsekAGRIEKLENEIQRLSEAHESLMRT--SSKREALEKTMRNKMDGEMRRLQ 384
Cdd:pfam17380 374 ISRMRELERLQMERQQKNERVRQELEA----ARKVKILEEERQRKIQQQKVEMEQirAEQEEARQREVRRLEEERAREME 449
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949 385 DFNRDLRERLESANRhLASKTQEAQAGSQDMVAKLLAQSYEQQQEQEKLEREMALLRGAIEDQRRHAELLEQALGNAQSR 464
Cdd:pfam17380 450 RVRLEEQERQQQVER-LRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKA 528
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2505756949 465 AA-----RAEEELRKKQAYVEKVERLQQalgQLQAACEKREQLELRLRTR 509
Cdd:pfam17380 529 IYeeerrREAEEERRKQQEMEERRRIQE---QMRKATEERSRLEAMERER 575
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
443-569 2.56e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 2.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949 443 AIEDQRRHAELLEQALGNAQSRAARAEEELRKKQAYVEKVERLQQALGQLQAACEKREQLELRLRTR--LEQELKALRAQ 520
Cdd:COG4717    92 ELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELreLEEELEELEAE 171
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2505756949 521 QRQTGTLAGGGGSHGGSAELSAL-RLSEQLREKEEQILALEADMTKWEQK 569
Cdd:COG4717   172 LAELQEELEELLEQLSLATEEELqDLAEELEELQQRLAELEEELEEAQEE 221
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
325-523 3.24e-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: 3.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949  325 ERLQRELESTSEKAGRIEKLENEIQRLSEAHESLMRTSSKREALEKTMRNKMDGEMRRLQDFNRDLRERLESANRHLASK 404
Cdd:COG4913    238 ERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEAR 317
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949  405 TQEAQAGSQDMVAKLLAqsyeqqqeqeKLEREMALLRGAIEDQRRHAELLEQALGNAQSRAARAEEELRK-KQAYVEKVE 483
Cdd:COG4913    318 LDALREELDELEAQIRG----------NGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPAsAEEFAALRA 387
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 2505756949  484 RLQQALGQLQAAcekREQLELRlRTRLEQELKALRAQQRQ 523
Cdd:COG4913    388 EAAALLEALEEE---LEALEEA-LAEAEAALRDLRRELRE 423
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
301-479 3.93e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 3.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949 301 TLGSAHLAQMETVLRENARLQRDNERLQRELESTSEkagRIEKLENEIQRLSEAHESLMRTSSKREALE--KTMRNKMDG 378
Cdd:COG4717    67 ELNLKELKELEEELKEAEEKEEEYAELQEELEELEE---ELEELEAELEELREELEKLEKLLQLLPLYQelEALEAELAE 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949 379 EMRRLQDFN------RDLRERLESANRHLASKTQEAQAGSQDMVAKLLAQSYEQQQEQEKLEREMALLRGAIEDQRRHAE 452
Cdd:COG4717   144 LPERLEELEerleelRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELE 223
                         170       180
                  ....*....|....*....|....*..
gi 2505756949 453 LLEQALGNAQSRAARAEEELRKKQAYV 479
Cdd:COG4717   224 ELEEELEQLENELEAAALEERLKEARL 250
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
103-562 5.43e-03

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 40.24  E-value: 5.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949  103 ELPTYE-EAKAHSQYYAAQQAGSRPHVGDRDPRGGVSGGGRRQDEALRELRHGHVRSLSERLLQLSLERNGARVPSHmss 181
Cdd:COG3321    862 PLPTYPfQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAA--- 938
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949  182 shsfPQLARSQQGPQPRGPPAEGPEPRGPPPQYPHAVMAQETAAVTDPRYRPRSSPHFQHAEVRILQAQVPPVFLQQQQY 261
Cdd:COG3321    939 ----AAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAA 1014
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949  262 QYLPQPQEHSPPLHPAALGHGPPSSFGPPAVEGPPSAQATLGSAHLAQMETVLRENARLQRDNERLQRELESTSEKAGRI 341
Cdd:COG3321   1015 AAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAA 1094
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949  342 EKLENEIQRLSEAHESLMRTSSKREALEKTMRNKMDGEMRRLQDFNRDLRERLESANRHLASKTQEAQAGSQDMVAKLLA 421
Cdd:COG3321   1095 LALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALL 1174
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505756949  422 QSYEQQQEQEKLEREMALLRGAIEDQRRHAELLEQALGNAQSRAARAEEELRKKQAYVEKVERLQQALGQLQAACEKREQ 501
Cdd:COG3321   1175 LALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAA 1254
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2505756949  502 LELRLRTRLEQELKALRAQQRQTGTLAGGGGSHGGSAELSALRLSEQLREKEEQILALEAD 562
Cdd:COG3321   1255 LLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAA 1315
PRK12705 PRK12705
hypothetical protein; Provisional
298-376 9.61e-03

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 39.31  E-value: 9.61e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2505756949 298 AQATLGSAHLAQMETVLRENARLQRDNERLQRELESTSEKAGRIEKLENeiqRLSEAHESLMRTSSKREALEKTMRNKM 376
Cdd:PRK12705   57 AKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLEN---QLEEREKALSARELELEELEKQLDNEL 132
 
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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